ID R7VE58_CAPTE Unreviewed; 2313 AA.
AC R7VE58;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=ATP-dependent helicase ATRX {ECO:0000256|ARBA:ARBA00031106};
GN ORFNames=CAPTEDRAFT_222005 {ECO:0000313|EMBL:ELU16914.1};
OS Capitella teleta (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Capitellidae; Capitella.
OX NCBI_TaxID=283909 {ECO:0000313|EMBL:ELU16914.1};
RN [1] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELU16914.1, ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELU16914.1,
RC ECO:0000313|Proteomes:UP000014760};
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:CapteP222005}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AMQN01004203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB292835; ELU16914.1; -; Genomic_DNA.
DR STRING; 283909.R7VE58; -.
DR EnsemblMetazoa; CapteT222005; CapteP222005; CapteG222005.
DR HOGENOM; CLU_000863_1_0_1; -.
DR OMA; HSGMDGN; -.
DR Proteomes; UP000014760; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd11726; ADDz_ATRX; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 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); 1.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR041430; ADD_ATRX.
DR InterPro; IPR044574; ARIP4-like.
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; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45797:SF1; HELICASE ARIP4; 1.
DR PANTHER; PTHR45797; RAD54-LIKE; 1.
DR Pfam; PF17981; ADD_ATRX; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022895};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000014760};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 159..318
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1408..1610
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1890..2076
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1839..1861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..700
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..925
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1066
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1250
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1277
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1765
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1792..1825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2313 AA; 262213 MW; 450A545B5AB42A2D CRC64;
MEAHNGSPAK DVAKENPDKE LEIGSNNEQS RENSPAPGKD SKSGSRSRRK PAKVHKVIED
DLDADPYMTM DIDIDSFLVN DEEKGDDPEA MDVGGAIQIL NESSGGPEPS TSKAPAPSVK
SNGDESIDID EKGNIILPEG TVVVEPEDAD SVPAGFKGGS RAESDDQVIV CTACRKQINT
NSINNTKKHP VLQVLICKRC YKWYMSDEIE QDSDGLDNQC RWCGEGGDLI CCDYCSNAFC
KDCIRRNLGQ HYLSQILEAG GLHMICYFRY LNFADFKLAD EKQKWHCFVC DPQPLTPLIT
ECNKIIAEVE KVCNEKERVR QESLKNTKPV TGAPKPVTAK KSTTQSGKHH QTARKSTTPQ
PPRAAPPPQS RSRTAPASTK GATVAMVQPS RIGIAEQIAK QAVQNMAMMR ARSQVRAPPP
KPTPKPTPKV TTPKPRQTLQ PVADIPINEF NVTPVLDRMF AAAQSMHMLL NSLKLELKHA
ARKAEDINQL QSAKQLVALK LKRAFAAYQK SFADIDAFAR NFQPIRKPQH STKRVIGQIA
RAGPSGKPTA EFLAKHGTKL KPNELRMVAG GTGLNHLMPA AKSQPSEVIE LSDSEEEVEE
RGKNGKGTSL KSKKRKVSEE EMKEKKKSKP DEKEEEKGEA KDEKKEEKED EKKDDEAEEE
KKSEKSENSE KEEEEEEEVK DKKEDEEEGE NGDENAEEGE KGEEKEEKDQ EASEDQNEES
KEEKQVEKEE NSSKEKDETP IESKNSDLNG NDEDISEGDD ELNPKFVGFK ALGPMEFDAS
DVSQVDGMDD PKDDVPPAMA EELRVFEESL RQAFTYENED NPKEDEKVSS EASDSDADLS
FEKVEAEFKK KKKHEGKEGE EEEEQEEPVP STSAKLPVPG RSREDIEAQR ILLKKCIDME
GPEDDDDEEE EEEEEVEEMV EVSDDSEDNT SVKSDDSDYD PSSTKRNTSR RKSPRGEDSG
DHDKSSRGRP KKSGHEKKEK KRIKKEEKEA DKKESRKLKK LQKDSDSEDD FEQEVKNLAK
LPKLRVNLKK LEVEGLEKAE KKDKKSEKKE KKEKKKKDEK PEFDLGLSSS SDDSDEDEVE
KPENGDVSLP DEPVEEIEED ENEKARKALL ARANNASDSE AESTSDSDFE SEQKKPQKVK
KTKEKKTAEK KSENEESDAE EIAKSRKKRF RDKLLTEKLS EDDDDSDVVV AKKTSRKRKQ
DEEEWNDSSD ESDINTKSKK KRRKKSESDD DDDDDDDDDD EIGEEEEEEE EESKKKGKKN
GKKGKNSKSK KSKRKRVKMA TDSSEDSSEE KDGSDKEDDE EDVDGKKRKK IRKILKDKKL
SVSTLSAAKA EEERRKRIEE RQKIYNEMTE TDMDSPTKCK ITTKLVLEFD ENKEPILEVN
PKLIRKLKPH QVEAVKFLWN SCVEDLERLR TEEGSGCILA HCMGLGKTLS VISFISTLMF
NEELTKIRTC LVVTPLNTVL NWQAEFAKWL GEDAMDVYEM SSVKNNWGRM DLLQSWQEGG
GIMIIGYELY RILTQHQRVK NKKQKKAFTE TLADPGILVN DRLVVVVNEL VNAGPDIVVC
DEGHILKNDA SGMSKAMNQI KTKRRIILTG TPLQNNLAEY HCMVSFVKPG LLGTRKEFCN
RFVNPITNGQ CSDSTSRDVK VMKRRAHILH DLLAGCVQRR DYSALTKFLP PKNEYVISVR
LSKVQMELYE RYLNTFTNRG MDSGPGCNKG ARLFSDYQNL MKIWTHPWVL RMDEIRQETK
RWNKEDDMES FLDDSEAETD ASFLADSSEE DTKKKKSSKI SEDEDDDLSL SEAEEVGPRR
TRGTRRNDKD EKADENGADK TEKEKKNFAG EVVKKWKTRS RTKDGTYESS EEEEEDKADQ
PLSTEWWGDL LTKEDHYNLE LGGKLSLLAE VLKMAGAIGD KVLVFSQSLL SLNLIEDFLE
HWDTSAEKLE EDEADEGEGV HLSGNHTWIH GADYFRMDGS TSAQLRQSWA EQFNQPSNDR
ARLFLISTKA GSLGINLVAA NRVIVFDASW NPTHDVQSIF RVYRFGQKKP TYVYRFLAQG
TMEEKIYERQ VTKLSLSSRV IDEHQIERHF SSSDLAELYL FKPDRLDDPE RIEEIPALPK
DRLLAELLTS KKEWLVRYLE HDSLLENQVD QELTEEERKA AWEEYENEKK GIVPQGARGA
GGMDHAMMLR QMMLMQQQQQ MQQQMPNYMS LMQQQHQALS LDNIMPDAQQ VAQQIFARNP
TMGTDELERR VQVYIQERMY IAKQQEARRL EALRSQQRPV PAGGASNSAQ YSQMLSSMLQ
SGGMTAAAVQ AMGQRMIPHS ASAPNLEEKA AKK
//
