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Conserved domains on  [gi|221474862|ref|NP_609577|]
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Neprilysin-like 7, isoform A [Drosophila melanogaster]

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 ...
52-666 1.26e-148

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: 445.66  E-value: 1.26e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  52 IDPCENFYEFSCGGWKKADLVPEQARNTSFLNAIQHKIDEQIQGFLQNATKRELEDlgvngttSAEIKAKQFYASCVEMK 131
Cdd:cd08662    1 VDPCDDFYQYACGNWLKNHPIPADKSSWGSFSELQDRNEEQLREILEEAASSAADS-------SAEQKAKDFYKSCMDEE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 132 ANLSLGYQYFMEH--DGDRLKERNATYDWMYINFMSKYDIYPLLALKVHYSTSSRKFDIL------LTLPSKVLAGFSE- 202
Cdd:cd08662   74 AIEKLGLKPLKPLldKIGGLPSLDDLAAELLLALLRRLGVSLLFGLGVSPDPKNSSRNILylgqpgLGLPDRDYYLDEEn 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 203 --------EQLKNMTREFGLDssAEKVKQFVENfnnLTQFERNLVSLAKS----RNETEQLN-FKEFLVKHKHDRLNWTR 269
Cdd:cd08662  154 aeireaykKYIAKLLELLGAD--EEEAEKLAED---VLAFETELAKISLSseelRDPEKTYNpLTLAELQKLAPSIDWKA 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 270 FFELAFNGSQESHWPVLNQLDNINDLVFFLEQTNLETLKGYIKMR--------------ELVKFYGLWKTQTKTGGVQSE 335
Cdd:cd08662  229 YLKALGPPADDPDKVIVSQPEYLKKLDKLLASTPLRTLKNYLIWRlldslapylskefrDARFFYGKALSGQKEPEPRWK 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 336 -CRSLSETYFNYALLPWFIGKVFDKERRADILSVAKDIKDTFYDLLDHHTWLDEDTRSQAKTKLASMDILVGYTDDLQHR 414
Cdd:cd08662  309 rCVELVNGALGEALGRLYVEKYFSEEAKADVEEMVENIKEAFKERLENLDWMDEETKKKALEKLDAMKVKIGYPDKWRDY 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 415 EVIDGVYSDINMTGNWFENLCILEGSRARIRLRSVDKALIP--LLMPTRTVNAYYADFLNLAFITIGMAQWPFYHIDFPD 492
Cdd:cd08662  389 SALDIYYDDLNVSDSYFENVLRLLRFETKRQLAKLGKPVDRteWSMSPQTVNAYYNPSLNEIVFPAGILQPPFFDPDAPD 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 493 VLKYAGVGNIIGHEMAHGFDSYCYQYNYDGKKTNWWSSASLRNFKERYRCLESQYNKF-ILMGVQTNGSLTSGDNIADNV 571
Cdd:cd08662  469 ALNYGGIGAVIGHEITHGFDDQGRQYDENGNLRNWWTNEDRKEFEERAQCLVDQYSNYeVPPGLHVNGKLTLGENIADNG 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 572 GTRMAYYAFKRKTGDKAwlEKPLRGVNFNNKQLFFVKFAQTWCNGKDNGDKLRRLKTDVHAYDEFRVQGTLSNMPEFSEA 651
Cdd:cd08662  549 GLRLAYRAYKKWLKENG--PELPGLEGFTPEQLFFLSFAQVWCSKYRPEALRQLLLTDPHSPGKFRVNGPLSNSPEFAEA 626
                        650
                 ....*....|....*
gi 221474862 652 FNCKLGTEMNPLKKC 666
Cdd:cd08662  627 FNCPPGSPMNPEKKC 641
 
Name Accession Description Interval E-value
M13 cd08662
Peptidase family M13 includes neprilysin and endothelin-converting enzyme I; The M13 family of ...
52-666 1.26e-148

