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Database: UniProt
Entry: A0A195BPK7_9HYME
LinkDB: A0A195BPK7_9HYME
Original site: A0A195BPK7_9HYME 
ID   A0A195BPK7_9HYME        Unreviewed;      1063 AA.
AC   A0A195BPK7;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=tubulin-glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00026108};
DE            EC=3.4.17.24 {ECO:0000256|ARBA:ARBA00026108};
GN   ORFNames=ALC53_02935 {ECO:0000313|EMBL:KYM88452.1};
OS   Atta colombica.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM88452.1, ECO:0000313|Proteomes:UP000078540};
RN   [1] {ECO:0000313|EMBL:KYM88452.1, ECO:0000313|Proteomes:UP000078540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM88452.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYM88452.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Atta colombica WGS genome.";
RL   Submitted (SEP-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}.
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DR   EMBL; KQ976424; KYM88452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A195BPK7; -.
DR   STRING; 520822.A0A195BPK7; -.
DR   Proteomes; UP000078540; 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; IPR040626; Pepdidase_M14_N.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF11; CYTOSOLIC CARBOXYPEPTIDASE 1; 1.
DR   Pfam; PF18027; Pepdidase_M14_N; 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:KYM88452.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000313|EMBL:KYM88452.1};
KW   Protease {ECO:0000313|EMBL:KYM88452.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078540}.
FT   DOMAIN          635..762
FT                   /note="Cytosolic carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18027"
FT   DOMAIN          792..894
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
SQ   SEQUENCE   1063 AA;  120962 MW;  31B7A81F9937D316 CRC64;
     MSANNKNADE VVSDALLEKL RTYAAKPQEA GDALRTIVAK IHMRITSSDR RIRERTLEKL
     WLKNSGAMES FIMTLENCKD YVANCSIAGI LHECISPRMI KGKSKERGSK NRSATRTSNR
     MAVIQLINLG ITQVLVKLLI NLQYADSIMI EVLTQDILWI LGQVAQRDQK FVSKMKLLNS
     IKVFHALLKQ HYNNSKTLLP LLLIIKTLAK NSFSLQTLVK DDITSTLEKT FISVGYTPHL
     KLRTLLECFK HLTTNKLCCN KFIKTRIVHL LMRIFERWER FDGQMRLKIC NYALNTLQHF
     CVIKAGRKAI KSNNGLQLLY RFCTSCPEDK AYDCLLSRIY GIINQCLDKK ELPVPEMSPA
     RFILSEVNVR ANSAESGSDI DSQANSVASI GRRYSDLDSG DDEESHDSRD TMDNEIHLGD
     EVDENKFFAG VFTSQRSEED LAGYHMFFKE LGNLQSQLHI VGSTNGKLID LYLMDAEQIN
     SPLAKAGKTK ISIKDFSKSN GTMKSCQLVN STHNLKILKD VSANVTDRQA YCVVASRVRS
     VIGFVKVAYP DLIGGDGLGK AEPLNTKDRK VCRAKLLTCV ERGLHAATTF QEVVYDLDAL
     ANSVSRGTSD DEWLFDNRDE KRIGKRNVDM KRLQFESRFE SGNLRKAIQI GPREYDLILT
     PDVNSGSRHQ WFYFEVSNME ATAYTFNIIN CEKTNSQFNF GMKPILFSVT EAQCGRPGWV
     RTGVDICYYR NCYQRSIKGK TYFTTSFTVM FPHAYDVCYL AYHFPYTYSR LMTNIWNWTK
     SVSVANVYFR AETLCETLND NENPVLTITS PDSKTNPIHT RKMIFLTSRV HPGESNASWV
     MHGTMEALLS DNQYANSLRD DYVFKIIPML NIEGVVNGCN RYGLTNEDLN RRWSNPNRMY
     HPVIYHTKGL MEYCARVLQR PPHVFVDYHG HSRRKNVFLF GCSRSGSWSA ADRAKPDQSV
     QYLMLPHLMQ RTSSAFALPL CSFKVERNKE STARVAVWRQ LGVPRSYTME SSFCGCDQGV
     LAGLHLDTEH LKAIGRDFCQ ALSMMKDGGS DWAIGKYVQI FCY
//
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