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Conserved domains on  [gi|568973391|ref|XP_006533121|]
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angiotensin-converting enzyme-like protein Ace3 isoform X7 [Mus musculus]

Protein Classification

M2 family metallopeptidase( domain architecture ID 11117514)

M2 family metallopeptidase similar to angiotensin converting enzyme (ACE), a zinc-dependent dipeptidyl carboxypeptidase

EC:  3.4.17.-
MEROPS:  M2
PubMed:  9629165|7674922

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_M2 pfam01401
Angiotensin-converting enzyme; Members of this family are dipeptidyl carboxydipeptidases ...
51-595 0e+00

Angiotensin-converting enzyme; Members of this family are dipeptidyl carboxydipeptidases (cleave carboxyl dipeptides) and most notably convert angiotensin I to angiotensin II. Many members of this family contain a tandem duplication of the 600 amino acid peptidase domain, both of these are catalytically active. Most members are secreted membrane bound ectoenzymes.


:

Pssm-ID: 460196  Cd Length: 581  Bit Score: 895.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391   51 YSEAQAKLFLQFYEQTAQVVLNEFMEATWNYVTNITKQNQKNMLQKEADRSQFMLYFSTRARMFRTDHFLNQDVKRMLRK 130
Cdd:pfam01401   2 TDEAEAREFLEEYNREAEKVLNESTEASWNYNTNITDENAQKMLEASLELAAFTKETAQEAKQFDWSNFQDPDLKRQFKK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  131 LQNIDKSALPTEDLlevtdrgpgrpgthtpapeRRYNRLLTYMETAYNRAEVCL--DEGPCLTLEPDLQEIMATSRDQKE 208
Cdd:pfam01401  82 LSVLGTAALPEDKL-------------------EELNTILSEMESIYSKAKVCLydDPGPCLSLEPDLTEIMATSRDYDE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  209 LLWAWQGWRDAVGRQLRPVFEDYVRLSNKAAQYNGYKDMGALWRSKYESDTLEEDLEQLYKELQPLYLNLHAYVRRSLYR 288
Cdd:pfam01401 143 LLWAWEGWRDAVGKPLRPLYERYVELSNEAAKLNGYADTGAYWRSWYESDTFEEDLERLFQQLKPLYLQLHAYVRRKLRE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  289 YYGPELIDLRGPIPAHLLGNMWAQSWNNILDLVLPYPTKAPEDITAIMKIQHWRPEKMFEEANLFFTSMGMLPAPPAFWI 368
Cdd:pfam01401 223 KYGPDVISLTGPIPAHLLGNMWAQSWSNIYDLVVPFPDKPNIDVTDAMVAQGYTAKKMFEEAEEFFTSLGLLPMPPEFWD 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  369 KSMMEKPADGREVECHTSSWNFYKFNDFRVKKCTEVTLEDLLSVFHQMGHIQYFLQYQNLSVIYQEGASPAFEEAVGSVI 448
Cdd:pfam01401 303 KSMLEKPTDGREVVCHASAWDFYNGKDFRIKMCTEVTMEDFFTVHHEMGHIQYYLQYKDQPVLFREGANPGFHEAVGDVL 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  449 ALSVSSHKYLLARGLLSQPHQDSEEEVNFLLGIALEKIAFIPFSYLVDKFRWKIFDGTISKITYNQEWWNFRLKYQGLCP 528
Cdd:pfam01401 383 ALSVSTPKHLKSIGLLDDVVEDEESDINFLLKQALDKIAFLPFGYLIDKWRWGVFSGEIPPEDYNKRWWELRLKYQGICP 462
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973391  529 PVPRSDDDFDPGAKFHIPANVPYIRYFLGLILQFQLHEALCEASGHVGPLHQCDNYNSKVAGKILGK 595
Cdd:pfam01401 463 PVPRTESDFDPGAKYHVPANVPYIRYFVSFILQFQFHKALCQAAGHTGPLHKCDIYGSKEAGAKLKE 529
 
Name Accession Description Interval E-value
Peptidase_M2 pfam01401
Angiotensin-converting enzyme; Members of this family are dipeptidyl carboxydipeptidases ...
51-595 0e+00

Angiotensin-converting enzyme; Members of this family are dipeptidyl carboxydipeptidases (cleave carboxyl dipeptides) and most notably convert angiotensin I to angiotensin II. Many members of this family contain a tandem duplication of the 600 amino acid peptidase domain, both of these are catalytically active. Most members are secreted membrane bound ectoenzymes.


