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Database: UniProt
Entry: A0A250WRS9_9CHLO
LinkDB: A0A250WRS9_9CHLO
Original site: A0A250WRS9_9CHLO 
ID   A0A250WRS9_9CHLO        Unreviewed;      1015 AA.
AC   A0A250WRS9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CEUSTIGMA_g1008.t1 {ECO:0000313|EMBL:GAX73557.1};
OS   Chlamydomonas eustigma.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX73557.1, ECO:0000313|Proteomes:UP000232323};
RN   [1] {ECO:0000313|EMBL:GAX73557.1, ECO:0000313|Proteomes:UP000232323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX73557.1,
RC   ECO:0000313|Proteomes:UP000232323};
RA   Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA   Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT   "Acidophilic green algal genome provides insights into adaptation to an
RT   acidic environment.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAX73557.1}.
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DR   EMBL; BEGY01000004; GAX73557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A250WRS9; -.
DR   STRING; 1157962.A0A250WRS9; -.
DR   OrthoDB; 168164at2759; -.
DR   Proteomes; UP000232323; Unassembled WGS sequence.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.60.40.3120; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR040626; Pepdidase_M14_N.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF9; CYTOSOLIC CARBOXYPEPTIDASE 6; 1.
DR   Pfam; PF18027; Pepdidase_M14_N; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000232323}.
FT   DOMAIN          185..273
FT                   /note="Cytosolic carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18027"
FT   DOMAIN          461..537
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
FT   REGION          140..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          713..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          927..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1015 AA;  109266 MW;  11ADA1566B02B391 CRC64;
     MSMSDVSVAT SSDSEGEEPK VYVKNDTDHA GEHNFQDYST KPKAQVVDRK LDILTECSTE
     AEAVRSHYQL QPRIYIDARS PILMADPTIE SVNDKASAAS VALVPGRNLA ASLPSTSVHG
     HASWAEEYCF KKQGFAIRHV SDTPTPTTPS SLLRSRSSRQ AEPSNTRRSL PCQQLPPPTG
     QLVFDGSFEG GNISAIQRSE DGSEYEVILR SDSLNSRYRL WFHFTATNAL PGQQVLFSIV
     NFSKGRSLFR HGMSPVVRSA KRPSWHRVPA KNTYYYKSAK HSNRYVLSFA FVFDQGNDKY
     EFAYSFPFTY TSLQYELGYL EFIGSPCMRR QLIARTPQLR RVDAVIISQP LLPCPLEGIG
     MEDSDSHPLH STHQRINTLN LTQLTSSLST TTYPVPPSTS YSRSVSFQGL RGQSAGSDTS
     FGTSGQRSSN RAAAAGMGAG TPRGPSPSLY SGVTNNGWSV GGGKRPVVFI TSRVHPGETP
     ASYVAQGLLA FLLGSDLRAA SLRSAITWVV VPMLNPDGVF LGNYRTDAGG VDLNRMWLTP
     AAPTMPALHH SLRLLKAYHD HPSFQVDFFI DIHAHSTSRR SFMFCNKPPS SSPAWMPPAN
     LYMDPTERVT RLPKIMSNLC PSFSLQHCLA EDSAVKASCA RRVAATVASH ALCYTLEVSF
     FHNTEVTVLT QPGDASNVDF SNTIEGYMDM GKSLALSFFE YYGLTVPAHM PSQVLQPSPQ
     QPQQAPNAVS SSSTSAASFR ACTPPRHSPV SSRSTVHIPN TSRSPSMPGP ASEADPADEP
     PTSQDRMSPN DQSLELSSKP DSRSSLGIRG PSSAQAPVAP PAVTVRQPAA SSVLRFPFNP
     NIENPVAFPS RGQRSLESSR PSMVLMRRYN SLAGMSKEVA PVKAAYGEPA AAAAGTPLML
     VISGKSGGTP STIKLLGNGQ VAGGQAAASS SSTQLSGEPL MSEGHPVPAY ASTQQGSSVN
     AALAGLNARR SEDVKQQPIS APGIAASSTT YALQLGGRIK SAAVHSKRFI APQNR
//
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