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Conserved domains on  [gi|1039774987|ref|XP_017177062|]
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kell blood group glycoprotein homolog isoform X6 [Mus musculus]

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 ...
1-366 1.42e-109

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: 333.95  E-value: 1.42e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987   1 MILGLVDTLSPALDTKFQEARRELIQELRKLKERPPlpaypRWMKCVEQTGAFFEPTLAALFVREAFGPSIQSAAMELFA 80
Cdd:cd08662   270 LIWRLLDSLAPYLSKEFRDARFFYGKALSGQKEPEP-----RWKRCVELVNGALGEALGRLYVEKYFSEEAKADVEEMVE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987  81 EIKDAVIIRLKKLSWISEETQKEALNKLAQLQVEMGAPKRAVKPDIATQEYNDIQLGPSFLQSFLSCVRSLRARNVQSFL 160
Cdd:cd08662   345 NIKEAFKERLENLDWMDEETKKKALEKLDAMKVKIGYPDKWRDYSALDIYYDDLNVSDSYFENVLRLLRFETKRQLAKLG 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 161 QPFPYHRWQKSPWEVNAYYSISDHMVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIF--------YQLLLPGGC 232
Cdd:cd08662   425 KPVDRTEWSMSPQTVNAYYNPSLNEIVFPAGILQPPFFDPDAPDALNYGGIGAVIGHEITHGFddqgrqydENGNLRNWW 504
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 233 PACDTHVLQEALLCLERHYAAFPLPSISSFNGSHTLLENAADIGGVAIAFQAYSKRIVEHTGELtLPNLDLSPYQLFFRS 312
Cdd:cd08662   505 TNEDRKEFEERAQCLVDQYSNYEVPPGLHVNGKLTLGENIADNGGLRLAYRAYKKWLKENGPEL-PGLEGFTPEQLFFLS 583
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774987 313 YAQVMCR-----GLSSQDPQDPHSPPSLRVHGPLSNTPDFAKHFHCPRGTLLNPSARCK 366
Cdd:cd08662   584 FAQVWCSkyrpeALRQLLLTDPHSPGKFRVNGPLSNSPEFAEAFNCPPGSPMNPEKKCR 642
 
Name Accession Description Interval E-value
M13 cd08662
Peptidase family M13 includes neprilysin and endothelin-converting enzyme I; The M13 family of ...
1-366 1.42e-109

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: 333.95  E-value: 1.42e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987   1 MILGLVDTLSPALDTKFQEARRELIQELRKLKERPPlpaypRWMKCVEQTGAFFEPTLAALFVREAFGPSIQSAAMELFA 80
Cdd:cd08662   270 LIWRLLDSLAPYLSKEFRDARFFYGKALSGQKEPEP-----RWKRCVELVNGALGEALGRLYVEKYFSEEAKADVEEMVE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987  81 EIKDAVIIRLKKLSWISEETQKEALNKLAQLQVEMGAPKRAVKPDIATQEYNDIQLGPSFLQSFLSCVRSLRARNVQSFL 160
Cdd:cd08662   345 NIKEAFKERLENLDWMDEETKKKALEKLDAMKVKIGYPDKWRDYSALDIYYDDLNVSDSYFENVLRLLRFETKRQLAKLG 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 161 QPFPYHRWQKSPWEVNAYYSISDHMVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIF--------YQLLLPGGC 232
Cdd:cd08662   425 KPVDRTEWSMSPQTVNAYYNPSLNEIVFPAGILQPPFFDPDAPDALNYGGIGAVIGHEITHGFddqgrqydENGNLRNWW 504
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 233 PACDTHVLQEALLCLERHYAAFPLPSISSFNGSHTLLENAADIGGVAIAFQAYSKRIVEHTGELtLPNLDLSPYQLFFRS 312
Cdd:cd08662   505 TNEDRKEFEERAQCLVDQYSNYEVPPGLHVNGKLTLGENIADNGGLRLAYRAYKKWLKENGPEL-PGLEGFTPEQLFFLS 583
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774987 313 YAQVMCR-----GLSSQDPQDPHSPPSLRVHGPLSNTPDFAKHFHCPRGTLLNPSARCK 366
Cdd:cd08662   584 FAQVWCSkyrpeALRQLLLTDPHSPGKFRVNGPLSNSPEFAEAFNCPPGSPMNPEKKCR 642
Peptidase_M13 pfam01431
Peptidase family M13; Mammalian enzymes are typically type-II membrane anchored enzymes which ...
176-367 1.95e-75

