Article title: Nucleotide-enrichment of live feed: a promising protocol for rearing of Atlantic cod Gadus morhua larvae
Journal: Marine Biotechnology
Authors: Carlos Frederico Ceccon Lanes, Sylvie Bolla, Jorge M.O. Fernandes, Ove Nicolaisen, Viswanath Kiron* and Igor Babiak
Affiliation: Faculty of Biosciences and Aquaculture, University of Nordland, N-8049 Bodø, Norway.
*Corresponding author: Faculty of Biosciences and Aquaculture, University of Nordland,
N-8049 Bodø, Norway. Tel.: +47 755 17399; fax: +47 755 17399.
E-mail address:
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
** * * *
G. morhua RLYGTRAFRDECKFKESLLANNYNAYESLIYPRSYIALSKHGRAKRGNKATTAQTVTHFL
D. labrax .....TV.H...... V.RG...... V...... M......
O. mykiss .....TV.H.....R..M.P...... SV.RG.....N....L...K.....M......
D. rerio ...... T..P...... S..KGF.M...... L...HR.SP.M......
M. musculus ...T.PS.H.....R.T..P...... DL.RGT...... Y..V...S.VSPIM......
H. sapiens ...A.PS.QE....R.T..P...... DL.QGT...... Y..V...S.VSPIM......
.
G. morhua P
D. labrax .
O. mykiss .
D. rerio .
M. musculus .
H. sapiens .
Fig. S1 Alignment of the deduced amino acid sequence of G. morhua fibroblast growth factor 6 (fgf6) with D. labrax (AAV90630), O. mykiss (CAA76422), D. rerio (AAO15997), M. musculus (NP_034334), and H. sapiens (EAW88847). Dots indicate identical residues. Fibroblast-growth factor (FGF) superfamily is boxed. Five heparin binding sites (glycine box) are indicated by asterisks and bold text indicates receptor interaction sites on conserved domain FGF
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua VKKKEKNLTEEMASQDESVAKLTKEKKALQESHQQTLDDLQAEEDKVNTLTKAKTKLEQQ
D. labrax TEN.V...... I...... A......
T. rubripes TEN.V...... I......
D. rerio TEN.V...... I...... A...... S......
G. gallus TEN.V...... AL..TI...... A......
M. musculus TEN.V...... GL..TI...... A...... I.....
H. sapiens TEN.V...S...TALE.NIS...... S...A...... V...... G.I.INA.....
70 80 90 100 110 120
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua VDDLEGSLEQEKKLRMDLERSKRKLEGDLKLAQETVMDLENDKQQSDEKIKKKDFETSQL
D. labrax ...... A...... SI...... E..L......
T. rubripes ...... A...... SI.....E...... R...I...
D. rerio ...... A...... SI...... E...... A..
G. gallus ...... A...... MT..ST...... L...L...... I..I
M. musculus ...... A...... SI..I..E...L..RL...E..M.N.
H. sapiens T...... A....A...... MS..SI.....E...IE..L...E..L...
130 140 150 160 170 180
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua LSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERL
D. labrax ...... SV...... S......
T. rubripes ......
D. rerio ......
G. gallus Q...... A..M...... TS...A..H......
M. musculus Q...... AI.I...... S...A....S......
H. sapiens QAR.D...VHSL.F...... HTL...I....S..A......
190
....|....|....|...
