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Conserved domains on  [gi|345842464|ref|NP_001230921.1|]
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disintegrin and metalloproteinase domain-containing protein 17 precursor [Cricetulus griseus]

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List of domain hits

Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
223-477 3.53e-151

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


:

Pssm-ID: 239798  Cd Length: 244  Bit Score: 445.66  E-value: 3.53e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 223 NTCKLLVVADHRFYKYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGERHFNmaK 302
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 303 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPGGKKnIYLNS 382
Cdd:cd04270   79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 383 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 462
Cdd:cd04270  151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229
                        250
                 ....*....|....*
gi 345842464 463 ESKAQECFQERSNKV 477
Cdd:cd04270  230 EVKSNSCFVERSQSF 244
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
580-642 5.53e-23

Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a multi-domain protein that acts as a sheddase; is involved in the cleavage and release of the soluble ectodomain of tumor necrosis factor alpha from the cell surface and in the trans-Golgi network, as well as in the release of various other targets such as cytokines and cell adhesion molecules. This links ADAM17 to a variety of biological processes, including cellular differentiation and the progression of cancer. It was shown that the enzymatic activity of ADAM17 is regulated via a protein-disulfide isomerase (PDI). Specifically, the disulfide bridges within a CxxC motif of the membrane-proximal domain (MPD) are isomerized by PDI; the conversion triggers a conformational change between a closed and an opened form of the MPD, which may constitute a molecular switch that triggers the shedding activity of ADAM17.


:

Pssm-ID: 271205  Cd Length: 60  Bit Score: 93.98  E-value: 5.53e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 345842464 580 PFCKREQeLESCACADTDNSCKVCCRNLSGPCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 642
Cdd:cd14246    1 PFCEREN-LQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
484-559 1.19e-24

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


:

Pssm-ID: 214490  Cd Length: 75  Bit Score: 99.30  E-value: 1.19e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 345842464   484 DEGEECDPGIMYLNNDTCCNS-DCTLKPGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGESYCTGNSSECPPPG 559
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDP 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
42-167 9.10e-08

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


:

Pssm-ID: 250707  Cd Length: 124  Bit Score: 51.13  E-value: 9.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464   42 YDILSLSNIQQHSVRKRDLQSATHLETLLTFSALKRHFKLYLTSSTERFSQNFRVVVV--DGKEESEYS-VKWQDFFSGH 118
Cdd:pfam01562   1 YEVVIPERLTGRGKRRRSRGQDAPERLSYSLTAEGKRLVLHLERNKGLLAPGFTVTTYneDGTLVTDSPfIQDHCYYHGY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 345842464  119 VVGEPDSRVLAHIGDDdvtVR--INTDGAEYNIEPLwrfvNDTKDKRMLVY 167
Cdd:pfam01562  81 VEGEPGSSVALSTCGG---LRglIQLENESYFIEPL----ESSDTFEHVVY 124
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
223-477 3.53e-151

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798  Cd Length: 244  Bit Score: 445.66  E-value: 3.53e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 223 NTCKLLVVADHRFYKYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGERHFNmaK 302
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 303 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPGGKKnIYLNS 382
Cdd:cd04270   79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 383 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 462
Cdd:cd04270  151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229
                        250
                 ....*....|....*
gi 345842464 463 ESKAQECFQERSNKV 477
Cdd:cd04270  230 EVKSNSCFVERSQSF 244
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
580-642 5.53e-23

Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a multi-domain protein that acts as a sheddase; is involved in the cleavage and release of the soluble ectodomain of tumor necrosis factor alpha from the cell surface and in the trans-Golgi network, as well as in the release of various other targets such as cytokines and cell adhesion molecules. This links ADAM17 to a variety of biological processes, including cellular differentiation and the progression of cancer. It was shown that the enzymatic activity of ADAM17 is regulated via a protein-disulfide isomerase (PDI). Specifically, the disulfide bridges within a CxxC motif of the membrane-proximal domain (MPD) are isomerized by PDI; the conversion triggers a conformational change between a closed and an opened form of the MPD, which may constitute a molecular switch that triggers the shedding activity of ADAM17.


