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Conserved domains on  [gi|564331629|ref|XP_006230563|]
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disintegrin and metalloproteinase domain-containing protein 8 isoform X6 [Rattus norvegicus]

Protein Classification

disintegrin and metalloproteinase domain-containing protein( domain architecture ID 12023311)

disintegrin and metalloproteinase domain-containing protein, also called metalloproteinase-disintegrin (ADAM), is a membrane-spanning multi-domain protein which may serve as an integrin ligand

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
196-395 1.90e-99

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: 306.92  E-value: 1.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  196 RYVELYVVADSQEFQKLGT-REAVRQRVLEVVNHVDKLYRELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  274 LLGRHPHDNVQLITGVDFIGTTVGLAKVSALCSR-HSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDENIPGCYCPipr 352
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 564331629  353 EGGGCIMTESIGSKFPKTFSRCSQVDLESFVTNHQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
51-152 9.03e-35

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: 128.59  E-value: 9.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629   51 YPESLSYALGTSEQVFTLHLRKNRDLLGSSYTETYSAANGSEVKEQLHEQDHCLYQGHVEGYEGSAASISTCAGLSGFFR 130
Cdd:pfam01562  23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
                          90       100
                  ....*....|....*....|....*.
gi 564331629  131 VGSTVHLIEPL---DADEEGQ-HAVY 152
Cdd:pfam01562 103 TENEEYLIEPLekySREEGGHpHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
412-486 1.05e-34

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: 126.65  E-value: 1.05e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564331629   412 ERGEQCDCGTPQDCQNPCCNATTCQLAKGAECAHGACCHECKVKPAGELCRPMKDKCDLEEFCDGQKPTCPEDAF 486
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ACR smart00608
ADAM Cysteine-Rich Domain;
488-607 1.14e-30

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 117.46  E-value: 1.14e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629   488 QNGTPCPG--GYCFDGSCPTLAQQCQALWGPGARAASDSCFAFSIPQG-----C---YGSMYP--SRINRCGVLFCEGGQ 555
Cdd:smart00608   1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIPcaPEDVKCGKLQCTNVS 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564331629   556 KP--LERSSCTFSSHHG--LCQALQTDSNTNT-YEFVLQGTKCEEGKVCMDGNCQDL 607
Cdd:smart00608  81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
PHA03247 super family cl33720
large tegument protein UL36; Provisional
638-819 6.92e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  638 APPYCAQLLADVPASESLPVSVVVVLVILVAAVVIGAGIVIYRKA------PKQIQRRSVAPKPTSGLSNPLFYTGDSSL 711
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspagplPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  712 PA---KSRPPDPPEMVSTNQPPRPIVKPKRPPpappgAMSSPPLPVPVYAPKAPNQLRPDPPTKPLPKLK-PKQVKPTFA 787
Cdd:PHA03247 2858 PGgdvRRRPPSRSPAAKPAAPARPPVRRLARP-----AVSRSTESFALPPDQPERPPQPQAPPPPQPQPQpPPPPQPQPP 2932
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564331629  788 PPTP-----PVKPGTGGTVPGVTQQGAGGSKVALKVP 819
Cdd:PHA03247 2933 PPPPprpqpPLAPTTDPAGAGEPSGAVPQPWLGALVP 2969
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
196-395 1.90e-99

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: 306.92  E-value: 1.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  196 RYVELYVVADSQEFQKLGT-REAVRQRVLEVVNHVDKLYRELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  274 LLGRHPHDNVQLITGVDFIGTTVGLAKVSALCSR-HSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDENIPGCYCPipr 352
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 564331629  353 EGGGCIMTESIGSKFPKTFSRCSQVDLESFVTNHQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
196-393 4.50e-81

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: 258.31  E-value: 4.50e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 196 RYVELYVVADSQEFQKLG-TREAVRQRVLEVVNHVDKLYRELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISVSGDAGETLNRFLDWKRSN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 274 LLGRHPHDNVQLITGVDFIGTTVGLAKVSALCSR-HSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDEniPGCYCPipr 352
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCG--- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564331629 353 eGGGCIMTESIGSkFPKTFSRCSQVDLESFVTNHQTGCLTN 393
Cdd:cd04269  156 -RSTCIMAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
51-152 9.03e-35

