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Conserved domains on  [gi|21356111|ref|NP_651314|]
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uncharacterized protein Dmel_CG11771 [Drosophila melanogaster]

Protein Classification

M3 family metallopeptidase( domain architecture ID 10157872)

M3 family metallopeptidase with varied activities, and contains the HEXXH motif that forms the active site in conjunction with a C-terminally-located Glu residue; similar to Arabidopsis thaliana cytosolic oligopeptidase A

EC:  3.4.24.-
Gene Ontology:  GO:0004222|GO:0008270|GO:0006508
MEROPS:  M3
PubMed:  7674922
SCOP:  3001975

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M3A_DCP cd06456
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ...
64-720 0e+00

Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl carboxypeptidase (DCP; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). This metal-binding M3A family also includes oligopeptidase A (OpdA; EC 3.4.24.70). DCP cleaves dipeptides off the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from Escherichia coli is inhibited by the anti-hypertensive drug captopril, an inhibitor of the mammalian angiotensin converting enzyme (ACE, also called peptidyl dipeptidase A). OpdA may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala. This family also includes Arabidopsis thaliana organellar oligopeptidase OOP (At5g65620), which plays a role in targeting peptide degradation in mitochondria and chloroplasts; it degrades peptide substrates that are between 8 to 23 amino acid residues, and shows a weak preference for hydrophobic residues (F/L) at the P1 position.


:

Pssm-ID: 341051 [Multi-domain]  Cd Length: 653  Bit Score: 623.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  64 EMCLGAIGQQASAVENSVKALESDLhsgKQLNAASIFRELDTVTGPLETTWGVAKALYLGNSTliptKSYMNIHERARNA 143
Cdd:cd06456   1 EHFVPAIEEAIAEQRAEIEAIEANP---EPPTFENTIEPLERAGEPLDRVWGVFSHLNSVNNS----DELRAAYEEVLPL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 144 RAAKFC----NQTVYKALKDASSDSG-----PDEQRMRQKFLLEGKLNGLTLDKDKQDGLKELLTHLGRERANFKNKVNM 214
Cdd:cd06456  74 LSAHSDaigqNEALFARVKALYDSREalgldPEQKRLLEKTLRDFVLSGAALSEEKKERLAEINEELSELSTKFSQNVLD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 215 AVHSFGQIITDFNLVRDFPPSLLEATARDPGQPMTGPWKITLQPQVVDGFLKHCPERMQRWNVWRASVLKASSQQEksLE 294
Cdd:cd06456 154 ATNAFSLVITDEAELAGLPESALAAAAEAAKARGKGGWLFTLDAPSYQPFLTYCDNRELREKVYRAYVTRASDGGE--FD 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 295 NSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVGSVDNLKQIFAKLLKFAGPAQSVELEKLQGFAQDSGCEYKLEAYDV 374
Cdd:cd06456 232 NSPIIEEILALRAEKAKLLGYKNYAEYSLATKMAKSPEAVLEFLEDLAEKAKPAAEKELAELQAFAKEEGGGDKLEPWDW 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 375 AYWRRKQLAAEHGLQDQKLREFFPLPRVLSGLFALSEKLFGIKIVEQPNAEVWHPAVKFYDVFDADsvnsSTPVGGFYVD 454
Cdd:cd06456 312 AYYAEKLRKEKYDLDEEELRPYFPLDRVLEGLFELAERLYGITFKERDDVPVWHPDVRVYEVFDAD----GELLGLFYLD 387
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 455 CYSKEHKfgRNNGWMVGIRNSNKSA--GLTPLCALIFNFSEPqsPDAKPPLLGYDDLQMLFKTFGSGLQHLLTQAGYSDL 532
Cdd:cd06456 388 LYARPGK--RGGAWMDSFRSRSRLLdsGQLPVAYLVCNFTPP--AGGKPALLSHDEVETLFHEFGHALHHLLTDVDYPSV 463
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 533 AGLSNIeWDASQVSGHVMSNFLDDPTVIRSLSGHFSSGEPLEAELSQKMRLLKTQLAGYNLCQDLYLADLDVELHRSNAF 612
Cdd:cd06456 464 SGTNVV-WDFVELPSQFMENWAWEPEVLKLYARHYETGEPLPDELIEKLLAARNFNAGFATLRQLAFALLDLALHSLYDP 542
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 613 -----WLEVVRKLWPVYQCMPLDKKDAHPCSLTDIFAGDWAAAQFSHLYSRLIAADISSSFAEQRSEenYAVVGRRYKQT 687
Cdd:cd06456 543 eapedVDAFEREVLKEYGVLPPIPPRRRSCSFSHIFSGGYAAGYYSYLWAEVLAADAFSAFEEAGGF--NRETGRRFRDT 620
                       650       660       670
                ....*....|....*....|....*....|...
gi 21356111 688 FLSCGGSVPTAEVFRRFQGRDPSAEALLKSLDI 720
Cdd:cd06456 621 ILSRGGSRDPMELFRAFRGRDPDIDALLRRRGL 653
 
Name Accession Description Interval E-value
M3A_DCP cd06456
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ...
64-720 0e+00

Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl carboxypeptidase (DCP; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). This metal-binding M3A family also includes oligopeptidase A (OpdA; EC 3.4.24.70). DCP cleaves dipeptides off the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from Escherichia coli is inhibited by the anti-hypertensive drug captopril, an inhibitor of the mammalian angiotensin converting enzyme (ACE, also called peptidyl dipeptidase A). OpdA may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala. This family also includes Arabidopsis thaliana organellar oligopeptidase OOP (At5g65620), which plays a role in targeting peptide degradation in mitochondria and chloroplasts; it degrades peptide substrates that are between 8 to 23 amino acid residues, and shows a weak preference for hydrophobic residues (F/L) at the P1 position.


