ID T0K8W1_COLGC Unreviewed; 1825 AA.
AC T0K8W1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=RecQ family ATP-dependent DNA helicase {ECO:0000313|EMBL:EQB49483.1};
GN ORFNames=CGLO_11178 {ECO:0000313|EMBL:EQB49483.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB49483.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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:EQB49483.1}.
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DR EMBL; AMYD01002314; EQB49483.1; -; Genomic_DNA.
DR STRING; 1237896.T0K8W1; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_16_0_1; -.
DR OMA; MAINWTT; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EQB49483.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT DOMAIN 946..1127
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1155..1301
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1584..1667
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1549..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1687..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1729..1825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..789
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1703
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1825 AA; 201732 MW; 5A62E2326D837A9A CRC64;
MGFNSILNTA KQLASNDEAN RDQQGSSQTS DQQGWDKVGD DAKKAFANYQ ADQAQGKGPD
YKEIGGVASA AYSAYNRGAD AGDLDERQKE QLGEDVVAGR SGRKKEPLKS GEEGVDGTQE
GCDGHDDEKS KKLNEELGRE GENVVAGEKK KLREGGFLHG KVDNTTEGIA AEDARGEYID
SSKEALEALS SSTAAQSGGR NEVSTSQADY TGSTDATSGE TGDLSDYTTL GRTTRSGRGI
TRKPSLAVKQ QQQQLLTPSS TTSGGRFQQA ITAQLEQQES TRNNRAAPPS SSQDRRHKPA
PVSTPDLLDD DDEILDLTGN DTILSSDSVA FDEGVTVWNE AQASRPEPLS KRGQKRKSTE
MSKTGDLDSD SDEFPDIYKT LGTPAPKSSR AAKSTKTIPS SIRRANTDKG MVEERTITQT
ISRTQRTYKM TDDPQERGTP RRLPMAVGGQ NAIGRTPSKA FRISSSPESN QRAKSAGLQS
TQQRPRPRVI QDSDDEFDDG DFDAELLATP SRSNFMPASA ARSRPASVPF GGADSSDELV
APDTPSRPQP TTLLPDDSLM SFEADTVQDD STNTLSQPTP SSQGKRSTVL KFILDNPDAM
KAKEMMIQEK LVHNSETFRN VLMDGSREDR NKHKAEKELL MTQQSCLKKA YELLKSHAKL
QGEKEVLVQQ IATAYGDGGD TEQDEIRLDE VSDKVRALEQ SIERHLPSVG IDGESFIDDY
RRSKAIVMST QPSHRTPARA SRSAQAAEEN DNQVIHQTQF PGSSRITDPR DRSPPPFPRS
KPPVPKSTKK SAPPIAKASR RDDFEDNYLD DIEDDFGAFD PEPPISRPLP SRRSPVKASR
PRAMDMSSDY GDDADADMLA LAQDFESRHS SSAETASKRR SILTATSGNL AQPPKSHEPL
KKREVSKAKL SIPPELMKHP WSPDVRRALK DRFRMRGFRP NQLEAINATL AGKDAFVLMP
TGGGKSLCYQ LPAIINSGKT RGITIVVSPL LSLMQDQVDH MSALNIQAVS LNGETTSQKR
NQIFSSFKER SPELFVQLLY VTPEMLNNSP SFMKALQTLH SGKRLARIVI DEAHCVSQWG
HDFRPDYKAL GKLRNHFPTV PIIALTATAT QNVIVDIKHN LGMDNCEVFC QSFNRPNLTY
EVRRKERELV HKIADLIQSK YDQQCGIIYT LSRKTSEQVA EKLRDKYGIL AHHYHAQMSP
EDRIDVQRQW QKDRIHVVVA TIAFGMGIDK PDVRFVIHHS VPKSLEGYYQ ETGRAGRDGN
PSDCILYFGY QDVVTLRKMI ADGDGNEDQK ERQRTMLNRV TAFCDNRENC RRVEILRYFG
EVFNGDECNK TCDNCRAGAV FEQQDFSDKA VGAIQTIRNH EKLTVNQCRE ILLGKKYPPN
IDEDPDDAHG IARGMKQHEV ERILDRLTAE EALEETNVVN KRAGIAIPYL IVGRNAHMFL
SGRRKLLLSV QVSDRGRESS APKPKKRTKK SKEADDVDTG AGPSRHVPPS TNVSSPAQAR
IQNKKKGKSM ATIFDTDEEE EMLLQQMEEQ DLSLHSNGYA KDGFVMSDDE DDAFEPLPKS
RNRSHASRDV GPRIEADGRL GDLDELHQDV VHNFVQEAKK LEEQLRNAQG LRKPLFSERS
FQEMAIRWTT TLPQMRKIPG IEIEKVDKFG TKFIPMVKRC RDNYNSMIGA MDAGDQYIVD
LISSDEDMDE DMEDDDDEEE EEASKYFNGP PPPLRPEVEA WNEQMRVNEL ETAPPTRGSS
GTRGRGGARG GKKPYRRASG GGYKKGGVTK RKASGGASRR SSGGTTASSS RNSTVTHFFP
RGGKRGGVSG GRSGGGGGSI GLMPH
//
