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Conserved domains on  [gi|768032502|ref|XP_011543835|]
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phosphate-regulating neutral endopeptidase PHEX isoform X2 [Homo sapiens]

Protein Classification

M13 family metallopeptidase( domain architecture ID 10171382)

M13 family metallopeptidase similar to neutral endopeptidase (neprilysin), which degrades and inactivates bioactive peptides, and to endothelin-converting enzyme, which catalyzes the hydrolysis of the bond between Trp-21 and Val-22 in big endothelin to form endothelin 1

EC:  3.4.24.-
MEROPS:  M13
SCOP:  3001975

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M13 cd08662
Peptidase family M13 includes neprilysin and endothelin-converting enzyme I; The M13 family of ...
1-488 0e+00

Peptidase family M13 includes neprilysin and endothelin-converting enzyme I; The M13 family of metallopeptidases includes neprilysin (neutral endopeptidase, NEP, enkephalinase, CD10, CALLA, EC 3.4.24.11), endothelin-converting enzyme I (ECE-1, EC 3.4.24.71), erythrocyte surface antigen KELL (ECE-3), phosphate-regulating gene on the X chromosome (PHEX), soluble secreted endopeptidase (SEP), and damage-induced neuronal endopeptidase (DINE)/X-converting enzyme (XCE). Proteins in this family fulfill a broad range of physiological roles due to the greater variation in the active site's S2' subsite allowing substrate specificity. NEP is expressed in a variety of tissues including kidney and brain, and is involved in many physiological and pathological processes, including blood pressure and inflammatory response. It degrades a wide array of substrates such as substance P, enkephalins, cholecystokinin, neurotensin and somatostatin. It is an important enzyme in the regulation of amyloid-beta (Abeta) protein that forms amyloid plaques that are associated with Alzeimers disease (AD). ECE-1 catalyzes the final rate-limiting step in the biosynthesis of endothelins via post-translational conversion of the biologically inactive big endothelins. Like NEP, it also hydrolyzes bradykinin, substance P, neurotensin, and Abeta. Endothelin-1 overproduction has been implicated in various diseases including stroke, asthma, hypertension, and cardiac and renal failure. Kell is a homolog of NEP and constitutes a major antigen on human erythrocytes; it preferentially cleaves big endothelin-3 to produce bioactive endothelin-3, but is also known to cleave substance P and neurokinin A. PHEX forms a complex interaction with fibroblast growth factor 23 (FGF23) and matrix extracellular phosphoglycoprotein, causing bone mineralization. A loss-of-function mutation in PHEX disrupts this interaction leading to hypophosphatemic rickets; X-linked hypophosphatemic (XLH) rickets is the most common form of metabolic rickets. ECEL1 is a brain metalloprotease which plays a critical role in the nervous regulation of the respiratory system, while DINE is abundantly expressed in the hypothalamus and its expression responds to nerve injury. A majority of these M13 proteases are prime therapeutic targets for selective inhibition.


:

Pssm-ID: 341056 [Multi-domain]  Cd Length: 642  Bit Score: 589.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502   1 MVDTAVLLGANSSRAEHDMKSVLRLEIKIAEIMIP-HENRTSEAMYNKMNISELSAMIPQFDWLGYIKKVIDtrlyphlk 79
Cdd:cd08662  164 IAKLLELLGADEEEAEKLAEDVLAFETELAKISLSsEELRDPEKTYNPLTLAELQKLAPSIDWKAYLKALGP-------- 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502  80 DISPSENVVVRVPQYFKDLFRILGSERKKTIANYLVWRMVYSRIPNLSRRFQYRWLEFSRVIQGTTTLLPQWDKCVNFIE 159
Cdd:cd08662  236 PADDPDKVIVSQPEYLKKLDKLLASTPLRTLKNYLIWRLLDSLAPYLSKEFRDARFFYGKALSGQKEPEPRWKRCVELVN 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 160 SALPYVVGKMFVDVYFQEDKKEMMEELVEGVRWAFIDMLEkENEWMDAGTKRKAKEKARAVLAKVGYPEFIMNDTHVNED 239
Cdd:cd08662  316 GALGEALGRLYVEKYFSEEAKADVEEMVENIKEAFKERLE-NLDWMDEETKKKALEKLDAMKVKIGYPDKWRDYSALDIY 394
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 240 LKAIKFSEaDYFGNVLQTRKYLAQSDFFWLRKAVPKTEWFTNPTTVNAFYSASTNQIRFPAGELQKPFFwGTEYPRSLSY 319
Cdd:cd08662  395 YDDLNVSD-SYFENVLRLLRFETKRQLAKLGKPVDRTEWSMSPQTVNAYYNPSLNEIVFPAGILQPPFF-DPDAPDALNY 472
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 320 GAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSTESEEKFKEKTKCMINQYSNYYWKKaGLNVKGKRTLGENIADNGGLR 399
Cdd:cd08662  473 GGIGAVIGHEITHGFDDQGRQYDENGNLRNWWTNEDRKEFEERAQCLVDQYSNYEVPP-GLHVNGKLTLGENIADNGGLR 551
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 400 EAFRAYRKWINDRrqglEEPLLPGITFTNNQLFFLSYAHVRCNSYRPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKAF 479
Cdd:cd08662  552 LAYRAYKKWLKEN----GPELPGLEGFTPEQLFFLSFAQVWCSKYRPEALRQLLLTDPHSPGKFRVNGPLSNSPEFAEAF 627

