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Database: UniProt
Entry: A0A010S9Y8_9PEZI
LinkDB: A0A010S9Y8_9PEZI
Original site: A0A010S9Y8_9PEZI 
ID   A0A010S9Y8_9PEZI        Unreviewed;      2224 AA.
AC   A0A010S9Y8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Sec63 Brl domain-containing protein {ECO:0000313|EMBL:EXF81548.1};
GN   ORFNames=CFIO01_03007 {ECO:0000313|EMBL:EXF81548.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF81548.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF81548.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF81548.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXF81548.1}.
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DR   EMBL; JARH01000366; EXF81548.1; -; Genomic_DNA.
DR   RefSeq; XP_007594823.1; XM_007594761.1.
DR   STRING; 1445577.A0A010S9Y8; -.
DR   KEGG; cfj:CFIO01_03007; -.
DR   eggNOG; KOG0951; Eukaryota.
DR   HOGENOM; CLU_000335_1_0_1; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR   CDD; cd18019; DEXHc_Brr2_1; 1.
DR   CDD; cd18021; DEXHc_Brr2_2; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041094; Brr2_helicase_PWI.
DR   InterPro; IPR048863; BRR2_plug.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR   Pfam; PF21188; BRR2_plug; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF18149; Helicase_PWI; 1.
DR   Pfam; PF02889; Sec63; 2.
DR   PIRSF; PIRSF039073; BRR2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
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:UP000020467}.
FT   DOMAIN          536..720
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          755..967
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1387..1563
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          64..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..217
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..269
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2224 AA;  251796 MW;  BA3A7B639EE1AB30 CRC64;
     MSNQDQHRDV SQYKYSAMSN LVLQADRRFV SRRNDEATGD PESLAGKLSI RDMGARVARE
     IAPKQKKSTG LTGVERGSLQ EGEDVLAREQ KKKKGEKAQP RGAGVLGTGD LFVEGIRYRP
     RTPATRATFE LILKIVSDNL GDVPQTAVIS AADVTLEFLK DDDLKDTEKK REIDDLLGVS
     MSAKEFNELV NLGKKVTDYD AQDEDEDMDD NADDADGAEL DERQGVAVVF EDSDDEEGGI
     VNEVREESSE DEEADEDEDE PAADANDAMD MEDDAMVIDS APRKQAQESK QAKSVSARDI
     DAFWLQRQIG KLYADSHEQH DKTTDALRIL SGEPDEQGGE DKSLREIEND LMELFDYEHH
     ELVQLLIENR EKVVWLTRHS RAETDEERAV VEREMASEGL QWILNEKFGK KGDDQKGRKM
     EIKMDLDAPS SLANAPPAED ERPQGLVGGL QPRKLINLEN LVFDQGNHLM SNPKVRLPEG
     STKRTFKGYE EIHVPPPKKR SDASDTLVPI TEMPEWSRLP FGTTKSLNKI QSKCYPTAFG
     DDGNMLICAP TGSGKTNVAM LTILREIGKN RNPETGDIEL DNFKIVYIAP LKALVQEQVG
     NFGKRLEPYG VKVSELTGDR QLTKAQIAET QIIVTTPEKW DVITRKATDL SYTNLVRLVI
     IDEIHLLHDD RGPVLESIVS RTIRKTEQTG EPVRLVGLSA TLPNYKDVAS FLRVDISTGL
     FHFDGSFRPC PLRQEFIGVT DRKAIKQLKT MNDVTYNKVI EHVGAKGNQM LIFVHSRKET
     AKTARYIRDK ALEMDTINQI LRHDAGSREV LNEAASQATD KDLKDILSYG FGIHHAGMNR
     IDRTDVEDLF ARGAIQVLVC TATLAWGVNL PAHTVIIKGT SVYSPEKGSW VELSPQDVLQ
     MLGRAGRPQY DTYGEGIIIT TQNEIQYYLS LLNQQLPIES QFVSKLVDNL NAEIVLGNVR
     SRDEGVEWLG YTYLFVRMLR SPGLYQVGAE YEDDEALEQK RVDLIHSAAS VLRKSNLIKY
     DEKTGKLQST ELGRIASHYY ITHGSMETYN NLIQPSITTI ELFRVFSLSA EFKYIPVRQD
     EKLELAKLLG RVPIPVKESI EEPHAKINVL LQAYISRLKL DGLALMADMV YVTQSAGRIL
     RAIFEITMKK GWASVAKTAL DLCKMAEKRM WPTMSPLRQF PNCPRDIVQK SERIEVSWSN
     YFDLDPPRMG ELLGMPKAGR TVCGLVAKFP RVEVQAQVQP LTRSMLRVEL SIAPNFEWDV
     EIHGPAESFW IFVEDCDGED ILFSDQFLLR KEYAESESNE HIVDFTVPIT EPMPPNYFIS
     VVSDRWMHSE TRLPVSFHKL ILPERFPPHT ELLELQPLPV AALKAKEYAK LYPDWDHFNR
     IQTQTFNSLY NTDQNVFVGA PTGSGKTVCA EFSLLRHWSK ADAGRAVYIA PFQELIDSRL
     DDWQKRLGGL RGGKTIEKLT GETTTDLKIL ERSDLILATP IQWDVLSRQW KRRKNVSTVE
     LFIADEVHLL GNNMGYVYEI IISRMHYIRT QTELPMRIIA LGVSLANARD LGEWIDAKKH
     DIYNFSPHVR PVPLELHIQS YTNPHFPSLM LSMAKPTYLA ITQMSADKPA IVFVPSRKQT
     RATTRDLLTA AFMDDDEDRF LHAEVEQMRP LLDRISEEAL AESLSHGVGY YHEALSQSDK
     RIVKHLYEHG AIQVLVASRD VCWELNSTAH LVIVMGTQYF EGREHRYVDY SLSEVLHMFG
     KALRPSKDGR GRGVLMLPSA KREFYKKFLN EALPVESHLH NYLHDAFVTE ISTKMIESGD
     DAINWTTFTY FYRRLLANPS FYSLTSTTQD GLSDYMSDLI QTTLQELSDS KIIELDEDDG
     SVAPQNAAMI AAYYNISYIT MQTFLLSLSA KTKLKGVLEI ITSATEFEAI QIRRHEEGIL
     RRIYDRIPVK MAEPVYDSAH FKAFVLLQAH FSRMQLPIDL AKDQEVIISK VLSLLSATVD
     ILSSDGHINA MNAMEMSQMV VQAMWDRDSP LKQIPHFTAE VVKVANEFGY VPIYAMLICK
     TNVEFSHSVK DIFDFMEAMN PEENPDYAKL VKRLGLSQKQ LGEAAAFTND KYPDIELEHS
     VLDEDDIRAN EPAYLSVQIQ RQVEEDEEFD PTVHAPFYPA KKLENWWLVV GEQTTKNLLA
     IKRVTIGREL KVKVEFTVPT AGKHDLKLFL MSDSYVGVDQ EREFSITAAE GMDVDDSDEE
     EDEE
//
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