ID A0A0A2IJE5_PENEN Unreviewed; 1001 AA.
AC A0A0A2IJE5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=PEX2_110640 {ECO:0000313|EMBL:KGO52422.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO52422.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO52422.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO52422.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC 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:KGO52422.1}.
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DR EMBL; JQFZ01000266; KGO52422.1; -; Genomic_DNA.
DR RefSeq; XP_016595172.1; XM_016748330.1.
DR AlphaFoldDB; A0A0A2IJE5; -.
DR STRING; 27334.A0A0A2IJE5; -.
DR GeneID; 27683751; -.
DR HOGENOM; CLU_000995_7_0_1; -.
DR OrthoDB; 5476523at2759; -.
DR PhylomeDB; A0A0A2IJE5; -.
DR Proteomes; UP000030143; 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:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17755; MCM4; 1.
DR Gene3D; 2.20.28.10; -; 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; IPR008047; MCM_4.
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:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF21128; MCM4_WHD; 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; PR01660; MCMPROTEIN4.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 579..787
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 542..569
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 110249 MW; 72F8A654C3C2A47A CRC64;
MSSPTQRRRG RSSKNSTASP SSSSRQEPPS SPTFQATPRA SRRLMAEGAA PSSSPIFFQS
SPTKGDNNAE TPDERMADAS STVDDGDRTP RGNPGVRDSS PIHYIPSSSP TRGFGRSDIR
SDIRSDALST ASSGLFVSPG GQGRRAGPRR SDLHSGGFGS TPSRRNRVFV DANGMPTGDT
MPRSDATFSN INPGTSEAEA MAGNSTRVIW GTNISIQDSM SAFKNFLYNF ATKYRLWADG
ATEDETRLMG ELAERHECIT MCNNMRRLGV TTFNLDAANL KSYPLTRKLW HQLSAYPQEI
IPLMDQALKD VMVDLALKEM DVLRSESQRA AQPRDRRGQP ILTSDNVLPT VDVPDLVGEV
EAMTFKVLPF GLDRTVNMRD LDPADMDKLV SIKGLVIRAT PIIPDMKEAF FRCSVCSYGV
QVDIDRGRIA EPTVCPRDSC KEKNSMQLLH NRCSFSDKQV IKLQETPDNI PDGQTPHSVS
LCVYDELVDV CKAGDRVEVT GIFRCNPMRV SARQRSQKSL FKTYIDVLHV QKFDRKKMGI
DMSTVEQEMS EQAAEADQAR KVSAEEEEKI KRTASRPDIY DLLSRSLAPS IYEMDDVKKG
ILLQMFGGTN KTFQKGGNPR YRGDINVLLC GDPSTSKSQL LRYVHKIAPR GVYTSGKGSS
AVGLTAYVTR DPETRQMVLE SGALVLSDGG VCCIDEFDKM NDSTRSVLHE VMEQQTVSIA
KAGIITTLNA RTSILASANP IGSRYNPKLA VPQNIDLPPT LLSRFDLVYL VLDRVDETED
RRLAKHLVGM YLEDNPENAS SQEILPIEFL TAYITYAKTN CHPAITPAAG AALTDAYVAM
RQLGDDIRAQ ERRITATTRQ LESMIRLSEA HARMRLSPEV TVGDVEEAVR LIRSAIKQAA
TDARTGLIDM GLLTEGSSAA DRRLRDDLKK AVLSRLDERG GVSGGAVRWT DLYRDVSEQS
DNKLDHNQFG DAVRSLETEG SVNVFGEGAR RSIRRAAMSM S
//