                 ....*....
gi 768032502 480 NCPPNSTMN 488
Cdd:cd08662  628 NCPPGSPMN 636
 
Name Accession Description Interval E-value
M13 cd08662
Peptidase family M13 includes neprilysin and endothelin-converting enzyme I; The M13 family of ...
1-488 0e+00

Peptidase family M13 includes neprilysin and endothelin-converting enzyme I; The M13 family of metallopeptidases includes neprilysin (neutral endopeptidase, NEP, enkephalinase, CD10, CALLA, EC 3.4.24.11), endothelin-converting enzyme I (ECE-1, EC 3.4.24.71), erythrocyte surface antigen KELL (ECE-3), phosphate-regulating gene on the X chromosome (PHEX), soluble secreted endopeptidase (SEP), and damage-induced neuronal endopeptidase (DINE)/X-converting enzyme (XCE). Proteins in this family fulfill a broad range of physiological roles due to the greater variation in the active site's S2' subsite allowing substrate specificity. NEP is expressed in a variety of tissues including kidney and brain, and is involved in many physiological and pathological processes, including blood pressure and inflammatory response. It degrades a wide array of substrates such as substance P, enkephalins, cholecystokinin, neurotensin and somatostatin. It is an important enzyme in the regulation of amyloid-beta (Abeta) protein that forms amyloid plaques that are associated with Alzeimers disease (AD). ECE-1 catalyzes the final rate-limiting step in the biosynthesis of endothelins via post-translational conversion of the biologically inactive big endothelins. Like NEP, it also hydrolyzes bradykinin, substance P, neurotensin, and Abeta. Endothelin-1 overproduction has been implicated in various diseases including stroke, asthma, hypertension, and cardiac and renal failure. Kell is a homolog of NEP and constitutes a major antigen on human erythrocytes; it preferentially cleaves big endothelin-3 to produce bioactive endothelin-3, but is also known to cleave substance P and neurokinin A. PHEX forms a complex interaction with fibroblast growth factor 23 (FGF23) and matrix extracellular phosphoglycoprotein, causing bone mineralization. A loss-of-function mutation in PHEX disrupts this interaction leading to hypophosphatemic rickets; X-linked hypophosphatemic (XLH) rickets is the most common form of metabolic rickets. ECEL1 is a brain metalloprotease which plays a critical role in the nervous regulation of the respiratory system, while DINE is abundantly expressed in the hypothalamus and its expression responds to nerve injury. A majority of these M13 proteases are prime therapeutic targets for selective inhibition.