G. morhua EEAGGATSAQIEMNKKRE
D. labrax ...... V......
T. rubripes ...... A......
D. rerio ...... A......
G. gallus ...... A...D......
M. musculus ......
H. sapiens ...S......
Fig. S2 Alignment of the deduced amino acid sequence of G. morhua myosin heavy chain (myhc) with D. labrax (ABC42922), T. rubripes (BAH56385), D. rerio (NP_001018321), G. gallus (AAA48972), M. musculus (NP_001034634), and H. sapiens (AAD29948). Dots indicate identical residues. The myosin tail domain is boxed
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua GALLQ---GPCEQG----KKLKVSEV-PVMLS--HRYVLLLPSDLASLLLGPSSEGGSPA
D. labrax .S.RP---EQL...----....A..S-GTTTT-----I...... R...S....T.SL
S. salar .G...---DRPGP.----...... L-GHADAPSN.TI....T....R...I....SGSP
O. mykiss .G...---DHPGP.----...... L-SHADAPFN.TI....T....R...I....SGSP
D. rerio ....HSVDSAIDP.----.RA..L..KGSSVLGGNKTI.I....V..R..SS.L..SGG-
G. gallus .S.F.QTGDRGGNASLAW.RV.ACKT-NGHNGVEQKTII..ST.I..K...Q.MDESG--
M. musculus .T...QPGDCAPTMSLSW.RV.GFIS-SEQNGTEQKTII.I.....CR...Q.MDESG--
H. sapiens .T...QPDDHAATTSLSW.RV.GCKS-SEQNGMEQKTII.I.....CR...Q.MDESG--
70 80 90
....|....|....|....|....|....|....|..
G. morhua ITLPQLTRYDCEVNAPVQGRQLLLQGEELLRALDQVN
D. labrax F...... D...... L....Y...... H..
S. salar F...... G...... S......
O. mykiss F...... G...... S......
D. rerio --...... D.HH......
G. gallus --.....S...... I..NRN......
M. musculus --.....S...... I..SRN......
H. sapiens --.....S...... I..SRN......
Fig. S3 Alignment of the deduced amino acid sequence of G. morhua hipoxia-inducible factor-1 (hif-1a ) with D. labrax (AAZ95453), S. salar (ACN10960), O. mykiss (AAK30364), D. rerio (AAQ91619), G. gallus (BAA34234), M. musculus (AAC53455), and H. sapiens (AAC50152). Dots indicate identical residues and dashes represent gaps. The Hif-1a C terminal transactivation domain is boxed
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua IWKKMR---GNSCAAIDRSHSSGPLAEPG-IGAMMPGSMSQRLSHLHQHREFLFPGSGSM
M. undulatus ...... ---ED..V.M...L.A.S...S.-M.R....G..SC..S.Q...KSQY....IG
F. heteroclitus V.....---.DG.--M...L.A.S.T.S.LM.R.L..NGP.FP.S.Q...TSQY..D.IR
D. rerio V...L.---HE...VME.KSL.SS.SDKSMAHN--G.MDH.HR------KSQYS.-NQN
M. musculus M..R.KSLM.GT.PLMPDKTI.ANM.PDEFTQKS.R.LGQPLRHLPPPQPPSTRSS-.EN
H. sapiens M..R.KNLR.G..PLMPDKPL.ANVPNDKFTQNP.R.LGHPLRHLPLPQPPSAISP-.EN
70 80 90 100 110 120
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua GPTKKAFP-QQCSYTEYNRLPSHTREGVVSRLLGPSMGSCYLPELTRYDCEVNIPLQGNL
M. undulatus SANE.P..PKS.N..Q..M...NKT..IA...... FE------
F. heteroclitus ..ND.P.SRKS...... P...NKT..IA...... TFEPSC...... V....S.
D. rerio .QPT.HYRE.F.N.R.F.MQ..SKMD.IA...I...FETYS...... V......
M. musculus AK.GFPPQCYASQFQD.GPPGAQKVS..A...... FEPYL...... V.VP.SS
H. sapiens SKSRFPPQCYATQ.QD.SLSSA.KVS.MA...... FE.YL...... V.VL.SS
130
....|....|....|.