Pssm-ID: 341051 [Multi-domain]  Cd Length: 653  Bit Score: 623.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  64 EMCLGAIGQQASAVENSVKALESDLhsgKQLNAASIFRELDTVTGPLETTWGVAKALYLGNSTliptKSYMNIHERARNA 143
Cdd:cd06456   1 EHFVPAIEEAIAEQRAEIEAIEANP---EPPTFENTIEPLERAGEPLDRVWGVFSHLNSVNNS----DELRAAYEEVLPL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 144 RAAKFC----NQTVYKALKDASSDSG-----PDEQRMRQKFLLEGKLNGLTLDKDKQDGLKELLTHLGRERANFKNKVNM 214
Cdd:cd06456  74 LSAHSDaigqNEALFARVKALYDSREalgldPEQKRLLEKTLRDFVLSGAALSEEKKERLAEINEELSELSTKFSQNVLD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 215 AVHSFGQIITDFNLVRDFPPSLLEATARDPGQPMTGPWKITLQPQVVDGFLKHCPERMQRWNVWRASVLKASSQQEksLE 294
Cdd:cd06456 154 ATNAFSLVITDEAELAGLPESALAAAAEAAKARGKGGWLFTLDAPSYQPFLTYCDNRELREKVYRAYVTRASDGGE--FD 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 295 NSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVGSVDNLKQIFAKLLKFAGPAQSVELEKLQGFAQDSGCEYKLEAYDV 374
Cdd:cd06456 232 NSPIIEEILALRAEKAKLLGYKNYAEYSLATKMAKSPEAVLEFLEDLAEKAKPAAEKELAELQAFAKEEGGGDKLEPWDW 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 375 AYWRRKQLAAEHGLQDQKLREFFPLPRVLSGLFALSEKLFGIKIVEQPNAEVWHPAVKFYDVFDADsvnsSTPVGGFYVD 454
Cdd:cd06456 312 AYYAEKLRKEKYDLDEEELRPYFPLDRVLEGLFELAERLYGITFKERDDVPVWHPDVRVYEVFDAD----GELLGLFYLD 387
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 455 CYSKEHKfgRNNGWMVGIRNSNKSA--GLTPLCALIFNFSEPqsPDAKPPLLGYDDLQMLFKTFGSGLQHLLTQAGYSDL 532
Cdd:cd06456 388 LYARPGK--RGGAWMDSFRSRSRLLdsGQLPVAYLVCNFTPP--AGGKPALLSHDEVETLFHEFGHALHHLLTDVDYPSV 463
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 533 AGLSNIeWDASQVSGHVMSNFLDDPTVIRSLSGHFSSGEPLEAELSQKMRLLKTQLAGYNLCQDLYLADLDVELHRSNAF 612
Cdd:cd06456 464 SGTNVV-WDFVELPSQFMENWAWEPEVLKLYARHYETGEPLPDELIEKLLAARNFNAGFATLRQLAFALLDLALHSLYDP 542
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 613 -----WLEVVRKLWPVYQCMPLDKKDAHPCSLTDIFAGDWAAAQFSHLYSRLIAADISSSFAEQRSEenYAVVGRRYKQT 687
Cdd:cd06456 543 eapedVDAFEREVLKEYGVLPPIPPRRRSCSFSHIFSGGYAAGYYSYLWAEVLAADAFSAFEEAGGF--NRETGRRFRDT 620
                       650       660       670
                ....*....|....*....|....*....|...
gi 21356111 688 FLSCGGSVPTAEVFRRFQGRDPSAEALLKSLDI 720
Cdd:cd06456 621 ILSRGGSRDPMELFRAFRGRDPDIDALLRRRGL 653
Peptidase_M3 pfam01432
Peptidase family M3; This is the Thimet oligopeptidase family, large family of mammalian and ...
264-720 3.40e-157

Peptidase family M3; This is the Thimet oligopeptidase family, large family of mammalian and bacterial oligopeptidases that cleave medium sized peptides. The group also contains mitochondrial intermediate peptidase which is encoded by nuclear DNA but functions within the mitochondria to remove the leader sequence.


Pssm-ID: 396149 [Multi-domain]  Cd Length: 450  Bit Score: 463.01  E-value: 3.40e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   264 FLKHCPERMQRWNVWRASVLKASsQQEKSLENSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVGSVDNLKQIFAKLLK 343
Cdd:pfam01432   1 LLKESPDRETRKKAYRAFYSRAE-AYRNTLENSALLEELLKLRAELAKLLGYPSYAEASLEDKMAKIPETVYDFLEELVN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   344 FAGPAQSVELEKLQGFAQDSGCEYKLEAYDVAYWRRKQLAAEHG-LQDQKLREFFPLPRVLS-GLFALSEKLFGIKIVEQ 421
Cdd:pfam01432  80 KLRPLLHRELELLKKLKKKELGLEELQPWDVAYYSEKQREELYDpLDQEELRPYFPLEQVLEkGLFGLFERLFGITFVLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   422 PNAEVWHPAVKFYDVFDADsvnSSTPVGGFYVDCYSKEHKfgRNNGWMVGIRNSNKSagltPLCALIFNFSEPQSpdAKP 501
Cdd:pfam01432 160 PLGEVWHEDVRFYSVFDEL---SGGLIGEFYLDLYPRKGK--RGGAYSFGLVPGRKD----PVPYLLCNFTKPSS--GKP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   502 PLLGYDDLQMLFKTFGSGLQHLLTQAGYSDLAGLsNIEWDASQVSGHVMSNFLDDPTVIRSLSGHFSSGEPLEAELSQKM 581
Cdd:pfam01432 229 SLLTHDDVETLFHEFGHSMHSLLSRTEYSYVSGT-NVPIDFAEIPSQFNENWLWEPLLLNLLSRHYETGEPIPAELLEKL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   582 RLLKTQLAGYNLCQDLYLADLDVELHRSNA------FWLEVVRKLWPVYQCMPLDKKDAHPCSLTDIFAGDWAAAQFSHL 655
Cdd:pfam01432 308 IKSKNVNAGLFLFRQLMFAAFDQEIHEAAEedqkldFLLEEYAELNKKYYGDPVTPDEASPLSFSHIFPHGYAANYYSYL 387
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356111   656 YSRLIAADISSSFAEQRSEEnyAVVGRRYKQTFLSCGGSVPTAEVFRRFQGRDPSAEALLKSLDI 720
Cdd:pfam01432 388 YATGLALDIFEKFFEQDPLN--RETGLRYYLEFLSRGGSLDPLELLKKFGGRMPSADALLRALGL 450
Dcp COG0339
Zn-dependent oligopeptidase, M3 family [Posttranslational modification, protein turnover, ...
52-716 1.54e-114

