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Conserved domains on  [gi|528491738|ref|XP_005155626|]
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neurolysin, mitochondrial isoform X3 [Danio rerio]

Protein Classification

M3 family metallopeptidase( domain architecture ID 10157865)

M3 family metallopeptidase contains the HEXXH motif that forms the active site in conjunction with a C-terminally-located Glu residue; similar to mammalian TOP (thimet oligopeptidase) or neurolysin, which hydrolyze oligopeptides such as neurotensin, bradykinin and dynorphin A

EC:  3.4.24.-
MEROPS:  M3
PubMed:  7674922|10493853

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M3A_TOP cd06455
Peptidase M3 thimet oligopeptidase (TOP), also includes neurolysin; Peptidase M3 Thimet ...
35-673 0e+00

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: 936.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  35 RHRTEKLIQRIKQANDTVGSVDIGKVCFENTLQVIADAKADYAASRHVLDFPQYVAPCKEVRFASTEADKRLSDFDVEVS 114
Cdd:cd06455    1 LATADEIIAEAKAVLDAIAALPPEDATFENTLLPLDEAENELSDASGPLTFLQSVSPDKEVRDASSEAEKKLSAFSIELS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 115 MRADVFQRLLVLQEKQSCDLLPESERFLGRLIKLGKRNGLHLSEDIQDEIKSISKQISELSIDFNRNLNEENTVLLFSKE 194
Cdd:cd06455   81 MREDLYRLVKAVYDKNEKKLDAESRRLLEKLLRDFRRNGLGLPDEKRERLKELKKEISELSIEFSKNLNEDNTGIWFTEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 195 DLVGLAESYANGLEKTEDGQYKVTLAYPHYFPLMKRCHVPETRRKMEKAFHSRCKDVNTAILEKLIELRARLANLLGFSS 274
Cdd:cd06455  161 ELEGVPEDFLDRLKKDDDGKYKVTLKYPDYFPVMKYAKNPETRKRMYLAFENRAYPENVPLLEEIVALRDELARLLGYKS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 275 HANYMLEMTMAKNSENVARFLDELYERLRPVGEQERHYLLSLKDADCERRGLEfdGQLHAWDMPYYMNQVEQVKFAVDKD 354
Cdd:cd06455  241 HADYVLEDRMAKTPEAVEAFLDDLREKLKPLAEKELAELLALKKEDLPEAGLP--GKLYPWDLAYYSRLLKKEEYSVDEE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 355 KLIEYFPLQVVTEGLLDIYQDLLGLKFQQVEKPHVWHDSVKLYSVLDSVTGNQIGQFYLDLHPREGKYSHAACFGLQPGC 434
Cdd:cd06455  319 KIREYFPLEHVVDGMLDIYEELFGLRFEEVDGAPVWHPDVRLYAVWDDDTGEFLGYLYLDLFPREGKYGHAANFPLQPGF 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 435 VGPDGERRMPVAAMVANFTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQVETDFVEVPSQMLENWVWE 514
Cdd:cd06455  399 TKPDGSRQYPVTALVCNFPKPTADKPSLLKHDEVVTLFHEFGHAMHDLLSRTKYARFHGTSVERDFVEAPSQMLENWCWD 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 515 KEPLRRMSRHYKDDSPIPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKDRA---DTAAEFAKLSKDILGIPA-TP 590
Cdd:cd06455  479 PEVLKRLSKHYKTGEPLPDELIEKLIKSRNFNSGLFYLRQLFLALFDLALHTPDSHealDLTKLWNELREEITLIPGpPE 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 591 GTNMTASFSHLAGGYDGQYYSYLWSEVYSMDIFFTRFKKeGILNPKVGREYRRVVLEAGGSVDGMEMLKTFLGREPCQDA 670
Cdd:cd06455  559 GTHGYASFGHLMGGYDAGYYGYLWSEVFAADMFYTFFKA-DPLNPEVGRRYRDKVLEPGGSRDEMELLEDFLGREPNSDA 637

                 ...
gi 528491738 671 FFQ 673
Cdd:cd06455  638 FLK 640
 
Name Accession Description Interval E-value
M3A_TOP cd06455
Peptidase M3 thimet oligopeptidase (TOP), also includes neurolysin; Peptidase M3 Thimet ...
35-673 0e+00