G. morhua HLLQGCDLLRALDQSA
M. undulatus ..FAE------
F. heteroclitus ...... Q....CI
D. rerio .....S...... AT
M. musculus T....R...... AT
H. sapiens T....G...... AT
Fig. S4 Alignment of the deduced amino acid sequence of G. morhua hipoxia-inducible factor-2 (hif-2a) with M. undulatus (ABD32159), F. heteroclitus (AAL95711), D. rerio (ABD33838), M. musculus (AAB41496), and H. sapiens (AAB41495). Dots indicate identical residues and dashes represent gaps. The Hif-1a C terminal transactivation domain is boxed
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
** *** * * *
G. morhua QRKVRSRDAARCRRSQETEIFYQLANALPLPHKVSAHLDKAAIMRVTLSFLRMHRLLRAG
M. amblycephala ...... V..E..HS....RRITS...... Y...N..IQSV
D. rerio ...... V..E..HS....RRIAS...... Y...N..IQS-
M. musculus L..EK...... S...... VL....HT..FARG...... S...L.I.Y...... CA..
H. sapiens L..EK...... S...... VL....HT..FARG...... S...L.I.Y...... CA..
70 80 90 100
....|....|....|....|....|....|....|....|....|....
G. morhua EMEGAEPKEEAEEDCMDGFYPRALAGFITVLTEEGDMVYVSDSVSKHIG
M. amblycephala --GPTKT.T.ET.NPT....QQ...... L.M...... IFL.E....Y..
D. rerio --GSTKSQT.KS.TPT....QQ...... L.M...... FL.E....Y..
M. musculus ----EWNQV.KGGEPL.AC.LK..E..VM...A....A.L.EN....L.
H. sapiens ----EWNQVG.GGEPL.AC.LK..E..VM...A....A.L.EN....L.
Fig. S5 Alignment of the deduced amino acid sequence of G. morhua hipoxia-inducible factor-3 (hif-3a) with M. amblycephala (ADF50045), D. rerio (AAQ94179), M. musculus (AAC72734), and H. sapiens (AAH80551). Dots indicate identical residues and dashes represent gaps. The helix–loop–helix domain is boxed. DNA binding sites are indicated by asterisks, bold text indicates E-box/N-box specificity site, and underlined text indicates dimerization interface
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua DLDVQYQGKCKKTCRDVLCPGSSTCVVDQTNNAYCVTCNRICPEVTSPEQYLCGNDGVTY
S. aurata ...... II.
S. salar ..E...... M...... QR..D.F...... II.
O. mykiss ...... Q...Q.F...... II.
T. rubripes ...... H...... II.
D. rerio ..E...... M..D...... II.
G. gallus E.E...... P...... I..
M. musculus E.E...... F...... PS.S......
H. sapiens E.E.....R...... F...... PA.S......
70 80 90 100 110 120
....|....|....|....|....|....|....|....|....|....|....|....|
A. cod ASACHLRRATCLLGRSIGVAYEGKCIKAKSCEDIQCSTGKKCLWDGRMSRGRCSLCEDAC
S. aurata ...... A...... A...... DET.
S. salar ...... Q...... A...... A...... E..
O. mykiss T...... T...... Q...... V...... A...... E..
T. rubripes ...... A...... A...... DET.
D. rerio ...... D..H..A...... AK...... AV.AES.
G. gallus ...... K...... L...... A...... FKVG....A..DEL.
M. musculus S...... K...... L...... T-...... GG...... SKVG...... DEL.
H. sapiens S...... K...... L...... TG...... FKVG...... DEL.
130 140 150 160
....|....|....|....|....|....|....|....|...
