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Conserved domains on  [gi|1835952171|gb|QJF77843|]
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angiotensin-converting enzyme 2 [Vampyrum spectrum]

Protein Classification

angiotensin-converting enzyme 2( domain architecture ID 11117526)

angiotensin-converting enzyme 2 is a carboxypeptidase which converts angiotensin I to angiotensin 1-9, and angiotensin II to the vasodilator angiotensin 1-7

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 ...
19-600 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: 949.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171  19 TPTEEEARIFLENFNTEAEELYHQSSLASWNYNTNITNENVQKM*EADQKWSTFYEEKSKLAKAYPLETIKDVKIKHQLQ 98
Cdd:pfam01401   1 STDEAEAREFLEEYNREAEKVLNESTEASWNYNTNITDENAQKMLEASLELAAFTKETAQEAKQFDWSNFQDPDLKRQFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171  99 ALQKNGL**********LNTILNTMSTIYSTGKVCKPNNPQECFLLaSSGLEDIMHNSKDYNERLWAWEGWRSTVGKQLR 178
Cdd:pfam01401  81 KLSVLGTAALPEDKLEELNTILSEMESIYSKAKVCLYDDPGPCLSL-EPDLTEIMATSRDYDELLWAWEGWRDAVGKPLR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 179 PLYEEYVVLKNEMARE*NYEDYGDYWRGDYETEgtsgyeysrnQLSKDVERTFAEIKPLYEHLHAYVRAKLMDTY-PSHI 257
Cdd:pfam01401 160 PLYERYVELSNEAAKLNGYADTGAYWRSWYESD----------TFEEDLERLFQQLKPLYLQLHAYVRRKLREKYgPDVI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 258 SPTGCLPAHLLGDMWGRFWTNLYDLTAPFPEKPTIDVTAAMVAQSWDAQRIFKEAEKFFVSVGLFNMTQGFWDNSMLTKP 337
Cdd:pfam01401 230 SLTGPIPAHLLGNMWAQSWSNIYDLVVPFPDKPNIDVTDAMVAQGYTAKKMFEEAEEFFTSLGLLPMPPEFWDKSMLEKP 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 338 DDGREVVCHPTAWDL-GKNDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYANQSFLLRNGANEGFHEAVGEIMSLSVATP 416
Cdd:pfam01401 310 TDGREVVCHASAWDFyNGKDFRIKMCTEVTMEDFFTVHHEMGHIQYYLQYKDQPVLFREGANPGFHEAVGDVLALSVSTP 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 417 KHLKVLGLLPsDFHEDNETDINFLLKQALNIVGTLPFTYMLEKWRWMVFKGEIPREQWMKKWWEMKREIVGVVEPMPHDE 496
Cdd:pfam01401 390 KHLKSIGLLD-DVVEDEESDINFLLKQALDKIAFLPFGYLIDKWRWGVFSGEIPPEDYNKRWWELRLKYQGICPPVPRTE 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 497 TYCDPASLFHVANDYSFIRYYTRTIFQFQFQEALCRIAQHEGPLHKCDISNSTAAGEKLL*MLQLGKSEPWTRALETFVG 576
Cdd:pfam01401 469 SDFDPGAKYHVPANVPYIRYFVSFILQFQFHKALCQAAGHTGPLHKCDIYGSKEAGAKLKEMLKLGSSKPWPEALEAITG 548
                         570       580
                  ....*....|....*....|....
gi 1835952171 577 KKQMDVRPLLNYFEPLFTWLKDQN 600
Cdd:pfam01401 549 QRKMDASALLEYFEPLIDWLKEQN 572
Collectrin pfam16959
Renal amino acid transporter; Collectrin is a single-pass transmembrane protein that is ...
617-745 8.42e-78

Renal amino acid transporter; Collectrin is a single-pass transmembrane protein that is homologous to the C-terminal region of human angiotensin-converting enzyme 2, ACE2, SwissProt:Q9BYF1, found in Peptidase_M2 pfam01401. Collectrin is critical for normal amino acid reabsorption in the kidney.


