ID T0LSR0_COLGC Unreviewed; 659 AA.
AC T0LSR0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=CGLO_09207 {ECO:0000313|EMBL:EQB51260.1};
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:EQB51260.1, 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|RuleBase:RU363044};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU363044};
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|RuleBase:RU363044}.
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:EQB51260.1}.
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DR EMBL; AMYD01001858; EQB51260.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LSR0; -.
DR STRING; 1237896.T0LSR0; -.
DR HOGENOM; CLU_001613_7_4_1; -.
DR OMA; CIKTCKP; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049163; Pif1-like_2B_dom.
DR PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR Pfam; PF05970; PIF1; 1.
DR Pfam; PF21530; Pif1_2B_dom; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU363044};
KW DNA damage {ECO:0000256|RuleBase:RU363044};
KW DNA recombination {ECO:0000256|RuleBase:RU363044};
KW DNA repair {ECO:0000256|RuleBase:RU363044};
KW Helicase {ECO:0000256|RuleBase:RU363044, ECO:0000313|EMBL:EQB51260.1};
KW Hydrolase {ECO:0000256|RuleBase:RU363044};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT DOMAIN 411..444
FT /note="DNA helicase Pif1-like 2B"
FT /evidence="ECO:0000259|Pfam:PF21530"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..631
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 72612 MW; 26FF8CE21DBF23AF CRC64;
MPLPDKSQND LPIPYPSAHN GSHFPPLASN APLATTIERF EATVTEAPIE KEVQPCPPPQ
DTATPATASD TNSQPLASDD RHTASPTNAS SADAGLRNLT NDEIKILKAE QAEHNLAPPE
KPKEPPLCAE QQHAMDLAMQ GHNVFITGSG GCGKSVLVKA LYRAFSALLQ GSGKTVDLIA
PTGQAALNIE GRTTYNYAGW TPDDLKKPLY SHDPNTYSLI RKAQGKKIFK RRVMSATRKD
TRPFGGVQMI VVGDFCQLPP VDPFQWCMAC GRGMRKIGAS SVCPDGHGIE FEAEDKWAFK
SPEWTRCNFK TVHLTKIHRQ QDEAFIGVLQ KCRLGRFLET DDVNLLLNHE SETENATELK
STKEEVAKRN KQKFDQIPGK IREYQAIDAV ECVQGETSQP PRNLDDHRYA QTLQLKANTP
VVLLANIDLD RGLCNGRQGT VIGFVPGSEV RRPEPPNRGN FEHDDDAYRA AETRHSKIVS
FLDRASASGE KFPLVQFSHG VRCVIGPDCS VIGFGDASPY SHLSRCQIPL AQGWAMTIHK
SQSLSLDRVT VDLAKIFEHG QAYVALSRAR SLRGLKIEGA TAAQLRSTFR VDYAVEQFME
TFEAADIEDN PAGAQEEDES SEEEEEVSEI SQEEYVSSYR EEGPLGQVPF LFDVEGSAR
//