A. cod PDSRGDEAVCASDNATYPSECAMKQAACSLGALLEVKHSGSCN
S. aurata .E..T...... T...... M.V......
S. salar SE..TG...... T...... V...T.....T...A......
O. mykiss .E..M...... T...... V...T.....T......
T. rubripes .E..T...... T...... M.V...I..A....
D. rerio .E..SE...... T...... V......
G. gallus .E.KS...... T...... E....M.V......
M. musculus ...KS..P...... A...... E....S.V......
H. sapiens ...KS..P...... A...... E....S.V......
Fig. S6 Alignment of the deduced amino acid sequence of G. morhua follistatin (fst) with S. aurata (AAT09419), S. salar (NP_001117068), O. mykiss (NP_001153960), T. rubripes (NP_001032947), D. rerio (AAD09175), G. gallus (CAA60915), M. musculus (NP_032072), and H. sapiens (AAH04107). Dots indicate identical residues and dashes represent gaps. The Kazal-like domains are boxed
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua MATPGSSVVLSDEEKGYDLDLFCIPKHYAADLERVYIPHGLILDRTERLAREIMKDMGGH
S. senegalensis ...SS.C..I....Q...... S...... E....
I. punctatus ..SSS.C..I..D.Q...... S...... M......
S. salar ..SSSPC..I..D.Q...... D..D......
D. rerio ..SSSPC..I....Q...... M...... D......
G. gallus ...HSPCI.IG.D.Q...... D...K...... M...... G....
M. musculus .P.RSP...I..D.P...... N...E...K.F...... M...... DV..E....
H. sapiens ...RSPG..I..D.P...... N...E.....F...... M...... DV..E....
70 80 90 100 110 120
....|....|....|....|....|....|....|....|....|....|....|....|
****
G. morhua HIVALCVLKGGYKFFADLLDYIKALNRNSDQSIPMTVDFIRLKSYSNDQSTGDIKVIGGD
S. senegalensis ...... R...... C...... E......
I. punctatus ...... R...... Q...... E......
S. salar ...... R...... C...... E......
D. rerio ...... R...... Q......
G. gallus ...... K...... C......
M. musculus ...... R...... C......
H. sapiens ...... R...... C......
130 140 150 160 170 180
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua DLSTLTGKNVLIVEDIIDTGKTMMTLLQLLKQYKPKMVKVASLLVKRTPRSVGYRPDFVG
S. senegalensis ...... K...E.....N...... Y.X
I. punctatus ...... Q...E.....N......
S. salar ...... K...... N...... I...I.
D. rerio ...... K...E.....N......
G. gallus ...... K...S.....N......
M. musculus ...... Q...S.V...S...... S......
H. sapiens ...... Q...S.VR..N...... K.....
190 200 210 220
....|....|....|....|....|....|....|....|..
G. morhua FEIPDKFVVGYALDYNEYFRDLNHICVISESAKESTR-----
S. senegalensis ..V...... TG.GEVQGMKST
I. punctatus ..V...... TG..KYKA----
S. salar ..V...... TG..KYKA----
D. rerio ..V...... TG..KYKA----
G. gallus ..V...... TG.QKYKA----
M. musculus ...... V.....TG.AKYKA----
H. sapiens ...... V.....TG.AKYKA----
Fig. S7 Alignment of the deduced amino acid sequence of G. morhua hypoxanthine–guanine phosphoribosyltransferase (hprt) with S. senegalensis (BAG12569), I. punctatus (ADO28551), S. salar (ACH70616), D. rerio (AAH46003), G. gallus (CAB46657), M. musculus (AAH83145), and H. sapiens (AAA36012). Dots indicate identical residues and dashes represent gaps. The nine residues that are directly involved in forming the phosphoribosylpyrophosphate loop are boxed. The pyrophosphate loops of the hprt are indicated by asterisks. The serine–tyrosine dipeptide that is generally conserved among the flexible loops of known hprt proteins is in bold font
