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Database: UniProt
Entry: A0A091DDL8_FUKDA
LinkDB: A0A091DDL8_FUKDA
Original site: A0A091DDL8_FUKDA 
ID   A0A091DDL8_FUKDA        Unreviewed;       381 AA.
AC   A0A091DDL8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Cytosolic carboxypeptidase 6 {ECO:0000313|EMBL:KFO20911.1};
GN   ORFNames=H920_17704 {ECO:0000313|EMBL:KFO20911.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO20911.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO20911.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO20911.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) 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}.
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DR   EMBL; KN124514; KFO20911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091DDL8; -.
DR   STRING; 885580.ENSFDAP00000020414; -.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
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; cd06908; M14_AGBL4_like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF9; CYTOSOLIC CARBOXYPEPTIDASE 6; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KFO20911.1};
KW   Hydrolase {ECO:0000313|EMBL:KFO20911.1};
KW   Protease {ECO:0000313|EMBL:KFO20911.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT   DOMAIN          65..203
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
FT   REGION          343..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  43633 MW;  201D6AE922774169 CRC64;
     MNHMHTYYSS LYLKRRLDLH LSIRFFPTFI ADLFLHIDYE VLKIVLIIDS VLFPHSCGNA
     ENLREGAEQK VIFITGRVHP GETPSSFVCQ GIIDFLVSHH PIACILREHL VFKIAPMLNP
     DGVYLGNYRC SLMGFDLNRH WLDPSPWAHP TLHGVKQLIV QMYNDPKTSL EFYIDIHAHS
     TMMNGFMYGN IFEDEERFQR QAIFPKLLCQ NAEDFSYSST SFNRDAVKAG TGRRFLGGLL
     DHTSYCYTLE VSFYSYIIGG TTAAVPYTEE ACILDRFPPA LDQPGVPKPD RDLRDMKLGR
     NVARTFLDYY RLNPLVEKVA LPMPRLRFWV VVPFCEAHDD LGKEKPPPYK HPLLRGPASN
     HPNGKGDKKS SVNHKDPSNP F
//
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