ID Q5CQF0_CRYPI Unreviewed; 857 AA.
AC Q5CQF0;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 132.
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=cgd4_970 {ECO:0000313|EMBL:EAK87642.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK87642.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK87642.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
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:EAK87642.1}.
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DR EMBL; AAEE01000009; EAK87642.1; -; Genomic_DNA.
DR RefSeq; XP_625698.1; XM_625698.1.
DR AlphaFoldDB; Q5CQF0; -.
DR STRING; 353152.Q5CQF0; -.
DR EnsemblProtists; EAK87642; EAK87642; cgd4_970.
DR GeneID; 3372687; -.
DR KEGG; cpv:cgd4_970; -.
DR VEuPathDB; CryptoDB:cgd4_970; -.
DR InParanoid; Q5CQF0; -.
DR OMA; DINVETH; -.
DR OrthoDB; 147095at2759; -.
DR Proteomes; UP000006726; Chromosome 4.
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: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: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; 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:UP000006726}.
FT DOMAIN 381..587
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 608..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 97188 MW; 311F38EEF17F4A15 CRC64;
MAIGVDNAHE KVRAYNDHIK DIQNFLENFE EYNENENSGE DVVMSNAREE TEKEGSIWKH
KKYMKSLQSI SNREKNVLYI EVDDILSFGK YENKVTEYNN LVHSILSNTK RYVQLIYIAA
DNCLPVPTRT NMIDFKLEEM NNTKRSESMK TCNVPAYLRS NFEVYIKASK RMPITPLREV
RAEYVGGYVQ VNCIVTRVSN VKPRIQVVNY TCEVCGSSIW QSVEGTNYMP LSDCESSQCK
NNKRTGNLKC NIKESKFTKF QEIRIQEPAD QVPTGNVPRT MKVIAMGENT RKLLPGMYVT
ISGVFLPVVK EGFQAFRSGL TAETYFEVHN VHSYISNKEV SLTDYEKKLV KQMEADEEKK
NREEALNSSG GGAYEVLHSQ FYDKLANSIA PEIFGMLDVK KGLLLQLIGG VTNQMNDGMK
IRGNIHILLM GDPGVAKSQL LNQITKIAPR SIYATGKGSS GVGLTASVVR DQNTSEVTLE
GGALVLADNG ICCIDEFDKM DESDRTAIHE VMEQQTVSIA KAGITTTLNA RSSVLAAANP
VSGRYDPRKS PVANMNLPDS LLSRFDLQFL LLDIPDKEKD LKLARHVLYV HKNEKAPSGD
FELDRSLSSI QRPGMGVNQT RSSAKKVRRR RNNDDREEDA ESENQDKSKS DQEQRVFSTV
FMRYFIEKAQ TYTPLVPKEL VSEIVEHYVE LRRREKIEQT REDWRKTYTT PRTLLGILRL
SQALARLRFS NIVERADFEE ATRLMIESKK SVTKPGNTSG FSNPGAKNKK HDFRDQIIEI
IKDLHNRQAE RTTRGGEDDE SMTDGMIEIS ISEIETRIAH RGLLKQQLEL VIDEYIELGV
LSKSKDGQFI SFITDFS
//
