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
//