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: 936.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  35 RHRTEKLIQRIKQANDTVGSVDIGKVCFENTLQVIADAKADYAASRHVLDFPQYVAPCKEVRFASTEADKRLSDFDVEVS 114
Cdd:cd06455    1 LATADEIIAEAKAVLDAIAALPPEDATFENTLLPLDEAENELSDASGPLTFLQSVSPDKEVRDASSEAEKKLSAFSIELS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 115 MRADVFQRLLVLQEKQSCDLLPESERFLGRLIKLGKRNGLHLSEDIQDEIKSISKQISELSIDFNRNLNEENTVLLFSKE 194
Cdd:cd06455   81 MREDLYRLVKAVYDKNEKKLDAESRRLLEKLLRDFRRNGLGLPDEKRERLKELKKEISELSIEFSKNLNEDNTGIWFTEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 195 DLVGLAESYANGLEKTEDGQYKVTLAYPHYFPLMKRCHVPETRRKMEKAFHSRCKDVNTAILEKLIELRARLANLLGFSS 274
Cdd:cd06455  161 ELEGVPEDFLDRLKKDDDGKYKVTLKYPDYFPVMKYAKNPETRKRMYLAFENRAYPENVPLLEEIVALRDELARLLGYKS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 275 HANYMLEMTMAKNSENVARFLDELYERLRPVGEQERHYLLSLKDADCERRGLEfdGQLHAWDMPYYMNQVEQVKFAVDKD 354
Cdd:cd06455  241 HADYVLEDRMAKTPEAVEAFLDDLREKLKPLAEKELAELLALKKEDLPEAGLP--GKLYPWDLAYYSRLLKKEEYSVDEE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 355 KLIEYFPLQVVTEGLLDIYQDLLGLKFQQVEKPHVWHDSVKLYSVLDSVTGNQIGQFYLDLHPREGKYSHAACFGLQPGC 434
Cdd:cd06455  319 KIREYFPLEHVVDGMLDIYEELFGLRFEEVDGAPVWHPDVRLYAVWDDDTGEFLGYLYLDLFPREGKYGHAANFPLQPGF 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 435 VGPDGERRMPVAAMVANFTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQVETDFVEVPSQMLENWVWE 514
Cdd:cd06455  399 TKPDGSRQYPVTALVCNFPKPTADKPSLLKHDEVVTLFHEFGHAMHDLLSRTKYARFHGTSVERDFVEAPSQMLENWCWD 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 515 KEPLRRMSRHYKDDSPIPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKDRA---DTAAEFAKLSKDILGIPA-TP 590
Cdd:cd06455  479 PEVLKRLSKHYKTGEPLPDELIEKLIKSRNFNSGLFYLRQLFLALFDLALHTPDSHealDLTKLWNELREEITLIPGpPE 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 591 GTNMTASFSHLAGGYDGQYYSYLWSEVYSMDIFFTRFKKeGILNPKVGREYRRVVLEAGGSVDGMEMLKTFLGREPCQDA 670
Cdd:cd06455  559 GTHGYASFGHLMGGYDAGYYGYLWSEVFAADMFYTFFKA-DPLNPEVGRRYRDKVLEPGGSRDEMELLEDFLGREPNSDA 637

                 ...
gi 528491738 671 FFQ 673
Cdd:cd06455  638 FLK 640
Peptidase_M3 pfam01432
Peptidase family M3; This is the Thimet oligopeptidase family, large family of mammalian and ...
227-677 5.71e-175

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: 506.92  E-value: 5.71e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  227 LMKRCHVPETRRKMEKAFHSRCKDV-----NTAILEKLIELRARLANLLGFSSHANYMLEMTMAKNSENVARFLDELYER 301
Cdd:pfam01432   1 LLKESPDRETRKKAYRAFYSRAEAYrntleNSALLEELLKLRAELAKLLGYPSYAEASLEDKMAKIPETVYDFLEELVNK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  302 LRPVGEQERHYLLSLKDADCErrglefDGQLHAWDMPYYMNQVEQVKFA-VDKDKLIEYFPL-QVVTEGLLDIYQDLLGL 379
Cdd:pfam01432  81 LRPLLHRELELLKKLKKKELG------LEELQPWDVAYYSEKQREELYDpLDQEELRPYFPLeQVLEKGLFGLFERLFGI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  380 KFQQVEKPHVWHDSVKLYSVLDSVTGNQIGQFYLDLHPREGKYSHAACFGLQPGCVGPdgerrmpVAAMVANFTKPTSTW 459
Cdd:pfam01432 155 TFVLEPLGEVWHEDVRFYSVFDELSGGLIGEFYLDLYPRKGKRGGAYSFGLVPGRKDP-------VPYLLCNFTKPSSGK 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  460 PSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQVETDFVEVPSQMLENWVWEKEPLRRMSRHYKDDSPIPDALLDKL 539
Cdd:pfam01432 228 PSLLTHDDVETLFHEFGHSMHSLLSRTEYSYVSGTNVPIDFAEIPSQFNENWLWEPLLLNLLSRHYETGEPIPAELLEKL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  540 IASRVANTGLMNLRQIVLSKADQTLHTKDRADTA-----AEFAKLSKDILGIPATPGTNMTASFSHL-AGGYDGQYYSYL 613
Cdd:pfam01432 308 IKSKNVNAGLFLFRQLMFAAFDQEIHEAAEEDQKldfllEEYAELNKKYYGDPVTPDEASPLSFSHIfPHGYAANYYSYL 387
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528491738  614 WSEVYSMDIfFTRFKKEGILNPKVGREYRRVVLEAGGSVDGMEMLKTFLGREPCQDAFFQCKGL 677
Cdd:pfam01432 388 YATGLALDI-FEKFFEQDPLNRETGLRYYLEFLSRGGSLDPLELLKKFGGRMPSADALLRALGL 450
Dcp COG0339
Zn-dependent oligopeptidase, M3 family [Posttranslational modification, protein turnover, ...
105-680 2.41e-169