Pssm-ID: 460196  Cd Length: 581  Bit Score: 895.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391   51 YSEAQAKLFLQFYEQTAQVVLNEFMEATWNYVTNITKQNQKNMLQKEADRSQFMLYFSTRARMFRTDHFLNQDVKRMLRK 130
Cdd:pfam01401   2 TDEAEAREFLEEYNREAEKVLNESTEASWNYNTNITDENAQKMLEASLELAAFTKETAQEAKQFDWSNFQDPDLKRQFKK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  131 LQNIDKSALPTEDLlevtdrgpgrpgthtpapeRRYNRLLTYMETAYNRAEVCL--DEGPCLTLEPDLQEIMATSRDQKE 208
Cdd:pfam01401  82 LSVLGTAALPEDKL-------------------EELNTILSEMESIYSKAKVCLydDPGPCLSLEPDLTEIMATSRDYDE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  209 LLWAWQGWRDAVGRQLRPVFEDYVRLSNKAAQYNGYKDMGALWRSKYESDTLEEDLEQLYKELQPLYLNLHAYVRRSLYR 288
Cdd:pfam01401 143 LLWAWEGWRDAVGKPLRPLYERYVELSNEAAKLNGYADTGAYWRSWYESDTFEEDLERLFQQLKPLYLQLHAYVRRKLRE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  289 YYGPELIDLRGPIPAHLLGNMWAQSWNNILDLVLPYPTKAPEDITAIMKIQHWRPEKMFEEANLFFTSMGMLPAPPAFWI 368
Cdd:pfam01401 223 KYGPDVISLTGPIPAHLLGNMWAQSWSNIYDLVVPFPDKPNIDVTDAMVAQGYTAKKMFEEAEEFFTSLGLLPMPPEFWD 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  369 KSMMEKPADGREVECHTSSWNFYKFNDFRVKKCTEVTLEDLLSVFHQMGHIQYFLQYQNLSVIYQEGASPAFEEAVGSVI 448
Cdd:pfam01401 303 KSMLEKPTDGREVVCHASAWDFYNGKDFRIKMCTEVTMEDFFTVHHEMGHIQYYLQYKDQPVLFREGANPGFHEAVGDVL 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  449 ALSVSSHKYLLARGLLSQPHQDSEEEVNFLLGIALEKIAFIPFSYLVDKFRWKIFDGTISKITYNQEWWNFRLKYQGLCP 528
Cdd:pfam01401 383 ALSVSTPKHLKSIGLLDDVVEDEESDINFLLKQALDKIAFLPFGYLIDKWRWGVFSGEIPPEDYNKRWWELRLKYQGICP 462
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973391  529 PVPRSDDDFDPGAKFHIPANVPYIRYFLGLILQFQLHEALCEASGHVGPLHQCDNYNSKVAGKILGK 595
Cdd:pfam01401 463 PVPRTESDFDPGAKYHVPANVPYIRYFVSFILQFQFHKALCQAAGHTGPLHKCDIYGSKEAGAKLKE 529
M2_ACE cd06461
Peptidase family M2, angiotensin converting enzyme (ACE); Peptidase family M2 angiotensin ...
59-595 0e+00

Peptidase family M2, angiotensin converting enzyme (ACE); Peptidase family 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, by removing two C-terminal amino acids. There are two forms of the enzyme in humans, the ubiquitous somatic ACE and the sperm-specific germinal ACE, both encoded by the same gene through transcription from alternative promoters. Somatic ACE has two tandem active sites with distinct catalytic properties, whereas germinal ACE, the function of which is largely unknown, has just a single active site. Recently, an ACE homolog, ACE2, has been identified in humans that differs from ACE; it preferentially removes carboxy-terminal hydrophobic or basic amino acids and appears to be important in cardiac function. ACE homologs (also known as members of the M2 gluzincin family) have been found in a wide variety of species, including those that neither have a cardiovascular system nor synthesize angiotensin. ACE is well-known as a key part of the renin-angiotensin system that regulates blood pressure and ACE inhibitors are important for the treatment of hypertension.


