ID A0A2U9BWS1_SCOMX Unreviewed; 1011 AA.
AC A0A2U9BWS1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=tubulin-glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00026108};
DE EC=3.4.17.24 {ECO:0000256|ARBA:ARBA00026108};
GN ORFNames=SMAX5B_018840 {ECO:0000313|EMBL:AWP07806.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP07806.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP07806.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; CP026252; AWP07806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BWS1; -.
DR STRING; 52904.ENSSMAP00000030684; -.
DR Proteomes; UP000246464; Chromosome 10.
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 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:SF5; CYTOSOLIC CARBOXYPEPTIDASE 4; 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:AWP07806.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|EMBL:AWP07806.1};
KW Protease {ECO:0000313|EMBL:AWP07806.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1011
FT /note="tubulin-glutamate carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016004008"
FT DOMAIN 460..589
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 619..725
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 174..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 113774 MW; A4366A366C005D3B CRC64;
MTAACLWVIQ VFSSSVSTAN LIGENHGLDV IFCLIPQYTT KHLHTIKAAI NTFAALLCTK
TNVCSVVSKG YISGLLRLYE DWYSKDTQHA AIEIRHTLLR CLHKVTHSTA GRQAVISQGG
LRLLYHTTQT DLLCKGLESL IDPSVQLMRK CLPKTPLPLT SDLSAYTFPL PGRAHAVPDV
ATDESREESD DEETEKNQEA PSTDYDDDLE TDLNKLCLRP DPDRPKDLLP QYGRLCPEHS
HDFTELDLSS EPEESSPSPL SSDEEAVLLN SLSLHSSRMD RRKTNSSNDL SNSSSGSQSQ
TETSTEGNTP ATAQFVAGDF QSHSSILVKE ARGEAPSILR GNEQDIEEEG TEEFHHCTMI
DSLLKRHGAC ILHHEPKLYR AAAAKTKSIP GFSILAFPDF WGHLHPPGHE PMAPRKPNIQ
REKVFEDVQR FLNTHDIINQ VVYDLEGSSL QCLSDSLRFF SNFECGNLRK AVQIRRYEYD
LILNADTNCS QHAQWFYFEV SNMVADVPYR FNVINCEKSN SQFNYGMQPV LFSVREALEG
RPHWVRTGTE ICYFRNHFCP AQGRCRTTFY TLTFTITFKH NEDVCYLAYH YPYTYSALKA
HLKVLQKSVD PAKCFFRQQI LCKSLAGNSC PVVTITASPA SRAWKDMLQL RNRPCIVLTA
RVHPGESNAS WVMKGTLEFL CSSDLVAQSL REAFVFKIIP MLNPDGVING MNRCDLNSED
LNRQWCKPDP VLSPTIYHTK GLLYYLNSIG RTPLVFCDYH GHSRKKNVFL YGCSVKETLW
QSGSAVDTVG LKENPGYRTI PKTLDRIAPA FSFNSCNYLV EKSRSATARV VVWREMGVLR
SYTMESTYNG CDQGIYKGLQ TGTRELQDMG LKFCHSLLSV TKDLKDLYSR RLIDLDYNIL
DHKSHNFFED DEPPCVEEIE YSTDCPKLKG TDLDSDINTN IANVDEEEDG GGSEDGHSGA
KQWQGSIGKS QQSSMKSCLF PHPIRQAAME KLSEKRDKCQ GVTIVNGQIT S
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