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Conserved domains on  [gi|308262848|gb|EFP06801|]
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CRE-MIG-17 protein [Caenorhabditis remanei]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
135-346 2.89e-59

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: 193.79  E-value: 2.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 135 EDEEERVLNEEIRRLEEDESRWNSTVEDEEFMNTTALDSNSTEqlissserrkkLRKFVDVTLEEMQENNSTEMALKMDS 214
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTN-----------LRLGIRISLEGLQILKGEQFAPPIDS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 215 KKGVDKFTIWLKEQQGLPRHEHAVLITKFDLIsingNSATQGMAYVGNICENGDSSSVVEDIG-AGLTSLIVAHEIGHSL 293
Cdd:cd04267   70 DASNTLNSFSFWRAEGPIRHDNAVLLTAQDFI----EGDILGLAYVGSMCNPYSSVGVVEDTGfTLLTALTMAHELGHNL 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308262848 294 GALHDGAYESA-DCDSNDNYLMAVAVSGsadrqsfLNSRKMSNCSINSIIENLK 346
Cdd:cd04267  146 GAEHDGGDELAfECDGGGNYIMAPVDSG-------LNSYRFSQCSIGSIREFLD 192
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
373-445 1.77e-21

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: 87.79  E-value: 1.77e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308262848  373 PGETVNLARQCQIAFGPTFKPCLHIGyfhgQSICERIWCSDGDSDECQTlNYFPAFDGTDCGYNMWCIEGLCV 445
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGD----EDVCSKLWCSNPGGSTCTT-KNLPAADGTPCGNKKWCLNGKCV 68
 
Name Accession Description Interval E-value
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
135-346 2.89e-59

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: 193.79  E-value: 2.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 135 EDEEERVLNEEIRRLEEDESRWNSTVEDEEFMNTTALDSNSTEqlissserrkkLRKFVDVTLEEMQENNSTEMALKMDS 214
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTN-----------LRLGIRISLEGLQILKGEQFAPPIDS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 215 KKGVDKFTIWLKEQQGLPRHEHAVLITKFDLIsingNSATQGMAYVGNICENGDSSSVVEDIG-AGLTSLIVAHEIGHSL 293
Cdd:cd04267   70 DASNTLNSFSFWRAEGPIRHDNAVLLTAQDFI----EGDILGLAYVGSMCNPYSSVGVVEDTGfTLLTALTMAHELGHNL 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308262848 294 GALHDGAYESA-DCDSNDNYLMAVAVSGsadrqsfLNSRKMSNCSINSIIENLK 346
Cdd:cd04267  146 GAEHDGGDELAfECDGGGNYIMAPVDSG-------LNSYRFSQCSIGSIREFLD 192
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
373-445 1.77e-21

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: 87.79  E-value: 1.77e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308262848  373 PGETVNLARQCQIAFGPTFKPCLHIGyfhgQSICERIWCSDGDSDECQTlNYFPAFDGTDCGYNMWCIEGLCV 445
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGD----EDVCSKLWCSNPGGSTCTT-KNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
221-352 1.22e-11

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: 63.86  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848  221 FTIWLKEQ-QGLPRHEHAVLITKFDLisingNSATQGMAYVGNICENGDSSSVVED--IGAGLTSLIVAHEIGHSLGALH 297
Cdd:pfam01421  73 FLKWRQEYlKKRKPHDVAQLLSGVEF-----GGTTVGAAYVGGMCSLEYSGGVNEDhsKNLESFAVTMAHELGHNLGMQH 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 308262848  298 DGAYESADCDSNDNYLMAVAVSGSAdrqsflnSRKMSNCSINSIIENLKEPTASC 352
Cdd:pfam01421 148 DDFNGGCKCPPGGGCIMNPSAGSSF-------PRKFSNCSQEDFEQFLTKQKGAC 195
 
Name Accession Description Interval E-value
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
135-346 2.89e-59

