|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
210-408 |
1.88e-86 |
|
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: 275.33 E-value: 1.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 210 KYVELYLVADYAEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRK- 288
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 289 LLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHD--SADCCSASAa 366
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622947979 367 dGGCIMAAATGHPFPKVFNGCNRRELDRYLQSGGGMCLSNMP 408
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
501-646 |
8.66e-52 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 177.94 E-value: 8.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 501 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDmNGEHRKCNTRDAKCGKIQCQSS 580
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947979 581 EARP-LESNAVPIDTTIimngRQIQCRGTHVYRGPEEegdmlDPGLVMTGTKCGYNHICFEGQCRNT 646
Cdd:smart00608 80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP-----DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
44-162 |
7.83e-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: 112.02 E-value: 7.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 44 ELIIPQwKTPESPVR------EKHPLKAELRVMAEGRELILDLEKNEQLFAPSYTETHYTSSGNPQTTTLKLEDHCFYHG 117
Cdd:pfam01562 1 EVVIPV-RLDPSRRRrslaseSTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622947979 118 TVRETELSSVTLSTCRGIRGLITVSSNlSYVIEPL-----PDSEGQHLIY 162
Cdd:pfam01562 80 HVEGHPDSSVALSTCSGLRGFIRTENE-EYLIEPLekysrEEGGHPHVVY 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
439-499 |
5.33e-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: 107.78 E-value: 5.33e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947979 439 NNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTNFY 499
Cdd:smart00050 15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| SAV_2336_NTERM super family |
cl49223 |
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ... |
807-904 |
6.50e-03 |
|
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.
The actual alignment was detected with superfamily member NF041121:
Pssm-ID: 469044 [Multi-domain] Cd Length: 473 Bit Score: 39.99 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 807 LPAHLSRAARNSPGPGSQIERTESSRRPPPSRPIPPAPNcilsqDFSRPRPPQKALPANPVPGRRSLPRPggaSPLRTPG 886
Cdd:NF041121 11 LAAQMGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPG-----DPPEPPAPEPAPLPAPYPGSLAPPPP---PPPGPAG 82
|
90
....*....|....*...
gi 1622947979 887 AGPQHSRPLAAPAPKVSP 904
Cdd:NF041121 83 AAPGAALPVRVPAPPALP 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
210-408 |
1.88e-86 |
|
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: 275.33 E-value: 1.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 210 KYVELYLVADYAEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRK- 288
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 289 LLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHD--SADCCSASAa 366
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622947979 367 dGGCIMAAATGHPFPKVFNGCNRRELDRYLQSGGGMCLSNMP 408
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
210-406 |
4.65e-84 |
|
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: 268.71 E-value: 4.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 210 KYVELYLVADYAEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRK- 288
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 289 LLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHDSADC-CSASaad 367
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtCGRS--- 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622947979 368 gGCIMAAATGHPfPKVFNGCNRRELDRYLQSGGGMCLSN 406
Cdd:cd04269 158 -TCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
501-646 |
8.66e-52 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 177.94 E-value: 8.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 501 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDmNGEHRKCNTRDAKCGKIQCQSS 580
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947979 581 EARP-LESNAVPIDTTIimngRQIQCRGTHVYRGPEEegdmlDPGLVMTGTKCGYNHICFEGQCRNT 646
Cdd:smart00608 80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP-----DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
502-610 |
1.27e-41 |
|
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: 147.76 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 502 DGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDmNGEHRKCNTRDAKCGKIQCQSSE 581
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRT-NGGYVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|
gi 1622947979 582 ARP-LESNAVPIDTTIimngRQIQCRGTHV 610
Cdd:pfam08516 80 ELPlLGEHATVIYTNI----NGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
44-162 |
7.83e-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: 112.02 E-value: 7.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 44 ELIIPQwKTPESPVR------EKHPLKAELRVMAEGRELILDLEKNEQLFAPSYTETHYTSSGNPQTTTLKLEDHCFYHG 117
Cdd:pfam01562 1 EVVIPV-RLDPSRRRrslaseSTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622947979 118 TVRETELSSVTLSTCRGIRGLITVSSNlSYVIEPL-----PDSEGQHLIY 162
Cdd:pfam01562 80 HVEGHPDSSVALSTCSGLRGFIRTENE-EYLIEPLekysrEEGGHPHVVY 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
439-499 |
5.33e-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: 107.78 E-value: 5.33e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947979 439 NNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTNFY 499
Cdd:smart00050 15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
439-497 |
1.94e-26 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 103.09 E-value: 1.94e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947979 439 NNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTN 497
Cdd:pfam00200 16 NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| SVAGG |
NF038115 |
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ... |
289-384 |
3.74e-03 |
|
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.
