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
//