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: 445.66  E-value: 1.26e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  52 IDPCENFYEFSCGGWKKADLVPEQARNTSFLNAIQHKIDEQIQGFLQNATKRELEDlgvngttSAEIKAKQFYASCVEMK 131
Cdd:cd08662    1 VDPCDDFYQYACGNWLKNHPIPADKSSWGSFSELQDRNEEQLREILEEAASSAADS-------SAEQKAKDFYKSCMDEE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 132 ANLSLGYQYFMEH--DGDRLKERNATYDWMYINFMSKYDIYPLLALKVHYSTSSRKFDIL------LTLPSKVLAGFSE- 202
Cdd:cd08662   74 AIEKLGLKPLKPLldKIGGLPSLDDLAAELLLALLRRLGVSLLFGLGVSPDPKNSSRNILylgqpgLGLPDRDYYLDEEn 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 203 --------EQLKNMTREFGLDssAEKVKQFVENfnnLTQFERNLVSLAKS----RNETEQLN-FKEFLVKHKHDRLNWTR 269
Cdd:cd08662  154 aeireaykKYIAKLLELLGAD--EEEAEKLAED---VLAFETELAKISLSseelRDPEKTYNpLTLAELQKLAPSIDWKA 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 270 FFELAFNGSQESHWPVLNQLDNINDLVFFLEQTNLETLKGYIKMR--------------ELVKFYGLWKTQTKTGGVQSE 335
Cdd:cd08662  229 YLKALGPPADDPDKVIVSQPEYLKKLDKLLASTPLRTLKNYLIWRlldslapylskefrDARFFYGKALSGQKEPEPRWK 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 336 -CRSLSETYFNYALLPWFIGKVFDKERRADILSVAKDIKDTFYDLLDHHTWLDEDTRSQAKTKLASMDILVGYTDDLQHR 414
Cdd:cd08662  309 rCVELVNGALGEALGRLYVEKYFSEEAKADVEEMVENIKEAFKERLENLDWMDEETKKKALEKLDAMKVKIGYPDKWRDY 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 415 EVIDGVYSDINMTGNWFENLCILEGSRARIRLRSVDKALIP--LLMPTRTVNAYYADFLNLAFITIGMAQWPFYHIDFPD 492
Cdd:cd08662  389 SALDIYYDDLNVSDSYFENVLRLLRFETKRQLAKLGKPVDRteWSMSPQTVNAYYNPSLNEIVFPAGILQPPFFDPDAPD 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 493 VLKYAGVGNIIGHEMAHGFDSYCYQYNYDGKKTNWWSSASLRNFKERYRCLESQYNKF-ILMGVQTNGSLTSGDNIADNV 571
Cdd:cd08662  469 ALNYGGIGAVIGHEITHGFDDQGRQYDENGNLRNWWTNEDRKEFEERAQCLVDQYSNYeVPPGLHVNGKLTLGENIADNG 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 572 GTRMAYYAFKRKTGDKAwlEKPLRGVNFNNKQLFFVKFAQTWCNGKDNGDKLRRLKTDVHAYDEFRVQGTLSNMPEFSEA 651
Cdd:cd08662  549 GLRLAYRAYKKWLKENG--PELPGLEGFTPEQLFFLSFAQVWCSKYRPEALRQLLLTDPHSPGKFRVNGPLSNSPEFAEA 626
                        650
                 ....*....|....*
gi 221474862 652 FNCKLGTEMNPLKKC 666
Cdd:cd08662  627 FNCPPGSPMNPEKKC 641
PepO COG3590
Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones];
43-669 1.29e-70

