ID T0KYJ2_COLGC Unreviewed; 1096 AA.
AC T0KYJ2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU367027};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU367027};
GN ORFNames=CGLO_02276 {ECO:0000313|EMBL:EQB57578.1};
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:EQB57578.1, 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 -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair by
CC homologous recombination and in genome maintenance. Capable of
CC unwinding D-loops. Plays a role in limiting crossover recombinants
CC during mitotic DNA double-strand break (DSB) repair. Component of a
CC FANCM-MHF complex which promotes gene conversion at blocked replication
CC forks, probably by reversal of the stalled fork.
CC {ECO:0000256|ARBA:ARBA00003813, ECO:0000256|RuleBase:RU367027}.
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 ECO:0000256|RuleBase:RU367027};
CC -!- SUBUNIT: Interacts with the MHF histone-fold complex to form the FANCM-
CC MHF complex. {ECO:0000256|ARBA:ARBA00011390,
CC ECO:0000256|RuleBase:RU367027}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367027}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC FANCM sub-subfamily. {ECO:0000256|ARBA:ARBA00009889,
CC ECO:0000256|RuleBase:RU367027}.
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:EQB57578.1}.
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DR EMBL; AMYD01000465; EQB57578.1; -; Genomic_DNA.
DR AlphaFoldDB; T0KYJ2; -.
DR STRING; 1237896.T0KYJ2; -.
DR HOGENOM; CLU_002513_0_1_1; -.
DR OMA; FMMRAIF; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd18033; DEXDc_FANCM; 1.
DR CDD; cd12091; FANCM_ID; 1.
DR CDD; cd18801; SF2_C_FANCM_Hef; 1.
DR Gene3D; 1.20.1320.20; hef helicase domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR039686; FANCM/Mph1-like_ID.
DR InterPro; IPR044749; FANCM_DEXDc.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR14025; FANCONI ANEMIA GROUP M FANCM FAMILY MEMBER; 1.
DR PANTHER; PTHR14025:SF20; FANCONI ANEMIA GROUP M PROTEIN; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
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:UP000015530}.
FT DOMAIN 179..347
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 523..683
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..957
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 122371 MW; 7705C0517CEFCE50 CRC64;
MDSDDYGEDI ADEDLYEALS QTQADPSSSV VPLAPSYNRV DTARQSFGSN SRAVSKSTAS
GFSRATNNKS TSDDLDDLPS DAFSSSPEPA FASRPAAPAP RTVNGLTRTN SATYRQTTLL
GGRVADDSPI QAAQPGFGRV YRGDKPQEPP AHHALDREAM KTWLYPTNLG ATRDYQFSIV
KNGIFNNTLV ALPTGLGKTF IAATVMLNYF RWTKDAKIVF VAPTKPLVAQ QVDACFNIAG
IARSETTLLT GDTAPALRVD EWQSKRVFFM TPQTLANDLS HGYADPKSIV LLVIDEAHRA
TGEYAYAKVV KLMRRFNPYF RVLALTATPG SKVETVQEII DNLGISHIEI RTEESIDIRQ
YVHQRNVEQV LLDPSDEMCE IKDLFTKALK PLMDKLTQQN IYYGRDPMSI TAYGLMQQQK
DWFANVGRRA NPGLQGMMRS IFSILQSLAH TIKLLNFHGV RPFYENLKEF RSEVEEKGAK
GSKYKKQILE SEHFQEMMSN MEKWLRIDGF ASHPKLTELQ DRILNHFMDN GGNSATRVIV
FSEYRDSAED IVQVLNRHKP LIKATVFVGQ ADSKRSAGMK QAEQIETIEK FKDGKYNVLV
ATSIGEEGLD IGQVDLIVCY DASSSPIRML QRMGRTGRKR AGNIILLLMR GKEEEAFARS
KDNYAEMQKI ISDGSKFNFR HDLSARIIPR DIRPEVVMQH IEIPIENTQN PALPEPKKRR
QPAKKKPPKK FHLPDGVELG FTKASDFGKP TAGAKRGRPP KQPEPTEADF IEDVPSLNSV
VLTDTQLAEL DRIYRSVPAS TTKIEETEMP NLTSYPLLQR RLRPVEKVQH GARTKKFVKL
CKKLSQQQDT ASRYTKPYGE KDTSRYKNIQ VPPFASDTED EGPPATRSVT EFSDDDDVVE
QSRPKKRVST GAVKPRSFMA ASALIDDGLN DMEEEESPPR RRPKPAAKKR GKKATKKARG
GINSDELGDD CLRDSDAMDT DGSDDGADLV DFVVSDDHPM SSMRPTSSNP PSSQTATPDS
PTRTETSKPF YVPTQFPPTQ ESVDSLLDDD DDLLSSTKRP STSRAQLDSE PDDTPQRQVG
GRQQRRRPVF DSDSDE
//
