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Database: UniProt
Entry: F2SVQ0_TRIRC
LinkDB: F2SVQ0_TRIRC
Original site: F2SVQ0_TRIRC 
ID   F2SVQ0_TRIRC            Unreviewed;       475 AA.
AC   F2SVQ0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Caspase family p10 domain-containing protein {ECO:0000259|PROSITE:PS50207};
GN   ORFNames=TERG_06622 {ECO:0000313|EMBL:EGD90394.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD90394.1, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC       family. {ECO:0000256|ARBA:ARBA00010884}.
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DR   EMBL; GG700655; EGD90394.1; -; Genomic_DNA.
DR   RefSeq; XP_003232630.1; XM_003232582.1.
DR   AlphaFoldDB; F2SVQ0; -.
DR   STRING; 559305.F2SVQ0; -.
DR   ESTHER; trirc-f2svq0; abh_upf0017.
DR   GeneID; 10373716; -.
DR   VEuPathDB; FungiDB:TERG_06622; -.
DR   eggNOG; KOG1838; Eukaryota.
DR   HOGENOM; CLU_032487_1_0_1; -.
DR   InParanoid; F2SVQ0; -.
DR   OMA; MMTTSWG; -.
DR   OrthoDB; 1655372at2759; -.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR012020; ABHD4.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   PANTHER; PTHR10794; ABHYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10794:SF63; ALPHA_BETA HYDROLASE 1, ISOFORM A; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT   DOMAIN          388..468
FT                   /note="Caspase family p10"
FT                   /evidence="ECO:0000259|PROSITE:PS50207"
FT   REGION          113..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  53819 MW;  5CC86DC8DA958997 CRC64;
     MGILSWFLPN GRVSFHHAGK SVILKRKPQK KGPGVDESKY ISLADLCKSA TPADCQLNPF
     LFNGHLQTAW TLMRTDDIPV YYKRWRFEGD SPDYRGSFEV DFVVPPYDVN KTSSSLTSEQ
     SDNGTFESST PPDSTHPSPR TSFFTKEEFS ALPSDDKKPM LVVLHGLSGG SHEPYLRNIV
     DPLHKQGWEV CVVNFRGCAN SKVTSSILYN ARATWDVRQT VRWLRKNFPF RPLFGIGFSL
     GANILTNYVG EEGEDCQLKA AVVCSNPWNL EVSSLALQRT WVGLQIYSKT MGASMRRLFE
     QHVDKLREHP RVNVERVRKT TYLHEFDREL QAPVWGYPTE TAYYRDASSI DSLFAVKIPL
     FAIQAEDDAI SSKEALPYLE MTKTPYAVMC TTSWGGHLSW FEYGGGRWFT KPVVNFLNKM
     VSEIDLDAPL TVVEEEMESK SNLNPAASPE RVDGPHPDFT PMRRKLHMPI PDGRE
//
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