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Database: UniProt
Entry: H0UUX1_CAVPO
LinkDB: H0UUX1_CAVPO
Original site: H0UUX1_CAVPO 
ID   H0UUX1_CAVPO            Unreviewed;       810 AA.
AC   H0UUX1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN   Name=MCM3 {ECO:0000313|Ensembl:ENSCPOP00000000780.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000000780.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000000780.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000000780.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00000600};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00000600};
CC   -!- SUBUNIT: Component of the MCM2-7 complex.
CC       {ECO:0000256|RuleBase:RU368061}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368061}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC       ECO:0000256|RuleBase:RU004070}.
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DR   EMBL; AAKN02018879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_013013542.1; XM_013158088.1.
DR   AlphaFoldDB; H0UUX1; -.
DR   STRING; 10141.ENSCPOP00000000780; -.
DR   Ensembl; ENSCPOT00000000873.3; ENSCPOP00000000780.3; ENSCPOG00000000867.4.
DR   GeneID; 100729563; -.
DR   CTD; 4172; -.
DR   VEuPathDB; HostDB:ENSCPOG00000000867; -.
DR   eggNOG; KOG0479; Eukaryota.
DR   GeneTree; ENSGT01050000244824; -.
DR   HOGENOM; CLU_000995_6_0_1; -.
DR   InParanoid; H0UUX1; -.
DR   OMA; NVYPQED; -.
DR   OrthoDB; 5476523at2759; -.
DR   TreeFam; TF106459; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000000867; Expressed in adrenal gland and 13 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0071162; C:CMG complex; IEA:Ensembl.
DR   GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:Ensembl.
DR   CDD; cd17754; MCM3; 1.
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   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
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:UP000005447}.
FT   DOMAIN          295..501
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          662..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   810 AA;  91229 MW;  C173266983DC3C69 CRC64;
     MAGTVVLDDV ELREAQRDYL DFLDDEEDQG IYQSKVRDMI SDSQYRLIVS VNDLRRKNEK
     RANLLLSNAF EELVAFQRAL KEFVASIDAT YAKQYEEFYI GLEGSFGSKH VSPRTLTSCF
     LSCVVCVEGI VTKCSLVRPK VVRSVHYCPA TKKTIERRYS DLTNLVAFPS SSVYPTKDEE
     NNPLETEYGL SVYKDHQIIT IQEMPEKAPA GQLPRSVDVI LDDDLVDKVK PGDRVQVVGT
     YRCLPGKKGG YTSGTFRTVL IACNVKQMSK DIQPSFSAED IAKIKKFSKT RSKDIFDQLA
     RSLAPSIHGH DYVKKAILCL LLGGVERDLE NGSHIRGDIN ILLIGDPSVA KSQLLRYVLC
     TAPRAIPTTG RGSSGVGLTA AVTTDQETGE RRLEAGAMVL ADRGVVCIDE FDKMSDMDRT
     AIHEVMEQGR VTIAKAGIHA RLNARCSVLA AANPVYGRYD QYKTPMENIG LQDSLLSRFD
     LLFIMLDQMD PEQDREISDH VLRMHRYRAP GEQDGDAMPL GSAVDILATD DPNFSQDDQQ
     DTQIYEKHDN LLHGTKKKRE KMVSAAFMKK YIHVAKIIKP VLTQESATYI AEEYSRLRSQ
     DSMSSDTART SPVTARTLET LIRLSTAHAK ARMSKTVDLQ DAEEAVELVQ YAYFKKVLEK
     EKKRKKRSED ESETEDDEEK SQEEHEQKRK RLRRKTRQSD AKDGDPYDPY DFSDTEEEMP
     QVHTPKTAES QETQESQKVE LSESRLKAFK AALLNVFQEA HAQSVGLTRL TESINQGKEE
     PFSAEEIQAA LDKMQDDNQV MLSEGIVFLI
//
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