ID R7TRE8_CAPTE Unreviewed; 1273 AA.
AC R7TRE8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=tubulin-glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00026108};
DE EC=3.4.17.24 {ECO:0000256|ARBA:ARBA00026108};
GN ORFNames=CAPTEDRAFT_228599 {ECO:0000313|EMBL:ELT96483.1};
OS Capitella teleta (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Capitellidae; Capitella.
OX NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT96483.1};
RN [1] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELT96483.1, ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT96483.1,
RC ECO:0000313|Proteomes:UP000014760};
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:CapteP228599}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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; AMQN01002247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB308810; ELT96483.1; -; Genomic_DNA.
DR AlphaFoldDB; R7TRE8; -.
DR STRING; 283909.R7TRE8; -.
DR EnsemblMetazoa; CapteT228599; CapteP228599; CapteG228599.
DR HOGENOM; CLU_007391_0_0_1; -.
DR OMA; LEYNMPS; -.
DR Proteomes; UP000014760; 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 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: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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000014760}.
FT DOMAIN 728..824
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 889..998
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 353..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..569
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..607
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 144158 MW; D549FFAE6EDEBBA7 CRC64;
MERQSRLMSF FQSLDRILSQ KNGAKTTQEE VQQIRCLSSK ILQHVSSSQD KIHRDIIAKN
VGYIDLLLTV LATSRDGCTT QNIVYILSEV VGKTNTGKRA SCLVAQGASH VLLQLIVYES
KESQVSEELL FSVHQVLSKI GPKDRKFGVK ARLSGALSVT LNLVKNLTNL KILHPVVHVL
KLYAINSVNA SYLGKNGAIS HLFKLLALSN RKYVTLSKYA LDTMVQLVKS KSNSARAIGQ
GGVPLLLTMY ADWHRVDTKN RHVNIRKAIL STLKHITNLR SGRRALIEAD GVSLLYSFCQ
EVADSRELET LVFMASIIMR KCFPRNRLPL VSLRSVVGFS LPQSEFHVVD AGEGQADENG
GYESSVDNDD DVSSEEDIDA RRAESDDENE NENSKLPPCE RSSDDLNMYA EFFSEQSEFN
SILEEEASYG IEDTIILPST FEYSSLDTRC SGLRSSQSAN SLLKKPSNRS LSPLIRISDG
QRLTESISDL KIVGSSSSFD DGKELRRPNL NSNPKRRSEG DLRPLMAPNA LRSAEKVEIS
PKSTKKPLHS KNSPKAKRRG SKTKSVKEKR EKKPRSGNHP VVHKIISEDY DSLADENSEE
DAGEDMEGND PPPSPAAPVV NAAEYAKIAA LTRSVGRFNK IAYPELKGSA SPPFKEAFYE
KRFGTQRQKI FEDIDRFINP EKPLDRVVYD LDSIVSTAGS TYTSAYSTHS NDDEERVRNR
SYCEHLGFNS QFESGNLRKA IQVRQYEYDL ILNPDVNTNH HHQWFYFEVS QMEAGVRYRF
NIVNCEKVNS QFNFGMRPVV YSVVEAMNGR PHWLRSGSEI CYYKNHFVRS SQTTGGVRGK
VYFTGTFTMT FKHERDVCYI AYHYPYPYTT MMYHLQDVEK NYDSSQIFYK RQKLTQTLAG
NDVPVLTITS HPHTYDKKGI QQLKNRSYIY LSSRVHPGES NASWVMRGTI NFLMSDKPSA
QALRDMYIFK IVPMLNPDGV INGNHRCSLT AEDLNRRWLH PCPHLHPTIF HSKGLLQYLN
LINRSPLVFC DYHGHSRRKN VFLYGCSPSL SWMTNDFNNP AVVGNRMEDQ GYKTLPKILQ
TLAPAFSFSN CNFVVEKSKE STARVVVWRE CGVMRSYTME STYCGCDQGN YKGYHINTRQ
HEEMGRRFCE ALARVRSRHY QKPLLPLTIT ADLLTSTGSD MQEPPVLTEN SSTKDDEQEE
TEIPVFKKRA KLLIFLSVAI RVEEGATCVE SVMVEPLALQ SNTSSSADNE EEDEEEVEEE
EEEEELNEEF LSN
//