Pssm-ID: 341055  Cd Length: 563  Bit Score: 767.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  59 FLQFYEQTAQVVLNEFMEATWNYVTNITKQNQKNMLQKEADRSQFMLYFSTRARMFRTDHFLNQDVKRMLRKLQNIDKSA 138
Cdd:cd06461    1 FLEEYNEEASKLYNRSAEAQWNYETNITDENLQALLEASLELSKFVKEAAENAKKFDWQDFLDPDLKRQLKLLSRLGVAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 139 LPTEDLlevtdrgpgrpgthtpapeRRYNRLLTYMETAYNRAEVCLDEGP---CLTLEPDLQEIMATSRDQKELLWAWQG 215
Cdd:cd06461   81 LDEEDL-------------------EELNELLSEMEKIYSTAKVCPYDNPsccCLLLEPDLTNILATSRDYDELLYAWKG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 216 WRDAVGRQLRPVFEDYVRLSNKAAQYNGYKDMGALWRSKYESDTLEEDLEQLYKELQPLYLNLHAYVRRSLYRYYGPELI 295
Cdd:cd06461  142 WRDAVGKKMRPLYEEYVELSNEAARLNGFADAGEYWRSSYEMDEFEEELERLWEQIKPLYEQLHAYVRRKLRKKYGDDVI 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 296 DLRGPIPAHLLGNMWAQSWNNILDLVLPYPTKAPEDITAIMKIQHWRPEKMFEEANLFFTSMGMLPAPPAFWIKSMMEKP 375
Cdd:cd06461  222 PKDGPIPAHLLGNMWAQSWSNIYDLVVPYPDKPSLDVTPELKKQNYTAKKMFKLAEEFFTSLGLPPLPKSFWEKSMFEKP 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 376 ADgREVECHTSSWNFYKFNDFRVKKCTEVTLEDLLSVFHQMGHIQYFLQYQNLSVIYQEGASPAFEEAVGSVIALSVSSH 455
Cdd:cd06461  302 PD-REVVCHASAWDFYNGDDFRIKMCTEVTMEDFLTVHHEMGHIQYYMAYKDQPVLFREGANPGFHEAIGDTIALSVSTP 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 456 KYLLARGLLSQPHQDSEEEVNFLLGIALEKIAFIPFSYLVDKFRWKIFDGTISKITYNQEWWNFRLKYQGLCPPVPRSDD 535
Cdd:cd06461  381 KHLKRLGLLDDNVDDEEADINFLLKQALDKIAFLPFGYLLDKWRWDVFSGEIPPDEYNEAWWELREKYQGIVPPVPRSEE 460
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 536 DFDPGAKFHIPANVPYIRYFLGLILQFQLHEALCEASGHVGPLHQCDNYNSKVAGKILGK 595
Cdd:cd06461  461 DFDPGAKYHIPANTPYIRYFLSTILQFQFHKALCKAAGHTGPLHKCDIYGSKEAGKKLKK 520
 
Name Accession Description Interval E-value
Peptidase_M2 pfam01401
Angiotensin-converting enzyme; Members of this family are dipeptidyl carboxydipeptidases ...
51-595 0e+00

Angiotensin-converting enzyme; Members of this family are dipeptidyl carboxydipeptidases (cleave carboxyl dipeptides) and most notably convert angiotensin I to angiotensin II. Many members of this family contain a tandem duplication of the 600 amino acid peptidase domain, both of these are catalytically active. Most members are secreted membrane bound ectoenzymes.


