ID Q9XXI9_CAEEL Unreviewed; 881 AA.
AC Q9XXI9;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 186.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=mcm-2 {ECO:0000313|EMBL:CAA19452.1,
GN ECO:0000313|WormBase:Y17G7B.5a};
GN ORFNames=CELE_Y17G7B.5 {ECO:0000313|EMBL:CAA19452.1}, Y17G7B.5
GN {ECO:0000313|WormBase:Y17G7B.5a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA19452.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA19452.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA19452.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0007829|PDB:8OUW}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.75 ANGSTROMS).
RX PubMed=37590372; DOI=10.1126/science.adi4932;
RA Xia Y., Sonneville R., Jenkyn-Bedford M., Ji L., Alabert C., Hong Y.,
RA Yeeles J.T.P., Labib K.P.M.;
RT "DNSN-1 recruits GINS for CMG helicase assembly during DNA replication
RT initiation in <i>Caenorhabditis elegans</i>.";
RL Science 0:eadi4932-eadi4932(2023).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; BX284602; CAA19452.1; -; Genomic_DNA.
DR PIR; T26498; T26498.
DR RefSeq; NP_001022416.1; NM_001027245.5.
DR PDB; 8OUW; EM; 3.75 A; 2=1-881.
DR AlphaFoldDB; Q9XXI9; -.
DR EMDB; EMD-17204; -.
DR SMR; Q9XXI9; -.
DR ComplexPortal; CPX-4482; MCM complex.
DR DIP; DIP-26513N; -.
DR IntAct; Q9XXI9; 1.
DR STRING; 6239.Y17G7B.5a.1; -.
DR EPD; Q9XXI9; -.
DR PaxDb; 6239-Y17G7B-5a; -.
DR PeptideAtlas; Q9XXI9; -.
DR EnsemblMetazoa; Y17G7B.5a.1; Y17G7B.5a.1; WBGene00003154.
DR GeneID; 174841; -.
DR KEGG; cel:CELE_Y17G7B.5; -.
DR UCSC; Y17G7B.5b; c. elegans.
DR AGR; WB:WBGene00003154; -.
DR WormBase; Y17G7B.5a; CE19038; WBGene00003154; mcm-2.
DR eggNOG; KOG0477; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_0_1_1; -.
DR InParanoid; Q9XXI9; -.
DR OMA; TYERVTT; -.
DR OrthoDB; 5476523at2759; -.
DR PhylomeDB; Q9XXI9; -.
DR Reactome; R-CEL-68867; Assembly of the pre-replicative complex.
DR Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR Reactome; R-CEL-68962; Activation of the pre-replicative complex.
DR Reactome; R-CEL-69052; Switching of origins to a post-replicative state.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003154; Expressed in embryo and 4 other cell types or tissues.
DR ExpressionAtlas; Q9XXI9; baseline and differential.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0042555; C:MCM complex; ISS:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0045120; C:pronucleus; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006279; P:premeiotic DNA replication; NAS:ComplexPortal.
DR CDD; cd17753; MCM2; 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; IPR008045; MCM2.
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:SF44; DNA REPLICATION LICENSING FACTOR MCM2; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF12619; MCM2_N; 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; PR01658; MCMPROTEIN2.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:8OUW};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|EPD:Q9XXI9,
KW ECO:0007829|PeptideAtlas:Q9XXI9};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 448..654
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 881 AA; 99323 MW; 859E85B2838D5618 CRC64;
MADRANNDDD VDRQPLPIAD DADDDVDGID EMFNNEDEDP EDEEGENLFG DDMERDYREQ
PELDQYSESG MDDASDVGSL SVSARRAAER EMAQRDQLLD DDALMYEDGD SEEVDTRRRG
RGRRGRGDAA DDDSVPMEEE DIPVDILENI RGRTIRDHVS DEAVAKEIER RFKNFLRSFH
EPGNKQTKYI QMIKSMAADN RESLEVSFTD LSDDNGEQNI SYFLPEAPNE MLAIMDRAAT
EVVMNMYPFY SRVCNEIKVR ISQLPVEEDI RMLRQVHLNM LIRTAGVVTI ASGILPQLAV
VKYDCVACGY LLGPFVQQND EEVRPTICPS CQGKGPFELN VENTVYHNYQ RITMQESPNK
VAAGRLPRSK DVILLGDLCD SCKPGDEIEV TGVYTNNFDG SLNYKQGFPV FNTLIHANHI
TNKDKMASDQ LTDEDIKAIR ELSQDPNISQ RVFSSIAPSI YGHDDVKRAI ALALFRGEAK
NPGAKHRLRG DINVLLCGDP GTAKSQFLRY AAHIAPRSVL TTGQGASAVG LTAYVQRHPV
TREWTLEAGA MVLADKGVCL IDEFDKMSDQ DRTSIHEAME QQSISISKAG IVTSLHARCT
VIAASNPIGG RYNPTRTFAE NVDLTEPILS RFDVLCVIRD SVDSVEDERL AKFVVGNHRT
HHPDAKKIVK EGDELEEDQM DERTGVRLIP QDLLRKYIIY AREKCHPTLP EQHSEKFSNI
FAQMRKESMA TGSVAITVRH VESMIRLSEA HAKLHLRSYV NDEDCAAAIR VMLESFVNTQ
KASIMRMMKK TFSRHLTENR SANELLLFIL KQLIRQQMHY ATARAAAGTI LQSVTIPESE
FIEKAQQLRI ENVKPFYTSE IFASNNFLYD PSKKTIVQEI F
//
