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Database: UniProt
Entry: A0A066XLS6_COLSU
LinkDB: A0A066XLS6_COLSU
Original site: A0A066XLS6_COLSU 
ID   A0A066XLS6_COLSU        Unreviewed;      2226 AA.
AC   A0A066XLS6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Putative Sec63 Brl domain-containing protein {ECO:0000313|EMBL:KDN66985.1};
GN   ORFNames=CSUB01_06887 {ECO:0000313|EMBL:KDN66985.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN66985.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN66985.1}.
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DR   EMBL; JMSE01000859; KDN66985.1; -; Genomic_DNA.
DR   STRING; 1173701.A0A066XLS6; -.
DR   eggNOG; KOG0951; Eukaryota.
DR   HOGENOM; CLU_000335_1_0_1; -.
DR   OMA; QTEIQYY; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000027238; 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; 2.
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:UP000027238}.
FT   DOMAIN          536..720
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          758..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          31..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2207..2226
FT                   /note="Disordered"
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..272
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2212..2226
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2226 AA;  251942 MW;  6FDB30C9F2BFEB7B CRC64;
     MSNQDQHRDV SQYKYSAMSN LVLQADRRFV SRRNDEATGD PESLAGKLSI RDMGARVARE
     SAPKQKKPTG LPDVERGRLQ EGEDVLAREQ RKKKGETAQP RGAGVLGTGD LLVEGIRYRP
     RTPATRATFE LILKIVSDNL GDVPQTAVIS AADVTLEFLK DDDLKDTEKK REIDDLLGVS
     MSAKEFNELV NLGKKITDYD AQDEDEDMDD NATDADGDEL DERQGVAVVF EDSEDEEGGI
     VNEVREESSE DEDADENEEP PAADAQEADE PDDDAMVIDS APKKQTQDAK QSKTVSARDI
     DAFWLQRQIG KLYTDSHEQH DKTTDALRLL SGEPDEQGGD EKSLREIEND LMELFDYEHH
     ELVQLLIENR EKVVWLTRHS RAETDEQRAV IEREMASEGL QWILNEKFGK KTDDQKGRKM
     EIKMDLDAPS SVANAPPAES ERPQGLVGGL QPRKLINLEN LVFDQGNHLM SNPKVRLPEG
     STKRTFKGYE EIHVPAPKKR SDPGDTLVPI TEMPEWSRLP FGTTKSLNKI QSKCYPTAFG
     DDGNMLICAP TGSGKTNVAM LTILREIGKN RNPETGDIDL DAFKIVYIAP LKALVQEQVG
     NFGKRLEPYG VKVSELTGDR QLTKQQIAET QIIVTTPEKW DVITRKATDL TYTNLVRLVI
     IDEIHLLHDD RGPVLESIVS RTIRKTEQTG EPVRLVGLSA TLPNYKDVAS FLRVDINTGL
     FHFDGSFRPC PLRQEFIGVT DRKAIKQLKT MNDVTYNKVI EHVGANRNQM LIFVHSRKET
     AKTARYIRDK ALEMDTINQI LRHDAGSREV LNEAASQATD KDLKDILPYG FGIHHAGMNR
     IDRTDVEDLF ARGAIQVLVC TATLAWGVNL PAHTVIIKGT SVYSPEKGSW VELSPQDVLQ
     MLGRAGRPQF DTYGEGIIIT TQNEIQYYLS LLNQQLPIES QFVSRLVDNL NAEIVLGNVR
     SRDEGVEWLG YTYLFVRMLR SPGLYQVGAE YEDDGALEQM RVDLIHSAAS VLRKSNLVKY
     DEKTGRLQST ELGRIASHYY ITHGSMETYN NLIQPSITTI ELFRVFSLSA EFKYIPVRQD
     EKLELAKLLG RVPIPVKESI EEPHAKINVL LQAYISRLKL DGLALMADMV YVTQSAGRIL
     RAIFEITMKK GWASVAKTAL DLCKMAEKRM WPTMSPLRQF PGCPRDIVQK AERIEVPWSN
     YFDLDPPRMG ELLGMPKAGR TVCSLVAKFP RVEVQAQVQP LTRSMLRVEL SISPNFEWDV
     EVHGPAESFW IFVEDCDGED ILFSDQFLLR KEYAESESNE HIVDFTVPIT EPMPPNYFIS
     VISDRWMHSE TRLPVSFHKL ILPERFPPHT ELLELQPLPV AALKAKEYAK LYPNWDHFNR
     IQTQTFNSLY NTDQNVFVGA PTGSGKTVCA EFALLRHWAK ADAGRAVYIA PFQELVDLRL
     DDWQKRLSGL RGGKTIEKLT GETTTDLKIL ERSDLVLATP IQWDVLSRQW KRRKNVSTVE
     LFIADEVHLL GNQMGYVYEI IVSRMHYIRT QTELPMRIIA LGVSLANARD LGEWIDAKKH
     DIYNFSPHVR PVPLELHIQS YTNPHFPSLM LSMAKPTYLA ITQMSADKPA IVFVPSRKQT
     RATTRDLLTA AFMDDDEDRF LHAEVEQMRP LLDRVSEEAL AEALSHGVGY YHEALSQSDK
     RIVKHLYEHG AIQVLVASRD VCWELNSTAH LVVVMGTQYF EGREHRYIDY SLSEILHMFG
     KALRASKDGR GRGVLMLPAA KRDFYKKFLN EALPVESHLH NYLHDAFVTE ISTKMIESGD
     DAINWTTFTY FYRRLLANPS FYSLTSTTQE GLSDYMSDLI QTTLQELSDS KIIELDEDDG
     SVAPQNAAMI AAYYNISYIT MQTFLLSLSA KTKLKGVLEI VTSATEFEAI QIRRHEEGIL
     RRIYDRIPVK MAEPVYDSAH FKAFVLLQAH FSRMQLPIDL AKDQEVIVSK VLSLLSATVD
     ILSSDGHLNA MNAMEMSQMV VQAMWDRDSP LKQIPHFTPE VVKVANEFGY VSSSSLILNG
     ANLDFFHSVK DIFDFMEAMN PDENPDYAKL VKRLGLSQKQ LGEAAAFTND KYPDIELEHS
     ILDEEEIRAN EPAYLSVQIQ RQVDEDGEFD PTVHAPFYPA KKLENWWLVI GEEATKNLLA
     IKRVTIGREL KVKLEFTVPT AGNHDLKLFL MSDSYVGVDQ EREFSITAAE GMDVDDSDEE
     EEEDEE
//
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