ID E5R0C0_ARTGP Unreviewed; 497 AA.
AC E5R0C0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=MGYG_01349 {ECO:0000313|EMBL:EFQ98316.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
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 peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR EMBL; DS989822; EFQ98316.1; -; Genomic_DNA.
DR RefSeq; XP_003177268.1; XM_003177220.1.
DR AlphaFoldDB; E5R0C0; -.
DR MEROPS; S10.014; -.
DR GeneID; 10032594; -.
DR VEuPathDB; FungiDB:MGYG_01349; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_12_3_1; -.
DR InParanoid; E5R0C0; -.
DR OMA; PYHYGLA; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF116; CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000256|RuleBase:RU361156};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 19..497
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5005128176"
SQ SEQUENCE 497 AA; 54730 MW; EC685D25BB68245C CRC64;
MRFTQLVAAA LCLGATEAAV APIDRARKVL GNQHAFDKRD TAGDAAKGAK HLTSKNKKFY
VDPNSIPNVP FSIGESYAGN LANTPAGNSS LFFWYFPSEN PEAKNEITIW LNGGPGCSSM
IGLLQENGPF LWQPGTEGPV KNPYAWSKLT NMVWVDQPAG TGFSPGPPTV KDEVDVANQF
SDFWKNFMDT FDLHHSDVYL AGESYAGQYI PYIASEMLDR KDSEYFNVRG ITVIDPSIGA
TEVIIDAPSV PAMHRFNNVL ALNESFVNDI TQKWESCGYK KFMDDALKFP PTGPLTVPGK
TPGCDVWDEI ITAVKKVNPC FNIYHLKDNC PSPSNPMNGP NNFFNNKQIQ EAIHANPTDY
RLCGESQIFG PHRNDRSVPS SFGPLASVIE RTNNTIIAHG DLDFLLFTEG SLASIQNMTW
GGLQGFQKEP SDKFYVPYKD GSEMGGAGFV GKTHRERGLT WATVDLAGHE IPQYAPTAGY
RLLEYMLGRV QSLTETH
//