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: 128.59  E-value: 9.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629   51 YPESLSYALGTSEQVFTLHLRKNRDLLGSSYTETYSAANGSEVKEQLHEQDHCLYQGHVEGYEGSAASISTCAGLSGFFR 130
Cdd:pfam01562  23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
                          90       100
                  ....*....|....*....|....*.
gi 564331629  131 VGSTVHLIEPL---DADEEGQ-HAVY 152
Cdd:pfam01562 103 TENEEYLIEPLekySREEGGHpHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
412-486 1.05e-34

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: 126.65  E-value: 1.05e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564331629   412 ERGEQCDCGTPQDCQNPCCNATTCQLAKGAECAHGACCHECKVKPAGELCRPMKDKCDLEEFCDGQKPTCPEDAF 486
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
412-484 5.49e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.58  E-value: 5.49e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564331629  412 ERGEQCDCGTPQDCQ-NPCCNATTCQLAKGAECAHGACCHECKVKPAGELCRPMKDKCDLEEFCDGQKPTCPED 484
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ACR smart00608
ADAM Cysteine-Rich Domain;
488-607 1.14e-30

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 117.46  E-value: 1.14e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629   488 QNGTPCPG--GYCFDGSCPTLAQQCQALWGPGARAASDSCFAFSIPQG-----C---YGSMYP--SRINRCGVLFCEGGQ 555
Cdd:smart00608   1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIPcaPEDVKCGKLQCTNVS 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564331629   556 KP--LERSSCTFSSHHG--LCQALQTDSNTNT-YEFVLQGTKCEEGKVCMDGNCQDL 607
Cdd:smart00608  81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
489-526 4.59e-13

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: 66.10  E-value: 4.59e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 564331629  489 NGTPCPG--GYCFDGSCPTLAQQCQALWGPGARAASDSCF 526
Cdd:pfam08516   1 DGTPCNNgqAYCYNGRCRDRDQQCQELFGKGAKSAPDACY 40
PHA03247 PHA03247
large tegument protein UL36; Provisional
638-819 6.92e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  638 APPYCAQLLADVPASESLPVSVVVVLVILVAAVVIGAGIVIYRKA------PKQIQRRSVAPKPTSGLSNPLFYTGDSSL 711
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspagplPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  712 PA---KSRPPDPPEMVSTNQPPRPIVKPKRPPpappgAMSSPPLPVPVYAPKAPNQLRPDPPTKPLPKLK-PKQVKPTFA 787
Cdd:PHA03247 2858 PGgdvRRRPPSRSPAAKPAAPARPPVRRLARP-----AVSRSTESFALPPDQPERPPQPQAPPPPQPQPQpPPPPQPQPP 2932
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564331629  788 PPTP-----PVKPGTGGTVPGVTQQGAGGSKVALKVP 819
Cdd:PHA03247 2933 PPPPprpqpPLAPTTDPAGAGEPSGAVPQPWLGALVP 2969
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
712-807 3.04e-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: 44.37  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 712 PAKSRPPDP-PEMVSTNQPPRPIVkpkrpppappgamssPPLPVPVYAPKAPNQLRPDPPTKPLPKLKPKQVKPTFAPPT 790
Cdd:NF033839 287 PGNKKPSAPkPGMQPSPQPEKKEV---------------KPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPK 351
                         90
                 ....*....|....*..
gi 564331629 791 PPVKPGTGGTVPGVTQQ 807
Cdd:NF033839 352 PEVKPQPEKPKPEVKPQ 368
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
710-811 6.84e-04

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 42.61  E-value: 6.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  710 SLPAKSR---PPDPPEMVSTNQPPRPivkpkrpppapPGAMSSPPLPVPVYAPKAPNQLRPDPPTKPLPKLKPKQVKPTf 786
Cdd:pfam07174  32 ALPAVAHadpEPAPPPPSTATAPPAP-----------PPPPPAPAAPAPPPPPAAPNAPNAPPPPADPNAPPPPPADPN- 99
                          90       100
                  ....*....|....*....|....*
gi 564331629  787 APPTPPVKPgtGGTVPGVTQQGAGG 811
Cdd:pfam07174 100 APPPPAVDP--NAPEPGRIDNAVGG 122
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
712-813 7.00e-03

