Protein : Qrob_P0562420.2 Q. robur
Protein Identifier  ? Qrob_P0562420.2 Organism . Name  Quercus robur
Score  75.1 Score Type  egn
Protein Description  (M=2) 3.4.17.22 - Metallocarboxypeptidase D. Code Enzyme  EC:3.4.17.22
Gene Prediction Quality  validated Protein length 

Sequence

Length: 236  
Kegg Orthology  K07752
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0 Synonyms

3 GO Terms

Identifier Name Description
GO:0008270 zinc ion binding Interacting selectively and non-covalently with zinc (Zn) ions.
GO:0006508 proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0004181 metallocarboxypeptidase activity Catalysis of the hydrolysis of C-terminal amino acid residues from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

39 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|cam:101510794 1 235 + 235 Gaps:1 48.07 491 71.19 7e-120 carboxypeptidase D-like
blastp_kegg lcl|gmx:100779927 1 235 + 235 Gaps:1 47.01 502 69.49 5e-115 carboxypeptidase D-like
blastp_kegg lcl|pvu:PHAVU_007G083600g 1 235 + 235 Gaps:1 47.77 494 68.64 2e-114 hypothetical protein
blastp_kegg lcl|tcc:TCM_035722 1 232 + 232 Gaps:3 42.46 544 71.43 1e-112 Carboxypeptidase D
blastp_kegg lcl|cic:CICLE_v10003457mg 1 231 + 231 Gaps:4 52.52 436 69.43 3e-110 hypothetical protein
blastp_kegg lcl|vvi:100249088 1 231 + 231 Gaps:2 46.86 493 68.83 6e-109 carboxypeptidase D-like
blastp_kegg lcl|cit:102628512 1 231 + 231 Gaps:4 47.51 482 69.00 8e-109 carboxypeptidase D-like
blastp_kegg lcl|cmo:103496589 1 231 + 231 Gaps:4 47.12 486 66.81 1e-107 carboxypeptidase D
blastp_kegg lcl|csv:101228303 1 231 + 231 Gaps:4 47.12 486 66.38 2e-107 carboxypeptidase D-like
blastp_kegg lcl|csv:101220508 1 231 + 231 Gaps:4 47.12 486 65.94 5e-107 carboxypeptidase D-like
blastp_pdb 2nsm_A 1 156 + 156 Gaps:7 35.76 439 39.49 2e-24 mol:protein length:439 Carboxypeptidase N catalytic chain
blastp_pdb 1qmu_A 18 160 + 143 Gaps:5 37.37 380 40.85 7e-24 mol:protein length:380 CARBOXYPEPTIDASE GP180 RESIDUES 503-882
blastp_pdb 1h8l_A 18 160 + 143 Gaps:5 37.37 380 40.85 7e-24 mol:protein length:380 CARBOXYPEPTIDASE GP180 RESIDUES 503-882
blastp_pdb 1uwy_A 1 156 + 156 Gaps:11 37.79 426 36.02 1e-23 mol:protein length:426 CARBOXYPEPTIDASE M
blastp_pdb 3mn8_D 1 160 + 160 Gaps:10 38.16 435 36.75 1e-22 mol:protein length:435 LP15968p
blastp_pdb 3mn8_C 1 160 + 160 Gaps:10 38.16 435 36.75 1e-22 mol:protein length:435 LP15968p
blastp_pdb 3mn8_B 1 160 + 160 Gaps:10 38.16 435 36.75 1e-22 mol:protein length:435 LP15968p
blastp_pdb 3mn8_A 1 160 + 160 Gaps:10 38.16 435 36.75 1e-22 mol:protein length:435 LP15968p
blastp_uniprot_sprot sp|O75976|CBPD_HUMAN 1 174 + 174 Gaps:29 35.14 1380 37.53 1e-24 Carboxypeptidase D OS Homo sapiens GN CPD PE 1 SV 2
blastp_uniprot_sprot sp|Q9JHW1|CBPD_RAT 1 174 + 174 Gaps:29 35.12 1378 37.40 1e-24 Carboxypeptidase D OS Rattus norvegicus GN Cpd PE 2 SV 2
blastp_uniprot_sprot sp|Q9JJN5|CBPN_MOUSE 1 160 + 160 Gaps:8 35.45 457 38.89 1e-24 Carboxypeptidase N catalytic chain OS Mus musculus GN Cpn1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9EQV8|CBPN_RAT 1 165 + 165 Gaps:8 36.54 457 38.92 2e-24 Carboxypeptidase N catalytic chain OS Rattus norvegicus GN Cpn1 PE 2 SV 1
blastp_uniprot_sprot sp|Q90240|CBPD_ANAPL 1 172 + 172 Gaps:39 35.71 1389 36.69 1e-23 Carboxypeptidase D OS Anas platyrhynchos GN CPD PE 1 SV 1
blastp_uniprot_sprot sp|O89001|CBPD_MOUSE 1 187 + 187 Gaps:34 36.09 1377 37.02 2e-23 Carboxypeptidase D OS Mus musculus GN Cpd PE 1 SV 2
blastp_uniprot_sprot sp|P37892|CBPE_LOPAM 18 162 + 145 Gaps:4 31.50 454 39.16 2e-23 Carboxypeptidase E OS Lophius americanus GN cpe PE 2 SV 1
blastp_uniprot_sprot sp|P83852|CBPD_LOPSP 18 160 + 143 Gaps:5 37.37 380 40.85 3e-23 Carboxypeptidase D (Fragment) OS Lophonetta specularioides GN CPD PE 1 SV 1
blastp_uniprot_sprot sp|P15169|CBPN_HUMAN 1 156 + 156 Gaps:7 34.28 458 38.85 3e-23 Carboxypeptidase N catalytic chain OS Homo sapiens GN CPN1 PE 1 SV 1
blastp_uniprot_sprot sp|P14384|CBPM_HUMAN 1 156 + 156 Gaps:11 36.34 443 36.02 4e-23 Carboxypeptidase M OS Homo sapiens GN CPM PE 1 SV 2
rpsblast_cdd gnl|CDD|199842 1 79 + 79 Gaps:8 29.69 293 47.13 4e-34 cd03858 M14_CP_N-E_like Peptidase M14 carboxypeptidase subfamily N/E-like. Carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single C-terminal amino acids from polypeptide chains and have a recognition site for the free C-terminal carboxyl group which is a key determinant of specificity. The N/E subfamily includes eight members of which five (CPN CPE CPM CPD CPZ) are considered enzymatically active while the other three are non-active (CPX1 PCX2 ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form rather they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions including prohormone processing regulation of peptide hormone activity alteration of protein-protein or protein-cell interactions and transcriptional regulation.
rpsblast_cdd gnl|CDD|199850 1 78 + 78 Gaps:6 28.67 293 46.43 5e-23 cd03868 M14_CPD_I Peptidase M14 carboxypeptidase subfamily N/E-like Carboxypeptidase D domain I subgroup. The first carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD EC 3.4.17.22) domain I. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single C-terminal amino acids from polypeptide chains and have a recognition site for the free C-terminal carboxyl group which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide three tandem repeats of CP-like domains separated by short bridge regions followed by a transmembrane domain and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. This Domain I family contains two contiguous surface cysteines that may become palmitoylated and target the enzyme to membranes thus regulating intracellular trafficking. CPD functions in the processing of proteins that transit the secretory pathway and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells CPD is present in the trans Golgi network and immature secretory vesicles but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans Golgi network such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE) it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down-regulation of CPD leads to down-modulation of TGF-beta CPD may have a role in a positive feedback loop. In D. melanogaster the CPD variant 1B short (DmCPD1Bs) is necessary and sufficient for viability of the fruit fly.