Zn-dependent oligopeptidase, M3 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440108 [Multi-domain]  Cd Length: 682  Bit Score: 360.51  E-value: 1.54e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  52 PDGLPAFSDITIEMCLGAI----GQQASAV------------ENSVKALEsdlHSGKQLN-AASIFRELDTV--TGPLEt 112
Cdd:COG0339  15 PYGLPPFDAIKPEHFEPAFeaalAEARAEIeaiaanpeaptfENTIEALE---RSGERLSrVWSVFSHLNSVdtNPELR- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 113 twgvakALYLGNSTLIpTKSYMNI--HER--ARnaraakfcnqtvYKALKDASSDSGPDEQRMRqkfLLEG-----KLNG 183
Cdd:COG0339  91 ------AAYNEVLPKL-SAHSDEIglNEAlfAR------------IKALYDSRDFLGLDPEQKR---LLENtlrdfVLSG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 184 LTLDKDKQDGLKELLTHLGRERANFKNKVNMAVHSFGQIITDFNLVRDFPPSLLEA---TARDPGQPmtGpWKITLQPQV 260
Cdd:COG0339 149 AALPEEDKARLREINEELAELSTKFSQNVLDATNAWALVVTDEAELAGLPESAIAAaaaAAKARGLE--G-WLITLDNPS 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 261 VDGFLKHCPERMQRWNVWRASVLKASSQQEksLENSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVGSVDNLKQIFAK 340
Cdd:COG0339 226 YQPVLTYADNRELREKLYRAYVTRASDGGE--FDNRPIIAEILALRAEKAKLLGYANYAEYSLADKMAKTPEAVLDFLRD 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 341 LLKFAGPAQSVELEKLQGFAQDSGCEYKLEAYDVAYWRRKQLAAEHGLQDQKLREFFPLPRVLSGLFALSEKLFGIKIVE 420
Cdd:COG0339 304 LAPAAKPAAERELAELQAFAAEEGGIFDLEPWDWAYYAEKLRQARYDLDEEELKPYFPLDRVLDGLFEVAERLYGLTFKE 383
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 421 QPNAEVWHPAVKFYDVFDADsvnsSTPVGGFYVDCYSKEHKfgRNNGWMVGIRNSNKSAGL--TPLCALIFNFSEPqsPD 498
Cdd:COG0339 384 RKDVPVYHPDVRVFEVFDAD----GELLGLFYLDLYAREGK--RGGAWMDSFRSQSRLDGElqLPVAYNVCNFTKP--VG 455
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 499 AKPPLLGYDDLQMLFKTFGSGLQHLLTQAGYSDLAGLsNIEWDA----SQvsghVMSNFLDDPTVIRSLSGHFSSGEPLE 574
Cdd:COG0339 456 GKPALLTHDEVTTLFHEFGHALHGMLTDVDYPSLSGT-NVPWDFvelpSQ----FMENWCWEPEVLALFARHYETGEPLP 530
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 575 AELSQKMRLLKTQLAGYNLCQDLYLADLDVELHRS---------NAFWLEVVRKlwpvYQCMPLDKKDAHPCSLTDIFAG 645
Cdd:COG0339 531 DELLDKLLAARNFNSGFATLRQLEFALLDMALHTLydpeagadvLAFEAEVLAE----VGVLPPVPPRRFSTYFSHIFAG 606
                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356111 646 DWAAAQFSHLYSRLIAADISSSFAEQ--RSEENyavvGRRYKQTFLSCGGSVPTAEVFRRFQGRDPSAEALLK 716
Cdd:COG0339 607 GYAAGYYSYKWAEVLDADAFSAFEEAgiFDRET----GQRFRDEILSRGGSRDPMELFKAFRGREPSIDALLR 675
PRK10911 PRK10911
oligopeptidase A; Provisional
49-720 4.95e-86

oligopeptidase A; Provisional


Pssm-ID: 182832 [Multi-domain]  Cd Length: 680  Bit Score: 285.56  E-value: 4.95e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   49 VLKPDGLPAFSDITIEMCLGAIgQQA-----SAVE------------NSVKAL-ESDLHSGK------QLNAASIFRELD 104
Cdd:PRK10911   5 LLTPFSLPPFSAIKPEHVVPAV-TKAlndcrEAVErvvaqgapytweNLCQPLaEVDDVLGRifspvsHLNSVKNSPELR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  105 TV---TGPL---ETTW-GVAKALYlgnstliptKSYMNIHERARNARAAKFCNQTVYKALKDAssdsgpdeqrmrqkfll 177
Cdd:PRK10911  84 EAyeqTLPLlseYSTWvGQHEGLY---------QAYRDLRDGDHYATLNTAQKKAVDNALRDF----------------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  178 egKLNGLTLDKDKQDGLKELLTHLGRERANFKNKVNMAVHSFGQIITDFNLVRDFPPSLLEAT-ARDPGQPMTGpWKITL 256
Cdd:PRK10911 138 --ELSGIGLPKEKQQRYGEIAARLSELGNQYSNNVLDATMGWTKLITDEAELAGMPESALAAAkAQAEAKEQEG-YLLTL 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  257 QPQVVDGFLKHCPERMQRWNVWRASVLKASSQQEKS--LENSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVGSVDNL 334
Cdd:PRK10911 215 DIPSYLPVMTYCDNQALREEMYRAYSTRASDQGPNAgkWDNSEVMEEILALRHELAQLLGFENYADKSLATKMAENPQQV 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  335 KQIFAKLLKFAGPAQSVELEKLQGFAQDSGCEYKLEAYDVAYWRRKQLAAEHGLQDQKLREFFPLPRVLSGLFALSEKLF 414
Cdd:PRK10911 295 LDFLTDLAKRARPQGEKELAQLRAFAKAEFGVDELQPWDIAYYSEKQKQHLYSISDEQLRPYFPENKAVNGLFEVVKRIY 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  415 GIKIVEQPNAEVWHPAVKFYDVFDAdsvnSSTPVGGFYVDCYSKEHKfgRNNGWM---VG-IRNSNKSAGlTPLCALIFN 490
Cdd:PRK10911 375 GITAKERKDVDVWHPDVRFFELYDE----NNELRGSFYLDLYARENK--RGGAWMddcVGqMRKADGSLQ-KPVAYLTCN 447
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  491 FSEPQSpdAKPPLLGYDDLQMLFKTFGSGLQHLLTQAGYSDLAGLSNIEWDASQVSGHVMSNFLDDPTVIRSLSGHFSSG 570
Cdd:PRK10911 448 FNRPVN--GKPALFTHDEVITLFHEFGHGLHHMLTRIETAGVSGISGVPWDAVELPSQFMENWCWEPEALAFISGHYETG 525
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  571 EPLEAELSQKMRLLKTQLAGYNLCQDLYLADLDVELH-----RSNAFWLEVVRKLWPVYQCMPLDKKDAHPCSLTDIFAG 645
Cdd:PRK10911 526 EPLPKELLDKMLAAKNYQAALFILRQLEFGLFDFRLHaefdpDQGAKILETLAEIKKQVAVVPSPSWGRFPHAFSHIFAG 605
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356111  646 DWAAAQFSHLYSRLIAADISSSFAEQrseenyAVVGRRYKQTF----LSCGGSVPTAEVFRRFQGRDPSAEALLKSLDI 720
Cdd:PRK10911 606 GYAAGYYSYLWADVLAADAFSRFEEE------GIFNRETGQSFldniLSRGGSEEPMELFKRFRGREPQLDAMLEHYGI 678
 
Name Accession Description Interval E-value
M3A_DCP cd06456
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ...
64-720 0e+00

Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl carboxypeptidase (DCP; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). This metal-binding M3A family also includes oligopeptidase A (OpdA; EC 3.4.24.70). DCP cleaves dipeptides off the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from Escherichia coli is inhibited by the anti-hypertensive drug captopril, an inhibitor of the mammalian angiotensin converting enzyme (ACE, also called peptidyl dipeptidase A). OpdA may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala. This family also includes Arabidopsis thaliana organellar oligopeptidase OOP (At5g65620), which plays a role in targeting peptide degradation in mitochondria and chloroplasts; it degrades peptide substrates that are between 8 to 23 amino acid residues, and shows a weak preference for hydrophobic residues (F/L) at the P1 position.


