ID A0A166MY08_EXIGL Unreviewed; 517 AA.
AC A0A166MY08;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=carboxypeptidase C {ECO:0000256|ARBA:ARBA00012446};
DE EC=3.4.16.5 {ECO:0000256|ARBA:ARBA00012446};
GN ORFNames=EXIGLDRAFT_847428 {ECO:0000313|EMBL:KZV78547.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV78547.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV78547.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV78547.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431}.
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; KV426848; KZV78547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166MY08; -.
DR STRING; 1314781.A0A166MY08; -.
DR InParanoid; A0A166MY08; -.
DR OrthoDB; 1447683at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.410; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZV78547.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 517 AA; 57405 MW; EA356269F6F0C47C CRC64;
MAAFGQDLKL DAADAEQQLG LPAVAQRHTR TRRRVGLAAV WLLALLVQSH LLGVISWPSW
PRFPWPWPWG RKHNSPYAPG SFYLTKTAVH LSEPKLCAVG KSYSGHIGVT GDEPDSPRRI
YYWFFEAQVA PETAPVIMTF GGGPGTSGMS NPMVGQSHCV VAENGTTLIP HDNAWSEHFN
LLAIDHPIGV GFSYGKGVNN SRDAAFDVYD FLQKFYVTFP QYSTNNFVVA SGSYGGTYVP
HVGTVINEQN KLVAAGRGVP GAQRIPLESL MISNPYSDPL SYYRWFLHQR CYNTDLYNST
TCTELYKVVP QCLEEVEFAL ENPLVPNKLA ALKTCDVLRE GDMHGRAQEN VKLECDGSVE
DCLPMFTWIS SFFNNATHKA ALGVPEDLSF QSLSNDVYLD FRRSGDLLQP VHLLYEPLLE
DGIRVLHYVG MLDCNCGWPA TFSFLKLLKT HFQNDFIAAS DVPWPTTDIA TVRAIGAGAG
NMTFVLMAEA GHMVTLDQPA LVKSIVERWV TNTPWFE
//
