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Database: UniProt
Entry: A0A3Q0G1F5_ALLSI
LinkDB: A0A3Q0G1F5_ALLSI
Original site: A0A3Q0G1F5_ALLSI 
ID   A0A3Q0G1F5_ALLSI        Unreviewed;      1221 AA.
AC   A0A3Q0G1F5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Cytosolic carboxypeptidase 1 {ECO:0000256|ARBA:ARBA00041044};
DE            EC=3.4.17.24 {ECO:0000256|ARBA:ARBA00026108};
DE   AltName: Full=ATP/GTP-binding protein 1 {ECO:0000256|ARBA:ARBA00043070};
DE   AltName: Full=Protein deglutamylase CCP1 {ECO:0000256|ARBA:ARBA00043068};
GN   Name=AGTPBP1 {ECO:0000313|RefSeq:XP_025053479.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025053479.1};
RN   [1] {ECO:0000313|RefSeq:XP_025053479.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O
CC         = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-
CC         glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-
CC         COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623;
CC         Evidence={ECO:0000256|ARBA:ARBA00029302};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC         Evidence={ECO:0000256|ARBA:ARBA00029302};
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   RefSeq; XP_025053479.1; XM_025197694.1.
DR   AlphaFoldDB; A0A3Q0G1F5; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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   CDD; cd06906; M14_Nna1; 1.
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; IPR033852; CBPC1/4.
DR   InterPro; IPR040626; Pepdidase_M14_N.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF24; 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|RefSeq:XP_025053479.1};
KW   Hydrolase {ECO:0000313|RefSeq:XP_025053479.1};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Protease {ECO:0000313|RefSeq:XP_025053479.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT   DOMAIN          718..807
FT                   /note="Cytosolic carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18027"
FT   DOMAIN          886..990
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
FT   REGION          371..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..393
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1221 AA;  137167 MW;  24D0E5AB60AC989D CRC64;
     MNKVKTTSEK SLASNSRIVV LLTQLEKINS ESLLVEADTA RYVTSKILHL AQSQEKTRKE
     MTAKGSTGVE VILSTLENTR DLQTTLNILS ILIELVSVGG GRRACILVSK GGTQILLQLL
     LGASKDSPPN EELMVQLHSL LAKIGPKGNH SRDKKFGVKA RINGALNISL NLVKQNLQNH
     RLILPCLQVL RVYSTNSVNA VSLGKNGVVE LMFKIIGPFS KKNTGLMKVA LDTLAALLKS
     KTNARRAVDR GYVQVLLTIY VDWHRHDSRH RHMLIRKGIL QCIKSVTNIK LGRKAFIDAN
     GMKILYNTSQ DCLAVRTLDP LVNTSSLIMR KCFPKNRLPL PTIKSAFHFQ LPVIPTSGPV
     AQLYSLPPEV DDVVDESDDN DDIETETETE NENEDDKDQH FKNDDIETDI DKLKPKQELG
     RPIEELKIYE QFFPELAENF QEYDLVSKEP KPFASATNLG GPIVVPTAGE EHPAEANQSV
     KGIAVKDHSS LQMEEYNKRP SFLDLPKKDH NKDSLQLQND QKKLLSSCQC LSQEIVKGLD
     RITLQNTSKS EQYYSTGCLI KKESKTSLTT PACNKPCQHV SSCGSGLFEG PSVQLGKLCC
     TGVDPDEEED SSSHSSGEQV LLEVPDMLPL HNPDLYIEIV KNTKSVPEYS EVAYPDYFGH
     IPPPFKEPIL ERPYGVQRTK IAQDIERLIH QNDIVDRVIY DLDNSSCSVP EEGDILKFNS
     KFESGNLRKV IQIRKNEYDL ILNSDINSNH YHQWFYFEVS GMKTGIGYRF NIINCEKSNS
     QFNYGMQPLM YSVQEALNAR PWWGRVGTDI CYYKNHFSRS SIAAGGQKGK SYYTITFTVS
     FPHKDDVCYF AYHYPYTYST LKMHLQKLES MHNPQQIYFR EDVLCETLAG NSCPLVTITA
     MPESNYYEHV CQFRNRPYVF LSARVHPGET NASWVMKGTL EYLMSSSPAA QSLRESYIFK
     IVPMLNPDGV INGNHRCSLS GEDLNRQWQN PNLDLHPTIY HAKGLLQYMA TIKRLPLVFC
     DYHGHSRKKN VFMYGCSIKE TMWHTDVSAA SCDVIEDLGY RALPKILSQT APAFCMSSCS
     FVVEKSKEST ARVVVWREIG VQRSYTMEST LCGCDQGKYK GLQIGTRELE EMGAKFCVGL
     LRLKRLTSPL EHNLPSSLLD IENELIESSC KVTSFSPHSS LMGKCPPTFG ICRQSSAVSG
     GCKSDPCPST QADRLSVFNK C
//
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