ID A0A1S3PJ14_SALSA Unreviewed; 2017 AA.
AC A0A1S3PJ14;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Probable helicase with zinc finger domain isoform X1 {ECO:0000313|RefSeq:XP_014027628.1, ECO:0000313|RefSeq:XP_014027637.1};
GN Name=LOC106585679 {ECO:0000313|RefSeq:XP_014027628.1,
GN ECO:0000313|RefSeq:XP_014027637.1};
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_014027637.1};
RN [1] {ECO:0000313|RefSeq:XP_014027628.1, ECO:0000313|RefSeq:XP_014027637.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014027628.1,
RC ECO:0000313|RefSeq:XP_014027637.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014027628.1; XM_014172153.1.
DR RefSeq; XP_014027637.1; XM_014172162.1.
DR GeneID; 106585679; -.
DR KEGG; sasa:106585679; -.
DR OrthoDB; 5405202at2759; -.
DR Proteomes; UP000087266; Chromosome ssa02.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18077; DEXXQc_HELZ; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR049569; HELZ_DEAD-box_1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF365; HELICASE WITH ZINC FINGER DOMAIN-RELATED; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|RefSeq:XP_014027628.1,
KW ECO:0000313|RefSeq:XP_014027637.1};
KW Helicase {ECO:0000313|RefSeq:XP_014027628.1,
KW ECO:0000313|RefSeq:XP_014027637.1};
KW Hydrolase {ECO:0000313|RefSeq:XP_014027628.1,
KW ECO:0000313|RefSeq:XP_014027637.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723};
KW Nucleotide-binding {ECO:0000313|RefSeq:XP_014027628.1,
KW ECO:0000313|RefSeq:XP_014027637.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 187..215
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 187..215
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1127..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1577..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1743..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1913..2017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1146
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1932..1952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1998..2017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2017 AA; 224980 MW; EE34F110ACA33C0A CRC64;
MADRRAEKSC EEASGSLARR EYEVAVSHCT DALLALGPPA LPSPGTPASN PPNDTVTPLR
SRALLYRIAA LLQLKNYDQA DEDCKHVLAE ELAKGDGSFQ ASLRCMLLDG SLHEVAGLLS
KSLFGEPLNG IVTKDLTRLK MLLSEIEAIR GEMATEYTDD NEEVMSLWSK VRDGWQFRPP
PRGVTSSEEY TLCKRFVEQG LCRYGAQCTS AHSQEELMEW QKRYASRLIR LKQQQESKHF
TENYMEALIE KWMNSLSPEK VLSDYLDGVN VEHSSNLSVT VTTKKSAHSW TFSLFCKPVR
KLYRIALLYD AHRPHFSITA VSVGDAGAQR LQAAAEGCQE WTAGEEALAA DNGMDHCVYT
VVVGFSTEIF GTFRQTIVFD FGSEPVLMQR IMVDAASIED LEHLMQARQQ LLMTAKRWDP
SCKTIVEFSP NETVDLDRSL LARYQIPLSA DQLFTQSVLD KTLTRDNYQA RLHDLLYIEE
IAQYKEVSKF NIKVNLQLVT SFMLTGISGG AKYAQNGQLF ARFKLTETLS EDTLAGRLVM
TKVNSVLLLP LARQEWCSQP PGVKERVYEA CIEEKTKDYI FLRICKDCCE ELGLIPDREL
QVELQFQLNR LPLCEMHYAL DRIKDNGILF PDASLTPTIP WSPNRQWDEQ LDPRLNAKQK
EAILAITTPL TIPLPPVLII GPYGTGKTFT LAQAVKHILR QDDSRVLICT HSNSAADLYI
KDYLHPYVEA GNAHARPLRV YFRNRWVKTV HPLVQQYCLI SNTQYTFQMP EREDILRHRV
VVVTLSTSQY LCQLDLEPGL FSHILLDEAA QAMECETIMP FALASKSTRI VLAGDHMQLS
PFVYSEFSRE RNLHVSLLDR LYEHYPAEFP CRILLCENYR SHEAIISYTS ELFYDGKLMA
SGKQPSHKDF YPLTFFTARG EDVQEKNSTA YYNNAEVFEI VERVEEMRKK WPVAWGKLDE
GSIGVVSPYA DQVFRIRAEL RKKRMHEVSV ERVLNVQGKQ FRVLFLSTVR TRHTCKHKQT
AIKRKEQLVE DSTEDLDYGF LSNYKLLNTA ITRAQSLVAV VGDPIALCSV GRCRKFWEKF
ISICHENASL HGITFEQIKA QLEALELKKT YVLNPLAPEF IPRALRPQPA QHPHHHQHHH
QHPHPQGHTA SKQPGPQQQQ QRSPPKGKGQ HANHTEHFPP EGFVQPNPAV LMGNPIRAFT
PPLGGTPGGM GKSPSPVQRI DPHTGASILY VPAVYGGNMV MSMPLPSVPI QLPWPGYQNR
FAMDPRIMSH QAAMAYNLNL LQAQNRGSPI PYGGVAHPSP LGMGQQTSPD KELQADSTRN
GKMDGCAKSE QIRLQTPERK TSEMKDKPGE CDPGGGRSLD SQTDGLGFPN AMLHRKDNSS
QRPLNYHLAP PNPAFAPHPV GRAFPPQYPG VSRLPFRVPS QHPGGGPAMG QPNQHHSAQL
SPAYDSGRHN PSFFGGVMAS HRVVPETEEE GPEEMGNSMR SQMGHQGGHH PALSQPSRVN
SFGEENQEGG LGDGMDPLAL EALSQQARLG QWGEPGPFLQ GGVAFPLPQQ LAHLAQPGLA
RFPPQLLARA NWRMSAGMED EAGGPPFTRF PGLLREMPPQ DQPDPRDLAE MQPPPQSRLL
QYRQVQSRSP GDPSSPSSAT SNHTGPFPPG PYPGRDPTSH ELDLLNNPGL QQHPGNQLYN
PNAYPHQLGH STTPPPQVKY LLQEAQWPHG GAGVAQNHML AQGQGFPYGL PIMAHPSRQE
QVHLMQLHHQ QQQQQHHQQQ QQQQQQGQGP GQEPYHPLSP RTTGATALHN VEEYEPRGPG
RPLYQRRISS SYPDEGSPAN AAAMTQQQPQ PCPGDPQEHP HQHPHPHQHT HQHPHAPYGY
PPPELWPGNG GGPGPFQNIP CNGASTLVQH QHRDLLVASK ALRQAAEEQM KAEAAVAAAQ
PPAHSLQHLG QFPPLMPNSK QQPQQQQQAP PEPGQGPGGP QNPGKPPTMS YASALRAPPK
PRARPEQVKK HSDPLSLLQE LSIGSSNGSN GYYSYFK
//
