ID A0A3Q1EK60_9TELE Unreviewed; 729 AA.
AC A0A3Q1EK60;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000004871.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000004871.1}
RP IDENTIFICATION.
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|RuleBase:RU368061};
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 AlphaFoldDB; A0A3Q1EK60; -.
DR STRING; 80966.ENSAPOP00000004871; -.
DR Ensembl; ENSAPOT00000009290.1; ENSAPOP00000004871.1; ENSAPOG00000006541.1.
DR GeneTree; ENSGT01050000244824; -.
DR InParanoid; A0A3Q1EK60; -.
DR Proteomes; UP000257200; 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: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:0032508; P:DNA duplex unwinding; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR CDD; cd17754; MCM3; 1.
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; IPR008046; Mcm3.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
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:SF103; DNA REPLICATION LICENSING FACTOR MCM3; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 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 DNA replication {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|RuleBase:RU368061};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|RuleBase:RU368061};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT DOMAIN 230..436
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 597..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 81825 MW; 9A805ADD931D9DB0 CRC64;
MNNAFVELLA FQRALKDLVA SVDATYAKQY EEFFVGLEGS FGSKHVSPRT LTSRLLGSMV
CVEGIITKCS LVRPKVVRSV HYCPATKKTM ERKYTDMTSL DAFPSSAIYP TKDEENNPLE
TEFGLSIYKD HQTITVQEMP EKAPAGQLPR SVDIILDNDL VDVVKPGDRV QVVGTYRCLP
GKKGGFTSGT FRTIMIACNV KQMSKDVSPH FSADDVAKIR NFSQTRSINV FDQLARSLAP
SIHGHEYIKK AILCMLLGGV EKVLENGSRI RGDINILLIG DPSVAKSQLL RYVLHTAPRA
IPTTGRGSSG VGLTAAVTTD QETGERRLEA GAMVLGDRGV VCIDEFDKMS DMDRTAIHEV
MEQGRVTIAK AGIHARLNAR CSVLAAANPV YGRYNQYKTP MENIGLQDSL LSRFDLLFIM
LDQMDPEHDR EISDHVLRMH RYRDPHEQEG AAMALGGTVD VLATEDPDAI EEEHEELQIY
EKHNNLLHGS RRKKDKIVSK EFMRKYIHIA KAVTPVLTEE AANHIAEEYS RLRSQDQLGA
DLARTSPVTA RTLETLIRLS TAHAKARMSK AVELQDSEVA VELVQFAYFK KVLEKEKKRS
RQDRDSGSEE DEDEDVSTQR SQRTQRKRGR RGSQGSEPYS PYDFSEDQEV PESKKSVLFL
SLHRLKEFKS SLFSVFQSAH AQSVKMTALM DDINKQRQDR FTEAEVRVAL ARMQDDNQVM
MADDIIFLI
//
