ID T0KQJ2_COLGC Unreviewed; 658 AA.
AC T0KQJ2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Peptidase S33 tripeptidyl aminopeptidase-like C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_05211 {ECO:0000313|EMBL:EQB54898.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB54898.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:EQB54898.1}.
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DR EMBL; AMYD01001041; EQB54898.1; -; Genomic_DNA.
DR AlphaFoldDB; T0KQJ2; -.
DR STRING; 1237896.T0KQJ2; -.
DR eggNOG; ENOG502RY03; Eukaryota.
DR HOGENOM; CLU_013364_5_2_1; -.
DR OMA; WAEIRMS; -.
DR OrthoDB; 1833441at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF25; PEPTIDASE S33 TRIPEPTIDYL AMINOPEPTIDASE-LIKE C-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 128..369
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 519..620
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 72872 MW; 616BE5C1C503E80B CRC64;
MDKSYPVGFG QADEPRQAHQ PRPRKTNAIR IAAIASGLIL YFSFPSFISL GDRPPSLPSL
PLADPEFDWL QIVPQEQFIY HPCFGGYQCA RLSVPINWND IANPARAAVA VIKVPAKVPV
TDPRYGGAIV LNPGGPGNSG VGQVLRKGRH MQIIVDAAHP ASTPDGFSDG KYFDIIGFDA
RAVNNTTPHL TCFPNKQSEL NFLARQPSDF LFGVSDTYVD LAWANYRAFG ESCATRRGDE
PNMAEFANTA QVVEDIVAMI ERHAEWREVE AQRIISSYDV SNFSKSDRER ILDTTRWRKG
VEKLNYWGVS YGTILGQTFS VMHPDRVSRV LIDGVVDPDD YYSAKWLKNL QDTDQILQRW
ASYCNQAPEA CPLASLHTPP SIINARLARL ANSLLEEPIP VAGTAEHGPT VIDYPDIMQL
FADSVYDQKL VEPYFELFSD LLDRNGTSAA ALKMEGDLIP LSLNADCDKD GSYSAACVRD
QGPSGFFAAI ACGDGPDLRN TSKAEFREYF KELRDQSDVL GASWSGHRML CINWKARPAW
RVEGPWTANT SYPLLIIGNT YDPVTPLRNA HRVSTLFPGS VVLHQNTEGH GLHASPSICT
GKAVRAYFQD GTLPEIDTVC EPEYRTWIGC VNPDGCDARS DEDQALWEAL SGINQNYR
//