Pssm-ID: 341051 [Multi-domain]  Cd Length: 653  Bit Score: 623.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  64 EMCLGAIGQQASAVENSVKALESDLhsgKQLNAASIFRELDTVTGPLETTWGVAKALYLGNSTliptKSYMNIHERARNA 143
Cdd:cd06456   1 EHFVPAIEEAIAEQRAEIEAIEANP---EPPTFENTIEPLERAGEPLDRVWGVFSHLNSVNNS----DELRAAYEEVLPL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 144 RAAKFC----NQTVYKALKDASSDSG-----PDEQRMRQKFLLEGKLNGLTLDKDKQDGLKELLTHLGRERANFKNKVNM 214
Cdd:cd06456  74 LSAHSDaigqNEALFARVKALYDSREalgldPEQKRLLEKTLRDFVLSGAALSEEKKERLAEINEELSELSTKFSQNVLD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 215 AVHSFGQIITDFNLVRDFPPSLLEATARDPGQPMTGPWKITLQPQVVDGFLKHCPERMQRWNVWRASVLKASSQQEksLE 294
Cdd:cd06456 154 ATNAFSLVITDEAELAGLPESALAAAAEAAKARGKGGWLFTLDAPSYQPFLTYCDNRELREKVYRAYVTRASDGGE--FD 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 295 NSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVGSVDNLKQIFAKLLKFAGPAQSVELEKLQGFAQDSGCEYKLEAYDV 374
Cdd:cd06456 232 NSPIIEEILALRAEKAKLLGYKNYAEYSLATKMAKSPEAVLEFLEDLAEKAKPAAEKELAELQAFAKEEGGGDKLEPWDW 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 375 AYWRRKQLAAEHGLQDQKLREFFPLPRVLSGLFALSEKLFGIKIVEQPNAEVWHPAVKFYDVFDADsvnsSTPVGGFYVD 454
Cdd:cd06456 312 AYYAEKLRKEKYDLDEEELRPYFPLDRVLEGLFELAERLYGITFKERDDVPVWHPDVRVYEVFDAD----GELLGLFYLD 387
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 455 CYSKEHKfgRNNGWMVGIRNSNKSA--GLTPLCALIFNFSEPqsPDAKPPLLGYDDLQMLFKTFGSGLQHLLTQAGYSDL 532
Cdd:cd06456 388 LYARPGK--RGGAWMDSFRSRSRLLdsGQLPVAYLVCNFTPP--AGGKPALLSHDEVETLFHEFGHALHHLLTDVDYPSV 463
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 533 AGLSNIeWDASQVSGHVMSNFLDDPTVIRSLSGHFSSGEPLEAELSQKMRLLKTQLAGYNLCQDLYLADLDVELHRSNAF 612
Cdd:cd06456 464 SGTNVV-WDFVELPSQFMENWAWEPEVLKLYARHYETGEPLPDELIEKLLAARNFNAGFATLRQLAFALLDLALHSLYDP 542
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 613 -----WLEVVRKLWPVYQCMPLDKKDAHPCSLTDIFAGDWAAAQFSHLYSRLIAADISSSFAEQRSEenYAVVGRRYKQT 687
Cdd:cd06456 543 eapedVDAFEREVLKEYGVLPPIPPRRRSCSFSHIFSGGYAAGYYSYLWAEVLAADAFSAFEEAGGF--NRETGRRFRDT 620
                       650       660       670
                ....*....|....*....|....*....|...
gi 21356111 688 FLSCGGSVPTAEVFRRFQGRDPSAEALLKSLDI 720
Cdd:cd06456 621 ILSRGGSRDPMELFRAFRGRDPDIDALLRRRGL 653
Peptidase_M3 pfam01432
Peptidase family M3; This is the Thimet oligopeptidase family, large family of mammalian and ...
264-720 3.40e-157

Peptidase family M3; This is the Thimet oligopeptidase family, large family of mammalian and bacterial oligopeptidases that cleave medium sized peptides. The group also contains mitochondrial intermediate peptidase which is encoded by nuclear DNA but functions within the mitochondria to remove the leader sequence.


Pssm-ID: 396149 [Multi-domain]  Cd Length: 450  Bit Score: 463.01  E-value: 3.40e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   264 FLKHCPERMQRWNVWRASVLKASsQQEKSLENSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVGSVDNLKQIFAKLLK 343
Cdd:pfam01432   1 LLKESPDRETRKKAYRAFYSRAE-AYRNTLENSALLEELLKLRAELAKLLGYPSYAEASLEDKMAKIPETVYDFLEELVN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   344 FAGPAQSVELEKLQGFAQDSGCEYKLEAYDVAYWRRKQLAAEHG-LQDQKLREFFPLPRVLS-GLFALSEKLFGIKIVEQ 421
Cdd:pfam01432  80 KLRPLLHRELELLKKLKKKELGLEELQPWDVAYYSEKQREELYDpLDQEELRPYFPLEQVLEkGLFGLFERLFGITFVLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   422 PNAEVWHPAVKFYDVFDADsvnSSTPVGGFYVDCYSKEHKfgRNNGWMVGIRNSNKSagltPLCALIFNFSEPQSpdAKP 501
Cdd:pfam01432 160 PLGEVWHEDVRFYSVFDEL---SGGLIGEFYLDLYPRKGK--RGGAYSFGLVPGRKD----PVPYLLCNFTKPSS--GKP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   502 PLLGYDDLQMLFKTFGSGLQHLLTQAGYSDLAGLsNIEWDASQVSGHVMSNFLDDPTVIRSLSGHFSSGEPLEAELSQKM 581
Cdd:pfam01432 229 SLLTHDDVETLFHEFGHSMHSLLSRTEYSYVSGT-NVPIDFAEIPSQFNENWLWEPLLLNLLSRHYETGEPIPAELLEKL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   582 RLLKTQLAGYNLCQDLYLADLDVELHRSNA------FWLEVVRKLWPVYQCMPLDKKDAHPCSLTDIFAGDWAAAQFSHL 655
Cdd:pfam01432 308 IKSKNVNAGLFLFRQLMFAAFDQEIHEAAEedqkldFLLEEYAELNKKYYGDPVTPDEASPLSFSHIFPHGYAANYYSYL 387
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356111   656 YSRLIAADISSSFAEQRSEEnyAVVGRRYKQTFLSCGGSVPTAEVFRRFQGRDPSAEALLKSLDI 720
Cdd:pfam01432 388 YATGLALDIFEKFFEQDPLN--RETGLRYYLEFLSRGGSLDPLELLKKFGGRMPSADALLRALGL 450
Dcp COG0339
Zn-dependent oligopeptidase, M3 family [Posttranslational modification, protein turnover, ...
52-716 1.54e-114