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


Pssm-ID: 442809 [Multi-domain]  Cd Length: 674  Bit Score: 242.37  E-value: 1.29e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  43 FLLSTMNRTIDPCENFYEFSCGGW-KKADLVPEQARNTSFlNAIQHKIDEQIQGFLQNATKRELEDlgvngtTSAEIKAK 121
Cdd:COG3590   28 IDLANMDTSVRPGDDFYRYVNGGWlKTTPIPADRSRWGSF-NELRERNEARLRAILEEAAAAPAAA------GSDEQKIG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 122 QFYASCVEMKANLSLGYQ----YFMEHDGdrLKERNATYDwmYINFMSKYDIYPLLALKV--HYSTSSRkfDIL------ 189
Cdd:COG3590  101 DLYASFMDEAAIEALGLAplkpDLARIDA--IKDKADLAA--LLAALHRAGVGGLFGFGVdaDLKNSTR--YIAylgqgg 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 190 LTLPSK-------------------------VLAGFSEEQLKNmtrefgldsSAEKVKQFvEnfnnlTQFERNLVSLAKS 244
Cdd:COG3590  175 LGLPDRdyylkddeksaeiraayvahvakmlELAGYDEADAAA---------AAEAVLAL-E-----TALAKAHWSRVEL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 245 RNETEQLN---FKEFLVKHKHdrLNWTRFFELAFNGSQESHwpVLNQLDNINDLVFFLEQTNLETLKGYIKMR------- 314
Cdd:COG3590  240 RDPEKTYNpmtVAELAKLAPG--FDWDAYLKALGLPAVDEV--IVGQPSFFKALDKLLASTPLEDWKAYLRWHlldsaap 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 315 ----ELVK----FYGlwktQTKTG----------GVQSECRSLSETyfnyallpwfIGKV-----FDKERRADILSVAKD 371
Cdd:COG3590  316 ylskAFVDanfdFYG----KTLSGqkeqrprwkrAVALVNGALGEA----------LGQLyveryFPPEAKARMEELVAN 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 372 IKDTFYDLLDHHTWLDEDTRSQAKTKLASMDILVGYTD---DlqhrevidgvYSDINMT-GNWFENlcILEGSRARIRlR 447
Cdd:COG3590  382 LRAAYRERIENLDWMSPETKAKALEKLAAFTPKIGYPDkwrD----------YSGLEIKrDDLVGN--VLRASAFEYQ-R 448
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 448 SVDKALIPL-----LMPTRTVNAYYadflNLAFITI----GMAQWPFYHIDFPDVLKYAGVGNIIGHEMAHGFD---Syc 515
Cdd:COG3590  449 ELAKLGKPVdrtewGMTPQTVNAYY----NPTMNEIvfpaAILQPPFFDPKADDAVNYGGIGAVIGHEITHGFDdqgS-- 522
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 516 yQYNYDGKKTNWWSSASLRNFKERYRCLESQYNKF-ILMGVQTNGSLTSGDNIADNVGTRMAYYAFKRKTGDKawlEKPL 594
Cdd:COG3590  523 -QFDGDGNLRNWWTPEDRAAFEARTKKLVAQYDAYePLPGLHVNGKLTLGENIADLGGLSIAYDAYKLSLKGK---EAPV 598
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 595 RGvNFNNKQLFFVKFAQTWCNgkdngdKLR------RLKTDVHAYDEFRVQGTLSNMPEFSEAFNCKLGTEM--NPLKKC 666
Cdd:COG3590  599 ID-GFTGDQRFFLGWAQVWRS------KARdealrqRLATDPHSPGEFRVNGPVRNLDAFYEAFDVKPGDKMylAPEDRV 671

                 ...
gi 221474862 667 VVW 669
Cdd:COG3590  672 RIW 674
Peptidase_M13 pfam01431
Peptidase family M13; Mammalian enzymes are typically type-II membrane anchored enzymes which ...
464-666 3.79e-53