Pssm-ID: 341056 [Multi-domain]  Cd Length: 642  Bit Score: 589.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502   1 MVDTAVLLGANSSRAEHDMKSVLRLEIKIAEIMIP-HENRTSEAMYNKMNISELSAMIPQFDWLGYIKKVIDtrlyphlk 79
Cdd:cd08662  164 IAKLLELLGADEEEAEKLAEDVLAFETELAKISLSsEELRDPEKTYNPLTLAELQKLAPSIDWKAYLKALGP-------- 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502  80 DISPSENVVVRVPQYFKDLFRILGSERKKTIANYLVWRMVYSRIPNLSRRFQYRWLEFSRVIQGTTTLLPQWDKCVNFIE 159
Cdd:cd08662  236 PADDPDKVIVSQPEYLKKLDKLLASTPLRTLKNYLIWRLLDSLAPYLSKEFRDARFFYGKALSGQKEPEPRWKRCVELVN 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 160 SALPYVVGKMFVDVYFQEDKKEMMEELVEGVRWAFIDMLEkENEWMDAGTKRKAKEKARAVLAKVGYPEFIMNDTHVNED 239
Cdd:cd08662  316 GALGEALGRLYVEKYFSEEAKADVEEMVENIKEAFKERLE-NLDWMDEETKKKALEKLDAMKVKIGYPDKWRDYSALDIY 394
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 240 LKAIKFSEaDYFGNVLQTRKYLAQSDFFWLRKAVPKTEWFTNPTTVNAFYSASTNQIRFPAGELQKPFFwGTEYPRSLSY 319
Cdd:cd08662  395 YDDLNVSD-SYFENVLRLLRFETKRQLAKLGKPVDRTEWSMSPQTVNAYYNPSLNEIVFPAGILQPPFF-DPDAPDALNY 472
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 320 GAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSTESEEKFKEKTKCMINQYSNYYWKKaGLNVKGKRTLGENIADNGGLR 399
Cdd:cd08662  473 GGIGAVIGHEITHGFDDQGRQYDENGNLRNWWTNEDRKEFEERAQCLVDQYSNYEVPP-GLHVNGKLTLGENIADNGGLR 551
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 400 EAFRAYRKWINDRrqglEEPLLPGITFTNNQLFFLSYAHVRCNSYRPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKAF 479
Cdd:cd08662  552 LAYRAYKKWLKEN----GPELPGLEGFTPEQLFFLSFAQVWCSKYRPEALRQLLLTDPHSPGKFRVNGPLSNSPEFAEAF 627

                 ....*....
gi 768032502 480 NCPPNSTMN 488
Cdd:cd08662  628 NCPPGSPMN 636
PepO COG3590
Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones];
7-497 3.08e-149

Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442809 [Multi-domain]  Cd Length: 674  Bit Score: 441.90  E-value: 3.08e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502   7 LLGANSSRAEHDMKSVLRLEIKIAEIMIPH-ENRTSEAMYNKMNISELSAMIPQFDWLGYIKKVidtrlyphlkDISPSE 85
Cdd:COG3590  207 LAGYDEADAAAAAEAVLALETALAKAHWSRvELRDPEKTYNPMTVAELAKLAPGFDWDAYLKAL----------GLPAVD 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502  86 NVVVRVPQYFKDLFRILGSERKKTIANYLVWRMVYSRIPNLSRRFQYRWLEF-SRVIQGTTTLLPQWDKCVNFIESALPY 164
Cdd:COG3590  277 EVIVGQPSFFKALDKLLASTPLEDWKAYLRWHLLDSAAPYLSKAFVDANFDFyGKTLSGQKEQRPRWKRAVALVNGALGE 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 165 VVGKMFVDVYFQEDKKEMMEELVEGVRWAFIDMLEKeNEWMDAGTKRKAKEKARAVLAKVGYPEfimndthVNEDLKAIK 244
Cdd:COG3590  357 ALGQLYVERYFPPEAKARMEELVANLRAAYRERIEN-LDWMSPETKAKALEKLAAFTPKIGYPD-------KWRDYSGLE 428
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 245 FSEADYFGNVLQTRKylaqsdFFWLR------KAVPKTEWFTNPTTVNAFYSASTNQIRFPAGELQKPFFwGTEYPRSLS 318
Cdd:COG3590  429 IKRDDLVGNVLRASA------FEYQRelaklgKPVDRTEWGMTPQTVNAYYNPTMNEIVFPAAILQPPFF-DPKADDAVN 501
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 319 YGAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSTESEEKFKEKTKCMINQYSNYYWKKaGLNVKGKRTLGENIADNGGL 398
Cdd:COG3590  502 YGGIGAVIGHEITHGFDDQGSQFDGDGNLRNWWTPEDRAAFEARTKKLVAQYDAYEPLP-GLHVNGKLTLGENIADLGGL 580
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 399 REAFRAYRKwindRRQGLEEPLLPGitFTNNQLFFLSYAHVRCNSYRPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKA 478
Cdd:COG3590  581 SIAYDAYKL----SLKGKEAPVIDG--FTGDQRFFLGWAQVWRSKARDEALRQRLATDPHSPGEFRVNGPVRNLDAFYEA 654
                        490       500
                 ....*....|....*....|
gi 768032502 479 FNCPPNSTMNR-GMDSCRLW 497
Cdd:COG3590  655 FDVKPGDKMYLaPEDRVRIW 674
Peptidase_M13 pfam01431
Peptidase family M13; Mammalian enzymes are typically type-II membrane anchored enzymes which ...
286-496 2.58e-79