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
*
G. morhua -----MSSAPFFPAHLCDVFKCAMCCLSRAHSLSLLLCVLTLTPAATEAGPETLCGAELV
D. labrax -----....LS.QW...... G....I.CS.T...... T..G......
S. aurata -----....LS.QW...... S....I.CS.T...... T..G.S......
S. salar -----...GH..QW.V.....S....I.CT.T...... S...G......
O. mykiss -----...GH..QW...... S....V.CT.T...... S...G......
D. rerio -----...GH..QG.W...... T.R..PST.T...V....A....TL......
G. gallus MEKINSL.TQLVKCCF..FL.VK.HTV.YI.FFY.G..L....SS.A-......
M. musculus ------M.SS.LFY.A..L..F.SST.-......
H. sapiens MGKISSLPTQL.KCCF..FL.VK.HTM.SS.LFY.A..L..F.SS..-......
70 80 90 100 110 120
....|....|....|....|....|....|....|....|....|....|....|....|
* *****
G. morhua DTLQFVCGERGFYFSKPTGYGPNARRPHNRGIVDECCFQICELRRLEMYCAPAKTSKAAR
D. labrax ...... S--...... S...... G....
S. aurata ...... -...... S--...... S......
S. salar ...... SS..S...... S...... V.SG....
O. mykiss ...... SS..S...... S...... V.SG....
D. rerio ...... D...... SS..S...... S...... V..G.SP.
G. gallus .A...... D...... SSS..L.HK...... S.D...... I.PP.S..
M. musculus .A...... P.....N...... SSI..APQT...... RS.D...... L.PT....
H. sapiens .A...... D.....N...... SSS..APQT...... RS.D...... L.PA.S..
130 140 150 160 170 180
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua SVRAQRHTDLPRGAKIAAKDR------RTAAQQPDKAKHKRPLS-GHNPSSCKEVHQKN
D. labrax ...... M..AP.VSTAGHKVDKGTE.RT...... T.N.KRPLP..SH..F......
S. aurata ...... M..AP.VSTAGHKVDKGTE.RT...... T.N.KRPLP..SH..F....P..
S. salar ...... M..TP.VSTAVQNVDRGTE.RT..H...T.T.K------......
O. mykiss ...... M..TP.VSTAVQSVDRGTE.RT..H...T.P.K------......
D. rerio .L...... I..------T.-----.K.I.-..SH......
G. gallus ...... M.KAQ.------...L..
M. musculus .I...... M.KTQ.------SPSLST
H. sapiens ...... M.KTQ.------...L..
190
....|....|....|....
G. morhua SSRGNSGGRNYRM------
D. labrax .....T...... ------
S. aurata .....A....------
S. salar .....T...... ------
O. mykiss .....T...... ------
D. rerio .....T...... ------
G. gallus T....T.N.....------
M. musculus NKKTKLQR.RKGSTFEEHK
H. sapiens A...SA.NK....------
Fig. S8 Alignment of the deduced amino acid sequence of G. morhua insulin-like growth factor-1 (igf-1) with D. labrax (AAV67967), S. aurata (ABQ52656), S. salar (NP_001117095), O. mykiss (AAA49412), D. rerio (NP_571900), G. gallus (NP_001004384), M. musculus (CAJ18571), and H. sapiens (CAG46659). Dots indicate identical residues and dashes represent gaps. The insulin-like growth factor superfamily is boxed. IGFBP binding surfaces are indicated by asterisks, igf-1 and insulin receptor binding sites are in bold font, and igf-2 receptor binding surfaces are underlined
