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Conserved domains on  [gi|767961654|ref|XP_011537602|]
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A disintegrin and metalloproteinase with thrombospondin motifs 14 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 273-460 9.97e-88

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: 280.66  E-value: 9.97e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  273 RFHGKEHVQNYVLTLMNIVDEIYHDESLGVHINIALVRLIMVGYRQSLSLIeRGNPSRSLEQVCRWAHSQQRQDPSHAEH 352
Cdd:cd04273    15 EFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRWQKKLNPPNDSDPEH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  353 HDHVVFLTRQDF----GPSGMQGYAPVTGMCHPLRSCALNHEDGFSSAFVIAHETGHVLGMEHDGQGNGCADETSLGSVM 428
Cdd:cd04273    94 HDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSCGPEGKDGHIM 173

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767961654  429 APLVQAAFHRFHWSRCSKLELSRYLPSY--DCLL 460
Cdd:cd04273   174 SPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 77-207 5.70e-34

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: 126.66  E-value: 5.70e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654    77 PRHSSHLRVARSPLHPGGTLwpgrvgrHSLYFNVTVFGKELHLRLRPNRRLVVPGSSVEW-QEDFRELFRQPLRQE-CVY 154
Cdd:pfam01562    5 PVRLDPSRRRRSLASESTYL-------DTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPVQTDhCYY 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767961654   155 TGGVTGMPGAAVAISNCDGLAGLIRTDSTDFFIEPLErgQQEKEASGRTHVVY 207
Cdd:pfam01562   78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 475-544 2.03e-23

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 94.33  E-value: 2.03e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   475 PGINYSMDEQCRFDFGSGYQTCLAFrTFEPCKQLWCSHPDNPYfCKTKKGPPLDGTECAPGKWCFKGHCI 544
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
ADAMTS_spacer1 super family cl20316
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 718-812 2.33e-21

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


The actual alignment was detected with superfamily member pfam05986:

Pssm-ID: 461796  Cd Length: 115  Bit Score: 90.33  E-value: 2.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   718 TVKGTLGKAsKQAGALKLVQIPAGARHIQIEALEKSPHRIVVKNqVTGSFILNPKGK-EATSRTFTAMGLEWEDAV-EDA 795
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRRsLPA 78

                           90
                   ....*....|....*..
gi 767961654   796 KESLKTSGPLPEAIAIL 812
Cdd:pfam05986   79 LEELHAPGPTQEDLEIQ 95
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 558-610 2.22e-16

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 74.16  E-value: 2.22e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767961654    558 WSSWTKFGSCSRSCGGGVRSRSRSCNNPSPAYGGRLCLGPMFEYQVCNSEECP 610
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 612-716 1.63e-08

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 53.56  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   612 TYEDFRAQQCAKRNSYYVHQN----AKHSW---VPYEPDDDAqkCELICQSADTGDVVFMNQVVHDGTRCSYRDP----- 679
Cdd:pfam19236    1 TQLEFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDAL--CRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgt 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 767961654   680 YSVCARGECVPVGCDKEVGSMKADDKCGVCGGDNSHC 716
Cdd:pfam19236   79 LSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 813-854 3.09e-06

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 45.14  E-value: 3.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767961654   813 CSATCGEGIQQRQVVCR------TNANSLghCEGD-RPDTVQVCSLPAC 854
Cdd:pfam19030    9 CSVTCGGGVQTRLVQCVqkgggsIVPDSE--CSAQkKPPETQSCNLKPC 55
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 942-1056 6.62e-04

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  942 TSLPPFSTPGSPLPGPQDPADAAEPPGKPTGSEDHQHGRATQLPGALDTSSPGTQ-HPFAPETPIPGASWSISPTTPGGL 1020
Cdd:PRK07764  600 PPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPkHVAVPDASDGGDGWPAKAGGAAPA 679

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767961654 1021 PWGWTQTPTPVPEDKGQPGEDLRHPGTSLPAASPVT 1056
Cdd:PRK07764  680 APPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQAD 715
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 273-460 9.97e-88