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: 231.92  E-value: 1.95e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 176 NAYYSISDHMVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLP--------GGCPACDTHVLQEALLCL 247
Cdd:pfam01431   1 NAYYQPNRNEIVFPAAILQPPFFDPNYPRAVNYGGIGNVIAHEITHGFDDQGAQfdkdgnlrSWWTDEDAEEFKDRAQCL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 248 ERHYAAFPLPS-ISSFNGSHTLLENAADIGGVAIAFQAYSKRivEHTGELTLPNLD-LSPYQLFFRSYAQVMCRGLSSQD 325
Cdd:pfam01431  81 IEQYSEYTPPDgTKCANGTLTLGENIADLGGLTIALRAYKKL--LSANETVLPGFEnLTPDQLFFRGAAQIWCMKQSPAE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1039774987 326 -----PQDPHSPPSLRVHGPLSNTPDFAKHFHCPRGTLLNPSARCKL 367
Cdd:pfam01431 159 vlrqlLVDPHSPPEFRVNGVMSNMPAFYEAFNCPEGDKMNPEPRCRL 205
PepO COG3590
Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones];
5-368 9.01e-60

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


Pssm-ID: 442809 [Multi-domain]  Cd Length: 674  Bit Score: 204.23  E-value: 9.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987   5 LVDTLSPALDTKFQEAR-----REL--IQELRklkerpplpayPRWMKCVEQTGAFFEPTLAALFVREAFGPSIQSAAME 77
Cdd:COG3590   309 LLDSAAPYLSKAFVDANfdfygKTLsgQKEQR-----------PRWKRAVALVNGALGEALGQLYVERYFPPEAKARMEE 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987  78 LFAEIKDAVIIRLKKLSWISEETQKEALNKLAQLQVEMGAPKRAvkpdiatQEYNDIQLGP-SFLQSFLSCVRSLRARNV 156
Cdd:COG3590   378 LVANLRAAYRERIENLDWMSPETKAKALEKLAAFTPKIGYPDKW-------RDYSGLEIKRdDLVGNVLRASAFEYQREL 450
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 157 QSFLQPFPYHRWQKSPWEVNAYYSISDHMVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFyqlllpggcpacD 236
Cdd:COG3590   451 AKLGKPVDRTEWGMTPQTVNAYYNPTMNEIVFPAAILQPPFFDPKADDAVNYGGIGAVIGHEITHGF------------D 518
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 237 ThvlQ----------------------EALL-CLERHYAAF-PLPSIsSFNGSHTLLENAADIGGVAIAFQAYSKriveH 292
Cdd:COG3590   519 D---QgsqfdgdgnlrnwwtpedraafEARTkKLVAQYDAYePLPGL-HVNGKLTLGENIADLGGLSIAYDAYKL----S 590
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 293 TGELTLPNLD-LSPYQLFFRSYAQVMCrglSSQDPQ--------DPHSPPSLRVHGPLSNTPDFAKHFHCPRGT--LLNP 361
Cdd:COG3590   591 LKGKEAPVIDgFTGDQRFFLGWAQVWR---SKARDEalrqrlatDPHSPGEFRVNGPVRNLDAFYEAFDVKPGDkmYLAP 667

                  ....*..
gi 1039774987 362 SARCKLW 368
Cdd:COG3590   668 EDRVRIW 674
 
Name Accession Description Interval E-value
M13 cd08662
Peptidase family M13 includes neprilysin and endothelin-converting enzyme I; The M13 family of ...
1-366 1.42e-109

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: 333.95  E-value: 1.42e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987   1 MILGLVDTLSPALDTKFQEARRELIQELRKLKERPPlpaypRWMKCVEQTGAFFEPTLAALFVREAFGPSIQSAAMELFA 80
Cdd:cd08662   270 LIWRLLDSLAPYLSKEFRDARFFYGKALSGQKEPEP-----RWKRCVELVNGALGEALGRLYVEKYFSEEAKADVEEMVE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987  81 EIKDAVIIRLKKLSWISEETQKEALNKLAQLQVEMGAPKRAVKPDIATQEYNDIQLGPSFLQSFLSCVRSLRARNVQSFL 160
Cdd:cd08662   345 NIKEAFKERLENLDWMDEETKKKALEKLDAMKVKIGYPDKWRDYSALDIYYDDLNVSDSYFENVLRLLRFETKRQLAKLG 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 161 QPFPYHRWQKSPWEVNAYYSISDHMVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIF--------YQLLLPGGC 232
Cdd:cd08662   425 KPVDRTEWSMSPQTVNAYYNPSLNEIVFPAGILQPPFFDPDAPDALNYGGIGAVIGHEITHGFddqgrqydENGNLRNWW 504
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 233 PACDTHVLQEALLCLERHYAAFPLPSISSFNGSHTLLENAADIGGVAIAFQAYSKRIVEHTGELtLPNLDLSPYQLFFRS 312
Cdd:cd08662   505 TNEDRKEFEERAQCLVDQYSNYEVPPGLHVNGKLTLGENIADNGGLRLAYRAYKKWLKENGPEL-PGLEGFTPEQLFFLS 583
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774987 313 YAQVMCR-----GLSSQDPQDPHSPPSLRVHGPLSNTPDFAKHFHCPRGTLLNPSARCK 366
Cdd:cd08662   584 FAQVWCSkyrpeALRQLLLTDPHSPGKFRVNGPLSNSPEFAEAFNCPPGSPMNPEKKCR 642
Peptidase_M13 pfam01431
Peptidase family M13; Mammalian enzymes are typically type-II membrane anchored enzymes which ...
176-367 1.95e-75

