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Database: UniProt
Entry: A0A0V1HDS1_9BILA
LinkDB: A0A0V1HDS1_9BILA
Original site: A0A0V1HDS1_9BILA 
ID   A0A0V1HDS1_9BILA        Unreviewed;      1034 AA.
AC   A0A0V1HDS1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=tubulin-glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00026108};
DE            EC=3.4.17.24 {ECO:0000256|ARBA:ARBA00026108};
GN   Name=AGTPBP1 {ECO:0000313|EMBL:KRZ08721.1};
GN   ORFNames=T11_2707 {ECO:0000313|EMBL:KRZ08721.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ08721.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ08721.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ08721.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] +
CC         H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-
CC         glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-
CC         COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555,
CC         ChEBI:CHEBI:149556; EC=3.4.17.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00024524};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC         Evidence={ECO:0000256|ARBA:ARBA00024524};
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:KRZ08721.1}.
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DR   EMBL; JYDP01000082; KRZ08721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1HDS1; -.
DR   Proteomes; UP000055024; 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; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF11; CYTOSOLIC CARBOXYPEPTIDASE 1; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KRZ08721.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000313|EMBL:KRZ08721.1};
KW   Protease {ECO:0000313|EMBL:KRZ08721.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT   DOMAIN          760..980
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
SQ   SEQUENCE   1034 AA;  118458 MW;  3D41EC6207BE179D CRC64;
     MVNAVDLCRK LCQQHTIGVN KDAEEWSHLA QQLHTKCSAD ANDKSVQELW DNFENIDETL
     LLNFLLCFEH CRNSEAIVWF TRILHQFISR PSADPKSRLQ LMAKLNGVSF LCKCLRWFLQ
     KFDETDEMVN VIQALIPVIQ IVGSVDGRFF MKVRFVGLLD ICINVMCNVA QYPLTESLLD
     FLTFACRSGQ NASALVKNEM MVPFLKKVFA ECEMTTPAVI RKYAELLFLM AKPKKTRKSL
     VSQGIIPSVL ELFQAFFGKD DDTSQINCNA ALGTLRLLTS TISGRQNLVA CNGLEIFRDL
     IRSFDESEAS SPLCSHMYHS ISSLCIRCLP MRPLPIENMK YPVDVSIVEI QHSTPDPPEA
     VSDSEDDIFV AAGFLTDTDD EAISHASQNE KPPIPLRMFQ KETHWYRFLT RELDYGTLLS
     KDSTFGNVLA KQTDNMLSEM ADLENFMLET NQRQRRKSIS SLREIRLSGK HRSITEQLLE
     KSQSGLPTWY HWIDYICQAV STRSVIPFET LGYPDIHGCY PNLPQQKLKC YPNALLNMVG
     HLLERLESNK DYIPKVVYDL DQLVTTRRTY DGSKFILNND IVKLGSSNPD TTSLQFESRF
     EGGNLRKVGP YEYDLILTPD TNQMNEHYHT YYFQVSNMLT EISYTLNIIN CVKTRSLYNS
     GMQPLVFSVT EALLGRPGWV RIGGNCVYYR NFYSRASSST PAKSSETVTS YYTASFNVHF
     RHRYDICYFA YHYPYTYTML KTHLVKTNQL LSLKKDIHFR TDVMCHTLSG NPVILVTVTE
     LGDRIQLKSR DIVVLSARIH PGESNASWMM HGMINYLISD HPFAKLARSK FIFKLIPMLN
     VDGVINGNHR CSLAGKDLNR QWVAPERSVY PSIYHTKNLI SYLHRIGRTP FVYCDFHGHS
     RKMNVFVYGN NPNLSWYSGD RLQKHGFEFY QFPEILDETS TAFELKYCAF TIKKNKEGSA
     RVAVWRDTGI SRAYTLEASY AGFDSGGYKG HQITTRDLIE MGEQFVESLV HLKKNVEQGK
     SPTRRFEIGA KQKE
//
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