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: 39.75  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 712 PAKSRP---PDP----PEMVSTNQPPRPIVkpkrpppappgamsSPPLPVPVYAPKaPNQLRPDPPTKPLPKLKPKQVKP 784
Cdd:NF033839 402 PEKPKPevkPQPekpkPEVKPQPEKPKPEV--------------KPQPEKPKPEVK-PQPEKPKPEVKPQPETPKPEVKP 466
                         90       100
                 ....*....|....*....|....*....
gi 564331629 785 TFAPPTPPVKPGTGGTVPGVTQQGAGGSK 813
Cdd:NF033839 467 QPEKPKPEVKPQPEKPKPDNSKPQADDKK 495
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
196-395 1.90e-99

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: 306.92  E-value: 1.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  196 RYVELYVVADSQEFQKLGT-REAVRQRVLEVVNHVDKLYRELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  274 LLGRHPHDNVQLITGVDFIGTTVGLAKVSALCSR-HSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDENIPGCYCPipr 352
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 564331629  353 EGGGCIMTESIGSKFPKTFSRCSQVDLESFVTNHQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
196-393 4.50e-81

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: 258.31  E-value: 4.50e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 196 RYVELYVVADSQEFQKLG-TREAVRQRVLEVVNHVDKLYRELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISVSGDAGETLNRFLDWKRSN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 274 LLGRHPHDNVQLITGVDFIGTTVGLAKVSALCSR-HSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDEniPGCYCPipr 352
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCG--- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564331629 353 eGGGCIMTESIGSkFPKTFSRCSQVDLESFVTNHQTGCLTN 393
Cdd:cd04269  156 -RSTCIMAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
196-391 2.18e-38

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: 141.99  E-value: 2.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 196 RYVELYVVADSQEFQKLGtREAVRQRVLEVVNHVDKLYRELS----FRVVLVGLEIWNKDKF--YISRYANVTLENFLSW 269
Cdd:cd04273    1 RYVETLVVADSKMVEFHH-GEDLEHYILTLMNIVASLYKDPSlgnsINIVVVRLIVLEDEESglLISGNAQKSLKSFCRW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 270 --REQNLLGRHP--HDNVQLITGVDF-----IGTTVGLAKVSALCSRH-SGAVNQDHtrsAIGVASTMAHELGHNLGMNH 339
Cdd:cd04273   80 qkKLNPPNDSDPehHDHAILLTRQDIcrsngNCDTLGLAPVGGMCSPSrSCSINEDT---GLSSAFTIAHELGHVLGMPH 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564331629 340 DENIPGCycpIPREGGGCIMTESIGSKF-PKTFSRCSQVDLESFVTNHQTGCL 391
Cdd:cd04273  157 DGDGNSC---GPEGKDGHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCL 206
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
51-152 9.03e-35

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: 128.59  E-value: 9.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629   51 YPESLSYALGTSEQVFTLHLRKNRDLLGSSYTETYSAANGSEVKEQLHEQDHCLYQGHVEGYEGSAASISTCAGLSGFFR 130
Cdd:pfam01562  23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
                          90       100
                  ....*....|....*....|....*.
gi 564331629  131 VGSTVHLIEPL---DADEEGQ-HAVY 152
Cdd:pfam01562 103 TENEEYLIEPLekySREEGGHpHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
412-486 1.05e-34

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: 126.65  E-value: 1.05e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564331629   412 ERGEQCDCGTPQDCQNPCCNATTCQLAKGAECAHGACCHECKVKPAGELCRPMKDKCDLEEFCDGQKPTCPEDAF 486
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
412-484 5.49e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.58  E-value: 5.49e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564331629  412 ERGEQCDCGTPQDCQ-NPCCNATTCQLAKGAECAHGACCHECKVKPAGELCRPMKDKCDLEEFCDGQKPTCPED 484
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
196-376 1.20e-32

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: 124.84  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 196 RYVELYVVADSQEFQKL-GTREAVRQRVLEVVNHVDKLYRELSF----RVVLVGLEIWNKDKFY--ISRYANVTLENFLS 268
Cdd:cd04267    1 REIELVVVADHRMVSYFnSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAppIDSDASNTLNSFSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 269 WREQnllGRHPHDNVQLITGVDFI-GTTVGLAKVSALC-SRHSGAVNQDHTrSAIGVASTMAHELGHNLGMNHDENipGC 346
Cdd:cd04267   81 WRAE---GPIRHDNAVLLTAQDFIeGDILGLAYVGSMCnPYSSVGVVEDTG-FTLLTALTMAHELGHNLGAEHDGG--DE 154
                        170       180       190
                 ....*....|....*....|....*....|
gi 564331629 347 YCPIPREGGGCIMTESIGSKFPKTFSRCSQ 376
Cdd:cd04267  155 LAFECDGGGNYIMAPVDSGLNSYRFSQCSI 184
ACR smart00608
ADAM Cysteine-Rich Domain;
488-607 1.14e-30

