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Conserved domains on  [gi|1953341994|ref|XP_038291150|]
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disintegrin and metalloproteinase domain-containing protein 29 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 206-396 3.52e-69

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 [Multi-domain]  Cd Length: 194  Bit Score: 227.50  E-value: 3.52e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 206 MYImELAVVVDHSLYVHIKKNISKFNEDLYAMVNIVDSIYDGMGLKLSLFGLEFWTERNYVQV-NDAHRSLRYFCVWKNS 284
Cdd:cd04269     1 KYV-ELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVsGDAGETLNRFLDWKRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 285 NFGLRLQHDTVHLFINQTVRGMS-GLGYRNGMCQPLQSCAIITTTNKTLNKIAIAIAHHLGHNLGMTHDDAFCKCGHPKC 363
Cdd:cd04269    80 NLLPRKPHDNAQLLTGRDFDGNTvGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTC 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1953341994 364 IMH-VSNPPVTAFSNCSYSYFWSYSLQF-AQCLFY 396
Cdd:cd04269   160 IMApSPSSLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
492-627 3.90e-57

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 192.19  E-value: 3.90e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994  492 DGIPC-NESAYCYEKKCNNRNDQCKQIFGEDAISASPSCYNSMNTRGDRFGNCGILKSTYIKCNVSDSQCGRIQCDKVTQ 570
Cdd:smart00608   2 DGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953341994  571 MPLLRDHSTVIHTHFNNVICWGIDYHFGMTiPDLGEVKDGTECGPEHICMNRKCVHL 627
Cdd:smart00608  82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
415-487 4.91e-33

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.96  E-value: 4.91e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953341994 415 EADEECDCGSLQSCSTDACCL-TNCTLTYGSICAFGLCCKDCQLLPPGIMCRKEVSECDLPEWCDGRSPFCPKD 487
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-159 9.23e-29

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: 460254  Cd Length: 128  Bit Score: 111.64  E-value: 9.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994  41 EVVIPLKIP------DTSRGMKPSGWLSYSLRFGGRRHIVHMKAKKYLLSRHLPVFTYTDQGALLEDQPFVPKDCYYHGY 114
Cdd:pfam01562   1 EVVIPVRLDpsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1953341994 115 VEGDPESLVSLSSCSgGFQGLLQINDFAYEIKPMTF----STKFEHLVY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
PspC_subgroup_2 super family cl41463
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 711-881 5.02e-07

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


The actual alignment was detected with superfamily member NF033839:

Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 53.23  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 711 KKEVPAQPDKQPQMVPPPPAKPEKKVPPPPPKPQKMIPPSPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPAKPQQK 790
Cdd:NF033839  329 KPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPE 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 791 PSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPLKSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSVTVGPSGK 870
Cdd:NF033839  409 VKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSK 488

                         170
                  ....*....|....*.
gi 1953341994 871 -----QRPSVTKNVPK 881
Cdd:NF033839  489 pqaddKKPSTPNNLSK 504
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 206-396 3.52e-69

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 [Multi-domain]  Cd Length: 194  Bit Score: 227.50  E-value: 3.52e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 206 MYImELAVVVDHSLYVHIKKNISKFNEDLYAMVNIVDSIYDGMGLKLSLFGLEFWTERNYVQV-NDAHRSLRYFCVWKNS 284
Cdd:cd04269     1 KYV-ELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVsGDAGETLNRFLDWKRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 285 NFGLRLQHDTVHLFINQTVRGMS-GLGYRNGMCQPLQSCAIITTTNKTLNKIAIAIAHHLGHNLGMTHDDAFCKCGHPKC 363
Cdd:cd04269    80 NLLPRKPHDNAQLLTGRDFDGNTvGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTC 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1953341994 364 IMH-VSNPPVTAFSNCSYSYFWSYSLQF-AQCLFY 396
Cdd:cd04269   160 IMApSPSSLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
492-627 3.90e-57

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 192.19  E-value: 3.90e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994  492 DGIPC-NESAYCYEKKCNNRNDQCKQIFGEDAISASPSCYNSMNTRGDRFGNCGILKSTYIKCNVSDSQCGRIQCDKVTQ 570
Cdd:smart00608   2 DGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953341994  571 MPLLRDHSTVIHTHFNNVICWGIDYHFGMTiPDLGEVKDGTECGPEHICMNRKCVHL 627
Cdd:smart00608  82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 492-595 8.85e-48

ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 165.10  E-value: 8.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 492 DGIPCNES-AYCYEKKCNNRNDQCKQIFGEDAISASPSCYNSMNTRGDRFGNCGILKSTYIKCNVSDSQCGRIQCDKVTQ 570
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 1953341994 571 MPLLRDHSTVIHTHFNNVICWGIDY 595
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 209-395 1.92e-40

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 Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 147.83  E-value: 1.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 209 MELAVVVDHSLYVHIKKNISKFNEDLYAMVNIVDSIYDGMGLKLSLFGLEFWTERNYVQVN-DAHRSLRYFCVWKNSNFG 287
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSgDANDTLRNFLKWRQEYLK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 288 LRLQHDTVHLFINQTVRG-MSGLGYRNGMCQPLQSCAIITTTNKTLNKIAIAIAHHLGHNLGMTHDDAF--CKCGH-PKC 363
Cdd:pfam01421  83 KRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPgGGC 162

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1953341994 364 IMH---VSNPPVtAFSNCSYSYFWSYSL-QFAQCLF 395
Cdd:pfam01421 163 IMNpsaGSSFPR-KFSNCSQEDFEQFLTkQKGACLF 197
Disintegrin pfam00200
Disintegrin;
415-487 4.91e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.96  E-value: 4.91e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953341994 415 EADEECDCGSLQSCSTDACCL-TNCTLTYGSICAFGLCCKDCQLLPPGIMCRKEVSECDLPEWCDGRSPFCPKD 487
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-159 9.23e-29

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: 460254  Cd Length: 128  Bit Score: 111.64  E-value: 9.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994  41 EVVIPLKIP------DTSRGMKPSGWLSYSLRFGGRRHIVHMKAKKYLLSRHLPVFTYTDQGALLEDQPFVPKDCYYHGY 114
Cdd:pfam01562   1 EVVIPVRLDpsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1953341994 115 VEGDPESLVSLSSCSgGFQGLLQINDFAYEIKPMTF----STKFEHLVY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 415-489 1.17e-28

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: 109.32  E-value: 1.17e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953341994  415 EADEECDCGSLQSCsTDACC-LTNCTLTYGSICAFGLCCKDCQLLPPGIMCRKEVSECDLPEWCDGRSPFCPKDVY 489
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 711-881 5.02e-07

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 53.23  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 711 KKEVPAQPDKQPQMVPPPPAKPEKKVPPPPPKPQKMIPPSPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPAKPQQK 790
Cdd:NF033839  329 KPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPE 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 791 PSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPLKSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSVTVGPSGK 870
Cdd:NF033839  409 VKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSK 488

                         170
                  ....*....|....*.
gi 1953341994 871 -----QRPSVTKNVPK 881
Cdd:NF033839  489 pqaddKKPSTPNNLSK 504
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 750-877 1.49e-06

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 51.69  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 750 SPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAptQPAKPQQKPSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPL 829
Cdd:NF033839  293 SAPKPGMQPSPQPEKKEVKPEPETPKPEVKP--QLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPE 370

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1953341994 830 KSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSvTVGPSGKQRPSVTK 877
Cdd:NF033839  371 KPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPE-KPKPEVKPQPEKPK 417
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 711-877 2.45e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.84  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 711 KKEVPAQPDKQPQMVPPPPAKPEKKVPPPPPKPQKMIPPSPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPAKPQQK 790
Cdd:NF033839  307 KKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPE 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 791 PSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPLKSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSvTVGPSGK 870
Cdd:NF033839  387 VKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE-TPKPEVK 465


                  ....*..
gi 1953341994 871 QRPSVTK 877
Cdd:NF033839  466 PQPEKPK 472
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 751-877 5.05e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.07  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 751 PAKPPQKAPTQPAKPPQKAptQPAKPQKKAPTQPAKPQQKPSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPLK 830
Cdd:NF033839  305 PEKKEVKPEPETPKPEVKP--QLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPET 382

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953341994 831 SQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSvTVGPSGKQRPSVTK 877
Cdd:NF033839  383 PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE-KPKPEVKPQPEKPK 428
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 756-881 7.68e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 46.30  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 756 QKAPTQPAKPPQKAPT-------QPAKPQKKAPTQPAKPQQKPSAQfsKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQP 828
Cdd:NF033839  281 QDTPKEPGNKKPSAPKpgmqpspQPEKKEVKPEPETPKPEVKPQLE--KPKPEVKPQPEKPKPEVKPQLETPKPEVKPQP 358

