ID K0KTZ4_WICCF Unreviewed; 1521 AA.
AC K0KTZ4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=SGS1 {ECO:0000313|EMBL:CCH44869.1};
GN ORFNames=BN7_4438 {ECO:0000313|EMBL:CCH44869.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH44869.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH44869.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCH44869.1}.
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DR EMBL; CAIF01000163; CCH44869.1; -; Genomic_DNA.
DR STRING; 1206466.K0KTZ4; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_22_1_1; -.
DR InParanoid; K0KTZ4; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR022758; Helicase_Sgs1.
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 NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF11408; Helicase_Sgs1; 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; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 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, ECO:0000313|EMBL:CCH44869.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328}.
FT DOMAIN 713..890
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 908..1064
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1327..1408
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 31..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..585
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1521 AA; 171201 MW; 2AFE19078943EC86 CRC64;
MKNNLDQHLQ WLEQSRAFVP KKPALQDITL AATANSNTTQ MGSRQAGRLE PASAPLRESS
NEFSPLLSNV EKTTRKSSGL RLARRENSTL KSSGSTSSTS KHSSPQPSTM PAPQQQGIIR
QTVTPAPAVI DLTFDDDMES TPTIPKKRHQ TEPIPMPSTT SKRQREQPND FTSDDFDDTE
LNEALDQHEI RRQASYNVAD VTLESNSTNP DRSLKAPDST RRLPTAPIST TVPIPVPSAP
RPIPAHPSVQ TSITATRTIS TTVPKFVSER ELLKAQQLHI DICERRIDLL LKRNIINEST
ALSEDEKKRK RNELNAQLVA LAKEQTSSKI ELNQLKLSPS SAQPIDKPSF DAPSLPPPSA
PARAQLPAPP PIPVPALNPM TSNLSNRANM EVLQSSRDPR ELRRNQDPRP QQFESVNSDL
EDFDESILID NNPRPNIRRP NNFEEEQEDL SFEGDGLVTS QINPEDQNPN TSDREFLEED
DQGSEDGEYE DADDMPNMES EHNNFVVDRR EVEDLANSSD EEHVDNGEDH LRHRYTNHDE
DNDEDDEIIG SDDDLEEVGG RKFSQIYSED LEMEDDDEDD EVIAPTYTYN EEREATNNPQ
DVIDLDLEIE SIDADTSYHA PPPAPRVQSQ RPQFQPPPTP PRRSIVNEDD FSNSLPSSPF
PDDFDDDELQ ELNGPIIPQL PPSETHEWTP EVFEKLRQIF KLSSFRQNQL EAVNATLSGK
DTFVLMPTGG GKSLCYQLPA VVKSGVTHGT TIVVSPLISL MQDQVEHLWE KNIKAGMINS
KGSPEERRTT FNLFVDGFLD LVYLSPEMIS ASNQAKNAID RLYRQGKLAR VVVDEAHCVS
SWGHDFRPDY KHLSYFKTNY PEIPVMALTA TANDHVKMDI IHNLNLKDPV FLKQSFNRTN
LFYEVLNKDK DHMKHIEMSI LGKFKDQTGI IYCHSKNACE QTSDKLINSG IKCAFYHAGM
TPEDRLDIQK AWQNGTIKVI CATIAFGMGI DKADVRFVIH LTLPRTLEGY YQETGRAGRD
GNYSYCTMFY GFRDARTLQN MISRDKDLDK AGKEKHLTKL RQVIQYCENS TDCRRQQVLQ
YFNEQFHKDQ CAKNCDNCKK GSDASTKFDK DVTEYAKKMT ELVKSIEHEK VTLIYCQDVF
KGSKSNKVTQ AGHDNLNEHG AGKELEKVDI ERIAFHLIAE KILEEFSIFN KAGFASSYIK
LGPQADKLLN NKKRIIMTFF TNSKRTRPGS GNTNASLNRA PSNNNNNTPR SRSRTLNRDE
INNFRFNGNE NGNGDGNASG IGTTATGGPS FTSARELVRS NSNLQHQPSI STPIRLGEAT
FANSQEKRDY SRAFISLKEA RDKAMSRLNV SASTSVASDR LLKTMARKLP QTDFEFKQLE
GFENEIQKGY FNYFKQVLQN FKNLKTNGNG NGSASKPQST ATNSRSIYFS NRDQEENLNV
INQLRQSQKP SNASQSQSLN QYSTQSKKRT KSSQSGNGKY KKYSKKKTYK NNNGSNGGNK
PTSSQKPKKV IRKPTQSAMP L
//