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: 280.66  E-value: 9.97e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  273 RFHGKEHVQNYVLTLMNIVDEIYHDESLGVHINIALVRLIMVGYRQSLSLIeRGNPSRSLEQVCRWAHSQQRQDPSHAEH 352
Cdd:cd04273    15 EFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRWQKKLNPPNDSDPEH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  353 HDHVVFLTRQDF----GPSGMQGYAPVTGMCHPLRSCALNHEDGFSSAFVIAHETGHVLGMEHDGQGNGCADETSLGSVM 428
Cdd:cd04273    94 HDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSCGPEGKDGHIM 173

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767961654  429 APLVQAAFHRFHWSRCSKLELSRYLPSY--DCLL 460
Cdd:cd04273   174 SPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 77-207 5.70e-34

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: 126.66  E-value: 5.70e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654    77 PRHSSHLRVARSPLHPGGTLwpgrvgrHSLYFNVTVFGKELHLRLRPNRRLVVPGSSVEW-QEDFRELFRQPLRQE-CVY 154
Cdd:pfam01562    5 PVRLDPSRRRRSLASESTYL-------DTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPVQTDhCYY 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767961654   155 TGGVTGMPGAAVAISNCDGLAGLIRTDSTDFFIEPLErgQQEKEASGRTHVVY 207
Cdd:pfam01562   78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 475-544 2.03e-23

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 94.33  E-value: 2.03e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   475 PGINYSMDEQCRFDFGSGYQTCLAFrTFEPCKQLWCSHPDNPYfCKTKKGPPLDGTECAPGKWCFKGHCI 544
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 278-463 1.25e-22

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: 96.99  E-value: 1.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   278 EHVQNYVLTLMNIVDEIYHDeslgvhINIalvRLIMVGyrqslslIE----------RGNPSRSLEQVCRWahsQQRQDP 347
Cdd:pfam01421   22 TVVRQRVFQVVNLVNSIYKE------LNI---RVVLVG-------LEiwtdedkidvSGDANDTLRNFLKW---RQEYLK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   348 SHAEHhDHVVFLTRQDFGpSGMQGYAPVTGMCHPLRSCALN---HEDGFSSAFVIAHETGHVLGMEHDGQGNGCADETSL 424
Cdd:pfam01421   83 KRKPH-DVAQLLSGVEFG-GTTVGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCPPGG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 767961654   425 GSVMAPLVQAAFHRfHWSRCSKLELSRYLPSYD--CLLDDP 463
Cdd:pfam01421  161 GCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 718-812 2.33e-21

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 90.33  E-value: 2.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   718 TVKGTLGKAsKQAGALKLVQIPAGARHIQIEALEKSPHRIVVKNqVTGSFILNPKGK-EATSRTFTAMGLEWEDAV-EDA 795
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRRsLPA 78

                           90
                   ....*....|....*..
gi 767961654   796 KESLKTSGPLPEAIAIL 812
Cdd:pfam05986   79 LEELHAPGPTQEDLEIQ 95
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 558-610 2.22e-16

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 74.16  E-value: 2.22e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767961654    558 WSSWTKFGSCSRSCGGGVRSRSRSCNNPSPAYGGRLCLGPMFEYQVCNSEECP 610
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 612-716 1.63e-08

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 53.56  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   612 TYEDFRAQQCAKRNSYYVHQN----AKHSW---VPYEPDDDAqkCELICQSADTGDVVFMNQVVHDGTRCSYRDP----- 679
Cdd:pfam19236    1 TQLEFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDAL--CRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgt 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 767961654   680 YSVCARGECVPVGCDKEVGSMKADDKCGVCGGDNSHC 716
Cdd:pfam19236   79 LSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
556-609 2.48e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.88  E-value: 2.48e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767961654   556 GGWSSWTkfgSCSRSCGGGVRSRSRSCNNPSPayGGRLCLGPMFEYQVCNSEEC 609
Cdd:pfam00090    1 SPWSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 813-854 3.09e-06

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 45.14  E-value: 3.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767961654   813 CSATCGEGIQQRQVVCR------TNANSLghCEGD-RPDTVQVCSLPAC 854
Cdd:pfam19030    9 CSVTCGGGVQTRLVQCVqkgggsIVPDSE--CSAQkKPPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 813-854 2.34e-05