Pssm-ID: 271205  Cd Length: 60  Bit Score: 93.98  E-value: 5.53e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 345842464 580 PFCKREQeLESCACADTDNSCKVCCRNLSGPCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 642
Cdd:cd14246    1 PFCEREN-LQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
223-451 2.43e-25

Metallo-peptidase family M12;


Pssm-ID: 257991  Cd Length: 191  Bit Score: 104.78  E-value: 2.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  223 NTCKLLVVADHRFYKYMGRgeeSTTTNYLIELIDRVDDIYRNTSwdnagfkgyGIQIEQIRILKSPQEvkpgerhfnmaK 302
Cdd:pfam13688   3 RTVALLVAADCSYVAAFGG---DAAQANIVNMVNTASNVYEREF---------NISLGLVNLTISDYT-----------D 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  303 SYPNEEKDAWDVKMLLEQFSFDIAEE-ASKVCLAHLFTYQDFDMGtlGLAYVGSPRANSHGGVCpkaYYSPGGkkniyln 381
Cdd:pfam13688  60 PYTSPPSSSGNASDLLSRFQLFSAWRgRQNDDLAYLFLDTNCSTG--GLAWLGQLCNSGSAGSV---NTSVTG------- 127
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345842464  382 sgltstknYGKTILTKEADLVTTHELGHNFGAEHDPDGLAE---CAPN---EDQGGKYVMYPIAVSgdheNNKMFS 451
Cdd:pfam13688 128 --------ANVVVRTATEWQVFAHEIGHNFGAVHDCDSSTTsqcCPPSsstCPAGGRYIMNYASSP----NSTYFS 191
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
484-559 1.19e-24

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


Pssm-ID: 214490  Cd Length: 75  Bit Score: 99.30  E-value: 1.19e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 345842464   484 DEGEECDPGIMYLNNDTCCNS-DCTLKPGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGESYCTGNSSECPPPG 559
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDP 74
Disintegrin pfam00200
Disintegrin;
484-558 2.91e-24

Disintegrin;


Pssm-ID: 249673  Cd Length: 76  Bit Score: 98.10  E-value: 2.91e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345842464  484 DEGEECDPGIMYLNNDTCCN-SDCTLKPGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGESYCTGNSSECPPP 558
Cdd:pfam00200   1 EEGEECDCGSPEECQDPCCDaTTCKLKPGAQCA--TGPCCDQCKFKPAGTVCRPASG-ECDLPEYCTGTSAECPPD 73
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
42-167 9.10e-08

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 250707  Cd Length: 124  Bit Score: 51.13  E-value: 9.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464   42 YDILSLSNIQQHSVRKRDLQSATHLETLLTFSALKRHFKLYLTSSTERFSQNFRVVVV--DGKEESEYS-VKWQDFFSGH 118
Cdd:pfam01562   1 YEVVIPERLTGRGKRRRSRGQDAPERLSYSLTAEGKRLVLHLERNKGLLAPGFTVTTYneDGTLVTDSPfIQDHCYYHGY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 345842464  119 VVGEPDSRVLAHIGDDdvtVR--INTDGAEYNIEPLwrfvNDTKDKRMLVY 167
Cdd:pfam01562  81 VEGEPGSSVALSTCGG---LRglIQLENESYFIEPL----ESSDTFEHVVY 124
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
478-514 1.77e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169  Cd Length: 38  Bit Score: 37.35  E-value: 1.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 345842464  478 CGNSRVDEGEECDPGIMYlNNDTcCNSDCTLKPGVQC 514
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTT-SGDG-CSATCRLEEGFAC 38
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
226-455 1.77e-14

