ID A0A179G002_METCM Unreviewed; 810 AA.
AC A0A179G002;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA replication licensing factor MCM7 {ECO:0000256|RuleBase:RU365012};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU365012};
GN Name=MCM7 {ECO:0000256|RuleBase:RU365012};
GN ORFNames=VFPPC_03066 {ECO:0000313|EMBL:OAQ70623.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ70623.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ70623.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ70623.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the replicative helicase essential for 'once per cell cycle' DNA
CC replication initiation and elongation in eukaryotic cells. The active
CC ATPase sites in the MCM2-7 ring are formed through the interaction
CC surfaces of two neighboring subunits such that a critical structure of
CC a conserved arginine finger motif is provided in trans relative to the
CC ATP-binding site of the Walker A box of the adjacent subunit. The six
CC ATPase active sites, however, are likely to contribute differentially
CC to the complex helicase activity. {ECO:0000256|RuleBase:RU365012}.
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:RU365012};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365012}.
CC -!- SIMILARITY: Belongs to the MCM family. {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:OAQ70623.1}.
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DR EMBL; LSBJ02000002; OAQ70623.1; -; Genomic_DNA.
DR RefSeq; XP_018147160.1; XM_018282615.1.
DR AlphaFoldDB; A0A179G002; -.
DR STRING; 1380566.A0A179G002; -.
DR GeneID; 28846609; -.
DR KEGG; pchm:VFPPC_03066; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000078397; Chromosome 2.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17758; MCM7; 1.
DR Gene3D; 2.20.28.10; -; 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; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008050; MCM7.
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:SF26; DNA REPLICATION LICENSING FACTOR MCM7; 1.
DR Pfam; PF00493; MCM; 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; PR01663; MCMPROTEIN7.
DR SMART; SM00382; AAA; 1.
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 Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU365012};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU365012};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365012};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365012};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365012};
KW Reference proteome {ECO:0000313|Proteomes:UP000078397}.
FT DOMAIN 391..597
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 52..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 90669 MW; A76BCB2799408DF8 CRC64;
MALREFKAPV DYELQQSAFE EFLKEFKTSP EHTIATAMGD ITIDEDDLSD EYDFMDEDDE
ATERRRKEKE SRRTPQHKYK LLLQQLADRT IEEITIDLDD VHAWESQTDE ELHLVDSIEL
NTKHYVDVLS KAVDAVMPQP STDVTFKDDV LDVLMARRQA RNRELQEAAE RDPTAENDKF
PAELIRRYTL VFKPRSGTVD EPAKALAVRQ VRGDHIGHLI TVRAIATRVS DVKPIVQVSA
YTCDRCGCEI FQPVSDKQYG PLTMCPSQDC TANQSKGQLN PSTRASKFLP FQEVKVQEMA
EQVPIGQIPR SLTVLCYGSS VRRINPGDVV DISGIFLPTP YTGFQAMKAG LLTDTYLEAH
HIHQHKKAYS EMIVDPRLVR RIDKYRQTGQ VYELLAKSIA PEIYGHLDVK KALLLLLIGG
VTKEMGDGMK IRGDINICLM GDPGVAKSQL LKYISKVAPR GVYTSGRGSS GVGLTAAVMR
DPVTDEMVLE GGALVLADNG ICCIDEFDKM DDTDRTAIHE VMEQQTISIS KAGISTTLNA
RTSILAAANP IYGRYNPRIS PVENINLPAA LLSRFDVLFL LLDTPSRESD EQLAKHVAFV
HMNNRHPDIG TDNVVFTPHE VRSYVAQART YRPVVPESVS DYMIKTYVRL RDQQQRAEKK
GKQFTHTTPR TLLGVVRLAQ ALARLRFSNQ VTQDDVDEAL RLIEASKESL NAEVNTGRRG
LNASSRIYNL VKALADSGAC RAEDAEDDDL GVELSMRKVK ERVIAKGFTE DQWLNALEEY
TTLDVWQTTG NGARLVFVTA GNDDEDGMDD
//
