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Conserved domains on  [gi|537544566|ref|NP_112219.3|]
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A disintegrin and metalloproteinase with thrombospondin motifs 10 isoform 1 preproprotein [Homo sapiens]

Protein Classification

Pep_M12B_propep and ZnMc_ADAMTS_like domain-containing protein (domain architecture ID 12023084)

protein containing domains Pep_M12B_propep, ZnMc_ADAMTS_like, TSP1, and PLAC

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) ...
239-454 4.71e-107

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: 336.52  E-value: 4.71e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  319 KSIVNHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273    81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 537544566  399 GMNHDGVGNSCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 454
Cdd:cd04273   153 GMPHDGDGNSCGPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAM_spacer1 super family cl20316
ADAM-TS Spacer 1; This family represents the Spacer-1 region from the ADAM-TS family of ...
706-818 1.46e-35

ADAM-TS Spacer 1; This family represents the Spacer-1 region from the ADAM-TS family of metalloproteinases.


The actual alignment was detected with superfamily member pfam05986:

Pssm-ID: 310520  Cd Length: 114  Bit Score: 133.51  E-value: 1.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   706 ETIEGVFSPASPGAGYEDVVWIPKGSVHIFIQDLNLSLSHLALK-GDQESLLLEGLPGTPQPHrLPLAGTTFQLRQGPDQ 784
Cdd:pfam05986    1 KTVKGTFTKALKSHGYNDVVTIPAGARHILIRELEASGNYLALKnADGEYYLNGNWTISWSGT-FEAAGTVFEYSRSDAA 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 537544566   785 VQSLEALGPINASLIVMVLARTE-LPALRYRFNAP 818
Cdd:pfam05986   80 PESLHATGPTNEPLTVQVLSQGAtNPGVRYEYFIP 114
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
40-180 2.25e-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: 307618  Cd Length: 125  Bit Score: 133.45  E-value: 2.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566    40 EIAFPTRVDHNGallafspppprRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAW--QRA 117
Cdd:pfam01562    1 EIVIPVRVDASG-----------RRRRSLSSEYPDRLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETYREDGTEVtdQPP 69
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 537544566   118 ARPHCLYAGHLQGQASSShVAISTCGGLHGLIVADEEEYLIEPLHGgpkgsrSPEESGPHVVY 180
Cdd:pfam01562   70 IQDHCHYQGHVEGEPDSS-AALSTCSGLRGVIRTGDEEYFIEPLES------SEEEGHPHVVY 125
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
550-602 5.95e-14

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


:

Pssm-ID: 214559  Cd Length: 53  Bit Score: 69.54  E-value: 5.95e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 537544566    550 WGPWTPWGDCSRTCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTDDCP 602
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
1069-1100 2.32e-06

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


:

Pssm-ID: 312271  Cd Length: 31  Bit Score: 47.10  E-value: 2.32e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 537544566  1069 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTC 1100
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYKQFCCRSC 30
GGN super family cl25800
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
867-1005 2.87e-05

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


The actual alignment was detected with superfamily member PHA02682:

Pssm-ID: 330621  Cd Length: 280  Bit Score: 47.16  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  867 SAHSKLPKRQRACNTEPCPPDWVVG---NWSL--CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleAChg 941
Cdd:PHA02682   24 SLFTKCPQATIPAPAAPCPPDADVDpldKYSVkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP----AC-- 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537544566  942 PTCPPewAALDWSECTPSCGPGlrhrvvlCKSADHRATLPPAHCSPAAKPPATMRCNLRRCPPA 1005
Cdd:PHA02682   96 PACAP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
1010-1054 1.31e-03

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


:

Pssm-ID: 214559  Cd Length: 53  Bit Score: 39.49  E-value: 1.31e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 537544566   1010 GEWGECSAQCGVGQRQRSVRCTSHTGQAS-HECTEAL---RPPTTQQCE 1054
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEDvetRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
239-454 4.71e-107

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: 336.52  E-value: 4.71e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  319 KSIVNHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273    81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 537544566  399 GMNHDGVGNSCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 454
Cdd:cd04273   153 GMPHDGDGNSCGPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAM_spacer1 pfam05986
ADAM-TS Spacer 1; This family represents the Spacer-1 region from the ADAM-TS family of ...
706-818 1.46e-35

ADAM-TS Spacer 1; This family represents the Spacer-1 region from the ADAM-TS family of metalloproteinases.