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
*
G. morhua ------HSVCHTCRRTERSIMTVKKMFSSSSALVFALAMTLYIFQGAS----AETLC
D. labrax METQKRHGH.TL....W...S.R.K..R.S...R..L....LA..VVEI..----.....
S. aurata METQQRHGR..L...... S.R.K....S...R..L....L...VVEV..----.....
S. salar METQKRHEH...... NTR.K..M.S..NRV..I...L....VEV..----.....
O. mykiss METQKRHEY...... NTR.K..M.S..NRV..I...L....VEV..----.....
T. rubripes METQHRNAAP.F...... I...K....S...H..L....L...VVEVT.----I....
D. rerio MEDQLKH--...... S..DSFVNK.I...W.IRMPICI.FL..SA.EV..----.....
G. gallus ------.CAARQI.LLL..FLA.ALDS.AAYGT.....
M. musculus ------MGIPVGK.MLV.LIS..FA.CCIAAYGP---G....
H. sapiens ------MGIP.GK.MLV.LTF..FASCCIAAYRP---S....
70 80 90 100 110 120
....|....|....|....|....|....|....|....|....|....|....|....|
* *****
G. morhua GGELVDALQFVCEDRGFYFSRPTSRTSSRRTQNRGIVEECCFRSCDLNLLEQYCAKPAKS
D. labrax ...... G.GNN......
S. aurata ...... GNN..P......
S. salar ...... SN...S......
O. mykiss ...... SN...S......
T. rubripes ...... G...... K.M......
D. rerio ...... SN...S...... S..N.A......
G. gallus ...... T.....G...... VG.-NN..-I...... A...T....SV..
M. musculus ...... T.....S...... S..ANR.S---...... A...T...T....
H. sapiens ...... T.....G...... A..V.R.S---...... A...T...T....
130 140 150 160 170 180
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua ERDASASALQGIPMMPPLKQEVQKKQHVNNKLSSYAVWDRKAAQRLRRGIPAILKARKFR
D. labrax ...V..TS..V..V..A.....PR....TV.Y.K.E..Q...... V....R.K.Y.
S. aurata ...V..TS..VL.V...... SR....TV.Y.K.E..Q...... V....R.K.Y.
S. salar ...V..TS..V...V.T...D.PR.-..TV.Y.K.E..Q...... V....R.....
O. mykiss ...V..TS..I...V.TI..D.PR.-..TV.Y.K.EA.Q...... V....R.....
T. rubripes ...V..TS..V..V..AV....PR....TV.H.K.E..Q...... V....R.K...
D. rerio ...V..TS..V..V..A.....PR.-..TV.Y.K.D..Q...... R.K...
G. gallus ...L..TS.A.---L.A.NK.SFQ.-PSHA.Y.K.N..QK.SS...Q.EV.G..R..RY.
M. musculus ...V.T.------QAVLPDDFPR-YPVG.FFQ.DT.R-QS.G.....L..L.R..RG.
H. sapiens ...V.TP------.TVLPDNFPR-YPVG.FFQ.DT.K-QST...... L..L.R..RGH
190 200 210 220
....|....|....|....|....|....|....|....|.
G. morhua RQAEKARAKAQE-QTHRPLISLPSKLPPVLLSTDNYVNH--
D. labrax .....IK.QE.A-IF...... A.....S.K-
S. aurata .....IK.QE.A-IF...... G...... A...... K-
S. salar ...V.IK.QE.A-MF.....T...... PP.....S.N-
O. mykiss ...V.IK.QE.A-MF.....T...... PP.....S.N-
T. rubripes .....IK.QE.T-VF...... T..S.I..K-
D. rerio ....RIK.QE.L-LH.....T...... I..P.E...S.K-
G. gallus W...GLQ.AEEARAM...... QR..APRASPEATGPQE
M. musculus ML.KELKEFREA-KR.....V..P.D.AHGGASSEMSSNHQ
H. sapiens VL.KELE.FREA-KR.....A..TQD.AHGGAPPEMASNRK
Fig. S9 Alignment of the deduced amino acid sequence of G. morhua insulin-like growth factor-2 (igf-2) with D. labrax (AAW29441), S. aurata (ABQ52655), S. salar (NP_001117119), O. mykiss (AAA49411), T. Rubripes (CAA17123), D. rerio (AAM75746), G. gallus (NP_001025513), M. musculus (AAH58615), and H. sapiens (AAA60088). Dots indicate identical residues and dashes represent gaps. The insulin-like growth factor superfamily is boxed, and the C-terminal insulin-like growth factor II E-peptide domain is shade-boxed. IGFBP binding surfaces are indicated by asterisks, igf-1 and insulin-receptor binding sites are in bold font, and igf-2 receptor binding surfaces are underlined