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953341994 829 LKSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSVtvgPSGKQRPSVTKNVPK 881
Cdd:NF033839  359 EKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEK---PKPEVKPQPEKPKPE 408
PRK12757 PRK12757
cell division protein FtsN; Provisional
 754-799 9.52e-05

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 45.03  E-value: 9.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1953341994 754 PPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPAKPQQKPSAQFSKSQ 799
Cdd:PRK12757  138 QPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKEKEQ 183
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 709-877 3.66e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 43.99  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 709 RKKKEVP---AQPDKQPQmvppppakpEKKVPPPPPKPQKMIPPSPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPA 785
Cdd:NF033839  289 NKKPSAPkpgMQPSPQPE---------KKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPE 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 786 KPQQKPSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPLKSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSvTV 865
Cdd:NF033839  360 KPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE-KP 438

                         170
                  ....*....|..
gi 1953341994 866 GPSGKQRPSVTK 877
Cdd:NF033839  439 KPEVKPQPEKPK 450
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 407-446 8.59e-04

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 [Multi-domain]  Cd Length: 38  Bit Score: 37.74  E-value: 8.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953341994 407 KRCGDGIVEADEECDCGSLQscSTDACCLTnCTLTYGSIC 446
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTT--SGDGCSAT-CRLEEGFAC 38
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
339-369 1.41e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 1.41e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1953341994 339 IAHHLGHNLGMTHddafckCGHPKCIMHVSN 369
Cdd:COG1913   127 AVHELGHLFGLGH------CPNPRCVMHFSN 151
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
754-870 9.06e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 39.67  E-value: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 754 PPQKAPTQpAKPPQKAP-----TQPAK--PQKKAP------TQPAKPQqkpsAQFSKSQQQLSAQTSKSQqqlsaqssks 820
Cdd:pfam03546  39 PAAKTPLQ-AKPSGKTPqvraaSAPAKesPRKGAPpvppgkTGPAAAQ----AQAGKPEEDSESSSEESD---------- 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953341994 821 qqklSAQPLKSQQKLSAQPSKsqqklsAQPSKSQQTLKSQSSVTVGPSGK 870
Cdd:pfam03546 104 ----SDGETPAAATLTTSPAQ------VKPLGKNSQVRPASTVGKGPSGK 143
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 206-396 3.52e-69

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 [Multi-domain]  Cd Length: 194  Bit Score: 227.50  E-value: 3.52e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 206 MYImELAVVVDHSLYVHIKKNISKFNEDLYAMVNIVDSIYDGMGLKLSLFGLEFWTERNYVQV-NDAHRSLRYFCVWKNS 284
Cdd:cd04269     1 KYV-ELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVsGDAGETLNRFLDWKRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 285 NFGLRLQHDTVHLFINQTVRGMS-GLGYRNGMCQPLQSCAIITTTNKTLNKIAIAIAHHLGHNLGMTHDDAFCKCGHPKC 363
Cdd:cd04269    80 NLLPRKPHDNAQLLTGRDFDGNTvGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTC 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1953341994 364 IMH-VSNPPVTAFSNCSYSYFWSYSLQF-AQCLFY 396
Cdd:cd04269   160 IMApSPSSLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
492-627 3.90e-57

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 192.19  E-value: 3.90e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994  492 DGIPC-NESAYCYEKKCNNRNDQCKQIFGEDAISASPSCYNSMNTRGDRFGNCGILKSTYIKCNVSDSQCGRIQCDKVTQ 570
Cdd:smart00608   2 DGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953341994  571 MPLLRDHSTVIHTHFNNVICWGIDYHFGMTiPDLGEVKDGTECGPEHICMNRKCVHL 627
Cdd:smart00608  82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 492-595 8.85e-48

ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 165.10  E-value: 8.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 492 DGIPCNES-AYCYEKKCNNRNDQCKQIFGEDAISASPSCYNSMNTRGDRFGNCGILKSTYIKCNVSDSQCGRIQCDKVTQ 570
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 1953341994 571 MPLLRDHSTVIHTHFNNVICWGIDY 595
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 209-395 1.92e-40