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: 193.79  E-value: 2.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 135 EDEEERVLNEEIRRLEEDESRWNSTVEDEEFMNTTALDSNSTEqlissserrkkLRKFVDVTLEEMQENNSTEMALKMDS 214
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTN-----------LRLGIRISLEGLQILKGEQFAPPIDS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 215 KKGVDKFTIWLKEQQGLPRHEHAVLITKFDLIsingNSATQGMAYVGNICENGDSSSVVEDIG-AGLTSLIVAHEIGHSL 293
Cdd:cd04267   70 DASNTLNSFSFWRAEGPIRHDNAVLLTAQDFI----EGDILGLAYVGSMCNPYSSVGVVEDTGfTLLTALTMAHELGHNL 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308262848 294 GALHDGAYESA-DCDSNDNYLMAVAVSGsadrqsfLNSRKMSNCSINSIIENLK 346
Cdd:cd04267  146 GAEHDGGDELAfECDGGGNYIMAPVDSG-------LNSYRFSQCSIGSIREFLD 192
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
373-445 1.77e-21

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: 87.79  E-value: 1.77e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308262848  373 PGETVNLARQCQIAFGPTFKPCLHIGyfhgQSICERIWCSDGDSDECQTlNYFPAFDGTDCGYNMWCIEGLCV 445
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGD----EDVCSKLWCSNPGGSTCTT-KNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
213-353 4.47e-21

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: 91.15  E-value: 4.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 213 DSKKGVDKFTIWLKEQQ-----GLPRHEHAVLITKFDLISINGNSATQGMAYVGNICENGDSSSVVEDIGAGlTSLIVAH 287
Cdd:cd04273   68 NAQKSLKSFCRWQKKLNppndsDPEHHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLS-SAFTIAH 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 308262848 288 EIGHSLGALHDGAYESADCDSNDNYLMAVAVSGSADRQSFlnsrkmSNCSINSIIENLKEPTASCV 353
Cdd:cd04273  147 ELGHVLGMPHDGDGNSCGPEGKDGHIMSPTLGANTGPFTW------SKCSRRYLTSFLDTGDGNCL 206
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
212-352 1.67e-17

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 81.24  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 212 MDSKKGVDKFTIWLKEQQGLPRHEHAVLITKFDLISINGNSA---TQGMAYVGNICeNGDSSSVVEDIGAGLTSLIV-AH 287
Cdd:cd04272   73 IDAAETLENFNEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLqtgTGGYAYVGGAC-TENRVAMGEDTPGSYYGVYTmTH 151
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308262848 288 EIGHSLGALHDGA---------YESADCDSNDNYLMAVAVSGsadrqsfLNSRKMSNCSINSIIENLKEPTASC 352
Cdd:cd04272  152 ELAHLLGAPHDGSpppswvkghPGSLDCPWDDGYIMSYVVNG-------ERQYRFSQCSQRQIRNVFRRLGASC 218
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
233-352 3.92e-13

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: 68.03  E-value: 3.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 233 RHEHAVLITKfdlisINGNSATQGMAYVGNICENGDSSSVVEDIGAGLTSL--IVAHEIGHSLGALHDGAYesadCD-SN 309
Cdd:cd04269   86 PHDNAQLLTG-----RDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFavTMAHELGHNLGMEHDDGG----CTcGR 156
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 308262848 310 DNYLMAVAVSGSadrqsflnSRKMSNCSINSIIENLKEPTASC 352
Cdd:cd04269  157 STCIMAPSPSSL--------TDAFSNCSYEDYQKFLSRGGGQC 191
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
221-352 1.22e-11

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: 63.86  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848  221 FTIWLKEQ-QGLPRHEHAVLITKFDLisingNSATQGMAYVGNICENGDSSSVVED--IGAGLTSLIVAHEIGHSLGALH 297
Cdd:pfam01421  73 FLKWRQEYlKKRKPHDVAQLLSGVEF-----GGTTVGAAYVGGMCSLEYSGGVNEDhsKNLESFAVTMAHELGHNLGMQH 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 308262848  298 DGAYESADCDSNDNYLMAVAVSGSAdrqsflnSRKMSNCSINSIIENLKEPTASC 352
Cdd:pfam01421 148 DDFNGGCKCPPGGGCIMNPSAGSSF-------PRKFSNCSQEDFEQFLTKQKGAC 195
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
251-326 2.30e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.82  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848  251 NSATQGMAYVGNICENGDSSSVVED-------IGAGLTSLIVAHEIGHSLGALHDGAYESAD---------CDSNDNYLM 314
Cdd:pfam13688 100 NCSGGGLAWLGQLCNSGSAGSVSTRvsgnnvvVSTATEWQVFAHEIGHNFGAVHDCDSSTSSqccppsnstCPAGGRYIM 179
                          90
                  ....*....|..
gi 308262848  315 AVAVSGSADRQS 326
Cdd:pfam13688 180 NPSSSPNSTDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
245-298 2.97e-10