Zn-dependent oligopeptidase, M3 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440108 [Multi-domain]  Cd Length: 682  Bit Score: 360.51  E-value: 1.54e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  52 PDGLPAFSDITIEMCLGAI----GQQASAV------------ENSVKALEsdlHSGKQLN-AASIFRELDTV--TGPLEt 112
Cdd:COG0339  15 PYGLPPFDAIKPEHFEPAFeaalAEARAEIeaiaanpeaptfENTIEALE---RSGERLSrVWSVFSHLNSVdtNPELR- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 113 twgvakALYLGNSTLIpTKSYMNI--HER--ARnaraakfcnqtvYKALKDASSDSGPDEQRMRqkfLLEG-----KLNG 183
Cdd:COG0339  91 ------AAYNEVLPKL-SAHSDEIglNEAlfAR------------IKALYDSRDFLGLDPEQKR---LLENtlrdfVLSG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 184 LTLDKDKQDGLKELLTHLGRERANFKNKVNMAVHSFGQIITDFNLVRDFPPSLLEA---TARDPGQPmtGpWKITLQPQV 260
Cdd:COG0339 149 AALPEEDKARLREINEELAELSTKFSQNVLDATNAWALVVTDEAELAGLPESAIAAaaaAAKARGLE--G-WLITLDNPS 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 261 VDGFLKHCPERMQRWNVWRASVLKASSQQEksLENSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVGSVDNLKQIFAK 340
Cdd:COG0339 226 YQPVLTYADNRELREKLYRAYVTRASDGGE--FDNRPIIAEILALRAEKAKLLGYANYAEYSLADKMAKTPEAVLDFLRD 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 341 LLKFAGPAQSVELEKLQGFAQDSGCEYKLEAYDVAYWRRKQLAAEHGLQDQKLREFFPLPRVLSGLFALSEKLFGIKIVE 420
Cdd:COG0339 304 LAPAAKPAAERELAELQAFAAEEGGIFDLEPWDWAYYAEKLRQARYDLDEEELKPYFPLDRVLDGLFEVAERLYGLTFKE 383
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 421 QPNAEVWHPAVKFYDVFDADsvnsSTPVGGFYVDCYSKEHKfgRNNGWMVGIRNSNKSAGL--TPLCALIFNFSEPqsPD 498
Cdd:COG0339 384 RKDVPVYHPDVRVFEVFDAD----GELLGLFYLDLYAREGK--RGGAWMDSFRSQSRLDGElqLPVAYNVCNFTKP--VG 455
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 499 AKPPLLGYDDLQMLFKTFGSGLQHLLTQAGYSDLAGLsNIEWDA----SQvsghVMSNFLDDPTVIRSLSGHFSSGEPLE 574
Cdd:COG0339 456 GKPALLTHDEVTTLFHEFGHALHGMLTDVDYPSLSGT-NVPWDFvelpSQ----FMENWCWEPEVLALFARHYETGEPLP 530
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 575 AELSQKMRLLKTQLAGYNLCQDLYLADLDVELHRS---------NAFWLEVVRKlwpvYQCMPLDKKDAHPCSLTDIFAG 645
Cdd:COG0339 531 DELLDKLLAARNFNSGFATLRQLEFALLDMALHTLydpeagadvLAFEAEVLAE----VGVLPPVPPRRFSTYFSHIFAG 606
                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356111 646 DWAAAQFSHLYSRLIAADISSSFAEQ--RSEENyavvGRRYKQTFLSCGGSVPTAEVFRRFQGRDPSAEALLK 716
Cdd:COG0339 607 GYAAGYYSYKWAEVLDADAFSAFEEAgiFDRET----GQRFRDEILSRGGSRDPMELFKAFRGREPSIDALLR 675
M3A_TOP cd06455
Peptidase M3 thimet oligopeptidase (TOP), also includes neurolysin; Peptidase M3 Thimet ...
150-718 2.02e-89

Peptidase M3 thimet oligopeptidase (TOP), also includes neurolysin; Peptidase M3 Thimet oligopeptidase (TOP; PZ-peptidase; endo-oligopeptidase A; endopeptidase 24.15; soluble metallo-endopeptidase; EC 3.4.24.15) family also includes neurolysin (endopeptidase 24.16, microsomal endopeptidase, mitochondrial oligopeptidase M, neurotensin endopeptidase, soluble angiotensin II-binding protein, thimet oligopeptidase II) which hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. TOP and neurolysin are neuropeptidases expressed abundantly in the testis, but are also found in the liver, lung and kidney. They are involved in the metabolism of neuropeptides under 20 amino acid residues long and cleave most bioactive peptides at the same sites, but recognize different positions on some naturally occurring and synthetic peptides; they cleave at distinct sites on the 13-residue bioactive peptide neurotensin, which modulates central dopaminergic and cholinergic circuits. TOP has been shown to degrade peptides released by the proteasome, limiting the extent of antigen presentation by major histocompatibility complex class I molecules, and has been associated with amyloid protein precursor processing.


Pssm-ID: 341050 [Multi-domain]  Cd Length: 642  Bit Score: 293.26  E-value: 2.02e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 150 NQTVYKALKDAS----SDSGPDEQRMRQKFLLEGKLNGLTLDKDKQDGLKEL---LTHLGREranfknkvnmavhsFGQI 222
Cdd:cd06455  82 REDLYRLVKAVYdkneKKLDAESRRLLEKLLRDFRRNGLGLPDEKRERLKELkkeISELSIE--------------FSKN 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 223 ITDFNLVRDF--------PPSLLEATARDPGqpmtGPWKITLQPQVVDGFLKHCPERMQRWNVWRASVLKASSqqekslE 294
Cdd:cd06455 148 LNEDNTGIWFteeelegvPEDFLDRLKKDDD----GKYKVTLKYPDYFPVMKYAKNPETRKRMYLAFENRAYP------E 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 295 NSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVGSVDNLKQIFAKLLKFAGPAQSVELEKLQGFAQ----DSGCEYKLE 370
Cdd:cd06455 218 NVPLLEEIVALRDELARLLGYKSHADYVLEDRMAKTPEAVEAFLDDLREKLKPLAEKELAELLALKKedlpEAGLPGKLY 297
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 371 AYDVAYWRRKQLAAEHGLQDQKLREFFPLPRVLSGLFALSEKLFGIKIVEQPNAEVWHPAVKFYDVFDADsvnSSTPVGG 450
Cdd:cd06455 298 PWDLAYYSRLLKKEEYSVDEEKIREYFPLEHVVDGMLDIYEELFGLRFEEVDGAPVWHPDVRLYAVWDDD---TGEFLGY 374
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 451 FYVDCYSKEHKFGRNNgwMVGIRNSNKSAGLT---PLCALIFNFSEPqSPDaKPPLLGYDDLQMLFKTFGSGLQHLLTQA 527
Cdd:cd06455 375 LYLDLFPREGKYGHAA--NFPLQPGFTKPDGSrqyPVTALVCNFPKP-TAD-KPSLLKHDEVVTLFHEFGHAMHDLLSRT 450
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 528 GYSDLAGlSNIEWD---A-SQvsghVMSNFLDDPTVIRSLSGHFSSGEPLEAELSQKMRLLKTQLAGYNLCQDLYLADLD 603
Cdd:cd06455 451 KYARFHG-TSVERDfveApSQ----MLENWCWDPEVLKRLSKHYKTGEPLPDELIEKLIKSRNFNSGLFYLRQLFLALFD 525
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 604 VELHRSN--------AFWLEVVRKLWPVYQCMPldkkDAHPCSLTDIFAGDWAAAQFSHLYSRLIAADISSSFAEQ--RS 673
Cdd:cd06455 526 LALHTPDshealdltKLWNELREEITLIPGPPE----GTHGYASFGHLMGGYDAGYYGYLWSEVFAADMFYTFFKAdpLN 601
                       570       580       590       600
                ....*....|....*....|....*....|....*....|....*
gi 21356111 674 EEnyavVGRRYKQTFLSCGGSVPTAEVFRRFQGRDPSAEALLKSL 718
Cdd:cd06455 602 PE----VGRRYRDKVLEPGGSRDEMELLEDFLGREPNSDAFLKEL 642
PRK10911 PRK10911
oligopeptidase A; Provisional
49-720 4.95e-86

