ID R9P545_PSEHS Unreviewed; 1014 AA.
AC R9P545;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=PHSY_003907 {ECO:0000313|EMBL:GAC96327.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC96327.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; DF238801; GAC96327.1; -; Genomic_DNA.
DR RefSeq; XP_012189914.1; XM_012334524.1.
DR AlphaFoldDB; R9P545; -.
DR STRING; 1305764.R9P545; -.
DR GeneID; 24109193; -.
DR eggNOG; KOG0478; Eukaryota.
DR HOGENOM; CLU_000995_7_1_1; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000014071; 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; 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; 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 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:UP000014071}.
FT DOMAIN 579..790
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 110741 MW; 6A2EB3F35C35F6AD CRC64;
MSTPGGPPSD AEMRDVEQRT PLAPASLSNR GPAGASSPLA FPSSSPFKSQ ASNARAPQSS
LGASSPLHFP TSSPSARTSR GQRTPLASAR RSQNAENRLP SSSSGVSRLD EPLFFPSSGG
TTPRHQRRGE IHSSVALSSP SLTRRNRADP SSQPQGAPAR SSSVFGGSQP AADGHSDALS
FSQHGVTSDA AAPGQDGVSK VIWGTNVSIG ETMEMFRSFL RGFRLKYRWA HAKKLGQPLP
PAATGNPAEG ERLVYEGYLR RMRITDQTNL NLRISDLEAF PPSKRLKMQL IRYPQEMVPI
MDQVLKDEML EMAYEDQKEA RDGMGGDMGL AEIELMETKL YKVRPYGADA INMRELNPSD
IDKLVTVRGL VIRATPIIPE MKQAFFRCLV CNHTVPVEID RGRIAEPDRC PRQVCNLQGS
MSLIHNRCEF SDRQVVRIQE TPDVVPDGQT PHTVSMCAYD ELVDVSKPGD RVEITGIFRS
TPVRVNPRQR SLKSLYKTFV DILHIKRTNG KRLGVDLSTR DASEQAAGPG AQAVGVGGEE
DDEDVEVQSG YGADAEDADA PRSQDLEDKL RSIAQRDDVY EVLSRSLAPS IYEMDDVKKG
ILLQLFGGTN KTISTGGGGG GPRYRGDINV LMVGDPGIAK SQILQYVHKI APRGVYASGK
GSSAVGLTAY VTRDPDTKQL VLESGALVLS DGGVCCIDEF DKMSEATRSV LHEVMEQQTL
SIAKAGIITT LNARASILAA ANPTGSRYNI NLPITKNIDL PPTLISRFDL VYLVLDKIDE
ANDRRLARHL VSLYLEDKPD TGGKDVLPIE TLTAYISYAR NRIQPILTKE AGDALAARYV
ELRKVGEDPR NAERRITATT RQLESMIRLS EAHARMRFAD EVIVDDVEEA ARLIREAAKS
SATDPRTGLI DLDLINTGRS HHQRKLAGDL RREFLQLLDE MGSMSGRATS PSGPSSTQPT
KAVRYVDLQK ALNEQSSAPV DQNDLYELVR TLESEGIVKT AGERERRTVR RISS
//