Peptidase family M13; Mammalian enzymes are typically type-II membrane anchored enzymes which are known, or believed to activate or inactivate oligopeptide (pro)-hormones such as opioid peptides. The family also contains a bacterial member believed to be involved with milk protein cleavage.


Pssm-ID: 279739 [Multi-domain]  Cd Length: 205  Bit Score: 246.17  E-value: 2.58e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502  286 NAFYSASTNQIRFPAGELQKPFFwGTEYPRSLSYGAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSTESEEKFKEKTKC 365
Cdd:pfam01431   1 NAYYQPNRNEIVFPAAILQPPFF-DPNYPRAVNYGGIGNVIAHEITHGFDDQGAQFDKDGNLRSWWTDEDAEEFKDRAQC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502  366 MINQYSNYYWKKAGLNVKGKRTLGENIADNGGLREAFRAYRKwindrRQGLEEPLLPGI-TFTNNQLFFLSYAHVRCNSY 444
Cdd:pfam01431  80 LIEQYSEYTPPDGTKCANGTLTLGENIADLGGLTIALRAYKK-----LLSANETVLPGFeNLTPDQLFFRGAAQIWCMKQ 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768032502  445 RPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKAFNCPPNSTMNRGmDSCRL 496
Cdd:pfam01431 155 SPAEVLRQLLVDPHSPPEFRVNGVMSNMPAFYEAFNCPEGDKMNPE-PRCRL 205
 
Name Accession Description Interval E-value
M13 cd08662
Peptidase family M13 includes neprilysin and endothelin-converting enzyme I; The M13 family of ...
1-488 0e+00

Peptidase family M13 includes neprilysin and endothelin-converting enzyme I; The M13 family of metallopeptidases includes neprilysin (neutral endopeptidase, NEP, enkephalinase, CD10, CALLA, EC 3.4.24.11), endothelin-converting enzyme I (ECE-1, EC 3.4.24.71), erythrocyte surface antigen KELL (ECE-3), phosphate-regulating gene on the X chromosome (PHEX), soluble secreted endopeptidase (SEP), and damage-induced neuronal endopeptidase (DINE)/X-converting enzyme (XCE). Proteins in this family fulfill a broad range of physiological roles due to the greater variation in the active site's S2' subsite allowing substrate specificity. NEP is expressed in a variety of tissues including kidney and brain, and is involved in many physiological and pathological processes, including blood pressure and inflammatory response. It degrades a wide array of substrates such as substance P, enkephalins, cholecystokinin, neurotensin and somatostatin. It is an important enzyme in the regulation of amyloid-beta (Abeta) protein that forms amyloid plaques that are associated with Alzeimers disease (AD). ECE-1 catalyzes the final rate-limiting step in the biosynthesis of endothelins via post-translational conversion of the biologically inactive big endothelins. Like NEP, it also hydrolyzes bradykinin, substance P, neurotensin, and Abeta. Endothelin-1 overproduction has been implicated in various diseases including stroke, asthma, hypertension, and cardiac and renal failure. Kell is a homolog of NEP and constitutes a major antigen on human erythrocytes; it preferentially cleaves big endothelin-3 to produce bioactive endothelin-3, but is also known to cleave substance P and neurokinin A. PHEX forms a complex interaction with fibroblast growth factor 23 (FGF23) and matrix extracellular phosphoglycoprotein, causing bone mineralization. A loss-of-function mutation in PHEX disrupts this interaction leading to hypophosphatemic rickets; X-linked hypophosphatemic (XLH) rickets is the most common form of metabolic rickets. ECEL1 is a brain metalloprotease which plays a critical role in the nervous regulation of the respiratory system, while DINE is abundantly expressed in the hypothalamus and its expression responds to nerve injury. A majority of these M13 proteases are prime therapeutic targets for selective inhibition.