:

Pssm-ID: 465322  Cd Length: 154  Bit Score: 247.94  E-value: 8.42e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 617 SIKVRISLKSALGDKAYEWNDNEMYFFQSSIAYAMREYFSNFKNKTIPFRAEDVWVSDLKPRVSFNFFVTSPYNMSDIIP 696
Cdd:pfam16959   1 AIKVRISLKTALGDKAYEWNENEMYLFKASVAYAMRKYFSREKNQTVPFQIENVLVCNETPRVSFWFVVTSPNNPSDLIP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1835952171 697 RSEVEEAIryRKSRGRINDAFRLDDNSLEFLGIQPTLEPPYQPAVTIWL 745
Cdd:pfam16959  81 KAEVEAAI--RMSRNRINNAFLLDDSTLEFLGIPPTLAPPVEPPVPIWL 127
 
Name Accession Description Interval E-value
Peptidase_M2 pfam01401
Angiotensin-converting enzyme; Members of this family are dipeptidyl carboxydipeptidases ...
19-600 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: 949.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171  19 TPTEEEARIFLENFNTEAEELYHQSSLASWNYNTNITNENVQKM*EADQKWSTFYEEKSKLAKAYPLETIKDVKIKHQLQ 98
Cdd:pfam01401   1 STDEAEAREFLEEYNREAEKVLNESTEASWNYNTNITDENAQKMLEASLELAAFTKETAQEAKQFDWSNFQDPDLKRQFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171  99 ALQKNGL**********LNTILNTMSTIYSTGKVCKPNNPQECFLLaSSGLEDIMHNSKDYNERLWAWEGWRSTVGKQLR 178
Cdd:pfam01401  81 KLSVLGTAALPEDKLEELNTILSEMESIYSKAKVCLYDDPGPCLSL-EPDLTEIMATSRDYDELLWAWEGWRDAVGKPLR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 179 PLYEEYVVLKNEMARE*NYEDYGDYWRGDYETEgtsgyeysrnQLSKDVERTFAEIKPLYEHLHAYVRAKLMDTY-PSHI 257
Cdd:pfam01401 160 PLYERYVELSNEAAKLNGYADTGAYWRSWYESD----------TFEEDLERLFQQLKPLYLQLHAYVRRKLREKYgPDVI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 258 SPTGCLPAHLLGDMWGRFWTNLYDLTAPFPEKPTIDVTAAMVAQSWDAQRIFKEAEKFFVSVGLFNMTQGFWDNSMLTKP 337
Cdd:pfam01401 230 SLTGPIPAHLLGNMWAQSWSNIYDLVVPFPDKPNIDVTDAMVAQGYTAKKMFEEAEEFFTSLGLLPMPPEFWDKSMLEKP 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 338 DDGREVVCHPTAWDL-GKNDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYANQSFLLRNGANEGFHEAVGEIMSLSVATP 416
Cdd:pfam01401 310 TDGREVVCHASAWDFyNGKDFRIKMCTEVTMEDFFTVHHEMGHIQYYLQYKDQPVLFREGANPGFHEAVGDVLALSVSTP 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 417 KHLKVLGLLPsDFHEDNETDINFLLKQALNIVGTLPFTYMLEKWRWMVFKGEIPREQWMKKWWEMKREIVGVVEPMPHDE 496
Cdd:pfam01401 390 KHLKSIGLLD-DVVEDEESDINFLLKQALDKIAFLPFGYLIDKWRWGVFSGEIPPEDYNKRWWELRLKYQGICPPVPRTE 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 497 TYCDPASLFHVANDYSFIRYYTRTIFQFQFQEALCRIAQHEGPLHKCDISNSTAAGEKLL*MLQLGKSEPWTRALETFVG 576
Cdd:pfam01401 469 SDFDPGAKYHVPANVPYIRYFVSFILQFQFHKALCQAAGHTGPLHKCDIYGSKEAGAKLKEMLKLGSSKPWPEALEAITG 548
                         570       580
                  ....*....|....*....|....