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as human ADAM8 and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 250606 [Multi-domain]  Cd Length: 197  Bit Score: 72.63  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  226 KLLVVADHRFYKYMGrGEESTTTNYLIELIDRVDDIYR--NTS--------WDNAgfkgygiqiEQIRILKSPQEVKpge 295
Cdd:pfam01421   4 ELVIVVDHGMFTKYG-SDLNKIRQRVHQIVNLVNEIYRplNIRvvlvgleiWSDG---------DKITVQGDANDTL--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  296 RHFNmaksypneekdAWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVGspranshgGVCpKAYYSPGgk 375
Cdd:pfam01421  71 HRFL-----------EWRETDLLKRKSHDNA---------QLLTGIDFDGNTIGAAYVG--------GMC-SPKRSVG-- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  376 knIYLnsgltstknYGKTILtkEADLVT-THELGHNFGAEHDPDGlAECApnedqGGKYVMYPIAVsgdHENNKMFSNCS 454
Cdd:pfam01421 120 --VVQ---------DHSPIV--LLVAVTmAHELGHNLGMTHDDIN-CTCG-----GGGCIMNPVAS---SSPSKKFSNCS 177

                  .
gi 345842464  455 K 455
Cdd:pfam01421 178 M 178
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
223-477 3.53e-151

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798  Cd Length: 244  Bit Score: 445.66  E-value: 3.53e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 223 NTCKLLVVADHRFYKYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGERHFNmaK 302
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 303 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPGGKKnIYLNS 382
Cdd:cd04270   79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 383 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 462
Cdd:cd04270  151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229
                        250
                 ....*....|....*
gi 345842464 463 ESKAQECFQERSNKV 477
Cdd:cd04270  230 EVKSNSCFVERSQSF 244
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
580-642 5.53e-23

Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a multi-domain protein that acts as a sheddase; is involved in the cleavage and release of the soluble ectodomain of tumor necrosis factor alpha from the cell surface and in the trans-Golgi network, as well as in the release of various other targets such as cytokines and cell adhesion molecules. This links ADAM17 to a variety of biological processes, including cellular differentiation and the progression of cancer. It was shown that the enzymatic activity of ADAM17 is regulated via a protein-disulfide isomerase (PDI). Specifically, the disulfide bridges within a CxxC motif of the membrane-proximal domain (MPD) are isomerized by PDI; the conversion triggers a conformational change between a closed and an opened form of the MPD, which may constitute a molecular switch that triggers the shedding activity of ADAM17.


Pssm-ID: 271205  Cd Length: 60  Bit Score: 93.98  E-value: 5.53e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 345842464 580 PFCKREQeLESCACADTDNSCKVCCRNLSGPCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 642
Cdd:cd14246    1 PFCEREN-LQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
223-463 9.81e-60

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795 [Multi-domain]  Cd Length: 192  Bit Score: 201.49  E-value: 9.81e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 223 NTCKLLVVADHRFYKYMgRGEESTTTNYLIELIDRVDDIYRNTSwdnaGFKGYGIQIEQIRILKSPQEVKPGErhfnmak 302
Cdd:cd04267    1 REIELVVVADHRMVSYF-NSDENILQAYITELINIANSIYRSTN----LRLGIRISLEGLQILKGEQFAPPID------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 303 sypneekdaWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDF-DMGTLGLAYVGSPranshggvcpkayyspggkKNIYLN 381
Cdd:cd04267   69 ---------SDASNTLNSFSFWRAEGPIRHDNAVLLTAQDFiEGDILGLAYVGSM-------------------CNPYSS 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 382 SGLTSTKNYgktilTKEADLVTTHELGHNFGAEHDPDGlaECAPNEDQGGKYVMYPIAVSgdhENNKMFSNCSKQSIYKT 461
Cdd:cd04267  121 VGVVEDTGF-----TLLTALTMAHELGHNLGAEHDGGD--ELAFECDGGGNYIMAPVDSG---LNSYRFSQCSIGSIREF 190

                 ..
gi 345842464 462 IE 463
Cdd:cd04267  191 LD 192
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
223-462 5.81e-28