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 117.46  E-value: 1.14e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629   488 QNGTPCPG--GYCFDGSCPTLAQQCQALWGPGARAASDSCFAFSIPQG-----C---YGSMYP--SRINRCGVLFCEGGQ 555
Cdd:smart00608   1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIPcaPEDVKCGKLQCTNVS 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564331629   556 KP--LERSSCTFSSHHG--LCQALQTDSNTNT-YEFVLQGTKCEEGKVCMDGNCQDL 607
Cdd:smart00608  81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
197-392 5.47e-19

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 86.64  E-value: 5.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 197 YVELYVVADSQEFQKLGTREAVRQRVLEVVNHVDKLYRELS---FRVVLVGLEIwNKDKFYISRYAN---------VTLE 264
Cdd:cd04272    2 YPELFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITI-SKDPDFEPYIHPinygyidaaETLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 265 NFLSW-REQNLLGRHphDNVQLITGVDFIGT--------TVGLAKVSALCSRHSGAVNQDhTRSAIGVASTMAHELGHNL 335
Cdd:cd04272   81 NFNEYvKKKRDYFNP--DVVFLVTGLDMSTYsggslqtgTGGYAYVGGACTENRVAMGED-TPGSYYGVYTMTHELAHLL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564331629 336 GMNHDENIPGCYCPIPREGGGC------IMTESIGSKFPKTFSRCSQVDLESFVTNHQTGCLT 392
Cdd:cd04272  158 GAPHDGSPPPSWVKGHPGSLDCpwddgyIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCLH 220
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
196-365 5.52e-17

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 79.77  E-value: 5.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  196 RYVELYVVADsQEFQKLGTREAVRQRVLEVVNHVDKL-YRELSFRVVLVGLEIWNKDKFYISRYANV-----TLENFLSW 269
Cdd:pfam13688   3 RTVALLVAAD-CSYVAAFGGDAAQANIINMVNTASNVyERDFNISLGLVNLTISDSTCPYTPPACSTgdssdRLSEFQDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  270 REQNllGRHPHDNVQLITGVDFigTTVGLAKVSALCSRHS-GAVNQDHTRSAIGVAS-----TMAHELGHNLGMNHD--- 340
Cdd:pfam13688  82 SAWR--GTQNDDLAYLFLMTNC--SGGGLAWLGQLCNSGSaGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDcds 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 564331629  341 -ENIPGC-----YCPIpreGGGCIMTESIGS 365
Cdd:pfam13688 158 sTSSQCCppsnsTCPA---GGRYIMNPSSSP 185
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
221-340 7.66e-15

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: 71.63  E-value: 7.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  221 RVLEVVNHVDKLY-RELSFRVVLVGLEIWNKDKF-YISRYANVTLENFLswreQNLLGRHPHDN---VQLITGVDFIGTT 295
Cdd:pfam13582   2 RIVSLVNRANTIYeRDLGIRLQLAAIIITTSADTpYTSSDALEILDELQ----EVNDTRIGQYGydlGHLFTGRDGGGGG 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 564331629  296 vGLAKVSALC-SRHSGAVNQDHTRSAIGVASTMAHELGHNLGMNHD 340
Cdd:pfam13582  78 -GIAYVGGVCnSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
489-526 4.59e-13

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: 66.10  E-value: 4.59e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 564331629  489 NGTPCPG--GYCFDGSCPTLAQQCQALWGPGARAASDSCF 526
Cdd:pfam08516   1 DGTPCNNgqAYCYNGRCRDRDQQCQELFGKGAKSAPDACY 40
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
196-382 2.06e-12

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: 66.01  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 196 RYVELYVVADSQEFQKLGTREAVRQRVLevvnhvdklyrelsfrvvlVGLEIWNKdkfyisrYANVTLenFLSwreqnLL 275
Cdd:cd00203    1 KVIPYVVVADDRDVEEENLSAQIQSLIL-------------------IAMQIWRD-------YLNIRF--VLV-----GV 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 276 GRHPHDNVQLITGVDFIGTTVGLAKVSALC-SRHSGAVNQDHTRSAIGVASTMAHELGHNLGMNHD------ENIPGCYC 348
Cdd:cd00203   48 EIDKADIAILVTRQDFDGGTGGWAYLGRVCdSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDhdrkdrDDYPTIDD 127
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564331629 349 PIPRE--GGGCIMTESIGSKFP---KTFSRCSQVDLESF 382
Cdd:cd00203  128 TLNAEddDYYSVMSYTKGSFSDgqrKDFSQCDIDQINKL 166
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
200-375 1.08e-11