Pssm-ID: 460196  Cd Length: 581  Bit Score: 895.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391   51 YSEAQAKLFLQFYEQTAQVVLNEFMEATWNYVTNITKQNQKNMLQKEADRSQFMLYFSTRARMFRTDHFLNQDVKRMLRK 130
Cdd:pfam01401   2 TDEAEAREFLEEYNREAEKVLNESTEASWNYNTNITDENAQKMLEASLELAAFTKETAQEAKQFDWSNFQDPDLKRQFKK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  131 LQNIDKSALPTEDLlevtdrgpgrpgthtpapeRRYNRLLTYMETAYNRAEVCL--DEGPCLTLEPDLQEIMATSRDQKE 208
Cdd:pfam01401  82 LSVLGTAALPEDKL-------------------EELNTILSEMESIYSKAKVCLydDPGPCLSLEPDLTEIMATSRDYDE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  209 LLWAWQGWRDAVGRQLRPVFEDYVRLSNKAAQYNGYKDMGALWRSKYESDTLEEDLEQLYKELQPLYLNLHAYVRRSLYR 288
Cdd:pfam01401 143 LLWAWEGWRDAVGKPLRPLYERYVELSNEAAKLNGYADTGAYWRSWYESDTFEEDLERLFQQLKPLYLQLHAYVRRKLRE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  289 YYGPELIDLRGPIPAHLLGNMWAQSWNNILDLVLPYPTKAPEDITAIMKIQHWRPEKMFEEANLFFTSMGMLPAPPAFWI 368
Cdd:pfam01401 223 KYGPDVISLTGPIPAHLLGNMWAQSWSNIYDLVVPFPDKPNIDVTDAMVAQGYTAKKMFEEAEEFFTSLGLLPMPPEFWD 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  369 KSMMEKPADGREVECHTSSWNFYKFNDFRVKKCTEVTLEDLLSVFHQMGHIQYFLQYQNLSVIYQEGASPAFEEAVGSVI 448
Cdd:pfam01401 303 KSMLEKPTDGREVVCHASAWDFYNGKDFRIKMCTEVTMEDFFTVHHEMGHIQYYLQYKDQPVLFREGANPGFHEAVGDVL 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  449 ALSVSSHKYLLARGLLSQPHQDSEEEVNFLLGIALEKIAFIPFSYLVDKFRWKIFDGTISKITYNQEWWNFRLKYQGLCP 528
Cdd:pfam01401 383 ALSVSTPKHLKSIGLLDDVVEDEESDINFLLKQALDKIAFLPFGYLIDKWRWGVFSGEIPPEDYNKRWWELRLKYQGICP 462
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973391  529 PVPRSDDDFDPGAKFHIPANVPYIRYFLGLILQFQLHEALCEASGHVGPLHQCDNYNSKVAGKILGK 595
Cdd:pfam01401 463 PVPRTESDFDPGAKYHVPANVPYIRYFVSFILQFQFHKALCQAAGHTGPLHKCDIYGSKEAGAKLKE 529
M2_ACE cd06461
Peptidase family M2, angiotensin converting enzyme (ACE); Peptidase family M2 angiotensin ...
59-595 0e+00

Peptidase family M2, angiotensin converting enzyme (ACE); Peptidase family 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, by removing two C-terminal amino acids. There are two forms of the enzyme in humans, the ubiquitous somatic ACE and the sperm-specific germinal ACE, both encoded by the same gene through transcription from alternative promoters. Somatic ACE has two tandem active sites with distinct catalytic properties, whereas germinal ACE, the function of which is largely unknown, has just a single active site. Recently, an ACE homolog, ACE2, has been identified in humans that differs from ACE; it preferentially removes carboxy-terminal hydrophobic or basic amino acids and appears to be important in cardiac function. ACE homologs (also known as members of the M2 gluzincin family) have been found in a wide variety of species, including those that neither have a cardiovascular system nor synthesize angiotensin. ACE is well-known as a key part of the renin-angiotensin system that regulates blood pressure and ACE inhibitors are important for the treatment of hypertension.


