ID A0A139I223_9PEZI Unreviewed; 993 AA.
AC A0A139I223;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN ORFNames=AC579_6565 {ECO:0000313|EMBL:KXT08632.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT08632.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT08632.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT08632.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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:KXT08632.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFZO01000421; KXT08632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139I223; -.
DR STRING; 113226.A0A139I223; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0031179; P:peptide modification; IEA:InterPro.
DR CDD; cd04794; euk_LANCL; 1.
DR CDD; cd15857; SNARE_SEC9C; 1.
DR CDD; cd15886; SNARE_SEC9N; 1.
DR Gene3D; 1.20.5.110; -; 2.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR12736; LANC-LIKE PROTEIN; 1.
DR PANTHER; PTHR12736:SF7; LANC-LIKE PROTEIN 3; 1.
DR Pfam; PF05147; LANC_like; 1.
DR PRINTS; PR01950; LANCSUPER.
DR SMART; SM01260; LANC_like; 1.
DR SMART; SM00397; t_SNARE; 2.
DR SUPFAM; SSF158745; LanC-like; 1.
DR SUPFAM; SSF58038; SNARE fusion complex; 2.
DR PROSITE; PS50192; T_SNARE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492}.
FT DOMAIN 399..461
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 1..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 286..313
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 108460 MW; 19794642039405F6 CRC64;
MPFGLKKSDK DGDLDSQKKS LFGSRSKAPK PGSPAPASNN PYAVPAQSSG NPYANKGSSN
PYANQAQNDP YMKSSASVAS SQPPTSSMGN LSISSQNTAP PAYGNGPAPN RYEKSPVPQG
GYGGAPQARY GREQAQYGGY GSDPYGTSSG PSQSRAGGYG GLGRTNSNET MGTDAGRNAL
FGDAAQRAAS KPSDPYAAQE SGRDNSYSNA GGYGSGETSG GYGAGPAREL TAEEQEEEDV
QAAKQEIRFI KQQDVASTRN ARRIAEQAEA TGRETLARLG AQGERIHNTE RNLDMASNQN
RLAEEKAREL KTLNRSMFAV HVANPFTAKK REEAANAIAL EKHQAERRQA DATRAEAYSS
TARQQQQQRD INGNVVRPNA TRNLADRAKY QFEADSEDDE MENEIEDNLE AIHRGARTLN
QLGKAMGNEI DSQNKHIDRI IGKTDKVDDQ IAVNQKEYGA LDGITIQDTA IVGGYEKLNI
ALVLAGFVLL SIGAQSVVAA PTSLQMAYQD YLVGYTHSRQ RSPPRVWTLH HSSPTSRRRA
SGAQKTPSWT CCAVAVVPVA ECLDLRHCNM PPRYFKNDAP LARRDPRRQL EASLTRLVTD
HPPASIKPGG GLFKGPVSVA YVFLVLQQMY PDMVIEGHAL GTWSAAYLKH AQENIISYPG
PSVGKCGITD DILSLLAIGA ASSKDVDMVN NLCDYSAEVL EEGTENELLY GRAGYLYLLR
MVKASFMDDP KTLQIITDNQ DDVVEAILDS PRPWKWRGKT YIGAVHGAMG IITQIVLTDP
KKYAEKLEAE LAVLLTYQYP ESGNFPSSVP PDRDRLVQIC HGAPGVVASL ESIKEHFSPA
IQDRINKAIT KGRECILERG LLTKEPCLCH GISGNALALE DKEFEHFLTY TTGHEMKSME
KDGMLEKSSA PESLWFGEAG RAWTWAVADR ADDEDYELTL RRRDERQMNC NESRESIMST
DSEFCALGMI LLLACDWLPT RYHSMNLLQK KAF
//
