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Database: UniProt
Entry: A0A1D2NME3_ORCCI
LinkDB: A0A1D2NME3_ORCCI
Original site: A0A1D2NME3_ORCCI 
ID   A0A1D2NME3_ORCCI        Unreviewed;      1265 AA.
AC   A0A1D2NME3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Cytosolic carboxypeptidase-like protein 5 {ECO:0000256|ARBA:ARBA00024141};
DE            EC=3.4.17.24 {ECO:0000256|ARBA:ARBA00026108};
DE   AltName: Full=ATP/GTP-binding protein-like 5 {ECO:0000256|ARBA:ARBA00032928};
DE   AltName: Full=Protein deglutamylase CCP5 {ECO:0000256|ARBA:ARBA00032753};
GN   ORFNames=Ocin01_00278 {ECO:0000313|EMBL:ODN06407.1};
OS   Orchesella cincta (Springtail) (Podura cincta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX   NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN06407.1, ECO:0000313|Proteomes:UP000094527};
RN   [1] {ECO:0000313|EMBL:ODN06407.1, ECO:0000313|Proteomes:UP000094527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Mixed pool {ECO:0000313|EMBL:ODN06407.1};
RX   PubMed=27289101; DOI=10.1093/gbe/evw134;
RA   Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA   Smit S., van Straalen N.M., Roelofs D.;
RT   "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT   in the Genome of the Collembolan Orchesella cincta.";
RL   Genome Biol. Evol. 8:2106-2117(2016).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + H2O = C-
CC         terminal L-alpha-aminoacyl-[tubulin] + L-glutamate;
CC         Xref=Rhea:RHEA:63796, Rhea:RHEA-COMP:16436, Rhea:RHEA-COMP:16437,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90782,
CC         ChEBI:CHEBI:149556; EC=3.4.17.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00024627};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797;
CC         Evidence={ECO:0000256|ARBA:ARBA00024627};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-
CC         glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208,
CC         Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:143622;
CC         Evidence={ECO:0000256|ARBA:ARBA00029299};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153;
CC         Evidence={ECO:0000256|ARBA:ARBA00029299};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000256|ARBA:ARBA00004186}. Midbody
CC       {ECO:0000256|ARBA:ARBA00004214}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODN06407.1}.
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DR   EMBL; LJIJ01000006; ODN06407.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D2NME3; -.
DR   STRING; 48709.A0A1D2NME3; -.
DR   OrthoDB; 168164at2759; -.
DR   Proteomes; UP000094527; Unassembled WGS sequence.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; 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:UniProtKB-KW.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   CDD; cd06236; M14_AGBL5_like; 1.
DR   Gene3D; 2.60.40.3120; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR034286; M14_AGBL5-like.
DR   InterPro; IPR040626; Pepdidase_M14_N.
DR   InterPro; IPR000834; Peptidase_M14.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF12; CYTOSOLIC CARBOXYPEPTIDASE-LIKE PROTEIN 5; 1.
DR   Pfam; PF18027; Pepdidase_M14_N; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:ODN06407.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protease {ECO:0000313|EMBL:ODN06407.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1016..1059
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          505..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1086..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1184..1204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1234..1265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..553
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..915
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1086..1116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1117..1133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1240..1254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1265 AA;  141001 MW;  B33B7473458C6BD0 CRC64;
     MTTAVCGPFT FSSEFDSGNF LKVEYVQSSP TPSTSQYSQP AYRNHDYEVN IWTKPDCHGT
     KFENGNRTWF YFSIRGGKSQ ETVKLNVLNL NKQVKLFAQG MQPVYRVLPE KPKWERVQDK
     LLINETGEHV CSISFKQRLP DNPLASTLYV AFTYPFSYKE LCELLNRFDK QFFPSQVGHR
     LNPMSDLPLT ASSTESDIYY HRECVCLSYE GRRVELITVT SMNGVSNARE ERLTNLFPIT
     SEPRPFKFPG KKVVFMSARV HPGETPSSFV LNGFLEFLLK PNHPQAILLR RLFVFKFIPI
     LNPDGVVRGH YRTDPRGVNL NRVYLNPSPV LHPPIYAARK LLLYYHNGVD WPDDYEYPVD
     AESTDMNDVS MEEMKCSENV DCCSSASLGG ESSMSSFPDH ADLSATPTAA ILQDNIEEGA
     GDCTKKEMKK PYTFVLSKAN SLCAGCGPFI DPNAEDAVMS AEDLQPSTSS CSLNDSGQSH
     HQCAFEACDE DSVFYENLSL KNSSSSLAAT SKESLPETPK RSSSRSSSGR RRRKGSVRER
     KKKVTKSASK AKTSKNNKKS DEAETTPYLQ MLLPSKPIEA TTRYKDKLRS KANISATLAN
     PVNYKISSPI SGPDSGLFLY LDMHGHTTKR GIFMYGNHFP DATKQAECML LPRLMAINSP
     HFDFSACNFT ERLMCMKDRR DGASREGSGR VACLKLTGLI RSYTLECNYN TGRIVNPMVT
     RTPAHGFLDS STSTVPPKFT IEIFEGIGVA LGESLLDLAG HPQSNLGKTE FRTLEGLRRS
     IVKRLKLSPE YKSPSSELTL KKSSSSTPGF ETNALFSPPK VIRKPKTKVL VQPTLGGPLG
     PKRENQNLPA DAKASGSQYK KLPLSPSVDC PTPGCSTAKE EAATTPPKMS LKKVMKKKSL
     TKVPTKGKGK KLKSKKKAEK SLEKLAAKKY SFGMRNGLID YRRWRKVIIK TCRASAPTNL
     KWISTQLLLG LQLKVSAMSA EVQEQVSEPE AASITPPNPP KATAEESLTK LEGHRCAICQ
     NILINACRID CGHTFCRHCL NVDKDDRLGG EKPTCFICDA AITEIRNTTD RDKEIDKLYT
     VLSTDERLSR ERDKSERKEL ETNFVKRPKQ EKSVDSDRNS NGSSGSGDAT YTTMPDNLDR
     ACWRDYGHDD NDEENLSEND DTPMYFCGSY TVWSDEHGSE ECHHVHGGED YDEGEESGSE
     EAVEASGYAN SPFPQPIVIH HTVQHIYHTV DAGERTGSES SGESGRHREV NPEWRGARPC
     LSTEI
//
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