ID A0A3D8QSZ0_9HELO Unreviewed; 1504 AA.
AC A0A3D8QSZ0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BP6252_10462 {ECO:0000313|EMBL:RDW64811.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW64811.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW64811.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW64811.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RDW64811.1}.
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DR EMBL; PDLM01000012; RDW64811.1; -; Genomic_DNA.
DR STRING; 1849047.A0A3D8QSZ0; -.
DR Proteomes; UP000256645; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 1.
DR CDD; cd18793; SF2_C_SNF; 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); 1.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000256645};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 357..561
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1162..1200
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1272..1428
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 20..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1504 AA; 170483 MW; 4B920E1927270CFD CRC64;
MGRNRAARAV GGGTVAALTL PSRRGGLHPS QRLPPAGIPE QPSNALDVAA NDLVANGLPE
SLIDFARHSG AFSKEPARKR QKTGEHSRND RTVTDLTGKS VQAPDFVTLC KASWEVRCIG
SKLSNLQTPL RREDIKAYIR LLPGERQSYV EIVDDDQRTI YWTTFPAEDE LSEEIKLAIE
IQNLSSKDWA RVEGKIWTIL DVVLFYKEDS DHLRLDFTIR WNVTTSPYNL HQATKKPAAI
SRLLNHYIPD DQIAYVNKWS PQDFYNSVHV PPKEDAQATS IQVDLLETEL YPFQKRSLQW
LLRREGVEWA SERIQKMQSP DPERLPHSFV QCKDVNGRIY YASNLYGVAT YDVTPFLSVE
QNTTGGILSE EMGLGKSVEV LSLITLHRRD LHAVANSSKV FDPYTEEEVT PTNTTLIITP
PAILGQWLSE IKRYAPSLKV MHYQGLRLHR ETPTTLLANL ADCDIVLTTY GVLSAELNFT
KLNPEKVLRG KKKYERPKSP LLELQFFRVA IDEAQMIESG VSAAAIVART IPRVHAWCIT
GTPVRNEVGD LQGLLIFLRK EPYASNKHVW SSLVSSHKHN FQTLFGSLAL RHSKQAVRDE
LRLPAQRRYV ITMPFTPIEE QHYQELFLQM CEEIGLDSEG TPTSDNWDPK RNSTTEAMRT
WLLRLRQTAL HPEVGGRNRR ALGNGDSPLR TVDQVLDAMM DQTDSTVRAD QRSLLMLKLK
RGQLFENSPR VKEALAIWTE AHQQAASIVA ECREQLRLEH QNVKANSGSS QSTESAKPSD
VDSDEADEQE EVDATSRLGV FRNRLRAALE IEHMAVFFLA NAHFQIKSNE ELTQPESPEF
EALDKLETEG YEKAKKIRQE ILLEIFRKAN KLMRTIAKKA ANQSFSEIPD FPTAPPKGGI
ESRRIMERLD ELGEALDAQA NQLDEWRENT IQFLLRPLVD EDDGVEITGD EYDSSTKTQD
EVLVYIMVLK AVITDRHEAL TGQENKLTEF DVKVALRLAK EGEGAFPQKT IELLAVRQQI
MPSKEMGSVR GVVADLRALA TSLRLDADNG SGRAQNELSI VNSQLKLVQK HLSDQSKASS
ALEKEIELFN TVSNARIEYY RQLQEVSDMV APYEGVNNER ILETILEEEA KLERKIATAK
AKRRYLLHLR EEAINPTEQR ICIICRESFE MGALTVCGHQ YCKECIKLWW SAHHNCPVCK
KKLTHADLHD ITYKPQELSI QAEEVSTVNQ QRSSSDAKPR KSAIYSEISK TKLAEIKNIE
LDGPSFTTKV DTLARHLIWL RESDPGAKSI IFSQFRDFLD VLARAFTRFR IGYASIDKPD
GITRFKEDPG TECFLLHARA HSSGLNLVNA SHVFLCEPLL NTALELQAIA RVDRIGQHQE
TSVWLYLVQD TVEESIHQLS VRRRMEHMGQ SLFKKKGKSK STTPEEILDS NLEEANSMEL
QQAALTKLLM KGGKGGEMVE NEDLWDCLFG GVEQRKQMRN SDLRHNTEVR RHLVAEAAEQ
RWEQ
//
