ID Q5CTY1_CRYPI Unreviewed; 970 AA.
AC Q5CTY1;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=cgd2_1100 {ECO:0000313|EMBL:EAK88850.1};
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:EAK88850.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK88850.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EAK88850.1}.
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DR EMBL; AAEE01000005; EAK88850.1; -; Genomic_DNA.
DR RefSeq; XP_626338.1; XM_626338.1.
DR AlphaFoldDB; Q5CTY1; -.
DR STRING; 353152.Q5CTY1; -.
DR EnsemblProtists; EAK88850; EAK88850; cgd2_1100.
DR GeneID; 3373593; -.
DR KEGG; cpv:cgd2_1100; -.
DR VEuPathDB; CryptoDB:cgd2_1100; -.
DR InParanoid; Q5CTY1; -.
DR OMA; LKDWPYS; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000006726; Chromosome 2.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
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; IPR031327; MCM.
DR InterPro; IPR008045; MCM2.
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:SF44; DNA REPLICATION LICENSING FACTOR MCM2; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF12619; MCM2_N; 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; PR01658; MCMPROTEIN2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006726};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 502..709
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 110388 MW; 75B72AB2F1DCCCF3 CRC64;
MSSNYRVHDD DESSQNSHDG NNSSSNGIAN ILLTQDPSDY SEAEEVAVDE VVYEEEIANE
SEEELGEDLY GDNFMNDYNK NPELDKYDPE MLDDTHYEDD IEAKRRADLA LDRMKSEKSQ
GKQTEIHHKY GISTFNADDG DEGEIEKRRK RREAFREMAD EAARGGAIVD INELIQDLPL
AEQSEWSEHV ENIIRRLFKV FLQDFKLSSM YKTISNGDNK LEGRNISFED LYYIKKIEEM
VQEEKTSLYV DVKHIFTFCY KLWDYLNLYP TPVIECFNQC AYEVVTSMYH SLYSGKSIMV
RLIGLDYIDQ LRDLRVEWLN QLIRVSGIIT RRTDILTKFK SLYMECVKCG CDNLGPYEDN
PLFESGSLSE SNSIMKNIGK CTDCQSKGPF VINREKTIYE NYQKLTIQES PGSVPAGRVP
RSREIIVSGD LVDYACPGEE IIVTGIYRTF RDQKLNIKSG FPILGTQILC NNIEKKHDAL
RKDDLTDEDY KKIKELSRDP DIKEKIVSSI APSIYGHNHI KTAIACSLFS GVRKQVEGKH
HHIRGDINVL IVGDPGLAKS QFLKYVEKSF DRTIYTSGKG ASAVGLTASV RRDPISGEWT
LEGGALVLAD EGICLIDEFD KMSDKDRVSI HEAMEQQSIS ISKAGIVTTL RARCSIIAAA
NPIFGKYDSS LTFKDNVDLT DPIISRFDVL AVLKDEVHPM KDELLANFVV QSHMNSQEMY
GSSGLDQDDQ EKKFSSGLSD TSQNCDQRFA PIDQKLLCKY IRYARKYCKP QIRSVDKEKI
ITFYSRIRQE AQQTGGISMT VRHIESIIRL AEAQAKMRLS PVVSNKDVDG AIGMVLESFI
QSQKYAVAQR LSKIFSRYKA LSSGFVDVLE NLLLQLFSDK IQKIKLRNWD EEQMNTIVEE
VDNLTVNLDE FIAIAEKIKL SHNVTLSYLK SSSFLKHYLI SETTDSMGNN IKIICKRSYT
DQDSQSQLSM
//