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
* * *
G. morhua AIKTVNESASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSH
D. rerio ...... V......
G. gallus ...... Y
M. musculus ...... A...... Y
H. sapiens ...... A...... Y
70 80 90 100 110
....|....|....|....|....|....|....|....|....|....|....|
*
G. morhua LRSLR--KE-NSTTQVLPPLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVA
D. rerio .....SKEQ-G.SS.S......
G. gallus .....PDT.-SNPG.AP.T......
M. musculus .....PEV.Q.NLVLIP.S.S......
H. sapiens .....PEM.-.NPVLAP.S.S......
Fig. S10 Alignment of the deduced amino acid sequence of G. morhua insulin-like growth factor receptor-1 (igf1r) with D. rerio (AAI63723), G. gallus (NP_990363), M. musculus (NP_034643), and H. sapiens (NP_000866). Dots indicate identical residues and dashes represent gaps. The protein kinase catalytic (PKC-like) superfamily is boxed. The active sites are in bold font, the ATP binding sites are indicated by asterisks, and the substrate binding sites are underlined
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua MSDTERTFIAVKPDGVQRGLVGDIIKRFEQKGFKLVAMKMTTAKVELLQQHYADLKERPF
S. aurata AEQK...... I...... II.E...... A...... G...MH.SQDH.EK...... G...
S. salar ..NE...... I...... R...... L....M.G..FIK.PES..KE...... D...
O. mykiss ..NE...... I...... R...... L...... G..FIQ.PES..KK...... D...
D. rerio SAK...... A...... M.E...... R.....FLQ.SED..K...I...D...
G. gallus AANC...... I...... E...... R.....FVH.SED..K...I...D...
M. musculus SGVN....L...... R...E.VR...R...... L.LVQ.SE...RE..VE.R.K..
H. sapiens SWTR...LV...... R....V.Q...RR..T..G...LQ.PESV.AE..Q..RRK..
70 80 90 100 110 120
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua FPSLVKYMSSGPVVAMVWEGLNAVKTGRVMLGETNPADSKPGTIRGDYCIQVGKNIIHGS
S. aurata ..T.ID...... KGV...... F..D.S......
S. salar ..G..S..T...... F.V...... F.....R......
O. mykiss ..G..S..A...... V...... R......
D. rerio Y.G...... L...... V...... F..E..R......
G. gallus Y.G.....N...... V...... F.....R......
M. musculus YSR...... QW.DV.HAS.ALI.A.D.G.AM...... F.ME....V....
H. sapiens Y.A.IR...... Y.V.RAS.A.I.H.DS.EAA...... FSVHISR.V..A.
130 140 150
....|....|....|....|....|....|....
G. morhua DSVESAKHEISLWFKDDEV------
S. aurata ...... NK...... T...LVSYTSCAFSWLY---
S. salar ...... NT..N....PE.LCSYTSCSSQWLY---
O. mykiss ...... NK..N....PE.LCSYTSCSSSWLY---
D. rerio ...D..NT...... PE.LVSFKSCAQQWIYE--
G. gallus ...... QK...... PA.LIDYRSCAHDWVYE--
M. musculus ...... HR..A...REA.LLCWEDSAGHWLYE--
H. sapiens ....G.QR..Q...QSS.LVSWADGGQHSSIHPA
Fig. S11 Alignment of the deduced amino acid sequence of G. morhua nucleoside diphosphate kinase (ndk) with S. aurata (ACF75416), S. salar (AAC03020), O. mykiss (AAO42980), D. rerio (NP_571001), G. gallus (AAB99856), M. musculus (AAD38976), and H. sapiens (AAK61230). Dots indicate identical residues and dashes represent gaps. The Ndk domain is boxed. The active site motifs are in bold font and the multimer interfaces are underlined
10 20 30 40 50 60
....|....|....|....|....|....|....|....|....|....|....|....|
G. morhua QSKTEPPLLRTGTRTIYTAGRPPWYNQRGAQSKEAFVIGLCGGSASGKTTVANNIIEALD
S. salar ...... NK...... VT.TTF...... K......
D. rerio LG...... EH...F...... K......
G. gallus .C.S...... SK...... EH.T...... G...... TM......
M. musculus .C.S...... SK...... EH.T...... A...G...... RM......
H. sapiens .C.S...... SK...... EH.T...... A...G...... RM......
70 80 90 100 110 120
....|....|....|....|....|....|....|....|....|....|....|....|
* *
G. morhua VPWVVLLSMDSFYKVLCEEDQALAASNDYNFDHPGAFDFELLVATLRKLKKGKSVKIPVY
S. salar ...... TKDE.E...K.E...... E...... TV...... I.V...