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 111.46  E-value: 5.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 223 NTCKLLVVADHRFYkymgrgEESTTTNYLIELIDRVDDIYRNtswdnagfkgygiqIEQIRILKSPQEVKpgerhfnmak 302
Cdd:cd00203    1 KVIPYVVVADDRDV------EEENLSAQIQSLILIAMQIWRD--------------YLNIRFVLVGVEID---------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 303 sypneekdawdvkmlleqfsfdiaeeasKVCLAHLFTYQDFDMGTLGLAYVGSPRaNSHGGVcpkayyspggkkniylns 382
Cdd:cd00203   51 ----------------------------KADIAILVTRQDFDGGTGGWAYLGRVC-DSLRGV------------------ 83
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 383 GLTSTKNYGktilTKEADLVTTHELGHNFGAEHDPDGLAEC--------APNEDQGGKYVMYPIAVSGDHENNKMFSNCS 454
Cdd:cd00203   84 GVLQDNQSG----TKEGAQTIAHELGHALGFYHDHDRKDRDdyptiddtLNAEDDDYYSVMSYTKGSFSDGQRKDFSQCD 159

                 ....*...
gi 345842464 455 KQSIYKTI 462
Cdd:cd00203  160 IDQINKLY 167
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
223-451 2.43e-25

Metallo-peptidase family M12;


Pssm-ID: 257991  Cd Length: 191  Bit Score: 104.78  E-value: 2.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  223 NTCKLLVVADHRFYKYMGRgeeSTTTNYLIELIDRVDDIYRNTSwdnagfkgyGIQIEQIRILKSPQEvkpgerhfnmaK 302
Cdd:pfam13688   3 RTVALLVAADCSYVAAFGG---DAAQANIVNMVNTASNVYEREF---------NISLGLVNLTISDYT-----------D 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  303 SYPNEEKDAWDVKMLLEQFSFDIAEE-ASKVCLAHLFTYQDFDMGtlGLAYVGSPRANSHGGVCpkaYYSPGGkkniyln 381
Cdd:pfam13688  60 PYTSPPSSSGNASDLLSRFQLFSAWRgRQNDDLAYLFLDTNCSTG--GLAWLGQLCNSGSAGSV---NTSVTG------- 127
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345842464  382 sgltstknYGKTILTKEADLVTTHELGHNFGAEHDPDGLAE---CAPN---EDQGGKYVMYPIAVSgdheNNKMFS 451
Cdd:pfam13688 128 --------ANVVVRTATEWQVFAHEIGHNFGAVHDCDSSTTsqcCPPSsstCPAGGRYIMNYASSP----NSTYFS 191
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
484-559 1.19e-24

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


Pssm-ID: 214490  Cd Length: 75  Bit Score: 99.30  E-value: 1.19e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 345842464   484 DEGEECDPGIMYLNNDTCCNS-DCTLKPGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGESYCTGNSSECPPPG 559
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDP 74
Disintegrin pfam00200
Disintegrin;
484-558 2.91e-24

Disintegrin;


Pssm-ID: 249673  Cd Length: 76  Bit Score: 98.10  E-value: 2.91e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345842464  484 DEGEECDPGIMYLNNDTCCN-SDCTLKPGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGESYCTGNSSECPPP 558
Cdd:pfam00200   1 EEGEECDCGSPEECQDPCCDaTTCKLKPGAQCA--TGPCCDQCKFKPAGTVCRPASG-ECDLPEYCTGTSAECPPD 73
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
247-458 3.86e-21

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 257890  Cd Length: 173  Bit Score: 91.97  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  247 TTNYLIELIDRVDDIYRNtswdnagfkGYGIQIEQIR----ILKSPQEVkpgerHFNMAKSYpneekDAWDVkMLLEQFS 322
Cdd:pfam13574   4 VLAAMVNTVNRVNGVYER---------DFNIRLVLVNndrlIFTDPATD-----PYNNNCNG-----GTWLS-ENQNLLS 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  323 FDIAEEasKVCLAHLFTyqDFDMGTLGLAYVGspranshgGVCPKAYyspggkkniyLNSGLTStkNYGKTiltkEADLV 402
Cdd:pfam13574  64 NLIGEA--NYDIGHLFS--TFGGGGLGLAWLG--------GICQKGS----------KGTGSTT--PSGDP----FEIDV 115
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 345842464  403 TTHELGHNFGAEHDPD-GLAECAPNEDQGGKYVMYPIAVSgdheNNKMFSNCSKQSI 458
Cdd:pfam13574 116 VAHEIGHQFGANHTFSgGCEGSSATEPGSGSTIMSYAGIC----NNTLFSPCSIGNI 168
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
226-469 9.65e-21

