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
//