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Database: UniProt
Entry: A0A3B4DRB9_PYGNA
LinkDB: A0A3B4DRB9_PYGNA
Original site: A0A3B4DRB9_PYGNA 
ID   A0A3B4DRB9_PYGNA        Unreviewed;       844 AA.
AC   A0A3B4DRB9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000026922.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000026922.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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:RU368062}.
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:RU368062};
CC   -!- SUBUNIT: Component of the MCM2-7 complex.
CC       {ECO:0000256|RuleBase:RU368062}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC       ECO:0000256|RuleBase:RU004070}.
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DR   RefSeq; XP_017573772.1; XM_017718283.1.
DR   RefSeq; XP_017573773.1; XM_017718284.1.
DR   AlphaFoldDB; A0A3B4DRB9; -.
DR   STRING; 42514.ENSPNAP00000026922; -.
DR   Ensembl; ENSPNAT00000003899.1; ENSPNAP00000026922.1; ENSPNAG00000012318.1.
DR   GeneID; 108439732; -.
DR   CTD; 4173; -.
DR   GeneTree; ENSGT01050000244824; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA 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:0001878; P:response to yeast; IEA:Ensembl.
DR   CDD; cd17755; MCM4; 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; IPR008047; MCM_4.
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:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF21128; MCM4_WHD; 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; PR01660; MCMPROTEIN4.
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   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU368062};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368062};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368062};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368062}.
FT   DOMAIN          439..647
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  94782 MW;  90D97DA4423A66AA CRC64;
     MSSPSSSARK RARSSNPPTP ASEDPLSLSP RPREPSTGEL QPMPTSPGTD MQSPAIQDTS
     LFSSPVARRS VPQSEVDMSS PLIYDTPSRG TPARQRPDLG SVRKAPQVDL NSEPPSGDAT
     VASEQTAGQR LVIWGTDVNV GTCKEKFQRF LQRFIDPSSR EDENACLDLN EPLYMQKLDE
     ISVVGDPVLN VNCGHIQTFD ADLYRQLICY PQEVIPTFDM AVNELFFDRY PDSVLEHQIQ
     VRPYNALKTR NMRSLNPEDI DQLITISGMV IRTSQLIPEM QEAFFRCQVC AFSTRVEVDR
     GRIAEPAVCR NCNTTHSMAL VHNRSVFSDK QMIKLQESPE DMPAGQTPHT TVVYAHNDLV
     DKVQPGDRVN ITGIYRAAPM RVNPRQSQVK SVYKTHIDAI HFRKTDERRL HGLEEENEQK
     LFTEERVSML KELAAKPDVY DRLSSALAPS IYEHEDIKKG ILLQLFGGTR KDFSQTGRGN
     FRAEINILLC GDPGTSKSQL LQYVYNLVPR GQYTSGKGSS AVGLTAYVMK DPETRQLVLQ
     TGALVLSDNG ICCIDEFDKM SDSTRSVLHE VMEQQTLSIA KAGIICQLNA RTSILAAANP
     VESQWNPKKT TIENIQLPHT LLSRFDLIFL MLDPQDEAYD RRLAHHLVSL YYQSEDQVEE
     EYLDMAVLKD YIAYARTYIN PRLCEEASQA LIEAYVDMRK IGSGRGMVSA YPRQLESLIR
     LAEAHAKVRF SDKVETIDVE EAKRLHREAL KQSATDPRTG FVDISILTTG MSATARKRKE
     EVAQALKKLI QSKGKMPAMK YQQLFDDLRG QSEAAITKDM FDEALRALTD EDYLTVTGKT
     VRLL
//
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