oligopeptidase A; Provisional


Pssm-ID: 182832 [Multi-domain]  Cd Length: 680  Bit Score: 285.56  E-value: 4.95e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111   49 VLKPDGLPAFSDITIEMCLGAIgQQA-----SAVE------------NSVKAL-ESDLHSGK------QLNAASIFRELD 104
Cdd:PRK10911   5 LLTPFSLPPFSAIKPEHVVPAV-TKAlndcrEAVErvvaqgapytweNLCQPLaEVDDVLGRifspvsHLNSVKNSPELR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  105 TV---TGPL---ETTW-GVAKALYlgnstliptKSYMNIHERARNARAAKFCNQTVYKALKDAssdsgpdeqrmrqkfll 177
Cdd:PRK10911  84 EAyeqTLPLlseYSTWvGQHEGLY---------QAYRDLRDGDHYATLNTAQKKAVDNALRDF----------------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  178 egKLNGLTLDKDKQDGLKELLTHLGRERANFKNKVNMAVHSFGQIITDFNLVRDFPPSLLEAT-ARDPGQPMTGpWKITL 256
Cdd:PRK10911 138 --ELSGIGLPKEKQQRYGEIAARLSELGNQYSNNVLDATMGWTKLITDEAELAGMPESALAAAkAQAEAKEQEG-YLLTL 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  257 QPQVVDGFLKHCPERMQRWNVWRASVLKASSQQEKS--LENSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVGSVDNL 334
Cdd:PRK10911 215 DIPSYLPVMTYCDNQALREEMYRAYSTRASDQGPNAgkWDNSEVMEEILALRHELAQLLGFENYADKSLATKMAENPQQV 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  335 KQIFAKLLKFAGPAQSVELEKLQGFAQDSGCEYKLEAYDVAYWRRKQLAAEHGLQDQKLREFFPLPRVLSGLFALSEKLF 414
Cdd:PRK10911 295 LDFLTDLAKRARPQGEKELAQLRAFAKAEFGVDELQPWDIAYYSEKQKQHLYSISDEQLRPYFPENKAVNGLFEVVKRIY 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  415 GIKIVEQPNAEVWHPAVKFYDVFDAdsvnSSTPVGGFYVDCYSKEHKfgRNNGWM---VG-IRNSNKSAGlTPLCALIFN 490
Cdd:PRK10911 375 GITAKERKDVDVWHPDVRFFELYDE----NNELRGSFYLDLYARENK--RGGAWMddcVGqMRKADGSLQ-KPVAYLTCN 447
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  491 FSEPQSpdAKPPLLGYDDLQMLFKTFGSGLQHLLTQAGYSDLAGLSNIEWDASQVSGHVMSNFLDDPTVIRSLSGHFSSG 570
Cdd:PRK10911 448 FNRPVN--GKPALFTHDEVITLFHEFGHGLHHMLTRIETAGVSGISGVPWDAVELPSQFMENWCWEPEALAFISGHYETG 525
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  571 EPLEAELSQKMRLLKTQLAGYNLCQDLYLADLDVELH-----RSNAFWLEVVRKLWPVYQCMPLDKKDAHPCSLTDIFAG 645
Cdd:PRK10911 526 EPLPKELLDKMLAAKNYQAALFILRQLEFGLFDFRLHaefdpDQGAKILETLAEIKKQVAVVPSPSWGRFPHAFSHIFAG 605
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356111  646 DWAAAQFSHLYSRLIAADISSSFAEQrseenyAVVGRRYKQTF----LSCGGSVPTAEVFRRFQGRDPSAEALLKSLDI 720
Cdd:PRK10911 606 GYAAGYYSYLWADVLAADAFSRFEEE------GIFNRETGQSFldniLSRGGSEEPMELFKRFRGREPQLDAMLEHYGI 678
M3A cd09605
Peptidase M3A family includes thimet oligopeptidase, dipeptidyl carboxypeptidase and ...
151-717 1.61e-54

Peptidase M3A family includes thimet oligopeptidase, dipeptidyl carboxypeptidase and mitochondrial intermediate peptidase; The M3-like family also called neurolysin-like family, is part of the "zincins" metallopeptidases, and includes M3, M2 and M32 families of metallopeptidases. The M3 family is subdivided into two subfamilies: the widespread M3A, represented by this CD, which comprises a number of high-molecular mass endo- and exopeptidases from bacteria, archaea, protozoa, fungi, plants and animals, and the small M3B, whose members are enzymes primarily from bacteria. Well-known mammalian/eukaryotic M3A endopeptidases are the thimet oligopeptidase (TOP; endopeptidase 3.4.24.15), neurolysin (alias endopeptidase 3.4.24.16), and the mitochondrial intermediate peptidase. The first two are intracellular oligopeptidases, which act only on relatively short substrates of less than 20 amino acid residues, while the latter cleaves N-terminal octapeptides from proteins during their import into the mitochondria. The M3A subfamily also contains several bacterial endopeptidases, called oligopeptidases A, as well as a large number of bacterial carboxypeptidases, called dipeptidyl peptidases (Dcp; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). The peptidases in the M3 family contain the HEXXH motif that forms part of the active site in conjunction with a C-terminally-located Glutamic acid (Glu) residue. A single zinc ion is ligated by the side-chains of the two Histidine (His) residues, and the more C-terminal Glu. Most of the peptidases are synthesized without signal peptides or propeptides, and function intracellularly.