Pssm-ID: 310520  Cd Length: 114  Bit Score: 133.51  E-value: 1.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   706 ETIEGVFSPASPGAGYEDVVWIPKGSVHIFIQDLNLSLSHLALK-GDQESLLLEGLPGTPQPHrLPLAGTTFQLRQGPDQ 784
Cdd:pfam05986    1 KTVKGTFTKALKSHGYNDVVTIPAGARHILIRELEASGNYLALKnADGEYYLNGNWTISWSGT-FEAAGTVFEYSRSDAA 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 537544566   785 VQSLEALGPINASLIVMVLARTE-LPALRYRFNAP 818
Cdd:pfam05986   80 PESLHATGPTNEPLTVQVLSQGAtNPGVRYEYFIP 114
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
40-180 2.25e-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: 307618  Cd Length: 125  Bit Score: 133.45  E-value: 2.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566    40 EIAFPTRVDHNGallafspppprRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAW--QRA 117
Cdd:pfam01562    1 EIVIPVRVDASG-----------RRRRSLSSEYPDRLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETYREDGTEVtdQPP 69
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 537544566   118 ARPHCLYAGHLQGQASSShVAISTCGGLHGLIVADEEEYLIEPLHGgpkgsrSPEESGPHVVY 180
Cdd:pfam01562   70 IQDHCHYQGHVEGEPDSS-AALSTCSGLRGVIRTGDEEYFIEPLES------SEEEGHPHVVY 125
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
239-457 8.19e-30

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


Pssm-ID: 307535  Cd Length: 199  Bit Score: 119.69  E-value: 8.19e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   239 RYVETLVVADKMMVAYHGRrDVE---QYVLAIMNIVAKLFQdsSLGSTVnILVTRLILLTEDQptLEITHHAGKSLDSFC 315
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGS-DVNvvrQRVFQVVNLVNSIYK--ELNIRV-VLVGLEIWTDEDK--IDVSGDANDTLRNFL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   316 KWQKSIVNHSghgnaipengvANHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSVNED-----IGLATafTI 390
Cdd:pfam01421   75 KWRQEYLKKR-----------KPHDVAQLLS------GRTFGGTTVGAAYPGGMCSPSYSGGVNLDhkinvEGFAV--TM 135
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537544566   391 AHEIGHTFGMNHDGVGN-SCGARGqdpAKLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 457
Cdd:pfam01421  136 AHELGHNLGMTHDDITGcKCPPGG---GCIMNPSAG-SSFGRKFSNCSQDDFEQFLLKQKGACLFNKP 199
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
550-602 5.95e-14

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


Pssm-ID: 214559  Cd Length: 53  Bit Score: 69.54  E-value: 5.95e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 537544566    550 WGPWTPWGDCSRTCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTDDCP 602
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
551-601 6.10e-07

Thrombospondin type 1 domain;


Pssm-ID: 306574  Cd Length: 49  Bit Score: 48.97  E-value: 6.10e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 537544566   551 GPWTPWGDCSRTCGGGVSSSSRHCDSPRPtiGGKYCLGERRRHRSCNTDDC 601
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIRVRQRTCKSPFP--GGEPCTGDAIETEACKMDKC 49
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
1069-1100 2.32e-06

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 312271  Cd Length: 31  Bit Score: 47.10  E-value: 2.32e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 537544566  1069 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTC 1100
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYKQFCCRSC 30
PHA02682 PHA02682
ORF080 virion core protein; Provisional
867-1005 2.87e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464  Cd Length: 280  Bit Score: 47.16  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  867 SAHSKLPKRQRACNTEPCPPDWVVG---NWSL--CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleAChg 941
Cdd:PHA02682   24 SLFTKCPQATIPAPAAPCPPDADVDpldKYSVkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP----AC-- 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537544566  942 PTCPPewAALDWSECTPSCGPGlrhrvvlCKSADHRATLPPAHCSPAAKPPATMRCNLRRCPPA 1005
Cdd:PHA02682   96 PACAP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
1010-1054 1.31e-03

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


Pssm-ID: 214559  Cd Length: 53  Bit Score: 39.49  E-value: 1.31e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 537544566   1010 GEWGECSAQCGVGQRQRSVRCTSHTGQAS-HECTEAL---RPPTTQQCE 1054
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEDvetRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
952-1003 8.99e-03

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


Pssm-ID: 214559  Cd Length: 53  Bit Score: 36.80  E-value: 8.99e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 537544566    952 DWSECTPSCGPGLRHRVVLCKsaDHRATLPPAHCSPAAkpPATMRCNLRRCP 1003
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSCC--SPPPQNGGGPCTGED--VETRACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
239-454 4.71e-107

