ID A0A1S3M229_SALSA Unreviewed; 1995 AA.
AC A0A1S3M229;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=LOC106569987 {ECO:0000313|RefSeq:XP_013997277.1};
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_013997277.1};
RN [1] {ECO:0000313|RefSeq:XP_013997277.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013997277.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR RefSeq; XP_013997277.1; XM_014141802.1.
DR GeneID; 106569987; -.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000087266; Chromosome ssa14.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd18056; DEXHc_CHD4; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF22; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 4; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 374..421
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 452..499
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 532..589
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 626..661
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 743..927
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1059..1208
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1995 AA; 226034 MW; ED7D13B66A9797AA CRC64;
MSGSEEDRDD FGAPEDRSLM HDEEEMSENE APKVKKKKKA KKSRENKSSK RRTSRREDVP
MSSPEPMETP EVDRDEERAV PHSDSEGSDY NPGKKKKKNR GGTSKEKKRS STSADRNGGG
KDKRKDPEPE EEEDEDDDDD SSEPKTSSQL LDDWGMEDID HVFSEEDYRS LTNYKAFSQY
VRPLIAAKNP KIAVSKMMMV LGAKWREFST NNPLRGSAAA NAALAAANVS AAVDSMVAEV
APPLAPAPVA EPQLPPAPPL KKAKTKEGKG PNARKKSKPT PKPVEKKKVA TKKVAPLKIK
LGGFNSKRKR SSSEEDEPDV ESDFDDASMN SVSVSDGSNS RSSRSKKPKS KPKKKKGQYS
AVEEDGDGYE TDHQDYCEVC QQGGEIILCD TCPRAYHMVC LDPDMENAPE GTWSCPHCEK
EGKQWEARED GSEEEEEEEE VEPEPEEDDH HMEFCRVCKD GGELLCCDSC PSSYHIHCLN
PPLPEIPNGE WICPRCTCPP MKGKVQKILT WRWGDPPPPT AIPRPPDLPA DQPDPAPLAG
RPDREFFAKW SNMSYWHCSW VSELQLELHC QVMFRNYQRK NDMDEPPSID FGEGDEEKST
KRKAKDPLYA KMEEKYYRFG IKIAWMMIHR ILNHSQDKKN NIHYLIKWKD LPYDQATWEA
EDMDIPEFDI FRQQYWNHRE LMMGDEGKPG KKMKVKGKTK RLDRPPENPV VDPTIKFERQ
PDYLDSTGGN LHPYQLEGLN WLRFSWAQGT DTILADEMGL GKTVQTAVFL YSLYKEGHSK
GPFLVSAPLS TIINWEREFE MWAPDMYVVT YVGDKDSRAV IRENEFSFEN NAIRGGKRAS
KMKKDSSVKF HVLLTSYELI TIDMAILGSI DWACLVVDEA HRLKNNQSKF FRVLNNYPLQ
HKLLLTGTPL QNNLEELFHL LNFLTPERFS NLEGFLEEFA DIAKEDQIKK LHDMLGPHML
RRLKADVFKH MPSKTELIVR VELSPMQKKY YKFILTRNFE ALNTRSGGNQ VSLLNVVMDL
KKCCNHPYLF PVAAMEAPKM PNGMYDGSAL TKSAGKLTLL QKMMRKLKDG GHRVLIFSQM
TKMLDLLEDF LENEGYKYER IDGSITGGMR QEAIDRFNAP GALQFAFLLS TRAGGLGINL
ATADTVIIYD SDWNPHNDIQ AFSRAHRIGQ NKKVMIYRFV TKASVEERIT QVAKKKMMLT
HLVVRPGLGS KTGSMSKQEL DDILKFGTEE LFKDELGKGD KEAGYWKRVA GENKEEDSQV
IHYDDMAVDR LLDRNQESET PEETEIGSMN EYLGSFKVAQ YVVKDEEEAE EEVQREIIKQ
EESVDPDYWE KLLRHHYEQQ QEDLARNLGK GKRIRKQVNY NDGSQEDRGS RRDWQDDQSD
NNSDYSVASE EGDEDFDERA EGGAANSRRP NRKGMRGDRD KPLPPLLARV GGNIEVLGFN
VRQRKAFLNA VMRYGMPPQD AFTTQWLVRD LRGKAEKEFK AYVSLFMRHL CEPGADGAET
FADGVPREGL SRQHVLTRIG VMSLIRKKVQ EFEHVNGQWS MPWMMELEES KKAAAAAAGA
HPDSPGKTPS TGTPADTQPN TPATAPKTPS TGTPADTQPN TPAPADDPSR TEDAVKDGEK
EEKKDSEGEK ESGKTEDPEI IAIPDEDEKT PSPEQKAKEE EEPMETDEPT NGEAEKKDGE
TAEKSAEGGE GTKSPAAEEK ADVSEVKSED SEAKAEDKKE EQTEKMDTTP ASEEKKEQKE
EKDGVKVEEP AKLQNGDSVK EGAAAGISEE KKKAKTRFMF NIADGGFTEL HSLWQNEERA
ATVTKKTNEI WHRRHDYWLL AGIIQHGYAR WQDIQNDVKY AILNEPFKAE MNRGNFLEIK
NKFLARRFKL LEQALVIEEQ LRRAAYLNMS EDPSHPSMAL NTRFSEVECL AESHQHLSKE
SMSGNKPANA VLHKVLKQLE ELLSDMKADV TRLPATIARI PPVAVRLQMS ERNILSRLAS
RGPEPQPQQQ QMSQQ
//
