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
//