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: 181.46  E-value: 3.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  464 NAYYADFLNLAFITIGMAQWPFYHIDFPDVLKYAGVGNIIGHEMAHGFDSYCYQYNYDGKKTNWWSSASLRNFKERYRCL 543
Cdd:pfam01431   1 NAYYQPNRNEIVFPAAILQPPFFDPNYPRAVNYGGIGNVIAHEITHGFDDQGAQFDKDGNLRSWWTDEDAEEFKDRAQCL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  544 ESQYNKFILM--GVQTNGSLTSGDNIADNVGTRMAYYAFKRKTGDKawlEKPLRGV-NFNNKQLFFVKFAQTWCNGKDNG 620
Cdd:pfam01431  81 IEQYSEYTPPdgTKCANGTLTLGENIADLGGLTIALRAYKKLLSAN---ETVLPGFeNLTPDQLFFRGAAQIWCMKQSPA 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 221474862  621 DKLRRLKTDVHAYDEFRVQGTLSNMPEFSEAFNCKLGTEMNPLKKC 666
Cdd:pfam01431 158 EVLRQLLVDPHSPPEFRVNGVMSNMPAFYEAFNCPEGDKMNPEPRC 203
 
Name Accession Description Interval E-value
M13 cd08662
Peptidase family M13 includes neprilysin and endothelin-converting enzyme I; The M13 family of ...
52-666 1.26e-148

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: 445.66  E-value: 1.26e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  52 IDPCENFYEFSCGGWKKADLVPEQARNTSFLNAIQHKIDEQIQGFLQNATKRELEDlgvngttSAEIKAKQFYASCVEMK 131
Cdd:cd08662    1 VDPCDDFYQYACGNWLKNHPIPADKSSWGSFSELQDRNEEQLREILEEAASSAADS-------SAEQKAKDFYKSCMDEE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 132 ANLSLGYQYFMEH--DGDRLKERNATYDWMYINFMSKYDIYPLLALKVHYSTSSRKFDIL------LTLPSKVLAGFSE- 202
Cdd:cd08662   74 AIEKLGLKPLKPLldKIGGLPSLDDLAAELLLALLRRLGVSLLFGLGVSPDPKNSSRNILylgqpgLGLPDRDYYLDEEn 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 203 --------EQLKNMTREFGLDssAEKVKQFVENfnnLTQFERNLVSLAKS----RNETEQLN-FKEFLVKHKHDRLNWTR 269
Cdd:cd08662  154 aeireaykKYIAKLLELLGAD--EEEAEKLAED---VLAFETELAKISLSseelRDPEKTYNpLTLAELQKLAPSIDWKA 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 270 FFELAFNGSQESHWPVLNQLDNINDLVFFLEQTNLETLKGYIKMR--------------ELVKFYGLWKTQTKTGGVQSE 335
Cdd:cd08662  229 YLKALGPPADDPDKVIVSQPEYLKKLDKLLASTPLRTLKNYLIWRlldslapylskefrDARFFYGKALSGQKEPEPRWK 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 336 -CRSLSETYFNYALLPWFIGKVFDKERRADILSVAKDIKDTFYDLLDHHTWLDEDTRSQAKTKLASMDILVGYTDDLQHR 414
Cdd:cd08662  309 rCVELVNGALGEALGRLYVEKYFSEEAKADVEEMVENIKEAFKERLENLDWMDEETKKKALEKLDAMKVKIGYPDKWRDY 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 415 EVIDGVYSDINMTGNWFENLCILEGSRARIRLRSVDKALIP--LLMPTRTVNAYYADFLNLAFITIGMAQWPFYHIDFPD 492
Cdd:cd08662  389 SALDIYYDDLNVSDSYFENVLRLLRFETKRQLAKLGKPVDRteWSMSPQTVNAYYNPSLNEIVFPAGILQPPFFDPDAPD 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 493 VLKYAGVGNIIGHEMAHGFDSYCYQYNYDGKKTNWWSSASLRNFKERYRCLESQYNKF-ILMGVQTNGSLTSGDNIADNV 571
Cdd:cd08662  469 ALNYGGIGAVIGHEITHGFDDQGRQYDENGNLRNWWTNEDRKEFEERAQCLVDQYSNYeVPPGLHVNGKLTLGENIADNG 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 572 GTRMAYYAFKRKTGDKAwlEKPLRGVNFNNKQLFFVKFAQTWCNGKDNGDKLRRLKTDVHAYDEFRVQGTLSNMPEFSEA 651
Cdd:cd08662  549 GLRLAYRAYKKWLKENG--PELPGLEGFTPEQLFFLSFAQVWCSKYRPEALRQLLLTDPHSPGKFRVNGPLSNSPEFAEA 626
                        650
                 ....*....|....*
gi 221474862 652 FNCKLGTEMNPLKKC 666
Cdd:cd08662  627 FNCPPGSPMNPEKKC 641
PepO COG3590
Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones];
43-669 1.29e-70