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 Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 147.83  E-value: 1.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 209 MELAVVVDHSLYVHIKKNISKFNEDLYAMVNIVDSIYDGMGLKLSLFGLEFWTERNYVQVN-DAHRSLRYFCVWKNSNFG 287
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSgDANDTLRNFLKWRQEYLK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 288 LRLQHDTVHLFINQTVRG-MSGLGYRNGMCQPLQSCAIITTTNKTLNKIAIAIAHHLGHNLGMTHDDAF--CKCGH-PKC 363
Cdd:pfam01421  83 KRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPgGGC 162

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1953341994 364 IMH---VSNPPVtAFSNCSYSYFWSYSL-QFAQCLF 395
Cdd:pfam01421 163 IMNpsaGSSFPR-KFSNCSQEDFEQFLTkQKGACLF 197
Disintegrin pfam00200
Disintegrin;
415-487 4.91e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.96  E-value: 4.91e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953341994 415 EADEECDCGSLQSCSTDACCL-TNCTLTYGSICAFGLCCKDCQLLPPGIMCRKEVSECDLPEWCDGRSPFCPKD 487
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-159 9.23e-29

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: 460254  Cd Length: 128  Bit Score: 111.64  E-value: 9.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994  41 EVVIPLKIP------DTSRGMKPSGWLSYSLRFGGRRHIVHMKAKKYLLSRHLPVFTYTDQGALLEDQPFVPKDCYYHGY 114
Cdd:pfam01562   1 EVVIPVRLDpsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1953341994 115 VEGDPESLVSLSSCSgGFQGLLQINDFAYEIKPMTF----STKFEHLVY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 415-489 1.17e-28

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: 109.32  E-value: 1.17e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953341994  415 EADEECDCGSLQSCsTDACC-LTNCTLTYGSICAFGLCCKDCQLLPPGIMCRKEVSECDLPEWCDGRSPFCPKDVY 489
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 207-395 8.36e-24

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: 100.01  E-value: 8.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 207 YIMELAVVVDHSLY-VHIKKNISKFnedLYAMVNIVDSIYD----GMGLKLSLFGLEFWTERNYVQVN--DAHRSLRYFC 279
Cdd:cd04273     1 RYVETLVVADSKMVeFHHGEDLEHY---ILTLMNIVASLYKdpslGNSINIVVVRLIVLEDEESGLLIsgNAQKSLKSFC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 280 VWKNS----NFGLRLQHDTVHLF------INQTVRGMSGLGYRNGMCQPLQSCAIITTTNKTLnkiAIAIAHHLGHNLGM 349
Cdd:cd04273    78 RWQKKlnppNDSDPEHHDHAILLtrqdicRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSS---AFTIAHELGHVLGM 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953341994 350 THDDAFCKCGH---PKCIMH---VSNPPVTAFSNCSYSYFWSYSLQ-FAQCLF 395
Cdd:cd04273   155 PHDGDGNSCGPegkDGHIMSptlGANTGPFTWSKCSRRYLTSFLDTgDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 209-382 8.10e-22

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  Cd Length: 192  Bit Score: 94.02  E-value: 8.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 209 MELAVVVDHS--LYVHIKKNISKFNedLYAMVNIVDSIY----DGMGLKLSLFGLEFWTERNYVQVN--DAHRSLRYFCV 280
Cdd:cd04267     3 IELVVVADHRmvSYFNSDENILQAY--ITELINIANSIYrstnLRLGIRISLEGLQILKGEQFAPPIdsDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 281 WKNSNfglRLQHDTVHLFINQTVRGMS--GLGYRNGMCQPLQSCAIITTTNKTLNKiAIAIAHHLGHNLGMTHDDAFC-- 356
Cdd:cd04267    81 WRAEG---PIRHDNAVLLTAQDFIEGDilGLAYVGSMCNPYSSVGVVEDTGFTLLT-ALTMAHELGHNLGAEHDGGDEla 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1953341994 357 --KCGHPKCIMHVSNPPVTA--FSNCSYSY 382
Cdd:cd04267   157 feCDGGGNYIMAPVDSGLNSyrFSQCSIGS 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 265-393 1.08e-09