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: 336.52  E-value: 4.71e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  239 RYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQ 318
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  319 KSIVNHSGhgnaipeNGVANHDTAVLITRYDICIYkNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTF 398
Cdd:cd04273    81 KKLNPPND-------SDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 537544566  399 GMNHDGVGNSCGARGQDPaKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLN 454
Cdd:cd04273   153 GMPHDGDGNSCGPEGKDG-HIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
239-446 2.06e-37

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: 141.40  E-value: 2.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  239 RYVETLVVADKMMVAYHgRRDVE---QYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFC 315
Cdd:cd04267     1 REIELVVVADHRMVSYF-NSDENilqAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  316 KWQKSivnhsghgnaipenGVANHDTAVLITRYDIciyknKPCGTLGLAPVGGMCERERSCSVNEDIGLA--TAFTIAHE 393
Cdd:cd04267    80 FWRAE--------------GPIRHDNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTllTALTMAHE 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 537544566  394 IGHTFGMNHDGVGNSCGARGQDPAKLMAAHITmKTNPFVWSSCSRDYITSFLD 446
Cdd:cd04267   141 LGHNLGAEHDGGDELAFECDGGGNYIMAPVDS-GLNSYRFSQCSIGSIREFLD 192
ADAM_spacer1 pfam05986
ADAM-TS Spacer 1; This family represents the Spacer-1 region from the ADAM-TS family of ...
706-818 1.46e-35

ADAM-TS Spacer 1; This family represents the Spacer-1 region from the ADAM-TS family of metalloproteinases.


Pssm-ID: 310520  Cd Length: 114  Bit Score: 133.51  E-value: 1.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   706 ETIEGVFSPASPGAGYEDVVWIPKGSVHIFIQDLNLSLSHLALK-GDQESLLLEGLPGTPQPHrLPLAGTTFQLRQGPDQ 784
Cdd:pfam05986    1 KTVKGTFTKALKSHGYNDVVTIPAGARHILIRELEASGNYLALKnADGEYYLNGNWTISWSGT-FEAAGTVFEYSRSDAA 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 537544566   785 VQSLEALGPINASLIVMVLARTE-LPALRYRFNAP 818
Cdd:pfam05986   80 PESLHATGPTNEPLTVQVLSQGAtNPGVRYEYFIP 114
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
40-180 2.25e-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: 307618  Cd Length: 125  Bit Score: 133.45  E-value: 2.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566    40 EIAFPTRVDHNGallafspppprRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAW--QRA 117
Cdd:pfam01562    1 EIVIPVRVDASG-----------RRRRSLSSEYPDRLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETYREDGTEVtdQPP 69
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 537544566   118 ARPHCLYAGHLQGQASSShVAISTCGGLHGLIVADEEEYLIEPLHGgpkgsrSPEESGPHVVY 180
Cdd:pfam01562   70 IQDHCHYQGHVEGEPDSS-AALSTCSGLRGVIRTGDEEYFIEPLES------SEEEGHPHVVY 125
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
239-455 3.41e-35

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


Pssm-ID: 239797  Cd Length: 194  Bit Score: 135.05  E-value: 3.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  239 RYVETLVVADKMMVAYHGRRD--VEQYVLAIMNIVAKLFQdsslgsTVNILVTrLILL---TEDQPtLEITHHAGKSLDS 313
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLskVRQRVIEIVNIVDSIYR------PLNIRVV-LVGLeiwTDKDK-ISVSGDAGETLNR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  314 FCKWQKSIVNHSghgnaIPengvanHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSVNEDIG---LATAFTI 390
Cdd:cd04269    73 FLDWKRSNLLPR-----KP------HDNAQLLT------GRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTM 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 537544566  391 AHEIGHTFGMNHDGVGNSCGARGQdpakLMAAHITmkTNPFVWSSCSRDYITSFLDSGLGLCLNN 455
Cdd:cd04269   136 AHELGHNLGMEHDDGGCTCGRSTC----IMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
239-457 8.19e-30

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


Pssm-ID: 307535  Cd Length: 199  Bit Score: 119.69  E-value: 8.19e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   239 RYVETLVVADKMMVAYHGRrDVE---QYVLAIMNIVAKLFQdsSLGSTVnILVTRLILLTEDQptLEITHHAGKSLDSFC 315
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGS-DVNvvrQRVFQVVNLVNSIYK--ELNIRV-VLVGLEIWTDEDK--IDVSGDANDTLRNFL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   316 KWQKSIVNHSghgnaipengvANHDTAVLITrydiciYKNKPCGTLGLAPVGGMCERERSCSVNED-----IGLATafTI 390
Cdd:pfam01421   75 KWRQEYLKKR-----------KPHDVAQLLS------GRTFGGTTVGAAYPGGMCSPSYSGGVNLDhkinvEGFAV--TM 135
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 537544566   391 AHEIGHTFGMNHDGVGN-SCGARGqdpAKLMAAHITmKTNPFVWSSCSRDYITSFLDSGLGLCLNNRP 457
Cdd:pfam01421  136 AHELGHNLGMTHDDITGcKCPPGG---GCIMNPSAG-SSFGRKFSNCSQDDFEQFLLKQKGACLFNKP 199
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
550-602 5.95e-14