Pssm-ID: 341068 [Multi-domain]  Cd Length: 587  Bit Score: 197.38  E-value: 1.61e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 151 QTVYKALKDASSDS-GPDEQRMRQKFLLEGKLNGLTLDKDKQDGLKELlthlgreranfknKVNMAvhsfgqiitdfNLV 229
Cdd:cd09605  87 QRIVKLQEDKKLVSlDPEARRYLELFIKDFERNGLHLDKEKRKRIKDL-------------NKKIS-----------DLC 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 230 RDFPPSLLEATARdpgqpmtgpwkitlqpQVVDGFLKHCPErmqrwnvwrasvlkassqqekslENSTHIEKIRGLRKRQ 309
Cdd:cd09605 143 SDFNKNLNPETRE----------------KAEKAFLTRCKA-----------------------ENLAILQELLSLRAQL 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 310 ANLLGYESFADMSMQTKMVGSVDNLKQIFAKLLKFAGPAQSVELEKLQGFaQDSGCEY--KLEAYDVAYWRRKQLAAEHG 387
Cdd:cd09605 184 AKLLGYSTHADRVLEGNMAKTPETVAQFLDELSQKLKPRGEKEREMILGL-KMKECEQdgEIMPWDPPYYMGQVREERYN 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 388 LQDQKLREFFPLPRVLSGLFALSEKLFGIKIVEQPNAEVWHPAVKFYDVFDADSVNsstpVGGFYVDCYSKEHKFGrnNG 467
Cdd:cd09605 263 VDQSLLKPYFPLGVVTEGLLIIYNELLGISFYAEQDAEVWHEDVRLYTVVDEAEEV----LGYFYLDFFPREGKYG--HA 336
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 468 WMVGIR-NSNKSAG--LTPLCALIFNFSEPQSpdAKPPLLGYDDLQMLFKTFGSGLQHLLTQAGYSDLAGlSNIEWDASQ 544
Cdd:cd09605 337 ACFGLQpGCLKEDGsrQLPVAALVLNFPKPSA--GSPSLLTHDEVRTLFHEFGHVMHQLCARTRYAHFSG-TNVPTDFVE 413
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 545 VSGHVMSNFLDDPTVIRSLSGHFSSGEPLEAELSQKMRLLKTQLAGYNLCQDLYLADLDVELH------RSNAFWLevvR 618
Cdd:cd09605 414 VPSQMLENWAWDVNQFARHSRHYQSGAPLPDELLEKLCESRLVNTGLDMLRQIVLAKLDQILHtkhplrNDTADEL---A 490
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 619 KLWPVYQCMPLDKKDAHPCSLTDIFAGdWAAAQFSHLYSRLIAADISSSFAEQrsEENYAVVGRRYKQTFLSCGGSVPTA 698
Cdd:cd09605 491 ELCEEILGLPATPGTNMPATFGHLAGG-YDAQYYGYLWSEVVAMDMFHECFKQ--EPLNREVGMRYRREILAPGGSEDPM 567
                       570
                ....*....|....*....
gi 21356111 699 EVFRRFQGRDPSAEALLKS 717
Cdd:cd09605 568 LMLRGFLQKCPKQSAFLFS 586
PRK10280 PRK10280
peptidyl-dipeptidase Dcp;
165-716 5.78e-43

peptidyl-dipeptidase Dcp;


Pssm-ID: 182353  Cd Length: 681  Bit Score: 165.77  E-value: 5.78e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  165 GPDEQRMR------QKFLLEGKlnglTLDKDKQDGLKELLTHLGRERANFKNKVNMAVHSFGQIITDFNLVRDFPPSLLE 238
Cdd:PRK10280 127 GLDSESIRlvevihQRFVLAGA----KLAQADKAKLKVLNTEAATLTSQFNQRLLAANKSGGLVVNDIHQLAGLSEQEIA 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  239 A---TARDPGQpmTGPWKITLQPQVVDGFLKHCPERMQRWNVWRASVLKAssqqEKSLENSTH--IEKIRGLRKRQANLL 313
Cdd:PRK10280 203 LaaeAAREKGL--DNRWLIPLLNTTQQPALAELRDRQTRENLFAAGWTRA----EKGDANDTRaiIQRLVEIRAQQAKLL 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  314 GYESFADMSMQTKMVGSVDNLKQIFAKLLKFAGPAQSVELEKLQGFAQDSGCEYKLEAYDVAYWRRKQLAAEHGLQDQKL 393
Cdd:PRK10280 277 GFPHYAAWKIADQMAKTPEAALNFMREIVPAARQRASDELASIQAVIDKQQGGFSAQAWDWAFYAEQVRREKYALDEAQL 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  394 REFFPLPRVLS-GLFALSEKLFGIKIVEQPNAEVWHPAVKFYDVFDADSVNSSTpvggFYVDCYSKEHKFGrnNGWMVGI 472
Cdd:PRK10280 357 KPYFELNTVLNeGVFWTANQLFGIKFVERFDIPVYHPDVRVWEIFDHNGVGLAL----FYGDFFARDSKSG--GAWMGNF 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  473 RNSNKSAGLTPLCALIFNFSEPQspDAKPPLLGYDDLQMLFKTFGSGLQHLLTQAGYSDLAGlSNIEWD----ASQVSGH 548
Cdd:PRK10280 431 VEQSTLNETRPVIYNVCNYQKPA--AGQPALLLWDDVITLFHEFGHTLHGLFARQRYATLSG-TNTPRDfvefPSQINEH 507
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  549 VMSNflddPTVIRSLSGHFSSGEPLEAELSQKMRLLKTQLAGYNLCQDLYLADLDVELH---------RSNAFWLEVVRK 619
Cdd:PRK10280 508 WASH----PQVFARYARHYQSGEAMPDELQEKMRNASLFNKGYDMSELLSAALLDMRWHcleeneamqDVDDFELRALVA 583
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111  620 LWPVYQCMPLDKKDAHpcsLTDIFAGDWAAAQFSHLYSRLIAADISSSFAEQ--RSEENyavvGRRYKQTFLSCGGSVPT 697
Cdd:PRK10280 584 ENLDLPAVPPRYRSSY---FAHIFGGGYAAGYYAYLWTQMLADDGYQWFVEQggLTREN----GQRFREAILSRGNSTDL 656
                        570
                 ....*....|....*....
gi 21356111  698 AEVFRRFQGRDPSAEALLK 716
Cdd:PRK10280 657 ERLYRQWRGHAPQIMPMLQ 675
M3A_MIP cd06457
Peptidase M3 mitochondrial intermediate peptidase (MIP); Peptidase M3 mitochondrial ...
267-718 3.54e-42

Peptidase M3 mitochondrial intermediate peptidase (MIP); Peptidase M3 mitochondrial intermediate peptidase (MIP; EC 3.4.24.59) belongs to the widespread subfamily M3A, that shows similarity to Thimet oligopeptidase (TOP). It is one of three peptidases responsible for the proteolytic processing of both nuclear and mitochondrial encoded precursor polypeptides targeted to various subcompartments of the mitochondria. It cleaves intermediate-size proteins initially processed by mitochondrial processing peptidase (MPP) to yield a processing intermediate with a typical N-terminal octapeptide that is sequentially cleaved by MIP to mature-size protein. MIP cleaves precursor proteins of respiratory components, including subunits of the electron transport chain and tri-carboxylic acid cycle enzymes, and components of the mitochondrial genetic machinery, including ribosomal proteins, translation factors, and proteins required for mitochondrial DNA metabolism. It has been suggested that the human MIP (HMIP polypeptide (gene symbol MIPEP) may be one of the loci predicted to influence the clinical manifestations of Friedreich's ataxia (FRDA), an autosomal recessive neurodegenerative disease caused by the lack of human frataxin. These proteins are enriched in cysteine residues, two of which are highly conserved, suggesting their importance to stability as well as in formation of metal binding sites, thus playing a role in MIP activity.