gi 1835952171 577 KKQMDVRPLLNYFEPLFTWLKDQN 600
Cdd:pfam01401 549 QRKMDASALLEYFEPLIDWLKEQN 572
M2_ACE cd06461
Peptidase family M2, angiotensin converting enzyme (ACE); Peptidase family M2 angiotensin ...
28-600 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: 846.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171  28 FLENFNTEAEELYHQSSLASWNYNTNITNENVQKM*EADQKWSTFYEEKSKLAKAYPLETIKDVKIKHQLQALQKNGL** 107
Cdd:cd06461     1 FLEEYNEEASKLYNRSAEAQWNYETNITDENLQALLEASLELSKFVKEAAENAKKFDWQDFLDPDLKRQLKLLSRLGVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 108 ********LNTILNTMSTIYSTGKVCKPNNPQECFLLASSGLEDIMHNSKDYNERLWAWEGWRSTVGKQLRPLYEEYVVL 187
Cdd:cd06461    81 LDEEDLEELNELLSEMEKIYSTAKVCPYDNPSCCCLLLEPDLTNILATSRDYDELLYAWKGWRDAVGKKMRPLYEEYVEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 188 KNEMARE*NYEDYGDYWRGDYETEgtsgyeysrnQLSKDVERTFAEIKPLYEHLHAYVRAKLMDTYPSH-ISPTGCLPAH 266
Cdd:cd06461   161 SNEAARLNGFADAGEYWRSSYEMD----------EFEEELERLWEQIKPLYEQLHAYVRRKLRKKYGDDvIPKDGPIPAH 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 267 LLGDMWGRFWTNLYDLTAPFPEKPTIDVTAAMVAQSWDAQRIFKEAEKFFVSVGLFNMTQGFWDNSMLTKPDDgREVVCH 346
Cdd:cd06461   231 LLGNMWAQSWSNIYDLVVPYPDKPSLDVTPELKKQNYTAKKMFKLAEEFFTSLGLPPLPKSFWEKSMFEKPPD-REVVCH 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 347 PTAWDLG-KNDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYANQSFLLRNGANEGFHEAVGEIMSLSVATPKHLKVLGLL 425
Cdd:cd06461   310 ASAWDFYnGDDFRIKMCTEVTMEDFLTVHHEMGHIQYYMAYKDQPVLFREGANPGFHEAIGDTIALSVSTPKHLKRLGLL 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 426 PSDfHEDNETDINFLLKQALNIVGTLPFTYMLEKWRWMVFKGEIPREQWMKKWWEMKREIVGVVEPMPHDETYCDPASLF 505
Cdd:cd06461   390 DDN-VDDEEADINFLLKQALDKIAFLPFGYLLDKWRWDVFSGEIPPDEYNEAWWELREKYQGIVPPVPRSEEDFDPGAKY 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 506 HVANDYSFIRYYTRTIFQFQFQEALCRIAQHEGPLHKCDISNSTAAGEKLL*MLQLGKSEPWTRALETFVGKKQMDVRPL 585
Cdd:cd06461   469 HIPANTPYIRYFLSTILQFQFHKALCKAAGHTGPLHKCDIYGSKEAGKKLKKMLSLGSSKPWPDALEELTGERELDASPL 548
                         570
                  ....*....|....*
gi 1835952171 586 LNYFEPLFTWLKDQN 600
Cdd:cd06461   549 LEYFQPLYDWLKEEN 563
Collectrin pfam16959
Renal amino acid transporter; Collectrin is a single-pass transmembrane protein that is ...
617-745 8.42e-78

Renal amino acid transporter; Collectrin is a single-pass transmembrane protein that is homologous to the C-terminal region of human angiotensin-converting enzyme 2, ACE2, SwissProt:Q9BYF1, found in Peptidase_M2 pfam01401. Collectrin is critical for normal amino acid reabsorption in the kidney.