10 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 2 71 70 PF00246 none Zinc carboxypeptidase IPR000834
PANTHER 1 179 179 PTHR11532:SF50 none none none
Phobius 190 212 23 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
PANTHER 1 179 179 PTHR11532 none none none
Gene3D 85 161 77 G3DSA:2.60.40.1120 none none IPR014766
Gene3D 6 79 74 G3DSA:3.40.630.10 none none none
SUPERFAMILY 85 167 83 SSF49464 none none IPR008969
SUPERFAMILY 2 79 78 SSF53187 none none none
Phobius 1 189 189 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 213 235 23 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none

1 Localization

Analysis Start End Length
TMHMM 190 212 22

13 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran1_2003_QTL2_peak_Bud_burst_A4 Qrob_Chr02 2 s_1B0H8U_259 s_1CB1VL_554 17 0 87 lod 3,3 8,7
Bourran2_2004_QTL9_peak_Bud_burst_3P Qrob_Chr02 2 s_1C34E9_788 v_12238_322 50 25 75 lod 4,4 10,1
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL2_d13Cf Qrob_Chr02 2 s_1AQA4Z_1644 s_1AK5QX_947 53.67 14,01 79,68 lod 5.6594 0.03
Bourran1_2004_QTL2_peak_Bud_burst_3P Qrob_Chr02 2 s_1AW12F_382 s_1A77MR_223 42 6 64 lod 3,6 9,6
Bourran_2000_2002_QTL2_Delta.F Qrob_Chr02 2 s_1CSO13_1244 s_1AVEUF_1540 55.44 46,71 63,68 lod 7.3232 0.058
Bourran2_2002_QTL7_peak_Bud_burst_3P Qrob_Chr02 2 s_1ANG6_1446 v_11270_161 40 29 52 lod 8,1 16
Bourran2_2002_QTL9_peak_Bud_burst_A4 Qrob_Chr02 2 s_1BFNDA_375 s_1A3VA1_2139 32,5 17 62 lod 3,1 4,2
Bourran2_2003_QTL8_peak_Bud_burst_3P Qrob_Chr02 2 s_1ANG6_1446 v_11270_161 40 0 72 lod 4,4 9,9
Bourran2_2014_nP_A4 Qrob_Chr11 11 s_1B58GB_1413 s_1A5BYY_1671 11,15 0 42,38 lod 1,8913 4,5
Bourran2_2015_nP_A4 Qrob_Chr02 2 s_1A0FUE_1868 s_1A1UAI_500 20,64 20,47 21,36 lod 5.8 10.9
Bourran2_2015_nPriLBD_A4 Qrob_Chr02 2 s_1CP5DI_1183 s_1A63ZX_1277 24,87 24,63 26,18 lod 3.8 7
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL6_d13Cf Qrob_Chr02 2 s_1AEP21_172 v_6048_204 46.33 22,5 65,23 lod 4.972 0.03
Bourran1_2004_QTL3_peak_Bud_burst_A4 Qrob_Chr02 2 s_1B0H8U_259 s_1CB1VL_554 17 0 46 lod 2,9 6,4

0 Targeting