ID T0K577_COLGC Unreviewed; 1034 AA.
AC T0K577;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=CGLO_13853 {ECO:0000313|EMBL:EQB47059.1};
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:EQB47059.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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:EQB47059.1}.
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DR EMBL; AMYD01003125; EQB47059.1; -; Genomic_DNA.
DR AlphaFoldDB; T0K577; -.
DR STRING; 1237896.T0K577; -.
DR eggNOG; KOG0478; Eukaryota.
DR HOGENOM; CLU_000995_7_0_1; -.
DR OMA; NRCSFAD; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0043596; C:nuclear replication fork; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17755; MCM4; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF21128; MCM4_WHD; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01660; MCMPROTEIN4.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT DOMAIN 615..823
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 114084 MW; CEA18FDFA93F09F8 CRC64;
MSSPTKRSTR SSTAGTTPRR STRNNPDADR SSPAPTQEPA AQTPSRTTRR SQLASSPLFY
ESSPAQGSSR NAPANGDVSS PLRGVSSSQN TNVGPAPSSP LRQDIDTQST GDGDRTPRAS
GMARESSPIR YDPSSSPGRG SVRPPQSDFR SESSGLFVSD RARSRRGDIH SEGFRTPRRR
LVLDPSGRVV TNAPGSDAPS FSNPDPNTSE ADRLGGAADS TIWGTSVSID DTFVTFKDFL
RNFTRKYQMY REGLSEAEVR EAPDAESKVY WEALENMLLL GGTRLFLNMQ DLNTYPPTRK
LYYHLQAYPQ EIIPIMDQSI HDMMVELARA EDLRERNSQS SAGDAARRSN TAPSSEPVFP
SSDHPETPSD APTPTDAPTP RPATDITSKE DQVSQMIYMV RPYGLEKITN LRDLNPSDMD
RLITIKGLVI RTTPIIPDMK DAFFRCNVCN HSVNVSIDRG KIREPTECPR TRCASKNSMQ
IIHNRCSFED KQVIKLQETP DAVPAGQTPH SVSICAYNEL VDFCKAGDRV EITGVFRVNP
VRVNPRQRTI KSVYRTFVDV VHIQKVDKKR MGLDASTLGV EGEEGETNDP NLQENRKITP
EDVEKIKETA ARPDIYELLA RSLAPSIYEM DDVKKGILLQ LFGGTNKTFQ KGGSPRYRGD
INVLLCGDPS TSKSQILSYV HKIAPRGIYT SGKGSSAVGL TAYVTRDPES RQLVLESGAL
VLSDGGVCCI DEFDKMSDAT RSVLHEVMEQ QTVSVAKAGI ITTLNARTSI LASANPIGSR
YNPDLPVPQN IDLPPTLLSR FDLVYLILDR VDEKSDARLA RHLLSLYLED KPESAATKED
ILPVEFLTSY IFYARSTINP TIAQDAAQEL VDQYLEMRKL GQDVRAAEKR ITATTRQLES
MIRLSEAHAK MRLSETVTRE DVQEAARLIR SALKTAATDS QGRIDMSLLT EGTSSADRRR
KEEIKEAVLH LLDELTSGGQ SVKWAEVARK LSEGASMPVE QADFNETMRT LEMEGLIMVS
GEGARRSVRR VAAV
//