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


Pssm-ID: 440108 [Multi-domain]  Cd Length: 682  Bit Score: 500.73  E-value: 2.41e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 105 RLSDFDVEVSMRADVFQRLLVLQE-KQSCDLLPESERFLGRLIKLGKRNGLHLSEDIQDEIKSISKQISELSIDFNRN-L 182
Cdd:COG0339   99 KLSAHSDEIGLNEALFARIKALYDsRDFLGLDPEQKRLLENTLRDFVLSGAALPEEDKARLREINEELAELSTKFSQNvL 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 183 NEEN--TVLLFSKEDLVGLAES-----YANGLEKTEDGqYKVTLAYPHYFPLMKRCHVPETRRKMEKAFHSRCKDV---- 251
Cdd:COG0339  179 DATNawALVVTDEAELAGLPESaiaaaAAAAKARGLEG-WLITLDNPSYQPVLTYADNRELREKLYRAYVTRASDGgefd 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 252 NTAILEKLIELRARLANLLGFSSHANYMLEMTMAKNSENVARFLDELYERLRPVGEQERHYLLSLKDADCErrglefDGQ 331
Cdd:COG0339  258 NRPIIAEILALRAEKAKLLGYANYAEYSLADKMAKTPEAVLDFLRDLAPAAKPAAERELAELQAFAAEEGG------IFD 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 332 LHAWDMPYYMNQVEQVKFAVDKDKLIEYFPLQVVTEGLLDIYQDLLGLKFQQVEKPHVWHDSVKLYSVLDSvTGNQIGQF 411
Cdd:COG0339  332 LEPWDWAYYAEKLRQARYDLDEEELKPYFPLDRVLDGLFEVAERLYGLTFKERKDVPVYHPDVRVFEVFDA-DGELLGLF 410
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 412 YLDLHPREGKYSHAACfglqPGCVG---PDGERRMPVAAMVANFTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRY 488
Cdd:COG0339  411 YLDLYAREGKRGGAWM----DSFRSqsrLDGELQLPVAYNVCNFTKPVGGKPALLTHDEVTTLFHEFGHALHGMLTDVDY 486
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 489 ADFSGTQVETDFVEVPSQMLENWVWEKEPLRRMSRHYKDDSPIPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKD 568
Cdd:COG0339  487 PSLSGTNVPWDFVELPSQFMENWCWEPEVLALFARHYETGEPLPDELLDKLLAARNFNSGFATLRQLEFALLDMALHTLY 566
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 569 RADTAAEFAKLSKDILG----IPATPGTNMTASFSHL-AGGYDGQYYSYLWSEVYSMDIfFTRFKKEGILNPKVGREYRR 643
Cdd:COG0339  567 DPEAGADVLAFEAEVLAevgvLPPVPPRRFSTYFSHIfAGGYAAGYYSYKWAEVLDADA-FSAFEEAGIFDRETGQRFRD 645
                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 528491738 644 VVLEAGGSVDGMEMLKTFLGREPCQDAFFQCKGLTQS 680
Cdd:COG0339  646 EILSRGGSRDPMELFKAFRGREPSIDALLRHRGLAAA 682
PRK10911 PRK10911
oligopeptidase A; Provisional
152-677 2.14e-108

oligopeptidase A; Provisional


Pssm-ID: 182832 [Multi-domain]  Cd Length: 680  Bit Score: 343.34  E-value: 2.14e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 152 NGLHLSEDIQDEIKSISKQISELSIDFNRNLNEEN---TVLLFSKEDLVGLAES-----YANGLEKTEDGqYKVTLAYPH 223
Cdd:PRK10911 140 SGIGLPKEKQQRYGEIAARLSELGNQYSNNVLDATmgwTKLITDEAELAGMPESalaaaKAQAEAKEQEG-YLLTLDIPS 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 224 YFPLMKRCHVPETRRKMEKAFHSRCKDV--------NTAILEKLIELRARLANLLGFSSHANYMLEMTMAKNSENVARFL 295
Cdd:PRK10911 219 YLPVMTYCDNQALREEMYRAYSTRASDQgpnagkwdNSEVMEEILALRHELAQLLGFENYADKSLATKMAENPQQVLDFL 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 296 DELYERLRPVGEQErhyLLSLKDADCERRGLEfdgQLHAWDMPYYMNQVEQVKFAVDKDKLIEYFPLQVVTEGLLDIYQD 375
Cdd:PRK10911 299 TDLAKRARPQGEKE---LAQLRAFAKAEFGVD---ELQPWDIAYYSEKQKQHLYSISDEQLRPYFPENKAVNGLFEVVKR 372
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 376 LLGLKFQQVEKPHVWHDSVKLYSVLDSvTGNQIGQFYLDLHPREGKYSHAacfgLQPGCVG----PDGERRMPVAAMVAN 451
Cdd:PRK10911 373 IYGITAKERKDVDVWHPDVRFFELYDE-NNELRGSFYLDLYARENKRGGA----WMDDCVGqmrkADGSLQKPVAYLTCN 447
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 452 FTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQ-VETDFVEVPSQMLENWVWEKEPLRRMSRHYKDDSP 530
Cdd:PRK10911 448 FNRPVNGKPALFTHDEVITLFHEFGHGLHHMLTRIETAGVSGISgVPWDAVELPSQFMENWCWEPEALAFISGHYETGEP 527
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 531 IPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKDRADTAAE----FAKLSKDILGIPATPGTNMTASFSHL-AGGY 605
Cdd:PRK10911 528 LPKELLDKMLAAKNYQAALFILRQLEFGLFDFRLHAEFDPDQGAKiletLAEIKKQVAVVPSPSWGRFPHAFSHIfAGGY 607
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528491738 606 DGQYYSYLWSEVYSMDIfFTRFKKEGILNPKVGREYRRVVLEAGGSVDGMEMLKTFLGREPCQDAFFQCKGL 677
Cdd:PRK10911 608 AAGYYSYLWADVLAADA-FSRFEEEGIFNRETGQSFLDNILSRGGSEEPMELFKRFRGREPQLDAMLEHYGI 678
 
Name Accession Description Interval E-value
M3A_TOP cd06455
Peptidase M3 thimet oligopeptidase (TOP), also includes neurolysin; Peptidase M3 Thimet ...
35-673 0e+00