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797  Cd Length: 194  Bit Score: 91.52  E-value: 9.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 226 KLLVVADHRFYKYMGRgEESTTTNYLIELIDRVDDIYRN----------TSWDNAgfkgygiqiEQIRILKSPQEVkpGE 295
Cdd:cd04269    4 ELVVVVDNSLYKKYGS-NLSKVRQRVIEIVNIVDSIYRPlnirvvlvglEIWTDK---------DKISVSGDAGET--LN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 296 RhFNmaksypneekdAWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVgspranshGGVCpKAYYSPG-- 373
Cdd:cd04269   72 R-FL-----------DWKRSNLLPRKPHDNA---------QLLTGRDFDGNTVGLAYV--------GGMC-SPKYSGGvv 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 374 --GKKNIYLNSGltstknygktiltkeadlVTTHELGHNFGAEHDPDGlaeCapnEDQGGKYVMYPIAVSGdhenNKMFS 451
Cdd:cd04269  122 qdHSRNLLLFAV------------------TMAHELGHNLGMEHDDGG---C---TCGRSTCIMAPSPSSL----TDAFS 173
                        250
                 ....*....|....*...
gi 345842464 452 NCSKQSIYKTIESKAQEC 469
Cdd:cd04269  174 NCSYEDYQKFLSRGGGQC 191
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
223-466 1.67e-14

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 257899  Cd Length: 194  Bit Score: 72.82  E-value: 1.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  223 NTCKLLVVADHRFYKYMGRGEESTTTNyLIELIDRVDDIYRNTswdnagfkgYGIQIEqiriLKSPQEV---KPGERHFN 299
Cdd:pfam13583   3 RTYRLAVVADYSYYSIFGGSVDKVKAF-INNVVARLNEVYGRN---------VGISLT----LIGDERLiytTSSTDPFN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  300 MAKSYPNEEKDAwdvkmlleqFSFDIAEEASkvCLAHLFT-YQDfdmgTLGLAYVGSPRANSHGGVCPKAyyspggkkni 378
Cdd:pfam13583  69 DYRDVLNERLAT---------FNSWRGSKNY--DLGHLFTmYTS----NCGLAWLGALCQNAKGGGVARP---------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  379 ylnsgltstknygktilTKEADLVTtHELGHNFGAEHDPDGLAECAPN--EDQGGKYVMYPIA-VSGDHennkmFSNCSK 455
Cdd:pfam13583 124 -----------------TKEFDIFA-HEIGHLFGAAHDCTISGETASSatEPDSGNTIMSYANdPSGTY-----FSPPSI 180
                         250
                  ....*....|.
gi 345842464  456 QSIYKTIESKA 466
Cdd:pfam13583 181 YLIHGTPCSDA 191
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
227-469 2.71e-13