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


Pssm-ID: 442809 [Multi-domain]  Cd Length: 674  Bit Score: 242.37  E-value: 1.29e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  43 FLLSTMNRTIDPCENFYEFSCGGW-KKADLVPEQARNTSFlNAIQHKIDEQIQGFLQNATKRELEDlgvngtTSAEIKAK 121
Cdd:COG3590   28 IDLANMDTSVRPGDDFYRYVNGGWlKTTPIPADRSRWGSF-NELRERNEARLRAILEEAAAAPAAA------GSDEQKIG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 122 QFYASCVEMKANLSLGYQ----YFMEHDGdrLKERNATYDwmYINFMSKYDIYPLLALKV--HYSTSSRkfDIL------ 189
Cdd:COG3590  101 DLYASFMDEAAIEALGLAplkpDLARIDA--IKDKADLAA--LLAALHRAGVGGLFGFGVdaDLKNSTR--YIAylgqgg 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 190 LTLPSK-------------------------VLAGFSEEQLKNmtrefgldsSAEKVKQFvEnfnnlTQFERNLVSLAKS 244
Cdd:COG3590  175 LGLPDRdyylkddeksaeiraayvahvakmlELAGYDEADAAA---------AAEAVLAL-E-----TALAKAHWSRVEL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 245 RNETEQLN---FKEFLVKHKHdrLNWTRFFELAFNGSQESHwpVLNQLDNINDLVFFLEQTNLETLKGYIKMR------- 314
Cdd:COG3590  240 RDPEKTYNpmtVAELAKLAPG--FDWDAYLKALGLPAVDEV--IVGQPSFFKALDKLLASTPLEDWKAYLRWHlldsaap 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 315 ----ELVK----FYGlwktQTKTG----------GVQSECRSLSETyfnyallpwfIGKV-----FDKERRADILSVAKD 371
Cdd:COG3590  316 ylskAFVDanfdFYG----KTLSGqkeqrprwkrAVALVNGALGEA----------LGQLyveryFPPEAKARMEELVAN 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 372 IKDTFYDLLDHHTWLDEDTRSQAKTKLASMDILVGYTD---DlqhrevidgvYSDINMT-GNWFENlcILEGSRARIRlR 447
Cdd:COG3590  382 LRAAYRERIENLDWMSPETKAKALEKLAAFTPKIGYPDkwrD----------YSGLEIKrDDLVGN--VLRASAFEYQ-R 448
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 448 SVDKALIPL-----LMPTRTVNAYYadflNLAFITI----GMAQWPFYHIDFPDVLKYAGVGNIIGHEMAHGFD---Syc 515
Cdd:COG3590  449 ELAKLGKPVdrtewGMTPQTVNAYY----NPTMNEIvfpaAILQPPFFDPKADDAVNYGGIGAVIGHEITHGFDdqgS-- 522
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 516 yQYNYDGKKTNWWSSASLRNFKERYRCLESQYNKF-ILMGVQTNGSLTSGDNIADNVGTRMAYYAFKRKTGDKawlEKPL 594
Cdd:COG3590  523 -QFDGDGNLRNWWTPEDRAAFEARTKKLVAQYDAYePLPGLHVNGKLTLGENIADLGGLSIAYDAYKLSLKGK---EAPV 598
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862 595 RGvNFNNKQLFFVKFAQTWCNgkdngdKLR------RLKTDVHAYDEFRVQGTLSNMPEFSEAFNCKLGTEM--NPLKKC 666
Cdd:COG3590  599 ID-GFTGDQRFFLGWAQVWRS------KARdealrqRLATDPHSPGEFRVNGPVRNLDAFYEAFDVKPGDKMylAPEDRV 671