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.57  E-value: 2.34e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 767961654    813 CSATCGEGIQQRQVVCRTNANSLG--HCEGDRPDTvQVCSLPAC 854
Cdd:smart00209   10 CSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVET-RACNEQPC 52
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 942-1056 6.62e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  942 TSLPPFSTPGSPLPGPQDPADAAEPPGKPTGSEDHQHGRATQLPGALDTSSPGTQ-HPFAPETPIPGASWSISPTTPGGL 1020
Cdd:PRK07764  600 PPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPkHVAVPDASDGGDGWPAKAGGAAPA 679

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767961654 1021 PWGWTQTPTPVPEDKGQPGEDLRHPGTSLPAASPVT 1056
Cdd:PRK07764  680 APPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQAD 715
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 273-460 9.97e-88

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: 280.66  E-value: 9.97e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  273 RFHGKEHVQNYVLTLMNIVDEIYHDESLGVHINIALVRLIMVGYRQSLSLIeRGNPSRSLEQVCRWAHSQQRQDPSHAEH 352
Cdd:cd04273    15 EFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLI-SGNAQKSLKSFCRWQKKLNPPNDSDPEH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  353 HDHVVFLTRQDF----GPSGMQGYAPVTGMCHPLRSCALNHEDGFSSAFVIAHETGHVLGMEHDGQGNGCADETSLGSVM 428
Cdd:cd04273    94 HDHAILLTRQDIcrsnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDGNSCGPEGKDGHIM 173

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767961654  429 APLVQAAFHRFHWSRCSKLELSRYLPSY--DCLL 460
Cdd:cd04273   174 SPTLGANTGPFTWSKCSRRYLTSFLDTGdgNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 77-207 5.70e-34

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: 126.66  E-value: 5.70e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654    77 PRHSSHLRVARSPLHPGGTLwpgrvgrHSLYFNVTVFGKELHLRLRPNRRLVVPGSSVEW-QEDFRELFRQPLRQE-CVY 154
Cdd:pfam01562    5 PVRLDPSRRRRSLASESTYL-------DTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyLDGGTGVESPPVQTDhCYY 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767961654   155 TGGVTGMPGAAVAISNCDGLAGLIRTDSTDFFIEPLErgQQEKEASGRTHVVY 207
Cdd:pfam01562   78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLE--KYSREEGGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 278-446 4.57e-25

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: 103.65  E-value: 4.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  278 EHVQNYVLTLMNIVDEIYHDESLGVHINIALVRLIMvgyRQSLSLIERGNP--SRSLEQVCRWAHSQqrqdpshAEHHDH 355
Cdd:cd04267    22 NILQAYITELINIANSIYRSTNLRLGIRISLEGLQI---LKGEQFAPPIDSdaSNTLNSFSFWRAEG-------PIRHDN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  356 VVFLTRQDFGPSGMQGYAPVTGMCHPLRSCAL--NHEDGFSSAFVIAHETGHVLGMEHDGQGNGCADETSLGS-VMAPLV 432
Cdd:cd04267    92 AVLLTAQDFIEGDILGLAYVGSMCNPYSSVGVveDTGFTLLTALTMAHELGHNLGAEHDGGDELAFECDGGGNyIMAPVD 171

                         170
                  ....*....|....
gi 767961654  433 QAAFHRfHWSRCSK 446
Cdd:cd04267   172 SGLNSY-RFSQCSI 184
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 475-544 2.03e-23

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 94.33  E-value: 2.03e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   475 PGINYSMDEQCRFDFGSGYQTCLAFrTFEPCKQLWCSHPDNPYfCKTKKGPPLDGTECAPGKWCFKGHCI 544
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNG-DEDVCSKLWCSNPGGST-CTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 273-461 2.11e-23

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: 98.84  E-value: 2.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  273 RFHGK--EHVQNYVLTLMNIVDEIYHDeslgVHINIALVRLIMVGYRQSLSLieRGNPSRSLEQVCRWahsqQRQDPSHA 350
Cdd:cd04269    15 KKYGSnlSKVRQRVIEIVNIVDSIYRP----LNIRVVLVGLEIWTDKDKISV--SGDAGETLNRFLDW----KRSNLLPR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  351 EHHDHVVFLTRQDFgPSGMQGYAPVTGMCHPLRSCALNHEDG---FSSAFVIAHETGHVLGMEHDG-----QGNGCadet 422
Cdd:cd04269    85 KPHDNAQLLTGRDF-DGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDDggctcGRSTC---- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767961654  423 slgsVMAPlvQAAFHRFHWSRCSKLELSRYLPSYD--CLLD 461
Cdd:cd04269   160 ----IMAP--SPSSLTDAFSNCSYEDYQKFLSRGGgqCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 278-463 1.25e-22