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: 65.86  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 200 LYVVADSQEFQKLGT--REAVRQRVLEVVNHVDKLYRELSFRVVL---VGLEIW----NKD--------KFYISRYANVT 262
Cdd:cd04270    5 LLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGGGfkgIGFQIKririHTTpdevdpgnKFYNKSFPNWG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 263 LENFLswrEQNLLGRHPHDN--VQLITGVDFIGTTVGLAKVSALCSRHSGAVNQDHTRSAIGVAS--------------- 325
Cdd:cd04270   85 VEKFL---VKLLLEQFSDDVclAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKKKylntgltttvnygkr 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564331629 326 --------TMAHELGHNLGMNHDENIPGCyCPIPREGGGCIMTESIGS---KFPKTFSRCS 375
Cdd:cd04270  162 vptkesdlVTAHELGHNFGSPHDPDIAEC-APGESQGGNYIMYARATSgdkENNKKFSPCS 221
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
217-349 9.30e-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: 56.10  E-value: 9.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  217 AVRQRVLEVVNHVDKLYR--ELSFRVVLVGL-EI---------WNKDKFyiSRYANVTLENFLSwreqNLLGRHPHDNVQ 284
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEpdDININGGLVNPgEIpattsasdsGNNYCN--SPTTIVRRLNFLS----QWRGEQDYCLAH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  285 LITGVDFIGTTVGLAKVSALCSRHSGAVnqdhtRSAIGVAST---------------MAHELGHNLGMNHDENIPGCYCP 349
Cdd:pfam13574  76 LVTMGTFSGGELGLAYVGQICQKGASSP-----KTNTGLSTTtnygsfnyptqewdvVAHEVGHNFGATHDCDGSQYASS 150
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
202-392 1.49e-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: 55.89  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 202 VVADSQEFQKLGTREAVRQRVLEVVNHVDKLYRElSFRVVL--VGLEI--------------WN---KDKFYISRyanvT 262
Cdd:cd04271    7 VAADCSYTKSFGSVEEARRNILNNVNSASQLYES-SFNISLglRNLTIsdascpstavdsapWNlpcNSRIDIDD----R 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 263 LENFLSWREQnllgRHPHDNV--QLITGVDfIGTTVGLAKVSALC-SRHSGAVNQDHTrSAIGVAST------MAHELGH 333
Cdd:cd04271   82 LSIFSQWRGQ----QPDDGNAfwTLMTACP-SGSEVGVAWLGQLCrTGASDQGNETVA-GTNVVVRTsnewqvFAHEIGH 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564331629 334 NLGMNHDENIPGCY---------CPIPRE----GGGCIMTESIGSKFpKTFSRCSQVDLESFV--TNHQTGCLT 392
Cdd:cd04271  156 TFGAVHDCTSGTCSdgsvgsqqcCPLSTStcdaNGQYIMNPSSSSGI-TEFSPCTIGNICSLLgrNPVRTSCLS 228
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
196-346 4.42e-07

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: 51.47  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  196 RYVELYVVADSQEFQKLGTREAVRQRVLEVVNHVDKLY-RELSFRVVLVG----------LEIWNKDKFyISRYANVTLE 264
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISdrdviytdssTDSFNADCS-GGDLGNWRLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  265 NFLSWReqnllGRHPHDNVQLITGVDFIGTTVGLAKVSALCSRHSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDENIP 344
Cdd:pfam13583  82 TLTSWR-----DSLNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQNAKASGVARSRDEWDIFAHEIGHTFGAVHDCSSQ 156