Pssm-ID: 341055  Cd Length: 563  Bit Score: 767.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  59 FLQFYEQTAQVVLNEFMEATWNYVTNITKQNQKNMLQKEADRSQFMLYFSTRARMFRTDHFLNQDVKRMLRKLQNIDKSA 138
Cdd:cd06461    1 FLEEYNEEASKLYNRSAEAQWNYETNITDENLQALLEASLELSKFVKEAAENAKKFDWQDFLDPDLKRQLKLLSRLGVAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 139 LPTEDLlevtdrgpgrpgthtpapeRRYNRLLTYMETAYNRAEVCLDEGP---CLTLEPDLQEIMATSRDQKELLWAWQG 215
Cdd:cd06461   81 LDEEDL-------------------EELNELLSEMEKIYSTAKVCPYDNPsccCLLLEPDLTNILATSRDYDELLYAWKG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 216 WRDAVGRQLRPVFEDYVRLSNKAAQYNGYKDMGALWRSKYESDTLEEDLEQLYKELQPLYLNLHAYVRRSLYRYYGPELI 295
Cdd:cd06461  142 WRDAVGKKMRPLYEEYVELSNEAARLNGFADAGEYWRSSYEMDEFEEELERLWEQIKPLYEQLHAYVRRKLRKKYGDDVI 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 296 DLRGPIPAHLLGNMWAQSWNNILDLVLPYPTKAPEDITAIMKIQHWRPEKMFEEANLFFTSMGMLPAPPAFWIKSMMEKP 375
Cdd:cd06461  222 PKDGPIPAHLLGNMWAQSWSNIYDLVVPYPDKPSLDVTPELKKQNYTAKKMFKLAEEFFTSLGLPPLPKSFWEKSMFEKP 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 376 ADgREVECHTSSWNFYKFNDFRVKKCTEVTLEDLLSVFHQMGHIQYFLQYQNLSVIYQEGASPAFEEAVGSVIALSVSSH 455
Cdd:cd06461  302 PD-REVVCHASAWDFYNGDDFRIKMCTEVTMEDFLTVHHEMGHIQYYMAYKDQPVLFREGANPGFHEAIGDTIALSVSTP 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 456 KYLLARGLLSQPHQDSEEEVNFLLGIALEKIAFIPFSYLVDKFRWKIFDGTISKITYNQEWWNFRLKYQGLCPPVPRSDD 535
Cdd:cd06461  381 KHLKRLGLLDDNVDDEEADINFLLKQALDKIAFLPFGYLLDKWRWDVFSGEIPPDEYNEAWWELREKYQGIVPPVPRSEE 460
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 536 DFDPGAKFHIPANVPYIRYFLGLILQFQLHEALCEASGHVGPLHQCDNYNSKVAGKILGK 595
Cdd:cd06461  461 DFDPGAKYHIPANTPYIRYFLSTILQFQFHKALCKAAGHTGPLHKCDIYGSKEAGKKLKK 520
M3_like cd06258
M3-like Peptidases, zincin metallopeptidases, include M2_ACE, M3A, M3B_PepF, and M32 families; ...
63-598 8.27e-95

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: 298.96  E-value: 8.27e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391  63 YEQTAQVVLNEFMEATWNYVTNITKQ-NQKNMLQKEADRSQFMLYFSTRARMFRTDH---FLNQDVKRMLRKLQNIDKSA 138
Cdd:cd06258    1 LNSREEKYSKAASLAHWDHDTNIGTEeRAAALEEASTLLSEFAEEDSLVALALVEPElsePLNEEYKRLVEKIQKLGKAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 139 lptedllevtdrgpgrpGTHTPAPERRYNRLLTYMETAYNraevcldegpcltlepdlqeimatsrdqkellwawqgwrd 218
Cdd:cd06258   81 -----------------GAIPKELFKEYNTLLSDFSKLWE---------------------------------------- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 219 avgrqLRPVFEDYVRLSNKAAQYNGYKDMGALWRSKYE----SDTLEEDLEQLYKELQPLYLNLHAYVRRSLYRYYGpel 294
Cdd:cd06258  104 -----LRPLLEKLVELRNQAARLLGYEDPYDALLDLYEagysTEVVEQDFEELKQAIPLLYKELHAIQRPKLHRDYG--- 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 295 idlrgpipahllgnmwaqswnnildlvlpYPTKAPEDITAIMKIQHWRPEKMFEEANLFFTSMGMLPAPPAFWIKSMMEK 374
Cdd:cd06258  176 -----------------------------FYYIPKFDVTSAMLKQKFDAEWMFEGALWFLQELGLEPGPLLTWERLDLYA 226
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 375 PAdgrEVECHTSSWNFYKfNDFRVKKCTEVTLEDLLSVFHQMGHIQYFLQYQNLSVIYQEGASPAFEEAVGSVIALSVSS 454
Cdd:cd06258  227 PL---GKVCHAFATDFGR-KDVRITTNYTVTRDDILTTHHEFGHALYELQYRTRFAFLGNGASLGFHESQSQFLENSVGT 302
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973391 455 HKYLLARGLLSQPHQDSEEEVNFLLGIALEKIAFIPFSYLVDKFRWKIFDGTISKITYNQEWWNFRLKYQGLCPPVPRSD 534
Cdd:cd06258  303 FKHLYSKHLLSGPQMDDESEEKFLLARLLDKVTFLPHIILVDKWEWAVFSGEIPKKPDLPSWWNLLYKEYLGVPPVPRDE 382
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568973391 535 DDFDPGAKFHIPA--NVPYIRYFLGLILQFQLHEALCEASGHVGplhQCDNYNSKVAGKILGKNHK 598
Cdd:cd06258  383 TYTDGWAQFHHWAgyDGYYIRYALGQVYAFQFYEKLCEDAGHEG---KCDIGNFDEAGQKLREILR 445
 
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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