Pssm-ID: 468358 [Multi-domain] Cd Length: 407 Bit Score: 40.92 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 289 LLAQKYHDNAQLITGMSFHGTTIGLAplmAMCSVYQSGGVNMDhsENAIGVAATMAHEMGHNFGMTHDSADccSASAADG 368
Cdd:NF038115 129 NAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVT--LDLYVATQTLAHELGHLFGLYNGHAE--SAECSEG 201
|
90
....*....|....*..
gi 1622947979 369 G-CIMAAATGHPFPKVF 384
Cdd:NF038115 202 GyRLMCGSLAENFENLF 218
|
|
| SAV_2336_NTERM |
NF041121 |
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ... |
807-904 |
6.50e-03 |
|
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.
Pssm-ID: 469044 [Multi-domain] Cd Length: 473 Bit Score: 39.99 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 807 LPAHLSRAARNSPGPGSQIERTESSRRPPPSRPIPPAPNcilsqDFSRPRPPQKALPANPVPGRRSLPRPggaSPLRTPG 886
Cdd:NF041121 11 LAAQMGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPG-----DPPEPPAPEPAPLPAPYPGSLAPPPP---PPPGPAG 82
|
90
....*....|....*...
gi 1622947979 887 AGPQHSRPLAAPAPKVSP 904
Cdd:NF041121 83 AAPGAALPVRVPAPPALP 100
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
800-908 |
7.86e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 40.24 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 800 GGSPPAPLPAhlsrAARNSPGPGSQIERTESSRRPPPSRPIPpapnciLSQDFSRPRPPQKALPANPVPGRRSLPRPGGA 879
Cdd:PRK12323 370 GGAGPATAAA----APVAQPAPAAAAPAAAAPAPAAPPAAPA------AAPAAAAAARAVAAAPARRSPAPEALAAARQA 439
|
90 100
....*....|....*....|....*....
gi 1622947979 880 SPLRTPGAGPQHSRPLAAPAPKVSPWEAP 908
Cdd:PRK12323 440 SARGPGGAPAPAPAPAAAPAAAARPAAAG 468
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
210-408 |
1.88e-86 |
|
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: 275.33 E-value: 1.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 210 KYVELYLVADYAEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRK- 288
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 289 LLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHD--SADCCSASAa 366
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622947979 367 dGGCIMAAATGHPFPKVFNGCNRRELDRYLQSGGGMCLSNMP 408
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
210-406 |
4.65e-84 |
|
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: 268.71 E-value: 4.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 210 KYVELYLVADYAEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRK- 288
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 289 LLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHDSADC-CSASaad 367
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtCGRS--- 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622947979 368 gGCIMAAATGHPfPKVFNGCNRRELDRYLQSGGGMCLSN 406
Cdd:cd04269 158 -TCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
501-646 |
8.66e-52 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 177.94 E-value: 8.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 501 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDmNGEHRKCNTRDAKCGKIQCQSS 580
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947979 581 EARP-LESNAVPIDTTIimngRQIQCRGTHVYRGPEEegdmlDPGLVMTGTKCGYNHICFEGQCRNT 646
Cdd:smart00608 80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP-----DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
502-610 |
1.27e-41 |
|
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: 147.76 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 502 DGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDmNGEHRKCNTRDAKCGKIQCQSSE 581
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRT-NGGYVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|
gi 1622947979 582 ARP-LESNAVPIDTTIimngRQIQCRGTHV 610
Cdd:pfam08516 80 ELPlLGEHATVIYTNI----NGVTCWGTDY 105
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
210-389 |
1.96e-33 |
|
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: 127.54 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 210 KYVELYLVADYAEFQKNRRDQDATKHKLIEIANYVDKFYRS----LNIRIALVGLEVWtHGNmCEVSENPYS---TLWSF 282
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlrLGIRISLEGLQIL-KGE-QFAPPIDSDasnTLNSF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 283 LSWRRKLLAQkyHDNAQLITGMSFH-GTTIGLAPLMAMCSVYQSGGVNMDHSENAIgVAATMAHEMGHNFGMTHDSADCC 361
Cdd:cd04267 79 SFWRAEGPIR--HDNAVLLTAQDFIeGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDGGDEL 155
|
170 180
....*....|....*....|....*....
