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Database: UniProt
Entry: V2YVT3_MONRO
LinkDB: V2YVT3_MONRO
Original site: V2YVT3_MONRO 
ID   V2YVT3_MONRO            Unreviewed;       849 AA.
AC   V2YVT3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=ATP-dependent DNA helicase CHL1 {ECO:0000256|ARBA:ARBA00017386};
DE   AltName: Full=ATP-dependent DNA helicase chl1 {ECO:0000256|ARBA:ARBA00016387};
DE   AltName: Full=Chromosome loss protein 1 {ECO:0000256|ARBA:ARBA00029709};
GN   ORFNames=Moror_12411 {ECO:0000313|EMBL:ESK95799.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK95799.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK95799.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95799.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
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:ESK95799.1}.
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DR   EMBL; AWSO01000061; ESK95799.1; -; Genomic_DNA.
DR   RefSeq; XP_007844886.1; XM_007846695.1.
DR   AlphaFoldDB; V2YVT3; -.
DR   STRING; 1381753.V2YVT3; -.
DR   KEGG; mrr:Moror_12411; -.
DR   HOGENOM; CLU_006515_2_0_1; -.
DR   OrthoDB; 124793at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   NCBIfam; TIGR00604; rad3; 1.
DR   PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ESK95799.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT   DOMAIN          9..416
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          212..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          85..123
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        212..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  95146 MW;  4A69837EA0901E29 CRC64;
     MSLELPTPEK FPAFPYSPPY PIQVELMRHL YAAIERRQVA IVESPTGTGK TLSLLCSSIT
     WLNDEKNRAR KGKLEELSGP GEPDDWVYEQ TREKARRELE DAEREYEERL ASARRREQAQ
     KAKMRARVVK KPRMLDVAKD LEEDESFLPE SEADEDDNLS PAVKALMAKF NKSSHQQNTE
     DPTCTKIYYA SRTHSQLTQV LPELQRLKIS HRRVDELPSS ERPSNKRKRY ESEENAEPSV
     SSRTVSLGSR KHLCINDDLR TKASDIDEAC RELLSEKGDR RCQYLPPLEE DHILNDFRDQ
     ILASPKDIED LANAGRMANV CPYFGSRRAI PQAELVTLPY NLLLQKNSRE ALGIDLKNQI
     VIIDEAHNLI STLLSLSTTR LTLQTLQTSF AQVGVYVSKF RNRLSAQNML HLKRLVAFLD
     ALRKYLSEWK TNNLSSSRKA EVLNTAELLG RLGRRIVGLN MLAIEQYLKS SKIARKIAGY
     AEKVSEKDAG SQQRSSRSGK GAVPPLHAVE DLLFSLAGAT EDGRVTLSLE GAKGQEEVVI
     KYQLLNPAPH FREVVNSARS VILAGGTMSP MSDIVDQLFF HLPIERISTF SCGHIINSSN
     LLTLAVTKGP HGGELDYKVG QQKNPDVIAE LASILLNFTH QIPAGMVVFF PSYNFLNTSK
     DVWSKSGVLN KLSAKKRIFF EPDDSANVEL VLQEYASAVQ NCTTKPGGAL LFAVIGAKLS
     EGLNFSDDLA RAVIVIGLPF ANLGSVELQE RMKYVKRLEQ NRAVPRQPGM KDAAAELYEN
     MCMNAVNQSI GRAIRHRGDW AALILLDQRY QTATISKKLP CWIGGNLKVA QSFGNAVKEL
     GTFFRNRRQ
//
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