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: 58.30  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 265 YVQVNDAHRSLRYFcvwKNSNFGLRL----QHDTVHLFINQTV-RGMSGLGYRNGMCQPLQSCAIITTTNKTLNKIAIAI 339
Cdd:cd00203    24 QSLILIAMQIWRDY---LNIRFVLVGveidKADIAILVTRQDFdGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTI 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953341994 340 AHHLGHNLGMTHDDAFCKCGHPKCIMHVSNPPVTAFsNCSYSYFWS-----YSLQFAQC 393
Cdd:cd00203   101 AHELGHALGFYHDHDRKDRDDYPTIDDTLNAEDDDY-YSVMSYTKGsfsdgQRKDFSQC 158
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
211-376 4.17e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 57.04  E-value: 4.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 211 LAVVVDHSLYvhikkniSKFNED-----LYAMVNIVDSI-YDGMGLKLSLFGLEFWTE--------RNYVQVNDAHRSLR 276
Cdd:pfam13688   7 LLVAADCSYV-------AAFGGDaaqanIINMVNTASNVyERDFNISLGLVNLTISDStcpytppaCSTGDSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 277 YFCVWKNsnfglRLQHDTVHLFINQTVRGmSGLGYRNGMCqPLQSCAIITTTNKTLNKIA------IAIAHHLGHNLGMT 350
Cdd:pfam13688  80 DFSAWRG-----TQNDDLAYLFLMTNCSG-GGLAWLGQLC-NSGSAGSVSTRVSGNNVVVstatewQVFAHEIGHNFGAV 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953341994 351 HD-DAFCK--CGHP---------KCIMHVSNPP-VTAFS 376
Cdd:pfam13688 153 HDcDSSTSsqCCPPsnstcpaggRYIMNPSSSPnSTDFS 191
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 711-881 5.02e-07

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 53.23  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 711 KKEVPAQPDKQPQMVPPPPAKPEKKVPPPPPKPQKMIPPSPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPAKPQQK 790
Cdd:NF033839  329 KPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPE 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 791 PSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPLKSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSVTVGPSGK 870
Cdd:NF033839  409 VKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSK 488

                         170
                  ....*....|....*.
gi 1953341994 871 -----QRPSVTKNVPK 881
Cdd:NF033839  489 pqaddKKPSTPNNLSK 504
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 750-877 1.49e-06

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 51.69  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 750 SPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAptQPAKPQQKPSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPL 829
Cdd:NF033839  293 SAPKPGMQPSPQPEKKEVKPEPETPKPEVKP--QLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPE 370

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1953341994 830 KSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSvTVGPSGKQRPSVTK 877
Cdd:NF033839  371 KPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPE-KPKPEVKPQPEKPK 417
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 270-381 1.78e-05

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 46.47  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 270 DAHRSLRYFCVWKNSNfglrlQHDTVHLFINQTVR-GMSGLGYRNGMCQPLQSCAIITT----------TNKTLNKIAIa 338
Cdd:pfam13574  54 TIVRRLNFLSQWRGEQ-----DYCLAHLVTMGTFSgGELGLAYVGQICQKGASSPKTNTglstttnygsFNYPTQEWDV- 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953341994 339 IAHHLGHNLGMTHD---DAFCKCGHPKC------------IM-HVSNPPVTAFSNCSYS 381
Cdd:pfam13574 128 VAHEVGHNFGATHDcdgSQYASSGCERNaatsvcsangsfIMnPASKSNNDLFSPCSIS 186
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 711-877 2.45e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.84  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 711 KKEVPAQPDKQPQMVPPPPAKPEKKVPPPPPKPQKMIPPSPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPAKPQQK 790
Cdd:NF033839  307 KKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPE 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 791 PSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPLKSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSvTVGPSGK 870
Cdd:NF033839  387 VKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE-TPKPEVK 465


                  ....*..
gi 1953341994 871 QRPSVTK 877
Cdd:NF033839  466 PQPEKPK 472
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 751-877 5.05e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.07  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 751 PAKPPQKAPTQPAKPPQKAptQPAKPQKKAPTQPAKPQQKPSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPLK 830
Cdd:NF033839  305 PEKKEVKPEPETPKPEVKP--QLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPET 382

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953341994 831 SQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSvTVGPSGKQRPSVTK 877
Cdd:NF033839  383 PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE-KPKPEVKPQPEKPK 428
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 756-881 7.68e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 46.30  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 756 QKAPTQPAKPPQKAPT-------QPAKPQKKAPTQPAKPQQKPSAQfsKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQP 828
Cdd:NF033839  281 QDTPKEPGNKKPSAPKpgmqpspQPEKKEVKPEPETPKPEVKPQLE--KPKPEVKPQPEKPKPEVKPQLETPKPEVKPQP 358