gi 1622947979 362 SASA-ADGGCIMAAATGHPFPKVFNGCNR 389
Cdd:cd04267 156 AFECdGGGNYIMAPVDSGLNSYRFSQCSI 184
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
210-404 |
2.32e-32 |
|
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: 125.04 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 210 KYVELYLVADYAEFQKNRRDQdaTKHKLIEIANYVDKFYR--SL--NIRIALVGLEVWTHGN-MCEVSENPYSTLWSFLS 284
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGED--LEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEDEEsGLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 285 WRRKLLAQ-----KYHDNAQLITGMSFHG-----TTIGLAPLMAMCSVYQSGGVNMDhseNAIGVAATMAHEMGHNFGMT 354
Cdd:cd04273 79 WQKKLNPPndsdpEHHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRSCSINED---TGLSSAFTIAHELGHVLGMP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622947979 355 HD-SADCCSASAADgGCIMAAATGHPF-PKVFNGCNRRELDRYLQSGGGMCL 404
Cdd:cd04273 156 HDgDGNSCGPEGKD-GHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCL 206
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
44-162 |
7.83e-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: 112.02 E-value: 7.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 44 ELIIPQwKTPESPVR------EKHPLKAELRVMAEGRELILDLEKNEQLFAPSYTETHYTSSGNPQTTTLKLEDHCFYHG 117
Cdd:pfam01562 1 EVVIPV-RLDPSRRRrslaseSTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622947979 118 TVRETELSSVTLSTCRGIRGLITVSSNlSYVIEPL-----PDSEGQHLIY 162
Cdd:pfam01562 80 HVEGHPDSSVALSTCSGLRGFIRTENE-EYLIEPLekysrEEGGHPHVVY 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
439-499 |
5.33e-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: 107.78 E-value: 5.33e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947979 439 NNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTNFY 499
Cdd:smart00050 15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
439-497 |
1.94e-26 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 103.09 E-value: 1.94e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947979 439 NNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTN 497
Cdd:pfam00200 16 NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
212-378 |
6.26e-19 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 85.55 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 212 VELYLVAD---YAEFqknrrDQDATKHKLIEIANYVD-KFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLS--- 284
Cdd:pfam13688 5 VALLVAADcsyVAAF-----GGDAAQANIINMVNTASnVYERDFNISLGLVNLTISDSTCPYTPPACSTGDSSDRLSefq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 285 WRRKLLAQKYHDNAQLITGMSFHGTtiGLAPLMAMCSVYQSGGVNMDHSENAIGVAA-----TMAHEMGHNFGMTHDSA- 358
Cdd:pfam13688 80 DFSAWRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDCDs 157
|
170 180
....*....|....*....|....*...