Pssm-ID: 465322  Cd Length: 154  Bit Score: 247.94  E-value: 8.42e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 617 SIKVRISLKSALGDKAYEWNDNEMYFFQSSIAYAMREYFSNFKNKTIPFRAEDVWVSDLKPRVSFNFFVTSPYNMSDIIP 696
Cdd:pfam16959   1 AIKVRISLKTALGDKAYEWNENEMYLFKASVAYAMRKYFSREKNQTVPFQIENVLVCNETPRVSFWFVVTSPNNPSDLIP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1835952171 697 RSEVEEAIryRKSRGRINDAFRLDDNSLEFLGIQPTLEPPYQPAVTIWL 745
Cdd:pfam16959  81 KAEVEAAI--RMSRNRINNAFLLDDSTLEFLGIPPTLAPPVEPPVPIWL 127
 
Name Accession Description Interval E-value
Peptidase_M2 pfam01401
Angiotensin-converting enzyme; Members of this family are dipeptidyl carboxydipeptidases ...
19-600 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: 949.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171  19 TPTEEEARIFLENFNTEAEELYHQSSLASWNYNTNITNENVQKM*EADQKWSTFYEEKSKLAKAYPLETIKDVKIKHQLQ 98
Cdd:pfam01401   1 STDEAEAREFLEEYNREAEKVLNESTEASWNYNTNITDENAQKMLEASLELAAFTKETAQEAKQFDWSNFQDPDLKRQFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171  99 ALQKNGL**********LNTILNTMSTIYSTGKVCKPNNPQECFLLaSSGLEDIMHNSKDYNERLWAWEGWRSTVGKQLR 178
Cdd:pfam01401  81 KLSVLGTAALPEDKLEELNTILSEMESIYSKAKVCLYDDPGPCLSL-EPDLTEIMATSRDYDELLWAWEGWRDAVGKPLR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 179 PLYEEYVVLKNEMARE*NYEDYGDYWRGDYETEgtsgyeysrnQLSKDVERTFAEIKPLYEHLHAYVRAKLMDTY-PSHI 257
Cdd:pfam01401 160 PLYERYVELSNEAAKLNGYADTGAYWRSWYESD----------TFEEDLERLFQQLKPLYLQLHAYVRRKLREKYgPDVI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 258 SPTGCLPAHLLGDMWGRFWTNLYDLTAPFPEKPTIDVTAAMVAQSWDAQRIFKEAEKFFVSVGLFNMTQGFWDNSMLTKP 337
Cdd:pfam01401 230 SLTGPIPAHLLGNMWAQSWSNIYDLVVPFPDKPNIDVTDAMVAQGYTAKKMFEEAEEFFTSLGLLPMPPEFWDKSMLEKP 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 338 DDGREVVCHPTAWDL-GKNDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYANQSFLLRNGANEGFHEAVGEIMSLSVATP 416
Cdd:pfam01401 310 TDGREVVCHASAWDFyNGKDFRIKMCTEVTMEDFFTVHHEMGHIQYYLQYKDQPVLFREGANPGFHEAVGDVLALSVSTP 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 417 KHLKVLGLLPsDFHEDNETDINFLLKQALNIVGTLPFTYMLEKWRWMVFKGEIPREQWMKKWWEMKREIVGVVEPMPHDE 496
Cdd:pfam01401 390 KHLKSIGLLD-DVVEDEESDINFLLKQALDKIAFLPFGYLIDKWRWGVFSGEIPPEDYNKRWWELRLKYQGICPPVPRTE 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 497 TYCDPASLFHVANDYSFIRYYTRTIFQFQFQEALCRIAQHEGPLHKCDISNSTAAGEKLL*MLQLGKSEPWTRALETFVG 576