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: 96.99  E-value: 1.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   278 EHVQNYVLTLMNIVDEIYHDeslgvhINIalvRLIMVGyrqslslIE----------RGNPSRSLEQVCRWahsQQRQDP 347
Cdd:pfam01421   22 TVVRQRVFQVVNLVNSIYKE------LNI---RVVLVG-------LEiwtdedkidvSGDANDTLRNFLKW---RQEYLK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   348 SHAEHhDHVVFLTRQDFGpSGMQGYAPVTGMCHPLRSCALN---HEDGFSSAFVIAHETGHVLGMEHDGQGNGCADETSL 424
Cdd:pfam01421   83 KRKPH-DVAQLLSGVEFG-GTTVGAAYVGGMCSLEYSGGVNedhSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCPPGG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 767961654   425 GSVMAPLVQAAFHRfHWSRCSKLELSRYLPSYD--CLLDDP 463
Cdd:pfam01421  161 GCIMNPSAGSSFPR-KFSNCSQEDFEQFLTKQKgaCLFNKP 200
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 718-812 2.33e-21

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 90.33  E-value: 2.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   718 TVKGTLGKAsKQAGALKLVQIPAGARHIQIEALEKSPHRIVVKNqVTGSFILNPKGK-EATSRTFTAMGLEWEDAV-EDA 795
Cdd:pfam05986    1 TVSGSFTEG-RAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSiSLNPTYPSLLGTVLEYRRsLPA 78

                           90
                   ....*....|....*..
gi 767961654   796 KESLKTSGPLPEAIAIL 812
Cdd:pfam05986   79 LEELHAPGPTQEDLEIQ 95
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 558-610 2.22e-16

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 74.16  E-value: 2.22e-16
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767961654    558 WSSWTKFGSCSRSCGGGVRSRSRSCNNPSPAYGGRLCLGPMFEYQVCNSEECP 610
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 352-453 1.10e-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: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  352 HHDHVVFLTRQDFgPSGMQGYAPVTGMCHPLRSCAL---NHEDGFSSAFVIAHETGHVLGMEHDGQGNGCADE------- 421
Cdd:cd00203    51 KADIAILVTRQDF-DGGTGGWAYLGRVCDSLRGVGVlqdNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYptiddtl 129

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767961654  422 ----TSLGSVMAPLVQAAFH--RFHWSRCSKLELSRYL 453
Cdd:cd00203   130 naedDDYYSVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 612-716 1.63e-08

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 53.56  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   612 TYEDFRAQQCAKRNSYYVHQN----AKHSW---VPYEPDDDAqkCELICQSADTGDVVFMNQVVHDGTRCSYRDP----- 679
Cdd:pfam19236    1 TQLEFMSQQCARTDGQPLRSSpggaSFYHWgaaVPHSQGDAL--CRHMCRAIGESFIMKRGDSFLDGTRCMPSGPredgt 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 767961654   680 YSVCARGECVPVGCDKEVGSMKADDKCGVCGGDNSHC 716
Cdd:pfam19236   79 LSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
556-609 2.48e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.88  E-value: 2.48e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767961654   556 GGWSSWTkfgSCSRSCGGGVRSRSRSCNNPSPayGGRLCLGPMFEYQVCNSEEC 609
Cdd:pfam00090    1 SPWSPWS---PCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 353-459 2.61e-08

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 55.44  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  353 HDHVVFLTRQDFGP-------SGMQGYAPVTGMCHPLRsCALNHEDG--FSSAFVIAHETGHVLGMEHDGQG-------- 415
Cdd:cd04272    95 PDVVFLVTGLDMSTysggslqTGTGGYAYVGGACTENR-VAMGEDTPgsYYGVYTMTHELAHLLGAPHDGSPppswvkgh 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767961654  416 ---NGCADEtsLGSVMAPLVQAAFHrFHWSRCSKLELSRYL--PSYDCL 459
Cdd:cd04272   174 pgsLDCPWD--DGYIMSYVVNGERQ-YRFSQCSQRQIRNVFrrLGASCL 219
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 559-609 1.51e-07