                  ..
gi 564331629  345 GC 346
Cdd:pfam13583 157 GE 158
PHA03247 PHA03247
large tegument protein UL36; Provisional
638-819 6.92e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  638 APPYCAQLLADVPASESLPVSVVVVLVILVAAVVIGAGIVIYRKA------PKQIQRRSVAPKPTSGLSNPLFYTGDSSL 711
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspagplPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  712 PA---KSRPPDPPEMVSTNQPPRPIVKPKRPPpappgAMSSPPLPVPVYAPKAPNQLRPDPPTKPLPKLK-PKQVKPTFA 787
Cdd:PHA03247 2858 PGgdvRRRPPSRSPAAKPAAPARPPVRRLARP-----AVSRSTESFALPPDQPERPPQPQAPPPPQPQPQpPPPPQPQPP 2932
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564331629  788 PPTP-----PVKPGTGGTVPGVTQQGAGGSKVALKVP 819
Cdd:PHA03247 2933 PPPPprpqpPLAPTTDPAGAGEPSGAVPQPWLGALVP 2969
PHA03247 PHA03247
large tegument protein UL36; Provisional
638-815 1.20e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  638 APPYCAQL--LADVPASESLPVSVVVVLVILVAAVVIGAGIviyRKAPKQIQRRSVAPKPTSGLSNPLFYTGDSSLPAKS 715
Cdd:PHA03247 2688 ARPTVGSLtsLADPPPPPPTPEPAPHALVSATPLPPGPAAA---RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTA 2764
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  716 RP--PDPPEMVSTNQPPRPIVKPKRPPPAPPGAMSSP------PLPVPVYAPKAPNQLRPDPPTKPLPKLKPKQVKPTFA 787
Cdd:PHA03247 2765 GPpaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdpadpPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844
                         170       180       190
                  ....*....|....*....|....*....|
gi 564331629  788 PPTPPVKPGtGGTVPG--VTQQGAGGSKVA 815
Cdd:PHA03247 2845 PPPPSLPLG-GSVAPGgdVRRRPPSRSPAA 2873
PHA03247 PHA03247
large tegument protein UL36; Provisional
650-803 5.98e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 5.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  650 PASESLPVSVVVVLVILVAAVVIGAGIV----IYRKAPKqiqrRSVAPKPT-------SGLSNPLFYTGDSSLPaksRPP 718
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSLPLGGSVApggdVRRRPPS----RSPAAKPAaparppvRRLARPAVSRSTESFA---LPP 2902
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  719 DPPEMVSTNQPPRPivkpkrpppappgAMSSPPLPVPVY-APKAPNQLRPDPPTKPLPKLKPkQVKPTFAPPTPPVkpgt 797
Cdd:PHA03247 2903 DQPERPPQPQAPPP-------------PQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAG-AGEPSGAVPQPWL---- 2964

                  ....*.
gi 564331629  798 GGTVPG 803
Cdd:PHA03247 2965 GALVPG 2970
PRK10819 PRK10819
transport protein TonB; Provisional
712-795 1.52e-04

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 44.29  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 712 PAKSRPPDPPEMVSTNQPPRPIvkpkrpppappgamSSPPLPVPVYAPKapnqlrPDPPTKPLPKLKPKQVKPTFAPPTP 791
Cdd:PRK10819  60 PPQAVQPPPEPVVEPEPEPEPI--------------PEPPKEAPVVIPK------PEPKPKPKPKPKPKPVKKVEEQPKR 119

                 ....
gi 564331629 792 PVKP 795
Cdd:PRK10819 120 EVKP 123
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
681-795 2.65e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.68  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 681 KAPKQIQRRSVAPKPTSGL----SNPLFYTGDSSLPAKSRPP-DPPEMVSTNQPPRPIVKPKRPPPAPPGAMSSPPLPVP 755
Cdd:PTZ00449 547 GKPGETKEGEVGKKPGPAKehkpSKIPTLSKKPEFPKDPKHPkDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKR 626
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564331629 756 VYAPKAPNqlRPDPPTKPLPKLKP---KQVKPTFAP--PTPPVKP 795
Cdd:PTZ00449 627 PESPKSPK--RPPPPQRPSSPERPegpKIIKSPKPPksPKPPFDP 669
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
712-807 3.04e-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: 44.37  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 712 PAKSRPPDP-PEMVSTNQPPRPIVkpkrpppappgamssPPLPVPVYAPKAPNQLRPDPPTKPLPKLKPKQVKPTFAPPT 790
Cdd:NF033839 287 PGNKKPSAPkPGMQPSPQPEKKEV---------------KPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPK 351
                         90
                 ....*....|....*..
gi 564331629 791 PPVKPGTGGTVPGVTQQ 807
Cdd:NF033839 352 PEVKPQPEKPKPEVKPQ 368
PRK11633 PRK11633
cell division protein DedD; Provisional
693-795 4.73e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 42.30  E-value: 4.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 693 PKPtsglsnplfytGDS----SLPA--KSRPPDPPE----MVSTNQPPRPIVKPkrpppappgAMSSPPLPVPVYAPKAP 762
Cdd:PRK11633  45 PKP-----------GDRdepdMMPAatQALPTQPPEgaaeAVRAGDAAAPSLDP---------ATVAPPNTPVEPEPAPV 104
                         90       100       110
                 ....*....|....*....|....*....|...
gi 564331629 763 NQLRPDPPTKPLPKLKPKQVKPTFAPPTPPVKP 795
Cdd:PRK11633 105 EPPKPKPVEKPKPKPKPQQKVEAPPAPKPEPKP 137
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
710-811 6.84e-04