Pssm-ID: 341056 [Multi-domain]  Cd Length: 642  Bit Score: 589.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502   1 MVDTAVLLGANSSRAEHDMKSVLRLEIKIAEIMIP-HENRTSEAMYNKMNISELSAMIPQFDWLGYIKKVIDtrlyphlk 79
Cdd:cd08662  164 IAKLLELLGADEEEAEKLAEDVLAFETELAKISLSsEELRDPEKTYNPLTLAELQKLAPSIDWKAYLKALGP-------- 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502  80 DISPSENVVVRVPQYFKDLFRILGSERKKTIANYLVWRMVYSRIPNLSRRFQYRWLEFSRVIQGTTTLLPQWDKCVNFIE 159
Cdd:cd08662  236 PADDPDKVIVSQPEYLKKLDKLLASTPLRTLKNYLIWRLLDSLAPYLSKEFRDARFFYGKALSGQKEPEPRWKRCVELVN 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 160 SALPYVVGKMFVDVYFQEDKKEMMEELVEGVRWAFIDMLEkENEWMDAGTKRKAKEKARAVLAKVGYPEFIMNDTHVNED 239
Cdd:cd08662  316 GALGEALGRLYVEKYFSEEAKADVEEMVENIKEAFKERLE-NLDWMDEETKKKALEKLDAMKVKIGYPDKWRDYSALDIY 394
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 240 LKAIKFSEaDYFGNVLQTRKYLAQSDFFWLRKAVPKTEWFTNPTTVNAFYSASTNQIRFPAGELQKPFFwGTEYPRSLSY 319
Cdd:cd08662  395 YDDLNVSD-SYFENVLRLLRFETKRQLAKLGKPVDRTEWSMSPQTVNAYYNPSLNEIVFPAGILQPPFF-DPDAPDALNY 472
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 320 GAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSTESEEKFKEKTKCMINQYSNYYWKKaGLNVKGKRTLGENIADNGGLR 399
Cdd:cd08662  473 GGIGAVIGHEITHGFDDQGRQYDENGNLRNWWTNEDRKEFEERAQCLVDQYSNYEVPP-GLHVNGKLTLGENIADNGGLR 551
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 400 EAFRAYRKWINDRrqglEEPLLPGITFTNNQLFFLSYAHVRCNSYRPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKAF 479
Cdd:cd08662  552 LAYRAYKKWLKEN----GPELPGLEGFTPEQLFFLSFAQVWCSKYRPEALRQLLLTDPHSPGKFRVNGPLSNSPEFAEAF 627

                 ....*....
gi 768032502 480 NCPPNSTMN 488
Cdd:cd08662  628 NCPPGSPMN 636
PepO COG3590
Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones];
7-497 3.08e-149

Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442809 [Multi-domain]  Cd Length: 674  Bit Score: 441.90  E-value: 3.08e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502   7 LLGANSSRAEHDMKSVLRLEIKIAEIMIPH-ENRTSEAMYNKMNISELSAMIPQFDWLGYIKKVidtrlyphlkDISPSE 85
Cdd:COG3590  207 LAGYDEADAAAAAEAVLALETALAKAHWSRvELRDPEKTYNPMTVAELAKLAPGFDWDAYLKAL----------GLPAVD 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502  86 NVVVRVPQYFKDLFRILGSERKKTIANYLVWRMVYSRIPNLSRRFQYRWLEF-SRVIQGTTTLLPQWDKCVNFIESALPY 164
Cdd:COG3590  277 EVIVGQPSFFKALDKLLASTPLEDWKAYLRWHLLDSAAPYLSKAFVDANFDFyGKTLSGQKEQRPRWKRAVALVNGALGE 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 165 VVGKMFVDVYFQEDKKEMMEELVEGVRWAFIDMLEKeNEWMDAGTKRKAKEKARAVLAKVGYPEfimndthVNEDLKAIK 244
Cdd:COG3590  357 ALGQLYVERYFPPEAKARMEELVANLRAAYRERIEN-LDWMSPETKAKALEKLAAFTPKIGYPD-------KWRDYSGLE 428
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 245 FSEADYFGNVLQTRKylaqsdFFWLR------KAVPKTEWFTNPTTVNAFYSASTNQIRFPAGELQKPFFwGTEYPRSLS 318
Cdd:COG3590  429 IKRDDLVGNVLRASA------FEYQRelaklgKPVDRTEWGMTPQTVNAYYNPTMNEIVFPAAILQPPFF-DPKADDAVN 501
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 319 YGAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSTESEEKFKEKTKCMINQYSNYYWKKaGLNVKGKRTLGENIADNGGL 398
Cdd:COG3590  502 YGGIGAVIGHEITHGFDDQGSQFDGDGNLRNWWTPEDRAAFEARTKKLVAQYDAYEPLP-GLHVNGKLTLGENIADLGGL 580
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502 399 REAFRAYRKwindRRQGLEEPLLPGitFTNNQLFFLSYAHVRCNSYRPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKA 478
Cdd:COG3590  581 SIAYDAYKL----SLKGKEAPVIDG--FTGDQRFFLGWAQVWRSKARDEALRQRLATDPHSPGEFRVNGPVRNLDAFYEA 654
                        490       500
                 ....*....|....*....|
gi 768032502 479 FNCPPNSTMNR-GMDSCRLW 497
Cdd:COG3590  655 FDVKPGDKMYLaPEDRVRIW 674
Peptidase_M13 pfam01431
Peptidase family M13; Mammalian enzymes are typically type-II membrane anchored enzymes which ...
286-496 2.58e-79