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: 936.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  35 RHRTEKLIQRIKQANDTVGSVDIGKVCFENTLQVIADAKADYAASRHVLDFPQYVAPCKEVRFASTEADKRLSDFDVEVS 114
Cdd:cd06455    1 LATADEIIAEAKAVLDAIAALPPEDATFENTLLPLDEAENELSDASGPLTFLQSVSPDKEVRDASSEAEKKLSAFSIELS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 115 MRADVFQRLLVLQEKQSCDLLPESERFLGRLIKLGKRNGLHLSEDIQDEIKSISKQISELSIDFNRNLNEENTVLLFSKE 194
Cdd:cd06455   81 MREDLYRLVKAVYDKNEKKLDAESRRLLEKLLRDFRRNGLGLPDEKRERLKELKKEISELSIEFSKNLNEDNTGIWFTEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 195 DLVGLAESYANGLEKTEDGQYKVTLAYPHYFPLMKRCHVPETRRKMEKAFHSRCKDVNTAILEKLIELRARLANLLGFSS 274
Cdd:cd06455  161 ELEGVPEDFLDRLKKDDDGKYKVTLKYPDYFPVMKYAKNPETRKRMYLAFENRAYPENVPLLEEIVALRDELARLLGYKS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 275 HANYMLEMTMAKNSENVARFLDELYERLRPVGEQERHYLLSLKDADCERRGLEfdGQLHAWDMPYYMNQVEQVKFAVDKD 354
Cdd:cd06455  241 HADYVLEDRMAKTPEAVEAFLDDLREKLKPLAEKELAELLALKKEDLPEAGLP--GKLYPWDLAYYSRLLKKEEYSVDEE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 355 KLIEYFPLQVVTEGLLDIYQDLLGLKFQQVEKPHVWHDSVKLYSVLDSVTGNQIGQFYLDLHPREGKYSHAACFGLQPGC 434
Cdd:cd06455  319 KIREYFPLEHVVDGMLDIYEELFGLRFEEVDGAPVWHPDVRLYAVWDDDTGEFLGYLYLDLFPREGKYGHAANFPLQPGF 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 435 VGPDGERRMPVAAMVANFTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQVETDFVEVPSQMLENWVWE 514
Cdd:cd06455  399 TKPDGSRQYPVTALVCNFPKPTADKPSLLKHDEVVTLFHEFGHAMHDLLSRTKYARFHGTSVERDFVEAPSQMLENWCWD 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 515 KEPLRRMSRHYKDDSPIPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKDRA---DTAAEFAKLSKDILGIPA-TP 590
Cdd:cd06455  479 PEVLKRLSKHYKTGEPLPDELIEKLIKSRNFNSGLFYLRQLFLALFDLALHTPDSHealDLTKLWNELREEITLIPGpPE 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 591 GTNMTASFSHLAGGYDGQYYSYLWSEVYSMDIFFTRFKKeGILNPKVGREYRRVVLEAGGSVDGMEMLKTFLGREPCQDA 670
Cdd:cd06455  559 GTHGYASFGHLMGGYDAGYYGYLWSEVFAADMFYTFFKA-DPLNPEVGRRYRDKVLEPGGSRDEMELLEDFLGREPNSDA 637

                 ...
gi 528491738 671 FFQ 673
Cdd:cd06455  638 FLK 640
M3A cd09605
Peptidase M3A family includes thimet oligopeptidase, dipeptidyl carboxypeptidase and ...
35-675 0e+00

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: 729.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  35 RHRTEKLIQRIKQANDTVGSVDIGKVCFENTLQVIADAKADYAASRHVLDFPQYVAPCKEVRFASTEADKRLSDFDVEVS 114
Cdd:cd09605    1 PERFHELIEQTKRVYDLVGTRACSTPPYENTLLALADLEVTLTRVRDLLDFPQHAHPEPEFREASEEADKKLSEFDEEMS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 115 MRADVFQRLLVLQE-KQSCDLLPESERFLGRLIKLGKRNGLHLSEDIQDEIKSISKQISELSIDFNRNLNeentvllfsk 193
Cdd:cd09605   81 MNEDLYQRIVKLQEdKKLVSLDPEARRYLELFIKDFERNGLHLDKEKRKRIKDLNKKISDLCSDFNKNLN---------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 194 edlvglaesyanglektedgqykvtlayphyfplmkrchvPETRRKMEKAFHSRCKDVNTAILEKLIELRARLANLLGFS 273
Cdd:cd09605  151 ----------------------------------------PETREKAEKAFLTRCKAENLAILQELLSLRAQLAKLLGYS 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 274 SHANYMLEMTMAKNSENVARFLDELYERLRPVGEQERHYLLSLKDADCErrgleFDGQLHAWDMPYYMNQVEQVKFAVDK 353
Cdd:cd09605  191 THADRVLEGNMAKTPETVAQFLDELSQKLKPRGEKEREMILGLKMKECE-----QDGEIMPWDPPYYMGQVREERYNVDQ 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 354 DKLIEYFPLQVVTEGLLDIYQDLLGLKFQQVEKPHVWHDSVKLYSVLDSVTGNqIGQFYLDLHPREGKYSHAACFGLQPG 433
Cdd:cd09605  266 SLLKPYFPLGVVTEGLLIIYNELLGISFYAEQDAEVWHEDVRLYTVVDEAEEV-LGYFYLDFFPREGKYGHAACFGLQPG 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 434 CVGPDGERRMPVAAMVANFTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQVETDFVEVPSQMLENWVW 513
Cdd:cd09605  345 CLKEDGSRQLPVAALVLNFPKPSAGSPSLLTHDEVRTLFHEFGHVMHQLCARTRYAHFSGTNVPTDFVEVPSQMLENWAW 424
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 514 EKEPLRRMSRHYKDDSPIPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKD--RADTAAEFAKLSKDILGIPATPG 591
Cdd:cd09605  425 DVNQFARHSRHYQSGAPLPDELLEKLCESRLVNTGLDMLRQIVLAKLDQILHTKHplRNDTADELAELCEEILGLPATPG 504
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 592 TNMTASFSHLAGGYDGQYYSYLWSEVYSMDIFFTRFKKEGiLNPKVGREYRRVVLEAGGSVDGMEMLKTFLGREPCQDAF 671
Cdd:cd09605  505 TNMPATFGHLAGGYDAQYYGYLWSEVVAMDMFHECFKQEP-LNREVGMRYRREILAPGGSEDPMLMLRGFLQKCPKQSAF 583

