ID A0A2A2LD41_9BILA Unreviewed; 580 AA.
AC A0A2A2LD41;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=DNA replication licensing factor MCM5 {ECO:0000256|RuleBase:RU368063};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368063};
GN ORFNames=WR25_17950 {ECO:0000313|EMBL:PAV84015.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV84015.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV84015.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV84015.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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:RU368063}.
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:RU368063};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368063}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368063}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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:PAV84015.1}.
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DR EMBL; LIAE01006898; PAV84011.1; -; Genomic_DNA.
DR EMBL; LIAE01006898; PAV84012.1; -; Genomic_DNA.
DR EMBL; LIAE01006898; PAV84014.1; -; Genomic_DNA.
DR EMBL; LIAE01006898; PAV84015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2LD41; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
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:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:UniProtKB-UniRule.
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; IPR008048; MCM5.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
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:SF42; DNA REPLICATION LICENSING FACTOR MCM5; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01661; MCMPROTEIN5.
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|RuleBase:RU368063};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU368063};
KW DNA-binding {ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368063};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368063};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368063};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231}.
FT DOMAIN 333..536
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 580 AA; 64563 MW; 41A868407548AACE CRC64;
MSNFDDPGLY YQERFFANDG VPDTGREMIA EYKQLTGQFR SFIREFSLGG FEMIYREQLK
KNYISGHYQL DVSLNHLKIY NEEAALKLRN HPGKFLPAFE EAAKSVADEI TQPRPEENKE
VHDIQVTLSL DEYSVPIRHL KSSQVSQIVK VSGIIVAATQ VRAKATRVTL QCRTCRHIVS
NLALKPGLEG FQLPRTCGAP QQGQLQRCPI DPYHIVPDKC VCVDYQTLKL QENPEDVPHG
EMPRHLQLYC DRYLTDKVAP GNRVTIIGVY SIKKMFQKKK GMDKSLSGIR TPYLRVLGIH
VETSGPGRSD FSEFTPQDER NFKEIAKRSD CCELIAKSIA PSIYGSSDIK KSIACLLFGG
SRKRLPDGLT RRGDINVLLL GDPGTAKSQL LKFVEQVAPI GVYTSGKGSS AAGLTASVIR
DPNSRSFIME GGAMVLADGG VVCIDEFDKM REDDRVAIHE AMEQQTISIA KAGITTTLNS
RCSVLAAANS VYGRWDDARG EENIDFMPTI LSRFDMIYIV KDSHDVQRDA TLARHVIEVH
VNASQANDRI QDHADVNLAA SQGATQMFDS DGLLTLRKNV
//
