ID A0A1S3Q8Q8_SALSA Unreviewed; 1935 AA.
AC A0A1S3Q8Q8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Titin-like isoform X2 {ECO:0000313|RefSeq:XP_014036287.1};
GN Name=LOC106590156 {ECO:0000313|RefSeq:XP_014036287.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014036287.1};
RN [1] {ECO:0000313|RefSeq:XP_014036287.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014036287.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000256|ARBA:ARBA00000636};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC {ECO:0000256|ARBA:ARBA00005816}.
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DR RefSeq; XP_014036287.1; XM_014180812.1.
DR GeneID; 106590156; -.
DR OrthoDB; 22809at2759; -.
DR Proteomes; UP000087266; Chromosome ssa29.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR PANTHER; PTHR45884; N-ACETYLTRANSFERASE ECO; 1.
DR PANTHER; PTHR45884:SF1; N-ACETYLTRANSFERASE ESCO1; 1.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1693..1732
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 1851..1919
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 1..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1542..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..75
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1093
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1935 AA; 209030 MW; 00A743A78F9EA2C5 CRC64;
MPAPKRQQTS QDPQTKRRKL DQNEVAMPSN KMTPASATSS KPHREGPSQR RNKKKPPAQR
KDRNKPSKSG RHSSKTRSAQ KATTRTKSNP LVKNAKLPKA TSTSSNNPNS KGTLKRPAKI
SKTASTESDE ELIRTRKPDC IRKYSNGDRG KRKGAQTNPS EAALPSDPVQ MDHNYGIPPA
SRGSHSECEQ SKTKGVTEST RSPKSQRDVK MATQASSVKA SDPVPGQPEQ VNQSSETQEM
QGDSVTTPTD EVNESVETKP DTQIMSPPAL VASSERASDP IPEQLNQSSE TQEMQGDSVT
TPTDEVNESV ETKPDTQIMS PPAIVASSER ASDPILEQLN QSSKMEGDSV TTPTDEVNES
VETKPDTQIM SPPAIVESSE RASDPIPEQL NQSSETQEMQ GDSVTTPTDE VNESVETKPD
TQIMSPPAIV ASSESASDPI PEQLNQSSKM EGDSVTTPTD EVNESVETKP DTQIMSPPAI
VASSERASDP IPEQLNQSSE TQGVQEGSVT TPTVQVNESV ESKLDACIKC ADPVSEQSTK
TQEMQENATG LVNERLETKV NAKILSPPAK GLVAYSSSSD SESESEENER KAVEESRDVT
METQVSSEKI SDPVHEQVNQ SSTSQQIQED SMTTSTYEVC EGPMTTPSES VDTKLDTNIK
SPPSIEAFSK DASDPVPEQV NQICIEIEDM QKNSMTTSPD EVVEHLDTKL DAKIDIPPPL
EASFEETHTV EVSESAGTTL DANIKCPHPA TVHVMQSTEM QEDSAPTPAD QVSESLDTKL
DIEVKSPPPV EVASEETSDN VSEQVKQSTE RQEVQDDSMT IPTDKLRESL ETMSGAKIKS
PPLEALFSAL KESSLCRHPL SDTMRSNVKE FLEVEDSLEI MKKDCDFGVT ESIECTLDLE
TPIIVEDMEI GHCVVEVVGE NGEDVDMDSD LEIIDNSKEV PEKTVQLTKG SENECRLDNS
EAGTEKKGTS SSNQDSTNSG KKEVAKKTQG SPEKPKKQQM NPQARTKARL AALAEQKAAA
SKKASRQLNL LALCEEIADD IATDTMLLKT EEEEEQVVTV EAEPSKEPEG PKPFTQAETV
PIPPTPAGPK EPSTPVVPAA AVSAPAKPPA PEPPQRRFFI SQVTVPLKIH EKKKLTRFQR
LRQVELQREK NMSWTMVKKL KSDQANQKMF PETEAKPAPT LLSTPAVAAP IPVTTTPPPP
SASPAAPTVA APCPTPAAAS PAVTPKLEPP KVEPPKVTPS KGPTLRKRTL PAVPPPMPNG
LKAQKAKPVA EYKPYKARPK YSFDDFQLDD EPKPTVQKAV LSTVQRAALR PTSTTIPRAA
VTLTTAAKHE DSKPTGQKTA VPTGQKAAVP TMQKTAVPTM QKTAVPTLQK AAVPTLQKAA
VPTLQKAAVP TLQKAAVPTL QKAAVPTLQK AAVPTVQKTA VPTVQKTAVP TVQKPAVPTG
QKTAVPAVQK TEVPAVQKTA VPAVQKPAVP AVQKPAVPAG QKPAVPSGQK PAVPSSQKPA
VPAAQKLAVP AAQKPAVPTA QKIVVPTTQK TAPTVQKAVV TKPTVQKAVE TPTPMPRNGK
HEDSKLTVQK AEVPKPTVQK ETVVPTLTPQ TEEKAEASPT PKTAKDEDYI APVSSPPFEE
APRDSVDKDQ CEEKPAVAEI KPASPEVKTE GTTTTESSDS VVVQSADNSS PLSDACLQKE
IKKLKEADKD ENQTTTDAGQ KHFGAVTCGV CGMLYSAANP EDESQHLHFH NQFISAVRYV
GWKKERILGE YPDGKIILVL PDDPKYALKK VEEIREMVDN DLGFQQLETK CPSQTKTFLF
ISNDKKVAGC LIAEHIQEGY RVIEEAVPEG SEGEKVMFER QRAWCCSTDP EPALCGISRI
WVFSMMRRTG IASRMIESLR NNFIYGSYLS KEEIAFSDPT PDGKLFATHY CGTSQFLVYN
FVSGTRSDQP SLSVV
//