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


Pssm-ID: 214559  Cd Length: 53  Bit Score: 69.54  E-value: 5.95e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 537544566    550 WGPWTPWGDCSRTCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTDDCP 602
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
240-453 3.93e-13

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 70.46  E-value: 3.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  240 YVETLVVADKMMVAYHGR-RDVEQYVLAIMNIVAKLFQDSSlGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSfckwQ 318
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRDLK-SPRIRLLLVGITISKDPDFEPYIHPINYGYIDA----A 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  319 KSIVNHSGHgnAIPENGVANHDTAVLITRYDICIYKNKPC--GTLGLAPVGGMCErERSCSVNEDigLATAF----TIAH 392
Cdd:cd04272    77 ETLENFNEY--VKKKRDYFNPDVVFLVTGLDMSTYSGGSLqtGTGGYAYVGGACT-ENRVAMGED--TPGSYygvyTMTH 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 537544566  393 EIGHTFGMNHDG---VGNSCGARG--QDPAK---LMaAHITMKTNPFVWSSCSRDYITSFLDSGLGLCL 453
Cdd:cd04272   152 ELAHLLGAPHDGsppPSWVKGHPGslDCPWDdgyIM-SYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
335-445 6.50e-13

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  Cd Length: 167  Bit Score: 69.09  E-value: 6.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  335 GVANHDTAVLITRYDiciyknKPCGTLGLAPVGGMCERERSCSVNED---IGLATAFTIAHEIGHTFGMNHDGVGNSC-- 409
Cdd:cd00203    48 EIDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDnqsGTKEGAQTIAHELGHALGFYHDHDRKDRdd 121
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 537544566  410 --------GARGQDPAKLMAAHIT--MKTNPFVWSSCSRDYITSFL 445
Cdd:cd00203   122 yptiddtlNAEDDDYYSVMSYTKGsfSDGQRKDFSQCDIDQINKLY 167
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
244-414 1.19e-10

Metallo-peptidase family M12;


Pssm-ID: 316230  Cd Length: 188  Bit Score: 62.41  E-value: 1.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   244 LVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSlgsTVNILVTRLILLTEDQPTleiTHHAGKSLDSfckwqKSIVN 323
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERNF---NISLGLVNLTITDYTDPY---TSSPTSSGNA-----SDLLN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   324 HSGHGNAipENGVANHDTAVLITrydiciykNKPCGTLGLAPVGGMCERERSCSVNEDIGLA-----TAFTIAHEIGHTF 398
Cdd:pfam13688   77 RFQSFSA--WRGTQNDDLAHLFL--------DTNCSGGGLAWLGQLCNSGSAGSVSTSVNVVvgtatEWQVFAHEIGHNF 146
                          170       180
                   ....*....|....*....|....*..
gi 537544566   399 GMNHD-----------GVGNSCGARGQ 414
Cdd:pfam13688  147 GAVHDcdssttsqccpPSSSTCPAGGR 173
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
359-445 3.02e-09

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


Pssm-ID: 316130  Cd Length: 192  Bit Score: 58.02  E-value: 3.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   359 GTLGLAPVGGMCERERSCsVNEDIGLATAFT-------------IAHEIGHTFGMNHDGVG--------NSCGARGQDPA 417
Cdd:pfam13574   84 GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsanyptqewdvVAHEVGHNFGATHDCDGsqyassgcERNAATSVCSA 162
                           90       100       110
                   ....*....|....*....|....*....|.
gi 537544566   418 K---LMAAhiTMKTNPFVWSSCSRDYITSFL 445
Cdd:pfam13574  163 NgsfIMNP--ASKSNNDLFSPCSISLICDVL 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
337-403 2.34e-08