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953341994 829 LKSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSVtvgPSGKQRPSVTKNVPK 881
Cdd:NF033839  359 EKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEK---PKPEVKPQPEKPKPE 408
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 211-379 8.44e-05

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 [Multi-domain]  Cd Length: 244  Bit Score: 45.06  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 211 LAVVVDHSLYVHI-KKNISKFNEDLYAMVNIVDSIY-----DGMGLKlslfGLEFWTERNYVQVNDAHRS------LRYF 278
Cdd:cd04270     5 LLLVADHRFYKYMgRGEEETTINYLISHIDRVDDIYrntdwDGGGFK----GIGFQIKRIRIHTTPDEVDpgnkfyNKSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 279 CVWKNSNFGLRL---QHDT----VHLFINQTVR-GMSGLGY-----RN---GMCQPLQ----------SCAIITTTN--- 329
Cdd:cd04270    81 PNWGVEKFLVKLlleQFSDdvclAHLFTYRDFDmGTLGLAYvgsprDNsagGICEKAYyysngkkkylNTGLTTTVNygk 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953341994 330 KTLNKIA-IAIAHHLGHNLGMTHD--DAFCKCGHP---KCIM--------HVSNppvTAFSNCS 379
Cdd:cd04270   161 RVPTKESdLVTAHELGHNFGSPHDpdIAECAPGESqggNYIMyaratsgdKENN---KKFSPCS 221
PRK12757 PRK12757
cell division protein FtsN; Provisional
 754-799 9.52e-05

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 45.03  E-value: 9.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1953341994 754 PPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPAKPQQKPSAQFSKSQ 799
Cdd:PRK12757  138 QPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKEKEQ 183
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 750-853 2.60e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.08  E-value: 2.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994  750 SPAKPPQKAPTQPAKPPQK--APTQPAKPQK--KAPTQPAKPQQK---------PSAQFSKSQQQLSAQtsksqqqlsaq 816
Cdd:PRK10263   746 TPIVEPVQQPQQPVAPQQQyqQPQQPVAPQPqyQQPQQPVAPQPQyqqpqqpvaPQPQYQQPQQPVAPQ----------- 814

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1953341994  817 ssksqqklsAQPLKSQQKLSAQP--SKSQQKLSAQPSKS 853
Cdd:PRK10263   815 ---------PQYQQPQQPVAPQPqyQQPQQPVAPQPQDT 844
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 709-877 3.66e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 43.99  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 709 RKKKEVP---AQPDKQPQmvppppakpEKKVPPPPPKPQKMIPPSPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPA 785
Cdd:NF033839  289 NKKPSAPkpgMQPSPQPE---------KKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPE 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 786 KPQQKPSAQFSKSQQQLSAQTSKSQQQLSAQSSKSQQKLSAQPLKSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSvTV 865
Cdd:NF033839  360 KPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE-KP 438

                         170
                  ....*....|..
gi 1953341994 866 GPSGKQRPSVTK 877
Cdd:NF033839  439 KPEVKPQPEKPK 450
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 407-446 8.59e-04

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 [Multi-domain]  Cd Length: 38  Bit Score: 37.74  E-value: 8.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953341994 407 KRCGDGIVEADEECDCGSLQscSTDACCLTnCTLTYGSIC 446
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTT--SGDGCSAT-CRLEEGFAC 38
PRK13808 PRK13808
adenylate kinase; Provisional
 750-806 1.10e-03

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 42.18  E-value: 1.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953341994 750 SPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPAKPQQKPSAQFSKSQQQLSAQT 806
Cdd:PRK13808  251 KAKKTAKKALKKAAKAVKKAAKKAAKAAAKAAKGAAKATKGKAKAKKKAGKKAAAGS 307
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 750-871 1.35e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 41.86  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 750 SPAK---PPQKAPTQPAK---PPQKAPTQPAK---PQKKAPTQPAKPQQKPSAQFSKSQQQLSAQTSKsqqqlsaqssks 820
Cdd:PTZ00436  235 PPAKaaaAPAKAAAAPAKaaaPPAKAAAPPAKaaaPPAKAAAPPAKAAAPPAKAAAPPAKAAAAPAKA------------ 302