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 69.19  E-value: 2.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 227 LLVVADHRFYKYMGRgeeSTTTNYLIELIDRVDDIYRNTSWDNAgfkgygIQIEQIRILKSPQEVKPGERHFNMAKS--- 303
Cdd:cd04273    5 TLVVADSKMVEFHHG---EDLEHYILTLMNIVASLYKDPSLGNS------INIVVVRLIVLEDEESGLLISGNAQKSlks 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 304 --------YPNEEKDA--WDVKMLLEQFSFDIAeeaSKVClahlftyqdfdmGTLGLAYVGspranshgGVCpkayySPg 373
Cdd:cd04273   76 fcrwqkklNPPNDSDPehHDHAILLTRQDICRS---NGNC------------DTLGLAPVG--------GMC-----SP- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 374 gKKNIYLN--SGLTSTknygktiltkeadLVTTHELGHNFGAEHDPDGlAECAPNEDQGgkYVMYPIAVSGDHEnnKMFS 451
Cdd:cd04273  127 -SRSCSINedTGLSSA-------------FTIAHELGHVLGMPHDGDG-NSCGPEGKDG--HIMSPTLGANTGP--FTWS 187
                        250
                 ....*....|....*...
gi 345842464 452 NCSKQSIYKTIESKAQEC 469
Cdd:cd04273  188 KCSRRYLTSFLDTGDGNC 205
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
42-167 9.10e-08

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 250707  Cd Length: 124  Bit Score: 51.13  E-value: 9.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464   42 YDILSLSNIQQHSVRKRDLQSATHLETLLTFSALKRHFKLYLTSSTERFSQNFRVVVV--DGKEESEYS-VKWQDFFSGH 118
Cdd:pfam01562   1 YEVVIPERLTGRGKRRRSRGQDAPERLSYSLTAEGKRLVLHLERNKGLLAPGFTVTTYneDGTLVTDSPfIQDHCYYHGY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 345842464  119 VVGEPDSRVLAHIGDDdvtVR--INTDGAEYNIEPLwrfvNDTKDKRMLVY 167
Cdd:pfam01562  81 VEGEPGSSVALSTCGG---LRglIQLENESYFIEPL----ESSDTFEHVVY 124
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
249-416 1.28e-07

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 257898  Cd Length: 122  Bit Score: 50.79  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  249 NYLIELIDRVDDIYRNTSwdnagfkgyGIQIEQIRILKSPqevkpgerhfnmAKSYPNEEKDA-WDVKMLLEQFSFDIAE 327
Cdd:pfam13582   2 AAINATVNRVNEVYERDL---------GIRLELVNIIILD------------SATDPYSSSNAnSTLDNLQTVFAARITA 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  328 EAskvCLAHLFTYQDFDmGTLGLAYVGspranshgGVCpkayySPGGKKNIylnsgltstkNYGKTILTKEADLVTTHEL 407
Cdd:pfam13582  61 GY---DIGHLFSGYDGG-GGCGLAYVG--------GVC-----NSGKKAGV----------SASSSPTGDCGIDVVAHEI 113

                  ....*....
gi 345842464  408 GHNFGAEHD 416
Cdd:pfam13582 114 GHNFGANHT 122
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
401-465 5.55e-07

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 50.11  E-value: 5.55e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 345842464 401 LVTTHELGHNFGAEHD---------PDGLAECAPNE----DQGGKYVMYPIAVSGDHEnnkmFSNCSKQSIYKTIESK 465
Cdd:cd04271  147 QVFAHEIGHTFGAVHDctsgtcsdgSVGSQQCCPLStstcDANGQYIMNPSSSSGITE----FSPCTIGNICSLLGRN 220
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
226-471 5.65e-07

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800 [Multi-domain]  Cd Length: 220  Bit Score: 50.04  E-value: 5.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 226 KLLVVADHRFYKYMGRGEEstTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEqirilKSPQEvKPGERHFNMA---- 301
Cdd:cd04272    4 ELFVVVDYDHQSEFFSNEQ--LIRYLAVMVNAANLRYRDLKSPRIRLLLVGITIS-----KDPDF-EPYIHPINYGyida 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 302 -------KSYPNEEKDawdvkmlleQFSFDIAEEASKVCLAHlFTYQDFDMGTLGLAYVGspranshgGVCPKayYSPG- 373
Cdd:cd04272   76 aetlenfNEYVKKKRD---------YFNPDVVFLVTGLDMST-YSGGSLQTGTGGYAYVG--------GACTE--NRVAm 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 374 GKKNIYLNSGLtstknygktiltkeadLVTTHELGHNFGAEHdpDGLAECAPNEDQGGK--------YVMypiaVSGDHE 445
Cdd:cd04272  136 GEDTPGSYYGV----------------YTMTHELAHLLGAPH--DGSPPPSWVKGHPGSldcpwddgYIM----SYVVNG 193
                        250       260
                 ....*....|....*....|....*..
gi 345842464 446 NNKM-FSNCSKQSIYKTIESKAQECFQ 471
Cdd:cd04272  194 ERQYrFSQCSQRQIRNVFRRLGASCLH 220
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
478-514 1.77e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169  Cd Length: 38  Bit Score: 37.35  E-value: 1.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 345842464  478 CGNSRVDEGEECDPGIMYlNNDTcCNSDCTLKPGVQC 514
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTT-SGDG-CSATCRLEEGFAC 38
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
338-445 3.56e-03