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


Pssm-ID: 316138  Cd Length: 122  Bit Score: 54.66  E-value: 2.34e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   337 ANHDTAVLITRYDiciyknkPCGTLGLAPVGGMCERERSCSVNEDI---GLATAFTIAHEIGHTFGMNHD 403
Cdd:pfam13582   60 YGYDLGHLFTGRD-------VGGGGGLAYVGSVCNSGSKAGVNGGSspyGDCGVDTFAHEIGHNFGANHT 122
TSP_1 pfam00090
Thrombospondin type 1 domain;
551-601 6.10e-07

Thrombospondin type 1 domain;


Pssm-ID: 306574  Cd Length: 49  Bit Score: 48.97  E-value: 6.10e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 537544566   551 GPWTPWGDCSRTCGGGVSSSSRHCDSPRPtiGGKYCLGERRRHRSCNTDDC 601
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIRVRQRTCKSPFP--GGEPCTGDAIETEACKMDKC 49
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
1069-1100 2.32e-06

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 312271  Cd Length: 31  Bit Score: 47.10  E-value: 2.32e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 537544566  1069 CKDvnKVAYCPLVLKFQFCSRAYFRQMCCKTC 1100
Cdd:pfam08686    1 CKD--KFANCSLVVQARLCSHKYYKQFCCRSC 30
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
359-452 6.50e-06

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


Pssm-ID: 239798  Cd Length: 244  Bit Score: 48.52  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  359 GTLGLAPV--------GGMCERERSCSVNEDI----GLATAF-------------TIAHEIGHTFGMNHDGVGNSCGARG 413
Cdd:cd04270   115 GTLGLAYVgsprdnsaGGICEKAYYYSNGKKKylntGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECAPGE 194
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 537544566  414 QDPAK-LMAAHITM--KTNPFVWSSCSRDYITSFLDSGLGLC 452
Cdd:cd04270   195 SQGGNyIMYARATSgdKENNKKFSPCSKKSISKVLEVKSNSC 236
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
239-441 2.84e-05

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


Pssm-ID: 316139  Cd Length: 203  Bit Score: 46.07  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   239 RYVETLVVADKMMVAYHGRRD-VEQYVLAIMNIVAKLFQdSSLGSTVNILVTRLILLTEDQPTLEITHHAGK-----SLD 312
Cdd:pfam13583    3 RVYRVAVATDCTYSASFTSVDeLRANINATVTTANEVYG-RDFNVSLALISDRDVIYTDSSTDSFNADCSGGdlgnwRLA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566   313 SFCKWQksivnhsghgnaipenGVANHDTAVLITRYdiciykNKPCGTLGLAPVGGMCERERSCSVNEDI--GLATAFTI 390
Cdd:pfam13583   82 TLTSWR----------------DSLNYDLAYLTLMT------RPSQNEVGVAWVGALCSSAYQNAKANGVarSRDEWDIF 139
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 537544566   391 AHEIGHTFGMNHDGVGNSCGARGQ-DPAK---LMA-AHITMKTNpfvWSSCSRDYI 441
Cdd:pfam13583  140 AHEIGHTFGAVHDCSSQGEGLSSStEDGSgqtIMSyASTASQTA---FSPCTIRNI 192
PHA02682 PHA02682
ORF080 virion core protein; Provisional
867-1005 2.87e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464  Cd Length: 280  Bit Score: 47.16  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537544566  867 SAHSKLPKRQRACNTEPCPPDWVVG---NWSL--CSRSCDAGVRSRSVvCQRRVSAAEEKAlDDSACPQPRPpvleAChg 941
Cdd:PHA02682   24 SLFTKCPQATIPAPAAPCPPDADVDpldKYSVkeAGRYYQSRLKANSA-CMQRPSGQSPLA-PSPACAAPAP----AC-- 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 537544566  942 PTCPPewAALDWSECTPSCGPGlrhrvvlCKSADHRATLPPAHCSPAAKPPATMRCNLRRCPPA 1005
Cdd:PHA02682   96 PACAP--AAPAPAVTCPAPAPA-------CPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPA 150
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
1010-1054 1.31e-03

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


Pssm-ID: 214559  Cd Length: 53  Bit Score: 39.49  E-value: 1.31e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 537544566   1010 GEWGECSAQCGVGQRQRSVRCTSHTGQAS-HECTEAL---RPPTTQQCE 1054
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGgGPCTGEDvetRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
952-1003 8.99e-03

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


Pssm-ID: 214559  Cd Length: 53  Bit Score: 36.80  E-value: 8.99e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 537544566    952 DWSECTPSCGPGLRHRVVLCKsaDHRATLPPAHCSPAAkpPATMRCNLRRCP 1003
Cdd:smart00209    6 EWSPCSVTCGGGVQTRTRSCC--SPPPQNGGGPCTGED--VETRACNEQPCP 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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