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Database: UniProt
Entry: A0A0V1LFN4_9BILA
LinkDB: A0A0V1LFN4_9BILA
Original site: A0A0V1LFN4_9BILA 
ID   A0A0V1LFN4_9BILA        Unreviewed;      1050 AA.
AC   A0A0V1LFN4;
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:KRZ58320.1};
GN   ORFNames=T02_14321 {ECO:0000313|EMBL:KRZ58320.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ58320.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ58320.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ58320.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-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:KRZ58320.1}.
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DR   EMBL; JYDW01000059; KRZ58320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1LFN4; -.
DR   STRING; 6335.A0A0V1LFN4; -.
DR   Proteomes; UP000054721; 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:KRZ58320.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000313|EMBL:KRZ58320.1};
KW   Protease {ECO:0000313|EMBL:KRZ58320.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT   DOMAIN          760..916
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
FT   REGION          1026..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1050 AA;  120431 MW;  B7469C4C50D8387B CRC64;
     MANAVELCRK LCQQHTIGVN KDAEEWSHLA KQLHTKCSVD ANDKSVQELW DNFENIDETL
     LLNFLLCFEH CRNSEAIVWF TKILQQFISR PSADPKSRLQ LMAKLNGVSF LCKCLRWFVR
     KFDETDEMIE VIQALIPIIQ IVGGVDGRFF MKVRFLGLLD MCINVMCNTA QYPLTESLLD
     FLAFACRSGQ NASALVKNEM MVPFLKKIFA GCEKTTPSVI RKYAELLFLM AKPKKTRKSL
     VSQGIIPSVL ELFRAFFGKD DNISQINCNA ALGTLRLLTS TISGRQNLVA CNGLEIFRDL
     IRSFDESEAS SPLCSHMYHS ISSLCIRCLP MRPLPIDNMK YPVDVSIVEI QHSTPDPPEA
     VSDSEDDISV AAGFLTDTDD EAMSRASQSE KPPIPLRIFQ KETHWYRFLT RELDYGTLLS
     KDGTFGNVSA KQTDNMLFEM ADLENFMLEI NQRQRRRSIS SLREIRLSGK HRSITEQLLE
     KSQSGMPTWY HWIDYCCQAV STRSVIPFES LGYPDMHGCY PNLPQQKLKC YPNALLNMVG
     HLLERLESNK DYIPKVVYDL DQLVATRRTY NTSKFILNND IVKLGRSNPN TTSLQFESRF
     EGGNLRKVGP YEYDLILTPD TNQMNEYYHT YYFQVSNMLT EISYTLNIIN CVKTRSLYNS
     GMQPLVFSVT EALLGRPGWV RIGGNCVYYR NFYSRGSSST AAKSSETVTS YYTASFNVHF
     RHRYDICYFA YHYPYTYTML KTHLVKTNQL LSLKKDIHFR TDVMCHTLSG NPVILVTVTE
     LGDRIQLKSR DIVVLSARIH PGESNSSWMM HGMINYLISD HPFAKLARSK FIFKLIPMLN
     VDGVINGNHR CSLAGKDLNR QWVAPERSMY PSIYHTKNLI SYLHRIGRTP FVKFVYCDFH
     GHSRKMNVFL YGNNPNLSWY TGDRLQKHGF EFYQFPEILD ETSTAFELKY CAFTIKKNKE
     GSARVAIWRD TGISRAYTLE ASYAGFDTGG YKGHQITTRD LIEMGEQFVE SLVRLKKSIE
     QGKSPTRRFE IGAEQKETET EKKKNSVAVE
//
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