                 ....
gi 528491738 672 FQCK 675
Cdd:cd09605  584 LFSR 587
M3A_DCP cd06456
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ...
62-677 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: 540.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  62 FENTLQVI--ADAKADYAAS--RHVLdfpqYVAPCKEVRFASTEADKRLSDFDVEVSMRADVFQRLLVLQE-KQSCDLLP 136
Cdd:cd06456   30 FENTIEPLerAGEPLDRVWGvfSHLN----SVNNSDELRAAYEEVLPLLSAHSDAIGQNEALFARVKALYDsREALGLDP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 137 ESERFLGRLIKLGKRNGLHLSEDIQDEIKSISKQISELSIDFNRN-LNEEN--TVLLFSKEDLVGLAES----YANGLEK 209
Cdd:cd06456  106 EQKRLLEKTLRDFVLSGAALSEEKKERLAEINEELSELSTKFSQNvLDATNafSLVITDEAELAGLPESalaaAAEAAKA 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 210 TEDGQYKVTLAYPHYFPLMKRCHVPETRRKMEKAFHSRCKDV----NTAILEKLIELRARLANLLGFSSHANYMLEMTMA 285
Cdd:cd06456  186 RGKGGWLFTLDAPSYQPFLTYCDNRELREKVYRAYVTRASDGgefdNSPIIEEILALRAEKAKLLGYKNYAEYSLATKMA 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 286 KNSENVARFLDELYERLRPVGEQERHYLLSLKDADcerrglEFDGQLHAWDMPYYMNQVEQVKFAVDKDKLIEYFPLQVV 365
Cdd:cd06456  266 KSPEAVLEFLEDLAEKAKPAAEKELAELQAFAKEE------GGGDKLEPWDWAYYAEKLRKEKYDLDEEELRPYFPLDRV 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 366 TEGLLDIYQDLLGLKFQQVEKPHVWHDSVKLYSVLDSvTGNQIGQFYLDLHPREGKYSHAACFGLQPGCVGPDGERRmPV 445
Cdd:cd06456  340 LEGLFELAERLYGITFKERDDVPVWHPDVRVYEVFDA-DGELLGLFYLDLYARPGKRGGAWMDSFRSRSRLLDSGQL-PV 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 446 AAMVANFTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQVETDFVEVPSQMLENWVWEKEPLRRMSRHY 525
Cdd:cd06456  418 AYLVCNFTPPAGGKPALLSHDEVETLFHEFGHALHHLLTDVDYPSVSGTNVVWDFVELPSQFMENWAWEPEVLKLYARHY 497
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 526 KDDSPIPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKDRADTAAEFAKLSKDIL---GIPATPGTN-MTASFSHL 601
Cdd:cd06456  498 ETGEPLPDELIEKLLAARNFNAGFATLRQLAFALLDLALHSLYDPEAPEDVDAFEREVLkeyGVLPPIPPRrRSCSFSHI 577
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528491738 602 -AGGYDGQYYSYLWSEVYSMDIfFTRFKKEGILNPKVGREYRRVVLEAGGSVDGMEMLKTFLGREPCQDAFFQCKGL 677
Cdd:cd06456  578 fSGGYAAGYYSYLWAEVLAADA-FSAFEEAGGFNRETGRRFRDTILSRGGSRDPMELFRAFRGRDPDIDALLRRRGL 653
Peptidase_M3 pfam01432
Peptidase family M3; This is the Thimet oligopeptidase family, large family of mammalian and ...
227-677 5.71e-175

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: 506.92  E-value: 5.71e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  227 LMKRCHVPETRRKMEKAFHSRCKDV-----NTAILEKLIELRARLANLLGFSSHANYMLEMTMAKNSENVARFLDELYER 301
Cdd:pfam01432   1 LLKESPDRETRKKAYRAFYSRAEAYrntleNSALLEELLKLRAELAKLLGYPSYAEASLEDKMAKIPETVYDFLEELVNK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  302 LRPVGEQERHYLLSLKDADCErrglefDGQLHAWDMPYYMNQVEQVKFA-VDKDKLIEYFPL-QVVTEGLLDIYQDLLGL 379
Cdd:pfam01432  81 LRPLLHRELELLKKLKKKELG------LEELQPWDVAYYSEKQREELYDpLDQEELRPYFPLeQVLEKGLFGLFERLFGI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  380 KFQQVEKPHVWHDSVKLYSVLDSVTGNQIGQFYLDLHPREGKYSHAACFGLQPGCVGPdgerrmpVAAMVANFTKPTSTW 459
Cdd:pfam01432 155 TFVLEPLGEVWHEDVRFYSVFDELSGGLIGEFYLDLYPRKGKRGGAYSFGLVPGRKDP-------VPYLLCNFTKPSSGK 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  460 PSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQVETDFVEVPSQMLENWVWEKEPLRRMSRHYKDDSPIPDALLDKL 539
Cdd:pfam01432 228 PSLLTHDDVETLFHEFGHSMHSLLSRTEYSYVSGTNVPIDFAEIPSQFNENWLWEPLLLNLLSRHYETGEPIPAELLEKL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  540 IASRVANTGLMNLRQIVLSKADQTLHTKDRADTA-----AEFAKLSKDILGIPATPGTNMTASFSHL-AGGYDGQYYSYL 613
Cdd:pfam01432 308 IKSKNVNAGLFLFRQLMFAAFDQEIHEAAEEDQKldfllEEYAELNKKYYGDPVTPDEASPLSFSHIfPHGYAANYYSYL 387
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528491738  614 WSEVYSMDIfFTRFKKEGILNPKVGREYRRVVLEAGGSVDGMEMLKTFLGREPCQDAFFQCKGL 677
Cdd:pfam01432 388 YATGLALDI-FEKFFEQDPLNRETGLRYYLEFLSRGGSLDPLELLKKFGGRMPSADALLRALGL 450
Dcp COG0339
Zn-dependent oligopeptidase, M3 family [Posttranslational modification, protein turnover, ...
105-680 2.41e-169

