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Database: UniProt
Entry: A0A1J9QVZ8_9PEZI
LinkDB: A0A1J9QVZ8_9PEZI
Original site: A0A1J9QVZ8_9PEZI 
ID   A0A1J9QVZ8_9PEZI        Unreviewed;       885 AA.
AC   A0A1J9QVZ8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   31-JUL-2019, entry version 15.
DE   SubName: Full=Snf2 family domain-containing protein {ECO:0000313|EMBL:OJD32553.1};
GN   ORFNames=BKCO1_37000179 {ECO:0000313|EMBL:OJD32553.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetes incertae sedis; Botryosphaeriales;
OC   Botryosphaeriaceae; Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD32553.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD32553.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD32553.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible
RT   with a hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OJD32553.1}.
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DR   EMBL; MNUE01000037; OJD32553.1; -; Genomic_DNA.
DR   OrthoDB; 132523at2759; -.
DR   Proteomes; UP000183809; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000183809};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN      317    492       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      627    678       RING-type. {ECO:0000259|PROSITE:PS50089}.
FT   DOMAIN      708    885       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   REGION        1     60       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS      1     20       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     45     59       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   885 AA;  98161 MW;  7AA556FB54FF7E03 CRC64;
     MSTAKRQNLF PNQQASKRAR LLSPPDQLQP PNVAHEAYPI TPISDSGADS AQPNTPIQPS
     ALRRDGRYYC FGTLCEVKVR MLKDEKALEE ACIPATDGWM QLRLTHKKNH LLQDSNGLDL
     AVLNQRTADA LQALDGMGAI RYEAYVTVQY WAAQIRAAKR TAKNTVVDIE VNVSGPLESG
     DEVGRVLSRA GLFLQPPSVL LPGTAYQNPH VIYLPGIQES SLDSAIPAAP RLADLNAGKL
     DIQAVLGCLD QSEDLAPTAV DERMVTTKLH EHQKGAVSFI IQREAKITPS AFSLWKPYEG
     SPRQPCYRHT VLDIKKQHPP KENFGGIVAD EMGLGKTLSM LAAIGITAES AKHFSKGLTG
     DPMQMKTKAT LVIVPSALIL QNWASEIKDT FQYLKYHGPR RPRDQKAVLD KNVVLTTYET
     VSADFVRGDS PLYQVAWFRV VLDEAHYICG QQTKRFCAAS ALQAQHRWCL TGTPIQNRLD
     DLSALIRFLK VPYLDNASSF NNYISRPIEQ NDTRGVVRLR SLLKSVCLRR TTELLTVPEP
     TIYSRRLDFT EAERDAYNQV AISYKKEMDE VVSGNRKGNS QLGLCQAILR LRRFCNNGSS
     LLRMSGSATQ AAEDMLSYMQ QAGEVACASC SRELQTIDDT EDSDSGVLAA CSHLLCSVCI
     RQTQLNHTDS GLQCPICRAP TQQLDLRLDS VDQQTSPALS EGNSYNTKLV ALYHDISQYK
     QSEKGIVFTA WRDTISVISS LLRTRKIDHC VVQGSMTIAE RKMSLDKFQS DPNCTILLMT
     FGTGSAGLNL TAASRIHIFE PQWNPSIESQ AIGRAVRLGQ KNRVTVVRYI MKNTVEEYME
     NTQTRKAQMA SIGWDAEKEE GAGGKLKLVA KMVFNTEMPP DVEMT
//
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