Cdd:pfam01401 469 SDFDPGAKYHVPANVPYIRYFVSFILQFQFHKALCQAAGHTGPLHKCDIYGSKEAGAKLKEMLKLGSSKPWPEALEAITG 548
                         570       580
                  ....*....|....*....|....
gi 1835952171 577 KKQMDVRPLLNYFEPLFTWLKDQN 600
Cdd:pfam01401 549 QRKMDASALLEYFEPLIDWLKEQN 572
M2_ACE cd06461
Peptidase family M2, angiotensin converting enzyme (ACE); Peptidase family M2 angiotensin ...
28-600 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: 846.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171  28 FLENFNTEAEELYHQSSLASWNYNTNITNENVQKM*EADQKWSTFYEEKSKLAKAYPLETIKDVKIKHQLQALQKNGL** 107
Cdd:cd06461     1 FLEEYNEEASKLYNRSAEAQWNYETNITDENLQALLEASLELSKFVKEAAENAKKFDWQDFLDPDLKRQLKLLSRLGVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 108 ********LNTILNTMSTIYSTGKVCKPNNPQECFLLASSGLEDIMHNSKDYNERLWAWEGWRSTVGKQLRPLYEEYVVL 187
Cdd:cd06461    81 LDEEDLEELNELLSEMEKIYSTAKVCPYDNPSCCCLLLEPDLTNILATSRDYDELLYAWKGWRDAVGKKMRPLYEEYVEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 188 KNEMARE*NYEDYGDYWRGDYETEgtsgyeysrnQLSKDVERTFAEIKPLYEHLHAYVRAKLMDTYPSH-ISPTGCLPAH 266
Cdd:cd06461   161 SNEAARLNGFADAGEYWRSSYEMD----------EFEEELERLWEQIKPLYEQLHAYVRRKLRKKYGDDvIPKDGPIPAH 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 267 LLGDMWGRFWTNLYDLTAPFPEKPTIDVTAAMVAQSWDAQRIFKEAEKFFVSVGLFNMTQGFWDNSMLTKPDDgREVVCH 346
Cdd:cd06461   231 LLGNMWAQSWSNIYDLVVPYPDKPSLDVTPELKKQNYTAKKMFKLAEEFFTSLGLPPLPKSFWEKSMFEKPPD-REVVCH 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 347 PTAWDLG-KNDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYANQSFLLRNGANEGFHEAVGEIMSLSVATPKHLKVLGLL 425
Cdd:cd06461   310 ASAWDFYnGDDFRIKMCTEVTMEDFLTVHHEMGHIQYYMAYKDQPVLFREGANPGFHEAIGDTIALSVSTPKHLKRLGLL 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 426 PSDfHEDNETDINFLLKQALNIVGTLPFTYMLEKWRWMVFKGEIPREQWMKKWWEMKREIVGVVEPMPHDETYCDPASLF 505
Cdd:cd06461   390 DDN-VDDEEADINFLLKQALDKIAFLPFGYLLDKWRWDVFSGEIPPDEYNEAWWELREKYQGIVPPVPRSEEDFDPGAKY 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 506 HVANDYSFIRYYTRTIFQFQFQEALCRIAQHEGPLHKCDISNSTAAGEKLL*MLQLGKSEPWTRALETFVGKKQMDVRPL 585
Cdd:cd06461   469 HIPANTPYIRYFLSTILQFQFHKALCKAAGHTGPLHKCDIYGSKEAGKKLKKMLSLGSSKPWPDALEELTGERELDASPL 548
                         570
                  ....*....|....*
gi 1835952171 586 LNYFEPLFTWLKDQN 600
Cdd:cd06461   549 LEYFQPLYDWLKEEN 563
M3_like cd06258
M3-like Peptidases, zincin metallopeptidases, include M2_ACE, M3A, M3B_PepF, and M32 families; ...
32-588 1.23e-136