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


Pssm-ID: 440108 [Multi-domain]  Cd Length: 682  Bit Score: 500.73  E-value: 2.41e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 105 RLSDFDVEVSMRADVFQRLLVLQE-KQSCDLLPESERFLGRLIKLGKRNGLHLSEDIQDEIKSISKQISELSIDFNRN-L 182
Cdd:COG0339   99 KLSAHSDEIGLNEALFARIKALYDsRDFLGLDPEQKRLLENTLRDFVLSGAALPEEDKARLREINEELAELSTKFSQNvL 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 183 NEEN--TVLLFSKEDLVGLAES-----YANGLEKTEDGqYKVTLAYPHYFPLMKRCHVPETRRKMEKAFHSRCKDV---- 251
Cdd:COG0339  179 DATNawALVVTDEAELAGLPESaiaaaAAAAKARGLEG-WLITLDNPSYQPVLTYADNRELREKLYRAYVTRASDGgefd 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 252 NTAILEKLIELRARLANLLGFSSHANYMLEMTMAKNSENVARFLDELYERLRPVGEQERHYLLSLKDADCErrglefDGQ 331
Cdd:COG0339  258 NRPIIAEILALRAEKAKLLGYANYAEYSLADKMAKTPEAVLDFLRDLAPAAKPAAERELAELQAFAAEEGG------IFD 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 332 LHAWDMPYYMNQVEQVKFAVDKDKLIEYFPLQVVTEGLLDIYQDLLGLKFQQVEKPHVWHDSVKLYSVLDSvTGNQIGQF 411
Cdd:COG0339  332 LEPWDWAYYAEKLRQARYDLDEEELKPYFPLDRVLDGLFEVAERLYGLTFKERKDVPVYHPDVRVFEVFDA-DGELLGLF 410
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 412 YLDLHPREGKYSHAACfglqPGCVG---PDGERRMPVAAMVANFTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRY 488
Cdd:COG0339  411 YLDLYAREGKRGGAWM----DSFRSqsrLDGELQLPVAYNVCNFTKPVGGKPALLTHDEVTTLFHEFGHALHGMLTDVDY 486
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 489 ADFSGTQVETDFVEVPSQMLENWVWEKEPLRRMSRHYKDDSPIPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKD 568
Cdd:COG0339  487 PSLSGTNVPWDFVELPSQFMENWCWEPEVLALFARHYETGEPLPDELLDKLLAARNFNSGFATLRQLEFALLDMALHTLY 566
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 569 RADTAAEFAKLSKDILG----IPATPGTNMTASFSHL-AGGYDGQYYSYLWSEVYSMDIfFTRFKKEGILNPKVGREYRR 643
Cdd:COG0339  567 DPEAGADVLAFEAEVLAevgvLPPVPPRRFSTYFSHIfAGGYAAGYYSYKWAEVLDADA-FSAFEEAGIFDRETGQRFRD 645
                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 528491738 644 VVLEAGGSVDGMEMLKTFLGREPCQDAFFQCKGLTQS 680
Cdd:COG0339  646 EILSRGGSRDPMELFKAFRGREPSIDALLRHRGLAAA 682
M3A_MIP cd06457
Peptidase M3 mitochondrial intermediate peptidase (MIP); Peptidase M3 mitochondrial ...
32-666 1.13e-126

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: 388.45  E-value: 1.13e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  32 EEIRHRTEKLIQRIKQANDTVGSVDIGKVcFE---NTLQVIADAkADYAasRHVldfpqyvAPCKEVRFASTEADKRLSD 108
Cdd:cd06457   19 RETLARCEDLVDRILNDDSPNESRKVVKL-LDdlsDTLCRVIDL-AEFV--RNV-------HPDPEFVEAAEEAYEELSE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 109 FdVEvSMRADV--FQRLLVLQEKQSC--DLLPESERFLGRLIKLGKRNGLHLSEDIQDEIKSISKQISELSIDFNRNLNE 184
Cdd:cd06457   88 Y-MN-ELNTNTglYDALKRVLEDPEIvaSLTEEERRVAKLLLRDFEKSGIHLPEEKRKKFVELSSEILSLGREFLQNASA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 185 ENtvllfskedlvglaesyanglektedgqykvtlayphyfplmkrchvPETRRKMEKAFHSRCKDvNTAILEKLIELRA 264
Cdd:cd06457  166 PD-----------------------------------------------EEVRKKVYLAYHSSSEE-QEEVLEELLKARA 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 265 RLANLLGFSSHANYMLEMTMAKNSENVARFLDELYERLRPVGEQERHYLLSLKDADCerrgLEFDGQLHAWDMPYYMNQV 344
Cdd:cd06457  198 ELAQLLGFPSYAHRALRDKMAKSPENVLSFLETLSDSLRPKAEKELEELRKLKRKHE----GLSSPTLMPWDRDYYTGLL 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 345 EQVKFAVDKDKLIEYFPLQVVTEGLLDIYQDLLGLKFQQVE-KPH-VWHDSVKLYSVLDSvTGNQIGQFYLDLHPREGKY 422
Cdd:cd06457  274 RAQARSSDASELSPYFSLGTVMEGLSRLFSRLYGIRLVPVPtQPGeVWHPDVRKLEVVHE-TEGLLGTIYCDLFERPGKP 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 423 SHAACFGLQPGC------VGPDGERRMPVAAMVANFTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQV 496
Cdd:cd06457  353 PGAAHFTIRCSRrlddddLGDGGSYQLPVVVLVCNFPPPSGSSPTLLSHSEVETLFHEMGHAMHSMLGRTRYQHVSGTRC 432
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 497 ETDFVEVPSQMLENWVWEKEPLRRMSRHYKDDSPIPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKD----RADT 572
Cdd:cd06457  433 ATDFVELPSILMEHFASDPRVLSLFARHYRTGEPLPEELLEKLCASKKLFSALETQQQILYALLDQVLHSEDpldsSFDS 512
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 573 AAEFAKLSKDILGIPATPGTNMTASFSHLAgGYDGQYYSYLWSEVYSMDIFFTRFKKeGILNPKVGREYRRVVLEAGGSV 652
Cdd:cd06457  513 TDILAELQNEYGLLPYVPGTAWQLRFGHLV-GYGATYYSYLFDRAIASKIWQKLFAK-DPLSREAGERLREEVLKHGGGR 590
                        650
                 ....*....|....
gi 528491738 653 DGMEMLKTFLGREP 666
Cdd:cd06457  591 DPWEMLADLLGEEE 604
PRK10911 PRK10911
oligopeptidase A; Provisional
152-677 2.14e-108