gi 1622947979 359 ----DCCSASA----ADGGCIMAAATGH 378
Cdd:pfam13688 158 stssQCCPPSNstcpAGGRYIMNPSSSP 185
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
210-395 |
1.26e-17 |
|
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: 81.41 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 210 KYVELYLVADyaefqKNRRDQDATKHKLIEIANYVDKFYRS-LNIRIALVGLEVWTHgnmcevsenpystlwsflswrrk 288
Cdd:cd00203 1 KVIPYVVVAD-----DRDVEEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEIDKA----------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 289 llaqkyhDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHDSADCC------- 361
Cdd:cd00203 53 -------DIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDrddypti 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622947979 362 ----SASAADGGCIMaaatgHPFPKVFNGCNRRELDRY 395
Cdd:cd00203 126 ddtlNAEDDDYYSVM-----SYTKGSFSDGQRKDFSQC 158
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
242-356 |
1.87e-12 |
|
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: 463926 [Multi-domain] Cd Length: 122 Bit Score: 65.08 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 242 NYVDKFYRS-LNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRKllaQKYHDNA---QLITGMSFHGTTiGLAPLM 317
Cdd:pfam13582 8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT---RIGQYGYdlgHLFTGRDGGGGG-GIAYVG 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622947979 318 AMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHD 356
Cdd:pfam13582 84 GVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
214-403 |
2.57e-10 |
|
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: 62.01 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 214 LYLVADYAEFQKNRRDQ-DATKHKLIEIANYVDKFYRSL--------NIRIALVGLEVWTHGNMCEVSENPY---STLWS 281
Cdd:cd04270 5 LLLVADHRFYKYMGRGEeETTINYLISHIDRVDDIYRNTdwdgggfkGIGFQIKRIRIHTTPDEVDPGNKFYnksFPNWG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 282 FLSWRRKLLAQKYHDN---AQLITGMSFHGTTIGLAPLMA--------MCSVYQ--SGGVN----------MDHSENAIG 338
Cdd:cd04270 85 VEKFLVKLLLEQFSDDvclAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKAYyySNGKKkylntgltttVNYGKRVPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622947979 339 VAA--TMAHEMGHNFGMTHDS--ADCCSASAADGGCIM--AAATG-HPFPKVFNGCNRRELDRYLQSGGGMC 403
Cdd:cd04270 165 KESdlVTAHELGHNFGSPHDPdiAECAPGESQGGNYIMyaRATSGdKENNKKFSPCSKKSISKVLEVKSNSC 236
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
211-404 |
4.84e-09 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 57.75 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 211 YVELYLVADYaEFQKNRRDQDATKHKLIEIANYVDKFYRSLN---IRIALVGLEVWTH-----GNMCEVSEN--PYSTLW 280
Cdd:cd04272 2 YPELFVVVDY-DHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDpdfepYIHPINYGYidAAETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 281 SFLSWRRKLLAQKYHDNAQLITGM---SFHG-----TTIGLAPLMAMCSVYqsgGVNMdhSENAIGV---AATMAHEMGH 349
Cdd:cd04272 81 NFNEYVKKKRDYFNPDVVFLVTGLdmsTYSGgslqtGTGGYAYVGGACTEN---RVAM--GEDTPGSyygVYTMTHELAH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947979 350 NFGMTHDSADCCS---------ASAADGGCIMAAATGHPFPKVFNGCNRRELDRYLQSGGGMCL 404
Cdd:cd04272 156 LLGAPHDGSPPPSwvkghpgslDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
232-376 |
7.28e-09 |
|
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: 56.48 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 232 ATKHKLIEIANYVDKFYR--SLNIRIALVG---LEVWTHGNmceVSENPYSTLWSFLSWRRKLLAQ----KYHDNAQLIT 302
Cdd:pfam13574 2 NVTENLVNVVNRVNQIYEpdDININGGLVNpgeIPATTSAS---DSGNNYCNSPTTIVRRLNFLSQwrgeQDYCLAHLVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 303 GMSFHGTTIGLAPLMAMC-----SVYQSGGVNMDHSENAIGVAAT----MAHEMGHNFGMTHdsaDCCSASAADGGCIMA 373
Cdd:pfam13574 79 MGTFSGGELGLAYVGQICqkgasSPKTNTGLSTTTNYGSFNYPTQewdvVAHEVGHNFGATH---DCDGSQYASSGCERN 155
|
...
