ID K7FH28_PELSI Unreviewed; 788 AA.
AC K7FH28;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:ENSPSIP00000007338.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000007338.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000007338.1}
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 EMBL; AGCU01177876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006137075.1; XM_006137013.2.
DR AlphaFoldDB; K7FH28; -.
DR STRING; 13735.ENSPSIP00000007338; -.
DR Ensembl; ENSPSIT00000007379.1; ENSPSIP00000007338.1; ENSPSIG00000006428.1.
DR GeneID; 102457004; -.
DR KEGG; pss:102457004; -.
DR CTD; 4172; -.
DR eggNOG; KOG0479; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_6_0_1; -.
DR OMA; NVYPQED; -.
DR OrthoDB; 5476523at2759; -.
DR TreeFam; TF106459; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
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 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:UP000007267}.
FT DOMAIN 272..478
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 639..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 88923 MW; A53AB57BEE78DDB3 CRC64;
MLQEDQGVYQ SKVRDMIHDN QYRLIVSINE LRRKNEKRAN RLLSSAFEEL VAFQRALKDF
VASIDATYAK QYEEFYIGLE GSFGSKHVTP RTLTSCLLGC MVCVEGIVTK CSLVRPKIVR
SVHYCPATKK TIERRYTDLT SLDAFPSSSV YPTKDEENNP LETEFGLSVY KDHQTITIQE
MPEKAPAGQL PRSVDIVLDD DLVDRVKPGD RIQVIGTYRC LPGKKGGYTS GTFRTIMIAC
HVKQMSKEVR PLYSATDVAK IKRFSKSRSK DIFDQLSRSL APSIHGHEYI KKAILCMLLG
GVEKILENGS RIRGDINILL IGDPSVAKSQ LLRYVLSTAP RAIPTTGRGS SGVGLTAAVT
TDQETGERRL EAGAMVLADR GVVCIDEFDK MSDIDRTAIH EVMEQGRVTI AKAGIHARLN
ARCSVLAAAN PVYGRYDQYK TPMENIGLQD SLLSRFDLLF IVLDQMDPEQ DREISDHVLR
MHRYRGPGEQ DGDAMPLGSA IEILATDDPN VMQEEEQELQ VYEKHDNLLH GPKRHKEKIV
SMEFMRKYIH VAKIIKPVLT QESANYIAEE YSRLRSQDQM SSDIARTSPV TARTLETLIR
LSTAHAKARM NKTIDLQDAE AAVELVHFAY FKKVLEKKKK RKKQADGDTE TEEEEESEGV
ERRKKRRKKA RPGDQEAKEG ESYDPYDFSD TEEEMPEVQA HTPKTPEPAV TGESKKMELA
DTRLKAFKAG LLEVFRAAHA QSVGLKSLME SINRDRSEPF SSDEVKVALE RMQDDNQIMM
SDEIIFLI
//