Pssm-ID: 341052 [Multi-domain]  Cd Length: 613  Bit Score: 162.34  E-value: 3.54e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 267 HCPERMQRWNVWRASvLKASSQQEKSLENSthiekirgLRKRQ--ANLLGYESFADMSMQTKMVGSVDNLKQIFAKLLK- 343
Cdd:cd06457 164 SAPDEEVRKKVYLAY-HSSSEEQEEVLEEL--------LKARAelAQLLGFPSYAHRALRDKMAKSPENVLSFLETLSDs 234
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 344 FAGPAQSvELEKLQGFAQDSGCEY--KLEAYDVAYWRRKQLAAEHGLQDQKLREFFPLPRVLSGLFALSEKLFGIKIVEQ 421
Cdd:cd06457 235 LRPKAEK-ELEELRKLKRKHEGLSspTLMPWDRDYYTGLLRAQARSSDASELSPYFSLGTVMEGLSRLFSRLYGIRLVPV 313
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 422 PNA--EVWHPAVKFYDVFDADSVnsstPVGGFYVDCYSKEHKF----------GRNNGWmvgirNSNKSAGL--TPLCAL 487
Cdd:cd06457 314 PTQpgEVWHPDVRKLEVVHETEG----LLGTIYCDLFERPGKPpgaahftircSRRLDD-----DDLGDGGSyqLPVVVL 384
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 488 IFNFSEPQSPdaKPPLLGYDDLQMLFKTFGSGLQHLLTQAGYSDLAG----LsniewDASQVSGHVMSNFLDDPTVIRSL 563
Cdd:cd06457 385 VCNFPPPSGS--SPTLLSHSEVETLFHEMGHAMHSMLGRTRYQHVSGtrcaT-----DFVELPSILMEHFASDPRVLSLF 457
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 564 SGHFSSGEPLEAELSQKMRLLKTQLAGYNLCQDLYLADLDVELHRSNA-----FWLEVVRKLWPVYQCMPlDKKDAHPCs 638
Cdd:cd06457 458 ARHYRTGEPLPEELLEKLCASKKLFSALETQQQILYALLDQVLHSEDPldssfDSTDILAELQNEYGLLP-YVPGTAWQ- 535
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 639 ltdifagdwaaAQFSH-----------LYSRLIAADI-SSSFAE---QRSeenyavVGRRYKQTFLSCGGSVPTAEVFRR 703
Cdd:cd06457 536 -----------LRFGHlvgygatyysyLFDRAIASKIwQKLFAKdplSRE------AGERLREEVLKHGGGRDPWEMLAD 598
                       490
                ....*....|....*
gi 21356111 704 FQGRDPSAEALLKSL 718
Cdd:cd06457 599 LLGEEELAEGLVEAM 613
M3_like cd06258
M3-like Peptidases, zincin metallopeptidases, include M2_ACE, M3A, M3B_PepF, and M32 families; ...
284-718 1.09e-10

M3-like Peptidases, zincin metallopeptidases, include M2_ACE, M3A, M3B_PepF, and M32 families; The peptidase M3-like family, also called neurolysin-like family, is part of the "zincin" metallopeptidases, and includes the M2, M3 and M32 families of metallopeptidases. The M2 angiotensin converting enzyme (ACE, EC 3.4.15.1) is a membrane-bound, zinc-dependent dipeptidase that catalyzes the conversion of the decapeptide angiotensin I to the potent vasopressor octapeptide angiotensin II. The M3 family is subdivided into two subfamilies: the widespread M3A, which comprises a number of high-molecular mass endo- and exopeptidases from bacteria, archaea, protozoa, fungi, plants and animals, and the small M3B, whose members are enzymes primarily from bacteria. Well-known mammalian/eukaryotic M3A endopeptidases are the thimet oligopeptidase (TOP; endopeptidase 3.4.24.15), neurolysin (alias endopeptidase 3.4.24.16), and the mitochondrial intermediate peptidase. The first two are intracellular oligopeptidases, which act only on relatively short substrates of less than 20 amino acid residues, while the latter cleaves N-terminal octapeptides from proteins during their import into the mitochondria. The M3A subfamily also contains several bacterial endopeptidases, called oligopeptidases A, as well as a large number of bacterial carboxypeptidases, called dipeptidyl peptidases (Dcp; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). M3B subfamily consists of oligopeptidase F (PepF) which hydrolyzes peptides containing 7-17 amino acid residues with fairly broad specificity. Peptidases in the M3 family contain the HEXXH motif that forms part of the active site in conjunction with a C-terminally-located Glutamic acid (Glu) residue. A single zinc ion is ligated by the side-chains of the two Histidine (His) residues, and the more C-terminal Glu. Most of the peptidases are synthesized without signal peptides or propeptides, and function intracellularly. There are similarities to the thermostable carboxypeptidases from Pyrococcus furiosus carboxypeptidase (PfuCP), and Thermus aquaticus (TaqCP), belonging to peptidase family M32. Little is known about function of this family, including carboxypeptidases Taq and Pfu.


Pssm-ID: 341049 [Multi-domain]  Cd Length: 473  Bit Score: 64.37  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 284 KASSQQEKSLENSTHIEKIRGLRKRQANLLGYESFADMSMQTKMVG-SVDNLKQIFAKLLKFAGPAQSVELEKLQGFAQD 362
Cdd:cd06258  93 TLLSDFSKLWELRPLLEKLVELRNQAARLLGYEDPYDALLDLYEAGySTEVVEQDFEELKQAIPLLYKELHAIQRPKLHR 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 363 SGCEYKLEAYDVaywrrkqlaaehglQDQKLREFFPLPRVLSGLFALSEKLFGIKIveqpnaevwhpavkfydvfdadsv 442
Cdd:cd06258 173 DYGFYYIPKFDV--------------TSAMLKQKFDAEWMFEGALWFLQELGLEPG------------------------ 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 443 nssTPVGGFYVDCYSKEHKfgRNNGWMVGIRNSNksagltplCALIFNFSEPQspdakppllgyDDLQMLFKTFGSGLQH 522
Cdd:cd06258 215 ---PLLTWERLDLYAPLGK--VCHAFATDFGRKD--------VRITTNYTVTR-----------DDILTTHHEFGHALYE 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 523 LLTQAGYSDLAGLSNIEWDASQvsGHVMSNFLDDPtvIRSLSGHFSSGEPLEAELSQKMRLLKTQLAGYNLCQDLYLADL 602
Cdd:cd06258 271 LQYRTRFAFLGNGASLGFHESQ--SQFLENSVGTF--KHLYSKHLLSGPQMDDESEEKFLLARLLDKVTFLPHIILVDKW 346
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356111 603 DVELH-------RSNAFWLEVVRKLWPVYQCMPLDKKDAHPCSLTDIFAGDwaAAQF-SHLYSRLIAADISSSFAEQRSE 674
Cdd:cd06258 347 EWAVFsgeipkkPDLPSWWNLLYKEYLGVPPVPRDETYTDGWAQFHHWAGY--DGYYiRYALGQVYAFQFYEKLCEDAGH 424
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 21356111 675 E------NYAVVGRRYKqTFLSCGGSVPTAEVFRRFQGRDPSAEALLKSL 718
Cdd:cd06258 425 EgkcdigNFDEAGQKLR-EILRLGGSRPPTELLKNATGKEPNIASFLLHI 473
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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