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 48.81  E-value: 1.51e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767961654   559 SSWTKFGSCSRSCGGGVRSRSRSCNNPsPAYGGRLClGPMFEYQVCNSEEC 609
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 813-854 3.09e-06

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 45.14  E-value: 3.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767961654   813 CSATCGEGIQQRQVVCR------TNANSLghCEGD-RPDTVQVCSLPAC 854
Cdd:pfam19030    9 CSVTCGGGVQTRLVQCVqkgggsIVPDSE--CSAQkKPPETQSCNLKPC 55
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
275-430 7.03e-06

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 47.80  E-value: 7.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   275 HGKEHVQNYVLTLMNIVDEIYHDESlgvHINIALVRLIMVGYRQSLSLIERGNPSRSLeqvcRWAHSQQRQDPSHAEHHD 354
Cdd:pfam13688   19 FGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPACSTGDSSD----RLSEFQDFSAWRGTQNDD 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654   355 HVVFLTRQDFGPSGMqgyAPVTGMCHPLRSCALNHEDGF--------SSAFVIAHETGHVLGMEHDGQGNGCADETSLGS 426
Cdd:pfam13688   92 LAYLFLMTNCSGGGL---AWLGQLCNSGSAGSVSTRVSGnnvvvstaTEWQVFAHEIGHNFGAVHDCDSSTSSQCCPPSN 168


                   ....
gi 767961654   427 VMAP 430
Cdd:pfam13688  169 STCP 172
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 813-854 2.34e-05

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.57  E-value: 2.34e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 767961654    813 CSATCGEGIQQRQVVCRTNANSLG--HCEGDRPDTvQVCSLPAC 854
Cdd:smart00209   10 CSVTCGGGVQTRTRSCCSPPPQNGggPCTGEDVET-RACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
813-854 6.75e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 41.25  E-value: 6.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 767961654   813 CSATCGEGIQQRQVVCRTNANSLGHCEGDRPDTvQVCSLPAC 854
Cdd:pfam00090    9 CSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIET-QACKMDKC 49
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 942-1056 6.62e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  942 TSLPPFSTPGSPLPGPQDPADAAEPPGKPTGSEDHQHGRATQLPGALDTSSPGTQ-HPFAPETPIPGASWSISPTTPGGL 1020
Cdd:PRK07764  600 PPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPkHVAVPDASDGGDGWPAKAGGAAPA 679

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767961654 1021 PWGWTQTPTPVPEDKGQPGEDLRHPGTSLPAASPVT 1056
Cdd:PRK07764  680 APPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQAD 715
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 562-609 1.89e-03

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 37.43  E-value: 1.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767961654   562 TKFGSCSRSCGGGVRSRSRSCNNPSP--AYGGRLCLG---PMfEYQVCNSEEC 609
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAqkkPP-ETQSCNLKPC 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
 950-1056 8.63e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  950 PGSPLPGPQDPA---------DAAEPPGKPTGSEDHQHGRATQLPGALDTSSPGTQHPFAPETPIPGASwSISPTTPGGl 1020
Cdd:PHA03247 2676 ASSPPQRPRRRAarptvgsltSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV-PAGPATPGG- 2753

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767961654 1021 pwgwtqtPTPVPEDKGQPGedlrhPGTSLPAASPVT 1056
Cdd:PHA03247 2754 -------PARPARPPTTAG-----PPAPAPPAAPAA 2777
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 945-1038 9.74e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.60  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961654  945 PPFSTPGSPLPGPQDPadaAEPPGKPTGSEDHQHGRATQlpGALDTSSPGTQHPFAPETPIPGASwsiSPTTPGGLPWGW 1024
Cdd:PHA03264  267 PPAPSGGSPAPPGDDR---PEAKPEPGPVEDGAPGRETG--GEGEGPEPAGRDGAAGGEPKPGPP---RPAPDADRPEGW 338

                          90
                  ....*....|....*....
gi 767961654 1025 TQTPT-----PVPEDKGQP 1038
Cdd:PHA03264  339 PSLEAitfppPTPATPAVP 357
 
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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