ID Q5CTT7_CRYPI Unreviewed; 862 AA.
AC Q5CTT7;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 08-NOV-2023, entry version 124.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=cgd2_1600 {ECO:0000313|EMBL:EAK88811.1};
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:EAK88811.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK88811.1, 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:RU368061}.
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:RU368061};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368061}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368061}.
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:EAK88811.1}.
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DR EMBL; AAEE01000005; EAK88811.1; -; Genomic_DNA.
DR RefSeq; XP_626382.1; XM_626382.1.
DR AlphaFoldDB; Q5CTT7; -.
DR STRING; 353152.Q5CTT7; -.
DR EnsemblProtists; EAK88811; EAK88811; cgd2_1600.
DR GeneID; 3373713; -.
DR KEGG; cpv:cgd2_1600; -.
DR VEuPathDB; CryptoDB:cgd2_1600; -.
DR InParanoid; Q5CTT7; -.
DR OMA; NVYPQED; -.
DR OrthoDB; 147095at2759; -.
DR Proteomes; UP000006726; Chromosome 2.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:UniProtKB-UniRule.
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; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008046; Mcm3.
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:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 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; PR01659; MCMPROTEIN3.
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 DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU368061};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368061};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368061};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368061};
KW Reference proteome {ECO:0000313|Proteomes:UP000006726}.
FT DOMAIN 311..517
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 700..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 96699 MW; 82D66328F0AA23B3 CRC64;
MLSSLSDSEL SEQLIQVYKS FLQGNDEYSS KIKQMAVENI ESGRILIELG DLRKISDELP
QKIINEPYLY VSPFEEVIKD LVDLEREIDK NSPLKSSQFN ARVGFSGWFG RNHLTPRGLT
ASNINKMVCV EGIISQCSIV KPKLVKSVHI SKGHLIGQND ISGGANQAFV EVRGHRDISC
LIKDRYIQSG VPSEDGQGNK MEVEIGLCRY KDTQKMTLQE LPEMIPTGQL PRSIEIIAED
DLVETIKPGD RVKIVGVYKP ISRRENNAIT GIFKVVIVAN NIQLLNKNVT SPELTPQEIR
IMKEISNRDD AFEILSRSFA SSLCGHEYIK KGLLLGILGG AEHNLENGTH IRGDIHTLLI
GEPSCGKSQL LRFVMSIAPL AISTTGRGCS GVGLTAAVTH DPDTKERRLE AGATVLADRG
IVCIDEFDKM SFSDRVAIHE VMEQQRVTIA KAGIQASLNA RCSIFAAANP VYGHFDDFME
LSRQIAFPDS LLSRFDLIFI VKDSRNSQQD RKIAAQVLAQ VRYNKNSSIN DTRINKANNN
FVIQPEYKDN DSNEKNEMND IWQPLSNKIA DKRSQNNSKG SSEDKVLTTS FLRKYIHYCK
YVRNTPKLTD EAAELVARIF TELRAKCMNQ SKGGTTCTTR TLEGIIRLAT AHSKLKMRDS
VIPEDVLIAF ELLSYAMFGE VIEKESLLNV VFEKDIENEL QQEDNSRNKR REEKKYQRSN
HPSKTPELNF LEENEHSIIA PPPSSIVTPS REKINRKESA ARGHQVALAA ANILREGSNT
DHGDFELADF KKKFITSCIA EQFSESGLEA MLEEELLKNI ISKSKEKGNN FMITNKDIKE
VLRILEEENR LMIAGDTIYS IV
//
