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Database: UniProt
Entry: A0A0M8P574_9EURO
LinkDB: A0A0M8P574_9EURO
Original site: A0A0M8P574_9EURO 
ID   A0A0M8P574_9EURO        Unreviewed;      1001 AA.
AC   A0A0M8P574;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=ACN38_g7586 {ECO:0000313|EMBL:KOS41544.1};
OS   Penicillium nordicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS41544.1, ECO:0000313|Proteomes:UP000037696};
RN   [1] {ECO:0000313|EMBL:KOS41544.1, ECO:0000313|Proteomes:UP000037696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS41544.1,
RC   ECO:0000313|Proteomes:UP000037696};
RA   Nguyen H.D., Seifert K.A.;
RT   "Genome sequencing of Penicillium nordicum.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS41544.1}.
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DR   EMBL; LHQQ01000129; KOS41544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8P574; -.
DR   STRING; 229535.A0A0M8P574; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000037696; 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:UP000037696}.
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          130..188
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"
SQ   SEQUENCE   1001 AA;  110224 MW;  7E833CA16E56232A CRC64;
     MSSPTQRRRG RPSKNSTASP SSSSRQEPPS SPTFQATPRA SRRLMGEGAA PSSSPIFFQS
     SPTKGDNNAE TPDERMADAS STVDDGDRTP RGNPGVRDSS PIHYIPSSSP TRGLGRSDIR
     SDIRSDALST ASSGLFVSPG GQGRRGGPRR SDLHSGGFGS TPSRRNRVFV DANGMPTGDT
     MPRSDATFSN INPGTSEAEA MAGNSTRVIW GTNISIQDSM SAFKNFLYNF ATKYRLWADG
     ATEDETRLMG ELAERHECIT MCNNMRRLGV TTFNLDAANL KSYPLTRKLW HQLSAYPQEI
     IPLMDQALKD VMVDLALKEM DVLRSESQRT AQPRDRRGQP ILTSDNVLPT VDVPDLVGEV
     EAMTFKVLPF GLDRTVNMRE LDPADMDKLV SIKGLVIRAT PIIPDMKEAF FRCSACSYGV
     QVDIDRGRIA EPTVCPRDSC KEKNSMQLLH NRCSFSDKQV IKLQETPDNI PDGQTPHSVS
     LCVYDELVDV CKAGDRVEVT GIFRCNPMRV SARQRSQKSL FKTYIDVLHV QKFDRKKMGI
     DLSTVEQEMS EQAAEADQAR KVSAEEEEKI KRTASRPDIY DLLSRSLAPS IYEMDDVKKG
     ILLQLFGGTN KTFQKGGNPR YRGDINVLLC GDPSTSKSQL LRYVHKIAPR GVYTSGKGSS
     AVGLTAYVTR DPETRQMVLE SGALVLSDGG VCCIDEFDKM NDSTRSVLHE VMEQQTVSIA
     KAGIITTLNA RTSILASANP IGSRYNPKLA VPQNIDLPPT LLSRFDLVYL VLDRVDETED
     RRLAKHLVGM YLEDNPENAS SQEILPIEFL TAYITYAKTN CHPVITPAAG AALTDAYVAM
     RQLGDDIRAQ ERRITATTRQ LESMIRLSEA HARMRLSTEV TVADVEEAVR LIRSAIKASA
     TDARTGLIDM GLLTEGSSAA DRRLRDDLKK AVLSRLDERG GVSGGAVRWT DLYRDVSEQS
     DNKLDHNQFG DVVRSLETEG SVNVFGEGAR RSIRRAAMTM S
//
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