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: 57.77  E-value: 2.97e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 308262848  245 LISINGNSATQGMAYVGNICENGDSSSVVEDIGA-GLTSLI-VAHEIGHSLGALHD 298
Cdd:pfam13582  67 LFTGRDGGGGGGIAYVGGVCNSGSKFGVNSGSGPvGDTGADtFAHEIGHNFGLNHT 122
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
254-354 3.31e-10

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


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 60.47  E-value: 3.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 254 TQGMAYV--------GNICENGD--SSSVVEDIGAGLTS--------------LIVAHEIGHSLGALHDgaYESADC--- 306
Cdd:cd04270  116 TLGLAYVgsprdnsaGGICEKAYyySNGKKKYLNTGLTTtvnygkrvptkesdLVTAHELGHNFGSPHD--PDIAECapg 193
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 308262848 307 -DSNDNYLM-AVAVSGSADrqsflNSRKMSNCSINSIIENLKEPTASCVK 354
Cdd:cd04270  194 eSQGGNYIMyARATSGDKE-----NNKKFSPCSKKSISKVLEVKSNSCFV 238
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
241-341 2.83e-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: 55.99  E-value: 2.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 241 TKFDLISINGNSATQGMAYVGNICENGDSSSVVEDIGAG--LTSLIVAHEIGHSLGALHDGAYESAD-----------CD 307
Cdd:cd00203   54 IAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkEGAQTIAHELGHALGFYHDHDRKDRDdyptiddtlnaED 133
                         90       100       110
                 ....*....|....*....|....*....|....
gi 308262848 308 SNDNYLMavavSGSADRQSFLNSRKMSNCSINSI 341
Cdd:cd00203  134 DDYYSVM----SYTKGSFSDGQRKDFSQCDIDQI 163
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
253-341 5.41e-08

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: 53.02  E-value: 5.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848  253 ATQGMAYVGNICENGDSSS-----VVEDIGAGLTS------LIVAHEIGHSLGALHDGAYESAD------------CDSN 309
Cdd:pfam13574  85 GELGLAYVGQICQKGASSPktntgLSTTTNYGSFNyptqewDVVAHEVGHNFGATHDCDGSQYAssgcernaatsvCSAN 164
                          90       100       110
                  ....*....|....*....|....*....|..
gi 308262848  310 DNYLMAVAvSGSadrqsflNSRKMSNCSINSI 341
Cdd:pfam13574 165 GSFIMNPA-SKS-------NNDLFSPCSISLI 188
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
221-341 8.81e-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: 49.54  E-value: 8.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848  221 FTIWLKEQQglprHEHAVLITKFDLISINGnsatqGMAYVGNICENGDSS---SVVEDIGAGLTslIVAHEIGHSLGALH 297
Cdd:pfam13583  83 LTSWRDSLN----YDLAYLTLMTGPSGQNV-----GVAWVGALCSSARQNakaSGVARSRDEWD--IFAHEIGHTFGAVH 151
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 308262848  298 DGAYE-----SADCDSNDNYLMAVAvsgSADRQSFLnsrkmSNCSINSI 341
Cdd:pfam13583 152 DCSSQgeglsSSTEDGSGQTIMSYA---STASQTAF-----SPCTIRNI 192
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
256-347 7.08e-05

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: 44.33  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308262848 256 GMAYVGNICENGDS----SSVVEDIGAGLTS---LIVAHEIGHSLGALHD--------GAYESAD--------CDSNDNY 312
Cdd:cd04271  113 GVAWLGQLCRTGASdqgnETVAGTNVVVRTSnewQVFAHEIGHTFGAVHDctsgtcsdGSVGSQQccplststCDANGQY 192
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308262848 313 LMavAVSGSADRQSFlnsrkmSNCSINSIIENLKE 347
Cdd:cd04271  193 IM--NPSSSSGITEF------SPCTIGNICSLLGR 219
 
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.
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