ID A0A7U2I271_PHANO Unreviewed; 665 AA. AC A0A7U2I271; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 24-JUL-2024, entry version 12. DE RecName: Full=Carboxypeptidase {ECO:0008006|Google:ProtNLM}; GN ORFNames=JI435_064330 {ECO:0000313|EMBL:QRC99089.1}; OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume OS blotch fungus) (Parastagonospora nodorum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae; OC Parastagonospora. OX NCBI_TaxID=321614 {ECO:0000313|EMBL:QRC99089.1, ECO:0000313|Proteomes:UP000663193}; RN [1] {ECO:0000313|Proteomes:UP000663193} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173) RC {ECO:0000313|Proteomes:UP000663193}; RX PubMed=25379341; DOI=10.1186/s12864-021-07699-8; RA Bertazzoni S., Jones D.A.B., Phan H.T., Tan K.-C., Hane J.K.; RT "Chromosome-level genome assembly and manually-curated proteome of model RT necrotroph Parastagonospora nodorum Sn15 reveals a genome-wide trove of RT candidate effector homologs, and redundancy of virulence-related functions RT within an accessory chromosome."; RL BMC Genomics 22:382-382(2021). 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; CP069031; QRC99089.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7U2I271; -. DR VEuPathDB; FungiDB:JI435_064330; -. DR Proteomes; UP000663193; Chromosome 9. DR GO; GO:0000324; C:fungal-type vacuole; IEA:TreeGrafter. DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro. 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 PANTHER; PTHR11802:SF189; 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. PE 3: Inferred from homology; KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Reference proteome {ECO:0000313|Proteomes:UP000663193}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..665 FT /note="Carboxypeptidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5030900932" FT REGION 174..193 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 665 AA; 73033 MW; C5503B0DF4649DB1 CRC64; MFSVVSSAAV VLLALAKPGV AQFPAAPEGR TVLESRFGEG VTITYKENNL CETKPGVKSY AGHVYLPPGT ADLGQGQDYP INSFFWFFEA RNDPKNAPLT IWLNGGPGSS SMHGLFTEHG PCQVNADSNS TRPADWSWNE NVNMLYFDQP VQVGFSYDTL QNITRDLVSG RVTSLDETTP VPEQNSTFLT GTFPSRNPNN TAFGSVNGAV ASWHFLQSWF QEFPHYLPND TRISLAAQSY GGRYGPAMMS FWEEQNQRIE NGTWDGSDGE QFILHLDTLM IVSGCIDRKI QYPYYPQQAF RENGFGIEAV NETIYNGMVA SIPECLERIQ KCRDAAAISD PENLGIDAGV NAVCEDAETW CRSNIVSPYT SNSGLDYYDI STQSPPSFPA GFHQGFLNRE WVQAELGVPL NWTGSSPQAS NAYRDIGDYP RDSWLEDLGF LLDNGIKVSL VYGDLDFACP WAGGDAVAKA IPWSGSNAYA SAQYAEIQTN DSYVGGLVRQ HGNLSYIRTY QAGHSIPSYQ PETAYKVFTR ALFNLDIATG TKPTGAGANY TTTGRAVPDV QLEPNMGGLS YCYTYAASSC RSWQVDMIRN GSAEICNWLF VDANSTQLFP EEIAKCRADW AGGNKTVTRR VDSRPVFTGD AVARRGSWLL VVLEVVVLGV LGRLL //