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796  Cd Length: 165  Bit Score: 37.86  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464 338 FTYQDFDMGTLGLAYVGSpRANSHGGvcpkayyspggkkNIYLNSGLTSTKNYGktILTKEADLVTTHELGHNFGAEHDP 417
Cdd:cd04268   49 SVIRWIPYNDGTWSYGPS-QVDPLTG-------------EILLARVYLYSSFVE--YSGARLRNTAEHELGHALGLRHNF 112
                         90       100       110
                 ....*....|....*....|....*....|..
gi 345842464 418 DGLAECAPNEDQGGKY----VMYPIAVSGDHE 445
Cdd:cd04268  113 AASDRDDNVDLLAEKGdtssVMDYAPSNFSIQ 144
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
226-455 1.77e-14

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as human ADAM8 and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 250606 [Multi-domain]  Cd Length: 197  Bit Score: 72.63  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  226 KLLVVADHRFYKYMGrGEESTTTNYLIELIDRVDDIYR--NTS--------WDNAgfkgygiqiEQIRILKSPQEVKpge 295
Cdd:pfam01421   4 ELVIVVDHGMFTKYG-SDLNKIRQRVHQIVNLVNEIYRplNIRvvlvgleiWSDG---------DKITVQGDANDTL--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  296 RHFNmaksypneekdAWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVGspranshgGVCpKAYYSPGgk 375
Cdd:pfam01421  71 HRFL-----------EWRETDLLKRKSHDNA---------QLLTGIDFDGNTIGAAYVG--------GMC-SPKRSVG-- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  376 knIYLnsgltstknYGKTILtkEADLVT-THELGHNFGAEHDPDGlAECApnedqGGKYVMYPIAVsgdHENNKMFSNCS 454
Cdd:pfam01421 120 --VVQ---------DHSPIV--LLVAVTmAHELGHNLGMTHDDIN-CTCG-----GGGCIMNPVAS---SSPSKKFSNCS 177

                  .
gi 345842464  455 K 455
Cdd:pfam01421 178 M 178
VSP pfam03302
Giardia variant-specific surface protein;
476-641 6.71e-03

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 38.41  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  476 KVCGNSRVDEGEECDPGiMYLNNDTCCNSDCTLKPGVQCSD--RNSPCCK-----NCQFETAQKKCQeainaTCKGESYC 548
Cdd:pfam03302  29 KACSNDKREVCEECNSN-NYLTPTSQCIDDCAKIGNYYYTTnaNNKKICKectvaNCKTCEDQGQCQ-----ACNDGFYK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345842464  549 TGNS-SECPPPGDAEDDTVCLDLGKCKAGKCIPFCKREQEL---ESCACADTDNSCKVC------------CRN-----L 607
Cdd:pfam03302 103 SGDAcSPCHESCKTCSGGTASDCTECLTGKALRYGNDGTKGtcgEGCTTGTGAGACKTCgltidgtsycseCATeteypQ 182
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 345842464  608 SGPCVP---YVDAEQKNLFLRKGK--PCTVGFCDMNGKC 641
Cdd:pfam03302 183 NGVCTStaaRATATCKASSVANGMcsSCANGYFRMNGGC 221
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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