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: 231.92  E-value: 1.95e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 176 NAYYSISDHMVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLP--------GGCPACDTHVLQEALLCL 247
Cdd:pfam01431   1 NAYYQPNRNEIVFPAAILQPPFFDPNYPRAVNYGGIGNVIAHEITHGFDDQGAQfdkdgnlrSWWTDEDAEEFKDRAQCL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 248 ERHYAAFPLPS-ISSFNGSHTLLENAADIGGVAIAFQAYSKRivEHTGELTLPNLD-LSPYQLFFRSYAQVMCRGLSSQD 325
Cdd:pfam01431  81 IEQYSEYTPPDgTKCANGTLTLGENIADLGGLTIALRAYKKL--LSANETVLPGFEnLTPDQLFFRGAAQIWCMKQSPAE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1039774987 326 -----PQDPHSPPSLRVHGPLSNTPDFAKHFHCPRGTLLNPSARCKL 367
Cdd:pfam01431 159 vlrqlLVDPHSPPEFRVNGVMSNMPAFYEAFNCPEGDKMNPEPRCRL 205
PepO COG3590
Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones];
5-368 9.01e-60

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


Pssm-ID: 442809 [Multi-domain]  Cd Length: 674  Bit Score: 204.23  E-value: 9.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987   5 LVDTLSPALDTKFQEAR-----REL--IQELRklkerpplpayPRWMKCVEQTGAFFEPTLAALFVREAFGPSIQSAAME 77
Cdd:COG3590   309 LLDSAAPYLSKAFVDANfdfygKTLsgQKEQR-----------PRWKRAVALVNGALGEALGQLYVERYFPPEAKARMEE 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987  78 LFAEIKDAVIIRLKKLSWISEETQKEALNKLAQLQVEMGAPKRAvkpdiatQEYNDIQLGP-SFLQSFLSCVRSLRARNV 156
Cdd:COG3590   378 LVANLRAAYRERIENLDWMSPETKAKALEKLAAFTPKIGYPDKW-------RDYSGLEIKRdDLVGNVLRASAFEYQREL 450
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 157 QSFLQPFPYHRWQKSPWEVNAYYSISDHMVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFyqlllpggcpacD 236
Cdd:COG3590   451 AKLGKPVDRTEWGMTPQTVNAYYNPTMNEIVFPAAILQPPFFDPKADDAVNYGGIGAVIGHEITHGF------------D 518
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 237 ThvlQ----------------------EALL-CLERHYAAF-PLPSIsSFNGSHTLLENAADIGGVAIAFQAYSKriveH 292
Cdd:COG3590   519 D---QgsqfdgdgnlrnwwtpedraafEARTkKLVAQYDAYePLPGL-HVNGKLTLGENIADLGGLSIAYDAYKL----S 590
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987 293 TGELTLPNLD-LSPYQLFFRSYAQVMCrglSSQDPQ--------DPHSPPSLRVHGPLSNTPDFAKHFHCPRGT--LLNP 361
Cdd:COG3590   591 LKGKEAPVIDgFTGDQRFFLGWAQVWR---SKARDEalrqrlatDPHSPGEFRVNGPVRNLDAFYEAFDVKPGDkmYLAP 667

                  ....*..
gi 1039774987 362 SARCKLW 368
Cdd:COG3590   668 EDRVRIW 674
Peptidase_M13_N pfam05649
Peptidase family M13; M13 peptidases are well-studied proteases found in a wide range of ...
1-118 1.71e-29

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: 117.01  E-value: 1.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774987   1 MILGLVDTLSPALDTKFQEARRELIQELRKLKERPplpaypRWMKCVEQTGAFFEPTLAALFVREAFGPSIQSAAMELFA 80
Cdd:pfam05649 271 LIWRLVRSLAPYLSDEFRDANFEFYGTLSGTKQRP------RWKRCVSLVNGLLGEALGRLYVKKYFPEEAKARVEELVE 344
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039774987  81 EIKDAVIIRLKKLSWISEETQKEALNKLAQLQVEMGAP 118
Cdd:pfam05649 345 NIKEAFRERLDELDWMDEETKKKALEKLDAMTVKIGYP 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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