ID F6Z6H7_CIOIN Unreviewed; 1194 AA.
AC F6Z6H7; A0A1W2WIL3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=LOC100179894 {ECO:0000313|Ensembl:ENSCINP00000004562.3};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000004562.3, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000004562.3}
RP IDENTIFICATION.
RG Ensembl;
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 helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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DR EMBL; EAAA01001228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EAAA01001229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002131753.1; XM_002131717.3.
DR AlphaFoldDB; F6Z6H7; -.
DR STRING; 7719.ENSCINP00000004562; -.
DR Ensembl; ENSCINT00000004562.3; ENSCINP00000004562.3; ENSCING00000002232.3.
DR GeneID; 100179894; -.
DR KEGG; cin:100179894; -.
DR GeneTree; ENSGT00940000159168; -.
DR HOGENOM; CLU_001103_14_3_1; -.
DR InParanoid; F6Z6H7; -.
DR OMA; TESKWLF; -.
DR OrthoDB; 5474026at2759; -.
DR TreeFam; TF312852; -.
DR Proteomes; UP000008144; Chromosome 14.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR029491; Helicase_HTH.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR PANTHER; PTHR13710:SF120; WERNER SYNDROME ATP-DEPENDENT HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF14493; HTH_40; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT DOMAIN 267..435
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 469..618
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 853..933
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 937..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 133769 MW; 62E7725AF22DFB1F CRC64;
MDGPDAVIDC LVNVCDKVQD FIAEIEENKF NLVNWTNQLR DSTDKILSNL SQNLDELRTT
LKSQWVKKGE KQTQNSTTLN QIEDCNANQI LSTPKSKQEK RTFKFKSVKK SPSLTPGKWS
IKDINDFDFE SLIQEEEDLK QETEKPVMRK DKVEDLFGDE VDFDLEDIDK IEEMYVGSLE
SKPSPGFSSS YEKKSSPDCY IIPADYGSCS IADNDFDNIE DSKSSDLDTS TTLDDPKYIA
PEKQYTDVLK EYFGHSKFRP MQWKIINTAL NDGRDQCVVM ATGYGKSLCY QYPPVYLDST
AICISPLISL MEDQVLKLHT SNIPAAFLGS AQKNKQETYR DMMGGKFRVV YITPEYAESC
SDVLEELNRN VGISLIAIDE AHCVSQWGHD FRAAYRNLGR LKTILPKVPI IALTATATPE
VRKDICNSLH LKNALITCTS FDRVNLYLDV YKKSGDPAAD LRGLMKQKTV RNKTVYSFEG
PTIIYCPTKK DTAKLGQAVK SLGVRCLIYH AGISMERRSE AHHKFVRDEV ECIVATVAFG
MGIDKPDVRK IIHYGAPKDI ESYYQEIGRA GRDGLPATCH TFFTSGDFNT NRFFLRDISS
AKFKDHKAGM ILKMEQYLTT TSCRRKAVLS HFDKRAESSI FGTEKCCDNC RSRSKQLKGM
GLSVENATPV EEEFDFSKEA QQLFEAVKIT GEKFGLGMPV AFICGSKGKK MFDRFTQHPK
FGSGGNHSQK WWRALGKSLL NEQYLKEKQM RKGSFGATVE IGPKGQEWIG KRQFSSNLPL
MLVPTIDLTN REMRTSSGPS NPTVSTTEGG KTLLPLIPGA GSMSKEKLNK LTLGPYLPTN
PTLNVVKKPT TVDKHSGPLY RLLLALRNEI AQDMDIPPHL VANNKDLLEL SKARPSTKDR
LLRVDGMSVV KVKRIGEPVL VVINSYCTEH EASFDNFDDE DEDFLPPSQA ARKRNDTGVP
TKPITDTVRT TYNLFHERCL TLEEISKERG LQISTLGTHL GDALSACYPV SFRHLGITED
LINLVEDTVR KPPINSDVSR LVPVKDRLGS SVDWSQLKII RTYLTHKYGL VAANQPPVAT
PKPASPAHTV KSKGFQPPVR NSSYNTPSSS SNTQQPGLLQ ISSKRDFSRS FLETPVQLAS
NTGSITLTED SPSTSNYFGE RSSTKKRKLP AWGKGTSNNA KKKFTFKRKS NNFL
//
