ID H6C1Z4_EXODN Unreviewed; 847 AA.
AC H6C1Z4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=HMPREF1120_05844 {ECO:0000313|EMBL:EHY57820.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY57820.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY57820.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY57820.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; JH226134; EHY57820.1; -; Genomic_DNA.
DR RefSeq; XP_009158281.1; XM_009160033.1.
DR AlphaFoldDB; H6C1Z4; -.
DR STRING; 858893.H6C1Z4; -.
DR GeneID; 20310483; -.
DR VEuPathDB; FungiDB:HMPREF1120_05844; -.
DR eggNOG; KOG0477; Eukaryota.
DR HOGENOM; CLU_000995_0_0_1; -.
DR InParanoid; H6C1Z4; -.
DR OMA; TYERVTT; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0043596; C:nuclear replication fork; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
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; 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; 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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 484..690
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 847 AA; 94844 MW; EDE176BFBF2C1332 CRC64;
MSAANRGPSN AGRRKRARDD EDEVMSSSPA ALPSSPPLLP TNENDDLEDD DLGPEDDLIG
DIDDADELAE EEDGIDLFGD TFMDDEREGR DQETYQGRMI DDEGDYDDLD LAERRQLEAR
LNKRDRELAR RRRMPAAFMP DDDDDAGIDL TRQPRRRRHH YDEDQEDMDL DENIMEEELS
LETLQDVKAS NITEWVTLPS VMKTIAREFK SFLTEYIDAN GTSVYGTRIR TLGEVNSESL
EVSYDHLSST KAILAYFLAN APAEMLKIFD KAAFEVVRLH YPNYELIHPE VHVRISDLPV
KYTLRQLRQS HLNCLVRVSG VVTRRTGVFP QLQMVKFTCN KCGVTLGPFA QESTSSEVKL
TFCPECQSRG PFTLNSEKTV YRNYQKLTLQ ESPGTVPAGR LPRHREVILL ADLIDKAKPG
EEIEVTGIYR NNYSGQLNNK NGFPVFATML EANHIIKTHD QLAGFRLTEE DERQIRALSK
DPNIVDKIVD SIAPSIYGHR DIKTAVALSL FGGVGKEAQG KHKIRGDINV LLLGDPGTAK
SQVLKYVEKT AHRAVFATGQ GASAVGLTAS VRRDPLTQEW TLEGGALVLA DRGTCLIDEF
DKMNDQDRTS IHEAMEQQTI SISKAGIVTT LQARCAIIAA ANPKGGRYNG MIPFSENVEL
TEPILSRFDI LCVVRDTVDP DEDERLANFV VKSHGRAHPT KLSVDGGDVA AMETEETDAI
NNGEPQQEGA IPQELLRKYI LYAREKCRPK LYQIDQDKVA RLFADMRRES LATGAYPITV
RHLEAIMRIA EAFCKMRLSD YCSSQDIDRA IAVTVDSFVG SQKISCKKAL ARAFAKYVDP
NTLARFV
//
