NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|78707567|ref|NP_611827|]
View 

sol narae, isoform A [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 313-542 7.58e-83

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


:

Pssm-ID: 239800  Cd Length: 220  Bit Score: 259.98  E-value: 7.58e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 313 IYPEVLVIVDYDGYRlHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIIISRGRDATPYLERNrvGRDAIDSAA 392
Cdd:cd04272   1 VYPELFVVVDYDHQS-EFFSNEQLIRYLAVMVNAANLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPI--NYGYIDAAE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 393 ALTDMGKYLFRERRLPVYDIAVAITKLDMcrRTSAYGECNRGTAGFAYVGGACVVNkrlekvnSVAIIEDTGG-FSGIIV 471
Cdd:cd04272  78 TLENFNEYVKKKRDYFNPDVVFLVTGLDM--STYSGGSLQTGTGGYAYVGGACTEN-------RVAMGEDTPGsYYGVYT 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78707567 472 AAHEVGHLLGAVHDGSPPPSYLGG-PGAQRCRWEDGYIMSDLRHTERGFRWSACTVQSFHHFLNGDTATCLH 542
Cdd:cd04272 149 MTHELAHLLGAPHDGSPPPSWVKGhPGSLDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCLH 220
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 556-619 2.29e-19

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: 82.39  E-value: 2.29e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78707567   556 PGTLLSLDAQCRRDRGTYACF---KDERVCAQLFCFDAQTGYCV-AYRPAAEGSACGNGYHCLDGRCT 619
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFcpnGDEDVCSKLWCSNPGGSTCTtKNLPAADGTPCGNKKWCLNGKCV 68
 
Name Accession Description Interval E-value
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 313-542 7.58e-83

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 259.98  E-value: 7.58e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 313 IYPEVLVIVDYDGYRlHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIIISRGRDATPYLERNrvGRDAIDSAA 392
Cdd:cd04272   1 VYPELFVVVDYDHQS-EFFSNEQLIRYLAVMVNAANLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPI--NYGYIDAAE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 393 ALTDMGKYLFRERRLPVYDIAVAITKLDMcrRTSAYGECNRGTAGFAYVGGACVVNkrlekvnSVAIIEDTGG-FSGIIV 471
Cdd:cd04272  78 TLENFNEYVKKKRDYFNPDVVFLVTGLDM--STYSGGSLQTGTGGYAYVGGACTEN-------RVAMGEDTPGsYYGVYT 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78707567 472 AAHEVGHLLGAVHDGSPPPSYLGG-PGAQRCRWEDGYIMSDLRHTERGFRWSACTVQSFHHFLNGDTATCLH 542
Cdd:cd04272 149 MTHELAHLLGAPHDGSPPPSWVKGhPGSLDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCLH 220
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 556-619 2.29e-19

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: 82.39  E-value: 2.29e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78707567   556 PGTLLSLDAQCRRDRGTYACF---KDERVCAQLFCFDAQTGYCV-AYRPAAEGSACGNGYHCLDGRCT 619
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFcpnGDEDVCSKLWCSNPGGSTCTtKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 375-485 3.43e-14

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: 69.32  E-value: 3.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567   375 TPYLERNrvGRDAIDSAAALTDMgkylfrERRLPVYDIAVAITKLDmcrrtsaygecNRGTAGFAYVGGACVVNKRlekv 454
Cdd:pfam13582  35 TPYTSSD--ALEILDELQEVNDT------RIGQYGYDLGHLFTGRD-----------GGGGGGIAYVGGVCNSGSK---- 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 78707567   455 nsVAIIEDTG--GFSGIIVAAHEVGHLLGAVHD 485
Cdd:pfam13582  92 --FGVNSGSGpvGDTGADTFAHEIGHNFGLNHT 122
 
Name Accession Description Interval E-value
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 313-542 7.58e-83

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 259.98  E-value: 7.58e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 313 IYPEVLVIVDYDGYRlHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIIISRGRDATPYLERNrvGRDAIDSAA 392
Cdd:cd04272   1 VYPELFVVVDYDHQS-EFFSNEQLIRYLAVMVNAANLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPI--NYGYIDAAE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 393 ALTDMGKYLFRERRLPVYDIAVAITKLDMcrRTSAYGECNRGTAGFAYVGGACVVNkrlekvnSVAIIEDTGG-FSGIIV 471
Cdd:cd04272  78 TLENFNEYVKKKRDYFNPDVVFLVTGLDM--STYSGGSLQTGTGGYAYVGGACTEN-------RVAMGEDTPGsYYGVYT 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78707567 472 AAHEVGHLLGAVHDGSPPPSYLGG-PGAQRCRWEDGYIMSDLRHTERGFRWSACTVQSFHHFLNGDTATCLH 542
Cdd:cd04272 149 MTHELAHLLGAPHDGSPPPSWVKGhPGSLDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCLH 220
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 316-542 2.96e-23

