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Database: UniProt
Entry: A0A162YSU4_DIDRA
LinkDB: A0A162YSU4_DIDRA
Original site: A0A162YSU4_DIDRA 
ID   A0A162YSU4_DIDRA        Unreviewed;       543 AA.
AC   A0A162YSU4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-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=EKO05_0001135 {ECO:0000313|EMBL:UPX10477.1}, EKO05_001132
GN   {ECO:0000313|EMBL:KAF9711623.1}, ST47_g8679
GN   {ECO:0000313|EMBL:KZM20207.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM20207.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM20207.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM20207.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
RN   [2] {ECO:0000313|EMBL:KAF9711623.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9711623.1};
RA   Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF9711623.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9711623.1};
RX   PubMed=32345704; DOI=10.1534/g3.120.401265;
RA   Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA   Debler J.W., Oliver R.P., Lee R.C.;
RT   "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT   ArME14.";
RL   G3 (Bethesda) 10:2131-2140(2020).
RN   [4] {ECO:0000313|EMBL:KAF9711623.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9711623.1};
RA   Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA   Debler J.W., Oliver R.P., Lee R.C.;
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:UPX10477.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:UPX10477.1};
RA   Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL   Submitted (MAR-2022) 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; RYYQ01000003; KAF9711623.1; -; Genomic_DNA.
DR   EMBL; JYNV01000284; KZM20207.1; -; Genomic_DNA.
DR   EMBL; CP095289; UPX10477.1; -; Genomic_DNA.
DR   STRING; 5454.A0A162YSU4; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
DR   Proteomes; UP000617380; Chromosome 2.
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:UP000076837};
KW   Signal {ECO:0000256|RuleBase:RU361156}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT   CHAIN           19..543
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT                   /id="PRO_5041471636"
SQ   SEQUENCE   543 AA;  60083 MW;  81EB53D4B56437B9 CRC64;
     MKLLNLVSGL LCASSALAFK RPTKHSLPRS VVEKRVANQP FSHPEIQKRA SRFLTNKTEA
     FAVNGSGIPE VPFDIGESYA GLLPISDSPD ETRKLFFWFF PSTAEQTPEH VTIWLNGGPG
     CSSLSGFLTE NGPFTWEAGT LAPVQNPYAW TNLTNMLWVE QPVGVGYSQG IPNITNEVEL
     AAEFRGFYKS FVDTFQTKHW KTYITGESYA GFYVPYIADG FISANDTEYF NLAGISINDP
     IIGDSTIQQQ VVILPFAELW QNLFYLNETF LEQVRDLQVH CNYSSYLDTY FKFPPPQGPF
     PLLPNPYTQA GECDMFDTFT DAISEINPCF NIYHVTETCP HPYSQLGIVN GGDYSPPGAV
     IYFNRTDVKE ALHAPVDTNW QQCTDKNVFG NGDIFSYASD TSVGPANSGA LQRVIEFTNN
     TIIGSGDLDM ILCTNGTLLA IQNMTWNGAQ GLSEYPATPL YAPYHPEYND GALAGAGFQG
     VWTAERGLTF YTARLAGHEL PGYTPGVAYR MLEILIGKVK DFSSTESFTT QTGNYSGEVP
     LYR
//
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