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 42.61  E-value: 6.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  710 SLPAKSR---PPDPPEMVSTNQPPRPivkpkrpppapPGAMSSPPLPVPVYAPKAPNQLRPDPPTKPLPKLKPKQVKPTf 786
Cdd:pfam07174  32 ALPAVAHadpEPAPPPPSTATAPPAP-----------PPPPPAPAAPAPPPPPAAPNAPNAPPPPADPNAPPPPPADPN- 99
                          90       100
                  ....*....|....*....|....*
gi 564331629  787 APPTPPVKPgtGGTVPGVTQQGAGG 811
Cdd:pfam07174 100 APPPPAVDP--NAPEPGRIDNAVGG 122
PHA03247 PHA03247
large tegument protein UL36; Provisional
688-820 9.99e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  688 RRSVAPKPTSglsnPLFYTGDSSLPAKSRPPDP-PEMVSTNQPPRPIVKPKRPPPAPPGAMSSPPLPVPVYAP------- 759
Cdd:PHA03247 2588 RPDAPPQSAR----PRAPVDDRGDPRGPAPPSPlPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvsr 2663
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564331629  760 --KAPNQLRPDPPTKPLPKLKPKQVKPTFAP-------------PTPPVKPGTGGT-VPGVTQQGAGGSKVALKVPI 820
Cdd:PHA03247 2664 prRARRLGRAAQASSPPQRPRRRAARPTVGSltsladpppppptPEPAPHALVSATpLPPGPAAARQASPALPAAPA 2740
PHA03247 PHA03247
large tegument protein UL36; Provisional
680-798 2.66e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  680 RKAPKQiQRRSVAPKPTSGLSNPLFYTGDSSLPAKSRPPDPPEmvSTNQPPRPIVKPKRPPPAPPGA-MSSPPLPVPVYA 758
Cdd:PHA03247 2665 RRARRL-GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPP--TPEPAPHALVSATPLPPGPAAArQASPALPAAPAP 2741
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 564331629  759 PKAPNQlrPDPPTKPLPKLKPkQVKPTFAPPTPPVKPGTG 798
Cdd:PHA03247 2742 PAVPAG--PATPGGPARPARP-PTTAGPPAPAPPAAPAAG 2778
PHA03247 PHA03247
large tegument protein UL36; Provisional
706-803 4.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629  706 TGDSSLPAKSRPPDPPEMVSTNQPPRPIVKPKRPPPAPPGAMSSPPLPVPVYAPKAPNQLRPDPPTkPLPKLKPKQVKPT 785
Cdd:PHA03247 2563 APDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPP-PSPSPAANEPDPH 2641
                          90
                  ....*....|....*...
gi 564331629  786 FAPPTPPVKPGTGGTVPG 803
Cdd:PHA03247 2642 PPPTVPPPERPRDDPAPG 2659
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
712-813 7.00e-03

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: 39.75  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331629 712 PAKSRP---PDP----PEMVSTNQPPRPIVkpkrpppappgamsSPPLPVPVYAPKaPNQLRPDPPTKPLPKLKPKQVKP 784
Cdd:NF033839 402 PEKPKPevkPQPekpkPEVKPQPEKPKPEV--------------KPQPEKPKPEVK-PQPEKPKPEVKPQPETPKPEVKP 466
                         90       100
                 ....*....|....*....|....*....
gi 564331629 785 TFAPPTPPVKPGTGGTVPGVTQQGAGGSK 813
Cdd:NF033839 467 QPEKPKPEVKPQPEKPKPDNSKPQADDKK 495
 
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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