ID A0A1J9R7B2_9PEZI Unreviewed; 756 AA.
AC A0A1J9R7B2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Pa domain-containing protein {ECO:0000313|EMBL:OJD37414.1};
GN ORFNames=BKCO1_700092 {ECO:0000313|EMBL:OJD37414.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD37414.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD37414.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD37414.1,
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 with a
RT 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 EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJD37414.1}.
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DR EMBL; MNUE01000007; OJD37414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9R7B2; -.
DR STRING; 236234.A0A1J9R7B2; -.
DR OrthoDB; 206729at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd04813; PA_1; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22765; RING FINGER AND PROTEASE ASSOCIATED DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22765:SF483; RING FINGER PROTEIN MUG145; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF17123; zf-RING_11; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..756
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012091684"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 728..756
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 130..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 80419 MW; C97E22FF6B5B6AD6 CRC64;
MRPLRLLLSL SSCVLAVTLL LYIAIPARDA HVSSSPHKKS KLSALFSLSA PALFPPSAII
SLTDDNSTFF LARPAAFGPP LPSKGLSGQL WTGSGFGGDT LTHGGLAAGV DGELGCSDVP
GWDERRGRLA SASHFEKASG TANDADASKP GRSRRGLLGA KSRSNAAPKP ESKPLNDDGT
DDHFHRVQPH NPNAPSWGKA SSESSDHADI QSLQESAEIA GRVVLLRRGG CGFLEKVKWA
QRRGGVAVIV GDDIRGGPLV TMYARGDTSN VTIPALFTSH TTAHLLSSLV PSGGLIENLP
TEDSLKLALG KASKPSKGPA SGPTFTSTSP ASKQTAGRAV SEDLAKSVQS PNGEVRGDVT
SREKPGWIRS LLAIFSSGSR KESATEESRR PPSSGNIDWI LVEDWEDEDP MRTRTATAAA
QKTSSTSLAL PGEFSDDFVI GVQDWRDPDL LPPKTEPSIN KKPTAQSKTK QSPGATSFSG
GNVLPGSGEY AELSSANAKF KPASSDKDSA AKEREHAKHG GWFGNLPWNK QPDAKAEAFT
QPFPASSFKP KASLKSTPTP TEIAMQSSRP GIQSGSDRHD GLWVTLTPTS MSNSPFFDTL
LVLVVSPLVT LTVVYALLLL RSRIRRRRWR APKSVVERLP VRTYQTLNSS DSSTSTSPIA
TPAAGSPRTP LLQSSSSSQA NSSRNRPRSR TAGDVTPQGL GRSVSPEEKA ETGLAAWRRK
YGGRQKECVV CLEEYVDGVS RVMSLPCGHE FHAECM
//