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: 413.36  E-value: 1.23e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171  32 FNTEAEELYHQSSLASWNYNTNITN-ENVQKM*EADQKWSTFYEEKSKLAKAY---PLETIKDVKIKHQLQALQKNGL** 107
Cdd:cd06258     1 LNSREEKYSKAASLAHWDHDTNIGTeERAAALEEASTLLSEFAEEDSLVALALvepELSEPLNEEYKRLVEKIQKLGKAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 108 ********--LNTILNTMSTIYStgkvckpnnpqecfllassgledimhnskdynerlwawegwrstvgkqLRPLYEEYV 185
Cdd:cd06258    81 GAIPKELFkeYNTLLSDFSKLWE------------------------------------------------LRPLLEKLV 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 186 VLKNEMARE*NYEDYGDYWRGDYETegtsgyEYSRNQLSKDVERTFAEIKPLYEHLHAYVRAKLMDTYPSHISptgclpa 265
Cdd:cd06258   113 ELRNQAARLLGYEDPYDALLDLYEA------GYSTEVVEQDFEELKQAIPLLYKELHAIQRPKLHRDYGFYYI------- 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 266 hllgdmwgrfwtnlydltapfpekPTIDVTAAMVAQSWDAQRIFKEAEKFFVSVGLFNMTQGFWDNSMLTKPDdgrEVVC 345
Cdd:cd06258   180 ------------------------PKFDVTSAMLKQKFDAEWMFEGALWFLQELGLEPGPLLTWERLDLYAPL---GKVC 232
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 346 HPTAWDLGKNDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYANQSFLLRNGANEGFHEAVGEIMSLSVATPKHLKVLGLL 425
Cdd:cd06258   233 HAFATDFGRKDVRITTNYTVTRDDILTTHHEFGHALYELQYRTRFAFLGNGASLGFHESQSQFLENSVGTFKHLYSKHLL 312
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 426 pSDFHEDNETDINFLLKQALNIVGTLPFTYMLEKWRWMVFKGEIPREQWMKKWWEMKREIVGVVEPMPHDETYCDPASLF 505
Cdd:cd06258   313 -SGPQMDDESEEKFLLARLLDKVTFLPHIILVDKWEWAVFSGEIPKKPDLPSWWNLLYKEYLGVPPVPRDETYTDGWAQF 391
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 506 HV--ANDYSFIRYYTRTIFQFQFQEALCRIAQHEGplhKCDISNSTAAGEKLL*MLQLGKSEPWTRALETFVGKKQMDVR 583
Cdd:cd06258   392 HHwaGYDGYYIRYALGQVYAFQFYEKLCEDAGHEG---KCDIGNFDEAGQKLREILRLGGSRPPTELLKNATGKEPNIAS 468

                  ....*
gi 1835952171 584 PLLNY 588
Cdd:cd06258   469 FLLHI 473
Collectrin pfam16959
Renal amino acid transporter; Collectrin is a single-pass transmembrane protein that is ...
617-745 8.42e-78

Renal amino acid transporter; Collectrin is a single-pass transmembrane protein that is homologous to the C-terminal region of human angiotensin-converting enzyme 2, ACE2, SwissProt:Q9BYF1, found in Peptidase_M2 pfam01401. Collectrin is critical for normal amino acid reabsorption in the kidney.


Pssm-ID: 465322  Cd Length: 154  Bit Score: 247.94  E-value: 8.42e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835952171 617 SIKVRISLKSALGDKAYEWNDNEMYFFQSSIAYAMREYFSNFKNKTIPFRAEDVWVSDLKPRVSFNFFVTSPYNMSDIIP 696
Cdd:pfam16959   1 AIKVRISLKTALGDKAYEWNENEMYLFKASVAYAMRKYFSREKNQTVPFQIENVLVCNETPRVSFWFVVTSPNNPSDLIP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1835952171 697 RSEVEEAIryRKSRGRINDAFRLDDNSLEFLGIQPTLEPPYQPAVTIWL 745
Cdd:pfam16959  81 KAEVEAAI--RMSRNRINNAFLLDDSTLEFLGIPPTLAPPVEPPVPIWL 127
 
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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