ID S3BZ46_OPHP1 Unreviewed; 1043 AA.
AC S3BZ46;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-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=F503_08323 {ECO:0000313|EMBL:EPE05792.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE05792.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE05792.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE05792.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(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; KE148155; EPE05792.1; -; Genomic_DNA.
DR AlphaFoldDB; S3BZ46; -.
DR STRING; 1262450.S3BZ46; -.
DR VEuPathDB; FungiDB:F503_08323; -.
DR eggNOG; KOG0478; Eukaryota.
DR HOGENOM; CLU_000995_7_1_1; -.
DR OMA; NRCSFAD; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000016923; 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:0051301; P:cell division; 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 Cell cycle {ECO:0000313|EMBL:EPE05792.1};
KW Cell division {ECO:0000313|EMBL:EPE05792.1};
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:UP000016923}.
FT DOMAIN 622..830
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 113817 MW; B4F67745B76EF7EB CRC64;
MSSPAGRRST RSSQAGTPGR PQRGSGPAST PGGLQAPASQ QLVSSPLLYE SSPAAEANMD
PSSPLRQMSN TQSTQDSLHD PDVPMQGIAP SSPLAQMETQ SSAGDRTPRA SRGLFGESSP
VRYFASSSPG RQLQSDLRSE TSGLFVSQRA GSTGPARSRR GDINSDSLLR TPRAHRVILN
EAGHVMSDIG GSETGSFATN NPDTSEAQVL GGMSQSLIWG TTVSIDDTFS AFKDFLRNFT
KKYRLWLDGK TELETADMPG AESKPYWETM QNMLLLGTSR LYVDIRDLKA YPRTNKLWYQ
AQAYPQEIVP IMDQSIHDLM SELAHAEVNR QKATAASLSQ SSAGGRAQSV GQSSELNFPS
SERGDEPATP RASQAQTETA QTLEDDVSKT VYIVRPYGLD KSTNLRDLNP ADMDRLISVK
GLVIRATPVI PDMKDAFFKC QACNHSVTVS LDRGKIREPT ECPRPSCGTS NSMQIVHNRC
IFEDKQVIKL QETPDAVPAG QTPHSVSVCV YNELVDFCKA GDRVLITGIF RVSPVRINPR
QRTINSVHKT YVDVLHIQKV DNKRLGVDPS TLDQDDEDVE AALMAEQLEA NGGAGTNRME
ETRSWTSDEE AKIKATAERP DIYDLLSRSL APSIYEMDDV KKGILLQLFG GTNKSFKKGG
SPKYRGDINV LLCGDPSTAK SQMLSYIHKI APRGVYTSGK GSSAVGLTAY VTRDPETRQL
VLESGALVLS DGGVCCIDEF DKMNDSTRSV LHEVMEQQTV SVAKAGIITT LNARTSILAS
ANPIGSRYNP DLPVPQNIDL PPTLLSRFDL VYLILDRADE KTDRRMAKHL LSMYLEDTPQ
SARSTNEILP VEFLTSFISY ARANVHPVLS NEAGKALVEA YVEMRKLGQD VRAAEKRITA
TTRQLESMIR LAEAHAKMRL SIEVTADDVR EAYRLIQSAL KTAATDSQGR IDMSLLTEGT
SAAERKRKAD LSAAILRMLD EALATGQTSM RYAEVSRRMA ETLNIPIEAA DMAECLRSLE
MDGSIAITGE GARRTIRRST GVA
//