Peptidase family M13; Mammalian enzymes are typically type-II membrane anchored enzymes which are known, or believed to activate or inactivate oligopeptide (pro)-hormones such as opioid peptides. The family also contains a bacterial member believed to be involved with milk protein cleavage.


Pssm-ID: 279739 [Multi-domain]  Cd Length: 205  Bit Score: 246.17  E-value: 2.58e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502  286 NAFYSASTNQIRFPAGELQKPFFwGTEYPRSLSYGAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSTESEEKFKEKTKC 365
Cdd:pfam01431   1 NAYYQPNRNEIVFPAAILQPPFF-DPNYPRAVNYGGIGNVIAHEITHGFDDQGAQFDKDGNLRSWWTDEDAEEFKDRAQC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502  366 MINQYSNYYWKKAGLNVKGKRTLGENIADNGGLREAFRAYRKwindrRQGLEEPLLPGI-TFTNNQLFFLSYAHVRCNSY 444
Cdd:pfam01431  80 LIEQYSEYTPPDGTKCANGTLTLGENIADLGGLTIALRAYKK-----LLSANETVLPGFeNLTPDQLFFRGAAQIWCMKQ 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768032502  445 RPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKAFNCPPNSTMNRGmDSCRL 496
Cdd:pfam01431 155 SPAEVLRQLLVDPHSPPEFRVNGVMSNMPAFYEAFNCPEGDKMNPE-PRCRL 205
Peptidase_M13_N pfam05649
Peptidase family M13; M13 peptidases are well-studied proteases found in a wide range of ...
1-227 1.25e-72

Peptidase family M13; M13 peptidases are well-studied proteases found in a wide range of organizms including mammals and bacteria. In mammals they participate in processes such as cardiovascular development, blood-pressure regulation, nervous control of respiration, and regulation of the function of neuropeptides in the central nervous system. In bacteria they may be used for digestion of milk.


Pssm-ID: 461703  Cd Length: 382  Bit Score: 234.89  E-value: 1.25e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502    1 MVDTAVLLGAnSSRAEHDMKSVLRLEIKIAEIMIPH-ENRTSEAMYNKMNISELSAMIPQFDWLGYIKKVidtrlyphLK 79
Cdd:pfam05649 166 IAKLLTLLGA-SEEAAALAEEVLAFETKLAKASLSReERRDPEKTYNPMTLAELQKLAPGIDWKAYLNAA--------GL 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032502   80 DISPSENVVVRVPQYFKDLFRILGSERKKTIANYLVWRMVYSRIPNLSRRFQYRWLEFSRVIQGTTTLlPQWDKCVNFIE 159
Cdd:pfam05649 237 PDVPSDEVIVSQPEYLKALSKLLAETPLRTLKNYLIWRLVRSLAPYLSDEFRDANFEFYGTLSGTKQR-PRWKRCVSLVN 315
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032502  160 SALPYVVGKMFVDVYFQEDKKEMMEELVEGVRWAFIDMLEkENEWMDAGTKRKAKEKARAVLAKVGYP 227
Cdd:pfam05649 316 GLLGEALGRLYVKKYFPEEAKARVEELVENIKEAFRERLD-ELDWMDEETKKKALEKLDAMTVKIGYP 382
 
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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