gi 1622947979 374 AAT 376
Cdd:pfam13574 156 AAT 158
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
230-377 |
2.53e-08 |
|
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: 55.51 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 230 QDATKHKLIEIANYVDKFYR-SLNIRIALVGLEVwthGNMCEVSENPYSTLWS---------------FLSWRrkllAQK 293
Cdd:cd04271 20 VEEARRNILNNVNSASQLYEsSFNISLGLRNLTI---SDASCPSTAVDSAPWNlpcnsrididdrlsiFSQWR----GQQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 294 YHDNAQLITGMSF--HGTTIGLAPLMAMCSVYQSGGVNMDHSeNAIGVAAT------MAHEMGHNFGMTHD--------- 356
Cdd:cd04271 93 PDDGNAFWTLMTAcpSGSEVGVAWLGQLCRTGASDQGNETVA-GTNVVVRTsnewqvFAHEIGHTFGAVHDctsgtcsdg 171
|
170 180
....*....|....*....|....*...
gi 1622947979 357 ---SADCCSASA----ADGGCIMAAATG 377
Cdd:cd04271 172 svgSQQCCPLSTstcdANGQYIMNPSSS 199
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
210-375 |
4.13e-06 |
|
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: 404471 Cd Length: 203 Bit Score: 48.77 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 210 KYVELYLVADYaEFQKNRRDQDATKHKLIEIANYVDKFY-RSLNIRIALVGL--------EVWTHGNMCEVSENPYSTLW 280
Cdd:pfam13583 3 RVYRVAVATDC-TYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDrdviytdsSTDSFNADCSGGDLGNWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 281 SFLSWRrkllAQKYHDNAQLITGMSFHGTTIGLAPLMAMC-SVYQSGGVNmdhsenaiGVAA------TMAHEMGHNFGM 353
Cdd:pfam13583 82 TLTSWR----DSLNYDLAYLTLMTGPSGQNVGVAWVGALCsSARQNAKAS--------GVARsrdewdIFAHEIGHTFGA 149
|
170 180
....*....|....*....|....*..
gi 1622947979 354 THDSAD-CCSASAA----DGGCIMAAA 375
Cdd:pfam13583 150 VHDCSSqGEGLSSStedgSGQTIMSYA 176
|
|
| SVAGG |
NF038115 |
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ... |
289-384 |
3.74e-03 |
|
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.
Pssm-ID: 468358 [Multi-domain] Cd Length: 407 Bit Score: 40.92 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 289 LLAQKYHDNAQLITGMSFHGTTIGLAplmAMCSVYQSGGVNMDhsENAIGVAATMAHEMGHNFGMTHDSADccSASAADG 368
Cdd:NF038115 129 NAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVT--LDLYVATQTLAHELGHLFGLYNGHAE--SAECSEG 201
|
90
....*....|....*..
gi 1622947979 369 G-CIMAAATGHPFPKVF 384
Cdd:NF038115 202 GyRLMCGSLAENFENLF 218
|
|
| SAV_2336_NTERM |
NF041121 |
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ... |
807-904 |
6.50e-03 |
|
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.
Pssm-ID: 469044 [Multi-domain] Cd Length: 473 Bit Score: 39.99 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 807 LPAHLSRAARNSPGPGSQIERTESSRRPPPSRPIPPAPNcilsqDFSRPRPPQKALPANPVPGRRSLPRPggaSPLRTPG 886
Cdd:NF041121 11 LAAQMGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPG-----DPPEPPAPEPAPLPAPYPGSLAPPPP---PPPGPAG 82
|
90
....*....|....*...
gi 1622947979 887 AGPQHSRPLAAPAPKVSP 904
Cdd:NF041121 83 AAPGAALPVRVPAPPALP 100
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
800-908 |
7.86e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 40.24 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947979 800 GGSPPAPLPAhlsrAARNSPGPGSQIERTESSRRPPPSRPIPpapnciLSQDFSRPRPPQKALPANPVPGRRSLPRPGGA 879
Cdd:PRK12323 370 GGAGPATAAA----APVAQPAPAAAAPAAAAPAPAAPPAAPA------AAPAAAAAARAVAAAPARRSPAPEALAAARQA 439
|
90 100
....*....|....*....|....*....
gi 1622947979 880 SPLRTPGAGPQHSRPLAAPAPKVSPWEAP 908
Cdd:PRK12323 440 SARGPGGAPAPAPAPAAAPAAAARPAAAG 468
|
|
| |
