ID A0A163K975_DIDRA Unreviewed; 1139 AA.
AC A0A163K975;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Zinc ion binding {ECO:0000313|EMBL:KZM26856.1};
GN ORFNames=ST47_g1969 {ECO:0000313|EMBL:KZM26856.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM26856.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM26856.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM26856.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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:KZM26856.1}.
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DR EMBL; JYNV01000090; KZM26856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163K975; -.
DR STRING; 5454.A0A163K975; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10579; CALCIUM-ACTIVATED CHLORIDE CHANNEL REGULATOR; 1.
DR PANTHER; PTHR10579:SF43; LOW QUALITY PROTEIN: EPITHELIAL CHLORIDE CHANNEL PROTEIN-LIKE ISOFORM X1-RELATED; 1.
DR Pfam; PF15411; PH_10; 1.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 127..173
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 430..550
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 620..793
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 125320 MW; 80E5039AAEE2738A CRC64;
MSNGFRAPLS GSRPPSLPHH TQKQNLIEAN LLELGLLGRK HQKKNKEKVV EFRSTADHSD
GGLRPGSRSS HNTSSTATAK LFSSYPQRND ASVDRQVPLH SARGMAGVLD IERSRTRRER
TFIGSDCAVC EEALEHTLRG ERILQLSCGH VSHEACFYEY IREFEAKECP TCNATLGLDT
SRGGNIDLEK IVRSVQAEAP QISSQSQGQG HSQSQRSHQN TPTPWDNQTM HSASGQTQGR
SRNGSDASAR FAPSHHTRQR DSSHSRERGS DRGGSMSRQH LRSDSGATGA ASSQDYAAAQ
DGRRHDYDVQ SMETSLSSPR ALLKNPIPAP TVTVRSEFPT LSKSRQQQSL TCLVTVEVVE
GKWRPDPEDM RGAPLLSLAS ATESSFGRPK SPARSRHAAY DFDTPYESEQ VLDETTEDLH
ARVDNWHGLD FSRFGKLRLH GQIRVGKDRQ SWQELECYLF SEMLICVKEK KGTAQPQWDN
TKASRSAKKS KCTLKGSILI KKHLNQVEHS PDDLILTLSL SVAELPSFHL QFPDRSQLEL
WRRALMDVRL DFPMSRGMPD YDQDHSGTEE DDYRRPKRVS SVNSSYGAAR STMTAPTEYT
SSRAGPPEPR LSGSVHVPID VVVVIPVSSS MQGLKINLLR DTLRFLVHNL GERDRMGLVT
FGSSGGGVPI VGMTGKAWRD WPKVLESIRP VGQKSLRADV VDGANVAMDL LMQRKSSNPL
SSILLISDSS TSDVESVDFV ISRAEAAKVS IHSFGLGLTH KPDTMIELST RTKASYTYVK
DWMMLRECVA GCLGSLQTTS HQNVRLKLRL PEGSPAKFVK ISGALQITKR ATGRDAEAAL
GDLRFGDKRD ILVQLAIAPD SGSPEQLLQD PWETIVSGLE ALGGPLDQDD SRTLSVEEVP
LIQADLTYGD ILREGTVSHL PRPSLLAITL LPSGPKKSST AFPPTPPIPP HPHVVQRRME
LLTSDMLTRS LTLVSRGQHE RAHHLLKETR SILKGLGKGG LPPLPPPGQR RHDAPSTTGS
TGTSSPTHSS GGDTRPRTPS PHANSPFTPA AGIDARTMHA LDAELESSLE WINHPAVFGR
DSRKAVLQAI GVISSQRAYT FRSPSESLWA ERVQGVKRLS ERSREWRESG DQEALMEEN
//
