ID A0A0N4WJQ4_HAEPC Unreviewed; 706 AA.
AC A0A0N4WJQ4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=HPLM_LOCUS11250 {ECO:0000313|EMBL:VDO42365.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001125801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001125801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO42365.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO42365.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU365012}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR EMBL; UZAF01017508; VDO42365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4WJQ4; -.
DR STRING; 6290.A0A0N4WJQ4; -.
DR WBParaSite; HPLM_0001125801-mRNA-1; HPLM_0001125801-mRNA-1; HPLM_0001125801.
DR OMA; AQHVTYV; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; Unassembled WGS sequence.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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; 2.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008050; MCM7.
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; SM00350; MCM; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|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}; Nucleus {ECO:0000256|RuleBase:RU365012};
KW Reference proteome {ECO:0000313|Proteomes:UP000268014}.
FT DOMAIN 342..521
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 706 AA; 78772 MW; 46142764DB585452 CRC64;
MSFDKESTDY DKHKAQVREF VENYYGLDEN GSKVFCYRDD VLRIAEREQV ALYVNLDDVF
RFDETLSTLI EGNARRFHRI FNEVIDEMVQ EALGGRQPPI RDALDAFIFQ RVHMDDQLKM
AEDFMGGSTQ EVRKKYPPQL LRRFEVVFKN RDAMKPLAVR DLKANCVGKL VTVTGIVIRA
TEVKPILEVM TYACDTCGAE VYQPINGPSF MPAVNCPSKD CVESKANGRL HMQVRGSKFN
KFQEIRIQEL SDQVPVGSIP RALTVNIYGE ATRQCAPGDL VRISGVLIPL LKTGFRQAGG
GLVTETFLEA HFVENVRCNV DDEDLGDDLT ENEVDLLAQD NLYDMLAYSI APEIYGLTDV
KKSLLLALVG GVDKNASGMK IRGCLNVLLM GDPGVAKSQL LSYVNRLAPR SQYTTGRGSS
GVGLTAAVVK DPLSGEMTLE GGALVMEQQT ISIAKAGIMT TLNARVAIIA AANPAFGRYN
PKRSIEQNID LPAALLSRFD LLWLIQDKPD RDGDKRLASH ITYVHMNSKQ PEVDGMKPVN
MRLIRRLIEV AQRKNPVVGD ALRERLVEMY VDMRRVSRES EDSTFASPRL LLSVIRMSTA
LARLRLSNVV MSDDIEEAIR LMQASKDSLR PEMQQQEIRQ SPVDRAFAIL RELCISTGDA
ITLQSALEAC ARKGVSEQAL QDTIKVHEAN GVIVVDAQKR IRFTMN
//