oligopeptidase A; Provisional


Pssm-ID: 182832 [Multi-domain]  Cd Length: 680  Bit Score: 343.34  E-value: 2.14e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 152 NGLHLSEDIQDEIKSISKQISELSIDFNRNLNEEN---TVLLFSKEDLVGLAES-----YANGLEKTEDGqYKVTLAYPH 223
Cdd:PRK10911 140 SGIGLPKEKQQRYGEIAARLSELGNQYSNNVLDATmgwTKLITDEAELAGMPESalaaaKAQAEAKEQEG-YLLTLDIPS 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 224 YFPLMKRCHVPETRRKMEKAFHSRCKDV--------NTAILEKLIELRARLANLLGFSSHANYMLEMTMAKNSENVARFL 295
Cdd:PRK10911 219 YLPVMTYCDNQALREEMYRAYSTRASDQgpnagkwdNSEVMEEILALRHELAQLLGFENYADKSLATKMAENPQQVLDFL 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 296 DELYERLRPVGEQErhyLLSLKDADCERRGLEfdgQLHAWDMPYYMNQVEQVKFAVDKDKLIEYFPLQVVTEGLLDIYQD 375
Cdd:PRK10911 299 TDLAKRARPQGEKE---LAQLRAFAKAEFGVD---ELQPWDIAYYSEKQKQHLYSISDEQLRPYFPENKAVNGLFEVVKR 372
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 376 LLGLKFQQVEKPHVWHDSVKLYSVLDSvTGNQIGQFYLDLHPREGKYSHAacfgLQPGCVG----PDGERRMPVAAMVAN 451
Cdd:PRK10911 373 IYGITAKERKDVDVWHPDVRFFELYDE-NNELRGSFYLDLYARENKRGGA----WMDDCVGqmrkADGSLQKPVAYLTCN 447
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 452 FTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQ-VETDFVEVPSQMLENWVWEKEPLRRMSRHYKDDSP 530
Cdd:PRK10911 448 FNRPVNGKPALFTHDEVITLFHEFGHGLHHMLTRIETAGVSGISgVPWDAVELPSQFMENWCWEPEALAFISGHYETGEP 527
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 531 IPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKDRADTAAE----FAKLSKDILGIPATPGTNMTASFSHL-AGGY 605
Cdd:PRK10911 528 LPKELLDKMLAAKNYQAALFILRQLEFGLFDFRLHAEFDPDQGAKiletLAEIKKQVAVVPSPSWGRFPHAFSHIfAGGY 607
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528491738 606 DGQYYSYLWSEVYSMDIfFTRFKKEGILNPKVGREYRRVVLEAGGSVDGMEMLKTFLGREPCQDAFFQCKGL 677
Cdd:PRK10911 608 AAGYYSYLWADVLAADA-FSRFEEEGIFNRETGQSFLDNILSRGGSEEPMELFKRFRGREPQLDAMLEHYGI 678
M3_like cd06258
M3-like Peptidases, zincin metallopeptidases, include M2_ACE, M3A, M3B_PepF, and M32 families; ...
94-673 1.69e-76

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: 253.12  E-value: 1.69e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738  94 EVRFASTEADKRLSDFDVEVSMRADVFQrllvlQEKQSCDLLPESERFLGRLIKLGKRNGLhlsediqdEIKSISKQISE 173
Cdd:cd06258   27 ERAAALEEASTLLSEFAEEDSLVALALV-----EPELSEPLNEEYKRLVEKIQKLGKAAGA--------IPKELFKEYNT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 174 LSIDFNRNLNeentvllfskedlvglaesyanglektedgqykvtlayphyfplmkrchvpetrrkmekafhsrckdvNT 253
Cdd:cd06258   94 LLSDFSKLWE--------------------------------------------------------------------LR 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 254 AILEKLIELRARLANLLGFSSHANYMLEMTMAK-NSENVARFLDELYERLrPVGEQERHYLLSLKDADCERRGlefdgql 332
Cdd:cd06258  106 PLLEKLVELRNQAARLLGYEDPYDALLDLYEAGySTEVVEQDFEELKQAI-PLLYKELHAIQRPKLHRDYGFY------- 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 333 hawdmpyymnqvEQVKFAVDKDKLIEYFPLQVVTEGLLDIYQDLLGLkfqqvekphvwhdsvklysvldsvTGNQIGQFY 412
Cdd:cd06258  178 ------------YIPKFDVTSAMLKQKFDAEWMFEGALWFLQELGLE------------------------PGPLLTWER 221
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 413 LDLHPREGKYSHAACFGLQpgcvgpdgerrMPVAAMVANFTKptstwpsllQHHEVETFFHEFGHIMHELCSRSRYAdFS 492
Cdd:cd06258  222 LDLYAPLGKVCHAFATDFG-----------RKDVRITTNYTV---------TRDDILTTHHEFGHALYELQYRTRFA-FL 280
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 493 GTQVETDFVEVPSQMLENWVWekEPLRRMSRHYKDDSPIPDALLDKLIASRVANTGLMNLRQIVLSKADQTLH---TKDR 569
Cdd:cd06258  281 GNGASLGFHESQSQFLENSVG--TFKHLYSKHLLSGPQMDDESEEKFLLARLLDKVTFLPHIILVDKWEWAVFsgeIPKK 358
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 570 ADTAAEFAKLSKDILGIPA----TPGTNMTASFSHLAgGYDGQYYSYLWSEVYSMDiFFTRFKKEG--------ILNPKV 637
Cdd:cd06258  359 PDLPSWWNLLYKEYLGVPPvprdETYTDGWAQFHHWA-GYDGYYIRYALGQVYAFQ-FYEKLCEDAghegkcdiGNFDEA 436
                        570       580       590
                 ....*....|....*....|....*....|....*.
gi 528491738 638 GREYRRvVLEAGGSVDGMEMLKTFLGREPCQDAFFQ 673
Cdd:cd06258  437 GQKLRE-ILRLGGSRPPTELLKNATGKEPNIASFLL 471
PRK10280 PRK10280
peptidyl-dipeptidase Dcp;
119-679 1.78e-63

