ID A0A178E6M4_9PLEO Unreviewed; 558 AA.
AC A0A178E6M4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=IQ07DRAFT_586014 {ECO:0000313|EMBL:OAL51646.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL51646.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL51646.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL51646.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR EMBL; KV441642; OAL51646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178E6M4; -.
DR STRING; 765867.A0A178E6M4; -.
DR InParanoid; A0A178E6M4; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000077535; 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; 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; 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:UP000077535};
KW Signal {ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 19..558
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5007949623"
SQ SEQUENCE 558 AA; 62004 MW; 384EF63F6E4BD40F CRC64;
MKLSTIFGTL ICASSALAGN SPHKLNVFNK VKPVLEKRVA SEPFRHPELQ KRASSFLTDK
SKPFAVNGTG IPEVPFDIGE SYAGLLPISD SPDETRKLFF WFFPSTLSTT PEEVVIWLNG
GPGCSSLSGF LTENGPFTWE SGTLAPVQNP YSWNNLTNVL WVEQPVGVGY SQGTPNITDE
VELAAEFRGF YKSFVDLFEL YHWKTYVTGE SYAGYYVPYI ADGFIQANDN KYFNLAGISI
NDPIIGDETI QQQVVILPYV EFWQNFLYLN DSFMETIRQH QKDCGYSEYY EKYFTFPPPK
GPFPVLPDPF STDNYTCDQF DNFYSAILEV NPCFNIYHIS ETCPHPYSQL GIVNTGDYSP
PGAEIYFNRT DVKVALHADV NSNWLQCTNI NVFGNGNASS NAQDASVGPA NNGVLQRVIE
YTNNTIIGSG DLDMLLSTNG TLFAIQNMTW NGAQGLQEYP ATPLYAPYHP EYNLGALAGA
GFQGVWSQER GLLFYTARLA GHELPGYTPG VALRMLEILL GHVEDFSSTE NFVTQSGNFT
GNGTIYKRGV IDMDQSFA
//
