ID A0A1D2VG64_9ASCO Unreviewed; 717 AA.
AC A0A1D2VG64;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA replication licensing factor MCM5 {ECO:0000256|RuleBase:RU368063};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368063};
GN ORFNames=ASCRUDRAFT_70963 {ECO:0000313|EMBL:ODV60457.1};
OS Ascoidea rubescens DSM 1968.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Ascoideaceae; Ascoidea.
OX NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV60457.1, ECO:0000313|Proteomes:UP000095038};
RN [1] {ECO:0000313|Proteomes:UP000095038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU368063}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR EMBL; KV454482; ODV60457.1; -; Genomic_DNA.
DR RefSeq; XP_020046764.1; XM_020191867.1.
DR AlphaFoldDB; A0A1D2VG64; -.
DR STRING; 1344418.A0A1D2VG64; -.
DR GeneID; 30965503; -.
DR InParanoid; A0A1D2VG64; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000095038; Unassembled WGS sequence.
DR GO; GO:0071162; C:CMG complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0031298; C:replication fork protection complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProt.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:UniProt.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:UniProt.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17756; MCM5; 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; IPR008048; MCM5.
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:SF42; DNA REPLICATION LICENSING FACTOR MCM5; 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; PR01661; MCMPROTEIN5.
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; 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|RuleBase:RU368063};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, 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}; Nucleus {ECO:0000256|RuleBase:RU368063};
KW Reference proteome {ECO:0000313|Proteomes:UP000095038}.
FT DOMAIN 320..526
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 717 AA; 80150 MW; A6E19A9F26AA40A9 CRC64;
MSAFDVAEVF SARVLPGEDT PNTSFSKIIK AFRSFILEFR LDTQFIYRDQ LRENLLRKEY
SLVVDSDDLI QFNEELQKKL YDSPAENIPL FEQAINEIAK KIAYLSSDEV PTDFPNCQLI
LKSNDSLISI RDLDAFHISK VVRIAGIIIS ASVLTSKPTS VQVVCRSCKH TMKIAVNSGF
GSVTLPNRCL APPNPGSEPN QCPLDPYVIV HDKSKFIDQQ ILKLQEAPDM VPVGEMPRHI
LLSADRYLTN KVVPGTRCTI VGIYSIYQSK VKNVQAVAIR NPYLRVLGIQ TDVDHTASGN
AIFTEEEEEE FIKLSRKPNL YESFAKSIAP SIYGNDDIKK AIACLLLSGS KKILPDGMRL
RGDINVLLLG DPGTAKSQLL KFAEKVSPIA IYTSGKGSSA AGLTASVQKD SSTREFYLEG
GAMVLADGGV ICIDEFDKMR DEDRVAIHEA MEQQTISIAK AGITTVLNSR TSVLAAANPI
FGTYDEMKSA GENIDFQTTI LSRFDMIFIV KDEHNEQRDI SIANHVMNIH LDKVHQVEGE
IPINKMKRYI SYCKAKCAPR LSEEAAEKLA SYFVEIRSEL SKRERMKSER SSIPITVRQL
EAIIRISEAL AKLHLSPVAT EEHVDEAIRL FRASTMDAAS QGSETRAELA SEVSKIEDQL
RRRLPIGWST SYKTIKKEFV NNKGFSQEAL DRALYILEKH ETIQFRFQRA NVFRCGA
//