peptidyl-dipeptidase Dcp;


Pssm-ID: 182353  Cd Length: 681  Bit Score: 223.55  E-value: 1.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 119 VFQRL-LVLQEKQSCDLLPESERFLGRLIKLGKRNGLHLSEDIQDEIKSISKQISELSIDFNRNL---NEENTVLLFSKE 194
Cdd:PRK10280 112 LFARVdAVWQQRESLGLDSESIRLVEVIHQRFVLAGAKLAQADKAKLKVLNTEAATLTSQFNQRLlaaNKSGGLVVNDIH 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 195 DLVGLAE-----SYANGLEKTEDGQYKVTLAYPHYFPLMKRCHVPETRRKMEKAFHSRCK--DVNT--AILEKLIELRAR 265
Cdd:PRK10280 192 QLAGLSEqeialAAEAAREKGLDNRWLIPLLNTTQQPALAELRDRQTRENLFAAGWTRAEkgDANDtrAIIQRLVEIRAQ 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 266 LANLLGFSSHANYMLEMTMAKNSENVARFLDELYERLRPVGEQERHYLLSLKDAdcERRGLefdgQLHAWDMPYYMNQVE 345
Cdd:PRK10280 272 QAKLLGFPHYAAWKIADQMAKTPEAALNFMREIVPAARQRASDELASIQAVIDK--QQGGF----SAQAWDWAFYAEQVR 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 346 QVKFAVDKDKLIEYFPLQ-VVTEGLLDIYQDLLGLKFQQVEKPHVWHDSVKLYSVLDSvTGNQIGQFYLDLHPREGKySH 424
Cdd:PRK10280 346 REKYALDEAQLKPYFELNtVLNEGVFWTANQLFGIKFVERFDIPVYHPDVRVWEIFDH-NGVGLALFYGDFFARDSK-SG 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 425 AACFGLQPGCVGPDGERrmPVAAMVANFTKPTSTWPSLLQHHEVETFFHEFGHIMHELCSRSRYADFSGTQVETDFVEVP 504
Cdd:PRK10280 424 GAWMGNFVEQSTLNETR--PVIYNVCNYQKPAAGQPALLLWDDVITLFHEFGHTLHGLFARQRYATLSGTNTPRDFVEFP 501
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 505 SQMLENWVWEKEPLRRMSRHYKDDSPIPDALLDKLIASRVANTGLMNLRQIVLSKADQTLHTKDRADT-----AAEFAKL 579
Cdd:PRK10280 502 SQINEHWASHPQVFARYARHYQSGEAMPDELQEKMRNASLFNKGYDMSELLSAALLDMRWHCLEENEAmqdvdDFELRAL 581
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 580 SKDILGIPATPGTNMTASFSHL-AGGYDGQYYSYLWSEVYSMDiFFTRFKKEGILNPKVGREYRRVVLEAGGSVDGMEML 658
Cdd:PRK10280 582 VAENLDLPAVPPRYRSSYFAHIfGGGYAAGYYAYLWTQMLADD-GYQWFVEQGGLTRENGQRFREAILSRGNSTDLERLY 660
                        570       580
                 ....*....|....*....|.
gi 528491738 659 KTFLGREPCQDAFFQCKGLTQ 679
Cdd:PRK10280 661 RQWRGHAPQIMPMLQHRGLNI 681
M3B_PepF cd09606
Peptidase family M3B, oligopeptidase F (PepF); Peptidase family M3 oligopeptidase F ...
395-528 3.79e-03

Peptidase family M3B, oligopeptidase F (PepF); Peptidase family M3 oligopeptidase F (oligendopeptidase) is mostly bacterial and includes oligoendopeptidase F from Geobacillus stearothermophilus. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids and may cleave proteins at Leu-Gly. The PepF gene is duplicated in Lactococcus lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid.


Pssm-ID: 341069 [Multi-domain]  Cd Length: 543  Bit Score: 40.53  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491738 395 KLYSVLDSVTGNQIgQF-----YLDLHPREGKYSHAACFGLQpgcvgpdgERRMPVaaMVANFTKptstwpsllQHHEVE 469
Cdd:cd09606  283 KMYHELSPETGEFF-DFmrengLLDLESRKGKAPGGYCTYLP--------EYKAPF--IFANFNG---------TSGDVD 342
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528491738 470 TFFHEFGHIMHELCSRsRYADFSGTQVETDFVEVPSQMLENWVWEKeplrrMSRHYKDD 528
Cdd:cd09606  343 VLTHEAGHAFQAYLSR-DLPLPEYRWPTMEAAEIHSMSMELLTWPW-----MELFFGED 395
 
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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