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Database: UniProt
Entry: A0A2H3I9X6_FUSOX
LinkDB: A0A2H3I9X6_FUSOX
Original site: A0A2H3I9X6_FUSOX 
ID   A0A2H3I9X6_FUSOX        Unreviewed;      1015 AA.
AC   A0A2H3I9X6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=AU210_001094 {ECO:0000313|EMBL:PCD45662.1};
OS   Fusarium oxysporum f. sp. radicis-cucumerinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD45662.1, ECO:0000313|Proteomes:UP000219602};
RN   [1] {ECO:0000313|EMBL:PCD45662.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD45662.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA   van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA   Rep M.;
RT   "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL   Environ. Microbiol. 18:4087-4102(2016).
RN   [2] {ECO:0000313|EMBL:PCD45662.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD45662.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA   van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA   Brankovics B., Houterman P.M., Arie T., Rep M.;
RT   "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT   multiple cucurbit species.";
RL   Sci. Rep. 7:9042-9042(2017).
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:PCD45662.1}.
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DR   EMBL; MABQ02000001; PCD45662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3I9X6; -.
DR   STRING; 327505.A0A2H3I9X6; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000219602; Chromosome 1.
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:UP000219602}.
FT   DOMAIN          595..803
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1015 AA;  111862 MW;  D8850C7AF55DE412 CRC64;
     MSSPTKRSTR SSATPRRAAG NSETPRQGNS QLDAPSSPLH YQSSSPGPSN QNNLPGDVSS
     PFGHMTNSQS DVPSPPLRQM TDTQSDLDPE RTPRANPTTP AYHGGSSPIH YEPSSSPGRS
     LRQQSELRSE SSGLFLGSQL GTPAPHRRGD INSDATRTPR ASRRVILDDA GRVVREGPAD
     GSDAASFANR DPNTSEADVL GGQGQSLIWG TTVSIDDTFA SFKEFLRNFT QKYRMYRDGA
     SDEDVQNAPD AESKPYWEAL ENMLLLGTTR LYLDISDLNL YPPTRKLWHQ IQAYPQEIVP
     VMDQSVHDMM VEIARAETLR NRQSQSSAGH QASQQSTQSS EPVFPSSDRP EEAPTPRTQP
     DQQQQASLED QVASSIYVVR PFGLDKTTNL RDLNPSDMDR LISIKGLVIR TTPVIPDMKD
     AFFRCNVCNH SVNVGLDRGK IREPTECPRE ICKSKNSMLI VHNRCSFEDK QVIKLQETPD
     AVPAGQTPHS VSVCVYNELV DFCKAGDRVE LTGIFRVSPV RVNPRQRALK SVHKTYVDVL
     HIQKVDKKRM GADPSTLGVA GEEEAEAGEN GIEETRKITI EDEEKIRETA ARDDIYELLA
     RSLAPSIYEM DDVKKGILLQ LFGGTNKTFQ KGGSPKYRGD INVLLCGDPS TAKSQMLSYV
     HKIAPRGVYT SGKGSSAVGL TAYVTRDPET RQLVLESGAL VLSDGGVCCI DEFDKMSDAT
     RSVLHEVMEQ QTVSVAKAGI ITTLNARTSI LASANPIGSR YNPDLPVPQN IDLPPTLLSR
     FDLVYLILDN ADEKNDRRLA KHLLSLYLED KPQSAPNKND ILPVEFLTLY ISYARSKIQP
     TISQEAAQEL VDCYVAMRSL GQDVRAADKR ITATTRQLES MIRLSEAHAK MRLSETVTRD
     DVREANRLIQ SALKTAATDA QGRIDMSLLT EGTSAADRKR RDELRTALLR LLDDMTAGGN
     TVRWTDVARR LSEGASIPVE QSEFNDVMRA LEAESAIMIT GEGARRTIRR VTSVA
//
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