ID A0A178BCQ9_9PLEO Unreviewed; 1485 AA.
AC A0A178BCQ9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=ATP-dependent DNA helicase {ECO:0000313|EMBL:OAL06830.1};
GN ORFNames=IQ06DRAFT_4260 {ECO:0000313|EMBL:OAL06830.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL06830.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL06830.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL06830.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KV441705; OAL06830.1; -; Genomic_DNA.
DR STRING; 765868.A0A178BCQ9; -.
DR InParanoid; A0A178BCQ9; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000077206; 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: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; 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; IPR018247; EF_Hand_1_Ca_BS.
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; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00487; DEXDc; 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; PS00018; EF_HAND_1; 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 Helicase {ECO:0000313|EMBL:OAL06830.1};
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:UP000077206};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 345..549
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1150..1188
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1258..1413
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 751..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1485 AA; 167022 MW; 639038E58C6367AA CRC64;
MPLFQGRIQV LSADSNNPGS IRRDLSDLSL EPQDASSNLR GFRELFAAPD VHVQAQGTHK
RRKLDSGNGA PVQSVDLDEH KSIVLANVSL DLTFPTLTQD GIPQDVSLPT GNPGSPLVVS
LESFQKIDST TFRAILFNPM TGYGTAIIAA AAKDLLDSIA PHLYTATALA TSSNGKRSRA
VSRAAFVHCL LFPHQAEHNV YTLKVGIRWT VGLSVVEAPS VAAKHMKDDL KLLARYLPSS
TTLGNAAWSI PDFFDAVHVP PSDIQVSPRI QQALSDTNLY PFQTRAVDWL LRREGVAFSS
SGNLESYNEN TTPTSFREIQ DATCRPCYVS QLRGMVVSDL ASAEGDTLQS LRGGILAEEM
GLGKTVELIA LMIHHKRTIT PGKHFDPYTG AYVTPSGATL IISPPSILEQ WISEINTHAP
ELKVFHYKGL PSPSAPKKEH ATATVDNLMR FDVVVTTYNV LSKEIHHATP PPDRSFRNIK
RHERRNSPLV DISWWRVCLD EAQMIESGVS QAARVARIIP RCNAWAISGT PLRKDVQDLR
GLLVFLRCDA FVNNKAVWDR LDKTSFTAIF NQIALRHTKD QIRAELRLPP QKRIVITVPF
TTIEEQNYTD MIRQMCDACW LSPEGLPLDT GRDASHPEVI ERMREWLVRL RQTCLHAHVG
RKNRKALGAK HGALRTVHEV LEVMIEQNDT NWKSESRDMI LQQLRLGHIT AYAGDIADRA
RSALPYYEEA LQEAQAYVRV CRDELLEEKA KIGSTEMPNE QQQSDAEDDK DGESLGRVPV
AQKALRSFLE LEHACNFFIG TTYHQIKEAE IATKPEEEVK HYDELESDWY QKAKIVRREL
LKTTKIRAQK QMSSVEARRP FQQIPHIDDL PDFGGIESRQ VLNTMDNISD FLNAQAEQLQ
LWRTKIVDIL LLRLTDDDDD DQEITGEEYD ESLKAQDELY VYIMALRTLV ADRNSAINGL
TDTLVEHELR AAEKQALRKD IDDDQDNRGH APELVIEVAQ TRRKLQSTLE GGSLKGVISG
IRSLTTTLQW RADGGDARAA GELAVLQKHM ARIQAIFAQQ AKIITELEKE QETFRSTMNQ
RLEYYRQFQH ISDTVSKYKE ELDETFDQRE FLKATKLRQQ KKDIVAGLKT KHTYLTHLRT
ENQAEEQAEC IICQDSIELG VLTTCGHKYC KECINQWWHQ HRTCPLCKQK LRSSDFKDIN
FKPSEIRAQE EVHDPAGSSQ ASSPTASNTS IYSDMSAATM KEIKMIDLDG SYGSKIDMIA
RHLFWIRAND PGAKSIIFSQ FGDFLEVLRE AFKKWRIGVS SITDREGIQK FKSDPAIDCF
LLDAKSDSSG LNLVNATYVF LCEPLINPAI ELQAIARVHR IGQQRPTTVF MYLISDTVEE
AIYDISVARR LEHISKAASR SGTATPAMHE NTLDKANSAE LQAAPLKALL RKKGNGEQVQ
EDDLWHCLFG RQRKVVKPVL DREVGRHLRA EAAEGRMTET APPGN
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