                 ...
gi 221474862 667 VVW 669
Cdd:COG3590  672 RIW 674
Peptidase_M13 pfam01431
Peptidase family M13; Mammalian enzymes are typically type-II membrane anchored enzymes which ...
464-666 3.79e-53

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: 181.46  E-value: 3.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  464 NAYYADFLNLAFITIGMAQWPFYHIDFPDVLKYAGVGNIIGHEMAHGFDSYCYQYNYDGKKTNWWSSASLRNFKERYRCL 543
Cdd:pfam01431   1 NAYYQPNRNEIVFPAAILQPPFFDPNYPRAVNYGGIGNVIAHEITHGFDDQGAQFDKDGNLRSWWTDEDAEEFKDRAQCL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  544 ESQYNKFILM--GVQTNGSLTSGDNIADNVGTRMAYYAFKRKTGDKawlEKPLRGV-NFNNKQLFFVKFAQTWCNGKDNG 620
Cdd:pfam01431  81 IEQYSEYTPPdgTKCANGTLTLGENIADLGGLTIALRAYKKLLSAN---ETVLPGFeNLTPDQLFFRGAAQIWCMKQSPA 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 221474862  621 DKLRRLKTDVHAYDEFRVQGTLSNMPEFSEAFNCKLGTEMNPLKKC 666
Cdd:pfam01431 158 EVLRQLLVDPHSPPEFRVNGVMSNMPAFYEAFNCPEGDKMNPEPRC 203
Peptidase_M13_N pfam05649
Peptidase family M13; M13 peptidases are well-studied proteases found in a wide range of ...
54-407 1.06e-34

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: 135.89  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862   54 PCENFYEFSCGGWKKADLVPEQARNTSFLNAIQHKIDEQIQGFLQNATKRELEDlgvngttSAEIKAKQFYASCVEMKAN 133
Cdd:pfam05649   1 PCDDFYQYACGGWLKNHPIPADKSSWGTFDELRERNEKQLREILEEAAASESDP-------GAVEKAKDLYKSCMDTDAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  134 LSLGYQYFMEHdgdrLKERNA------TYDWM-YINFMSKYDIYPLLALKV--HYSTSSRKfdIL------LTLPSKV-- 196
Cdd:pfam05649  74 EKLGLKPLKPL----LDEIGGplankdKFDLLeTLAKLRRYGVDSLFGFGVgpDDKNSSRN--ILyldqpgLGLPDRDyy 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  197 LAGFSEEQ-------LKNMTREFGLDSSAEKVKQFVENfnnLTQFERNLVSLAKSRNETEQ-------LNFKEFLVKHKH 262
Cdd:pfam05649 148 LKDRDEKSaeireayKAYIAKLLTLLGASEEAAALAEE---VLAFETKLAKASLSREERRDpektynpMTLAELQKLAPG 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  263 drLNWTRFFELAFNGSQESHWPVLNQLDNINDLVFFLEQTNLETLKGYIKMR-----------ELVK----FYGlwktqt 327
Cdd:pfam05649 225 --IDWKAYLNAAGLPDVPSDEVIVSQPEYLKALSKLLAETPLRTLKNYLIWRlvrslapylsdEFRDanfeFYG------ 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221474862  328 KTGGVQSE-----CRSLSETYFNYALLPWFIGKVFDKERRADILSVAKDIKDTFYDLLDHHTWLDEDTRSQAKTKLASMD 402
Cdd:pfam05649 297 TLSGTKQRprwkrCVSLVNGLLGEALGRLYVKKYFPEEAKARVEELVENIKEAFRERLDELDWMDEETKKKALEKLDAMT 376

                  ....*
gi 221474862  403 ILVGY 407
Cdd:pfam05649 377 VKIGY 381
 
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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