ID A0A1J9R6P3_9PEZI Unreviewed; 905 AA.
AC A0A1J9R6P3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Saff domain-containing protein {ECO:0000313|EMBL:OJD37198.1};
GN ORFNames=BKCO1_8000110 {ECO:0000313|EMBL:OJD37198.1};
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:OJD37198.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD37198.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD37198.1,
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:OJD37198.1}.
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DR EMBL; MNUE01000008; OJD37198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9R6P3; -.
DR STRING; 236234.A0A1J9R6P3; -.
DR OrthoDB; 2056337at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
DR CDD; cd09264; AP_Syp1_MHD; 1.
DR CDD; cd07650; F-BAR_Syp1p_like; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR InterPro; IPR049609; Syp1-like_MHD.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF54; SUPPRESSOR OF YEAST PROFILIN DELETION; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF10291; muHD; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR PROSITE; PS51072; MHD; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000183809}.
FT DOMAIN 628..887
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 236..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 31..58
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 236..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 97303 MW; B3BF351BB012D390 CRC64;
MELSRKDYPA MLESLQPTQA VAVLNDRVKH IQKVNADIAD FLQERRRLED QYAQGLRKLA
ARQLPDAGAD LGVFTLPWQR IVGATEALAE SHHSLAHKLD TDVERPLRDF DKTNREMQAM
SNISGNMAHM AKEIDSAQKR ADKLKEKGAK APAGKVATAS TDVENANQQW SSQAPFVFEQ
LQAVDESRIN QLRDALTQFQ TLELDAIDRT RGPTEQCLGV ILEVQTADEI KTFSLKTTSG
KPKLETQRGR NQAQASSSST PAMQPPPTPD DGSSQRSGSG GSPVVPAEPR LRPAVQEQKH
GGLHGLKRLG TVLGRRKSTA PYARTSSPDR KSSSPNLGAA FSSFGSRGNK SRDADHRPAS
PSRLAESQLP SSPEASESIA SPVRPESASV DRTNGISPVP EDEPRDSEMM NGGQSSGIPQ
LQEPLQPTSA SSVSLEPQKD ADGYTVPATS ATSDLFAQVE ADAAAESVPP QFKVDIRNAP
IQEEDSGEAE SAMANVANTL RMQAAPTKRS NTTRGRRDVR NTIFVPSTSQ GPDLPPFAEP
TNAPPLPIPA SPSSSPLPSA SPNLSAVSPQ IPIPASPPSA RPQSPLRPAS HRLNLGDDHA
ASDTQSIRSG RSLSSSYSHT VRHPDMHEPG LNSSIVETVS TWFEHGHVTR AVVIGELALA
YNPPDLSVPF GNETIRLENF PVLEKVAPNP TFVDQVADKA GDYSINLSSI TRTQVAFKYQ
VHLDENNIAS FAPIALTPAW KVEPTQTSVI LNYSLNPAFR LAAGHTSVTL SNVVLIMHLD
PAGSRSSHCQ SKPVGTFSKE KSLIYWRLGD VTLSADQPAQ ALRARFYTDT EAKPGNIEAR
WEMTGENASG HGSGLDVSQM VQAGEAVEVE DDPFADESAA PSSPAITWKD VPVIKRISSG
TYTAV
//