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953341994 821 qqklSAQPLKSQQ---KLSAQPSKSQQKLSAQPSKSQQTLKSQSSVTVGPSGKQ 871
Cdd:PTZ00436  303 ----AAAPAKAAAapaKAAAPPAKAAAPPAKAATPPAKAAAPPAKAAAAPVGKK 352
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
339-369 1.41e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 1.41e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1953341994 339 IAHHLGHNLGMTHddafckCGHPKCIMHVSN 369
Cdd:COG1913   127 AVHELGHLFGLGH------CPNPRCVMHFSN 151
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 750-794 1.46e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 42.57  E-value: 1.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1953341994  750 SPAKPPQKAPTQPAKPPQKAPTQPAKPQKKAPTQPAKPQQKPSAQ 794
Cdd:PRK12270    74 PPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118
PRK10927 PRK10927
cell division protein FtsN;
753-881 3.07e-03

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 40.82  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 753 KPPQKAPTQPA------KPPQKAPTQP---AKPQKKAPTQPAKPQQKPSAQFSKSQQQLSAQTSKSQQQLSaqssksqqk 823
Cdd:PRK10927   93 QPGVRAPTEPSaggevkTPEQLTPEQRqllEQMQADMRQQPTQLVEVPWNEQTPEQRQQTLQRQRQAQQLA--------- 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 824 lSAQPLKSQQKLSAQPSKSQQKLSAQPSKSQQTLKSQSSVTVGPSGK--QRPSVTKNVPK 881
Cdd:PRK10927  164 -EQQRLAQQSRTTEQSWQQQTRTSQAAPVQAQPRQSKPASTQQPYQDllQTPAHTTAQSK 222
PRK11633 PRK11633
cell division protein DedD; Provisional
 750-794 3.61e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 39.99  E-value: 3.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1953341994 750 SPAKPPQKAPTQPAKPPQKAPTQPA-KPQKKAPTQPA-KPQQKPSAQ 794
Cdd:PRK11633   94 NTPVEPEPAPVEPPKPKPVEKPKPKpKPQQKVEAPPApKPEPKPVVE 140
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 718-805 4.52e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994  718 PDKQPQMVPPPPAKPEKKVPPPPPKPQKMIPPSPAKPPQK--------APTQPAKPPQKaPTQPaKPQKKAPTQPAKPQQ 789
Cdd:PRK10263   751 PVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQyqqpqqpvAPQPQYQQPQQ-PVAP-QPQYQQPQQPVAPQP 828

                           90
                   ....*....|....*.
gi 1953341994  790 kpsaQFSKSQQQLSAQ 805
Cdd:PRK10263   829 ----QYQQPQQPVAPQ 840
PRK10905 PRK10905
cell division protein DamX; Validated
 744-806 5.80e-03

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 39.92  E-value: 5.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953341994 744 QKMIPPSPAKPPQKAPTQPAKPPQKAPTQPAkpqkKAPTQPAKPQQKPSAQFSKSQQQLSAQT 806
Cdd:PRK10905  165 PKKPQATAKTEPKPVAQTPKRTEPAAPVAST----KAPAATSTPAPKETATTAPVQTASPAQT 223
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 332-369 6.04e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 38.43  E-value: 6.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1953341994 332 LNKIAIAIAHHLGHNLGMTHddafckCGHPKCIMHVSN 369
Cdd:cd11375   120 LERLLKEAVHELGHLFGLDH------CPYYACVMNFSN 151
PHA03378 PHA03378
EBNA-3B; Provisional
 750-792 6.74e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 6.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1953341994 750 SPAKPPQKAPTQpAKPPQKAPTqPAKPQKKAPTQPAKPQQKPS 792
Cdd:PHA03378  722 GRARPPAAAPGR-ARPPAAAPG-RARPPAAAPGRARPPAAAPG 762
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
754-870 9.06e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 39.67  E-value: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953341994 754 PPQKAPTQpAKPPQKAP-----TQPAK--PQKKAP------TQPAKPQqkpsAQFSKSQQQLSAQTSKSQqqlsaqssks 820
Cdd:pfam03546  39 PAAKTPLQ-AKPSGKTPqvraaSAPAKesPRKGAPpvppgkTGPAAAQ----AQAGKPEEDSESSSEESD---------- 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953341994 821 qqklSAQPLKSQQKLSAQPSKsqqklsAQPSKSQQTLKSQSSVTVGPSGK 870
Cdd:pfam03546 104 ----SDGETPAAATLTTSPAQ------VKPLGKNSQVRPASTVGKGPSGK 143
 
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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