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: 98.08  E-value: 2.96e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 316 EVLVIVDYDGYRLHGGDNLQvkRYFISFWNGVDLRYR----------------LLKGPririsiaGIIISRGRDATPYLE 379
Cdd:cd04273   4 ETLVVADSKMVEFHHGEDLE--HYILTLMNIVASLYKdpslgnsinivvvrliVLEDE-------ESGLLISGNAQKSLK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 380 R-NRVGRDAIDSAAAltDMGKylfrerrlpvYDIAVAITKLDMCRRTSaygecNRGTAGFAYVGGACvvnkrlEKVNSVA 458
Cdd:cd04273  75 SfCRWQKKLNPPNDS--DPEH----------HDHAILLTRQDICRSNG-----NCDTLGLAPVGGMC------SPSRSCS 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 459 IIEDTgGFSGIIVAAHEVGHLLGAVHDGSPPpsylggpgaqRC--RWEDGYIMS-DLRHTERGFRWSACTVQSFHHFLNG 535
Cdd:cd04273 132 INEDT-GLSSAFTIAHELGHVLGMPHDGDGN----------SCgpEGKDGHIMSpTLGANTGPFTWSKCSRRYLTSFLDT 200


                ....*..
gi 78707567 536 DTATCLH 542
Cdd:cd04273 201 GDGNCLL 207
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 556-619 2.29e-19

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: 82.39  E-value: 2.29e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78707567   556 PGTLLSLDAQCRRDRGTYACF---KDERVCAQLFCFDAQTGYCV-AYRPAAEGSACGNGYHCLDGRCT 619
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFcpnGDEDVCSKLWCSNPGGSTCTtKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 314-534 9.39e-17

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: 79.00  E-value: 9.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 314 YPEVLVIVDYDGYRLHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIiisrgrdatpyLERNRvGRDAIDSAAA 393
Cdd:cd04267   2 EIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLRLGIRISLEG-----------LQILK-GEQFAPPIDS 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 394 LTDMGKYLF---RERRLPVYDIAVAITKLDMCrrtsaygecNRGTAGFAYVGGACvvnkrlEKVNSVAIIEDTGG-FSGI 469
Cdd:cd04267  70 DASNTLNSFsfwRAEGPIRHDNAVLLTAQDFI---------EGDILGLAYVGSMC------NPYSSVGVVEDTGFtLLTA 134

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78707567 470 IVAAHEVGHLLGAVHDGspppsylGGPGAQRCRWEDGYIMSDLRHTERGFRWSACTVQSFHHFLN 534
Cdd:cd04267 135 LTMAHELGHNLGAEHDG-------GDELAFECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 375-485 3.43e-14

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: 69.32  E-value: 3.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567   375 TPYLERNrvGRDAIDSAAALTDMgkylfrERRLPVYDIAVAITKLDmcrrtsaygecNRGTAGFAYVGGACVVNKRlekv 454
Cdd:pfam13582  35 TPYTSSD--ALEILDELQEVNDT------RIGQYGYDLGHLFTGRD-----------GGGGGGIAYVGGVCNSGSK---- 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 78707567   455 nsVAIIEDTG--GFSGIIVAAHEVGHLLGAVHD 485
Cdd:pfam13582  92 --FGVNSGSGpvGDTGADTFAHEIGHNFGLNHT 122
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 314-543 4.29e-10

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: 59.55  E-value: 4.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 314 YPEVLVIVDYDGYRLHGGDNLQVKRYFISFWNGVDLRYR------LLKGpririsiagiiisrgrdatpyLE----RN-- 381
Cdd:cd04269   2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRplnirvVLVG---------------------LEiwtdKDki 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 382 RVGRDAIDSAAALTDMGKYLFRERRlpVYDIAVAITKLDMcrrtsaygecNRGTAGFAYVGGACVVNkrlekvNSVAIIE 461
Cdd:cd04269  61 SVSGDAGETLNRFLDWKRSNLLPRK--PHDNAQLLTGRDF----------DGNTVGLAYVGGMCSPK------YSGGVVQ 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 462 D----TGGFSGIIvaAHEVGHLLGAVHDGSPPpsylggpgaqRCRwEDGYIMSdlRHTERG-FRWSACTVQSFHHFLNGD 536
Cdd:cd04269 123 DhsrnLLLFAVTM--AHELGHNLGMEHDDGGC----------TCG-RSTCIMA--PSPSSLtDAFSNCSYEDYQKFLSRG 187


                ....*..
gi 78707567 537 TATCLHN 543
Cdd:cd04269 188 GGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 435-545 4.17e-09

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: 56.93  E-value: 4.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567   435 TAGFAYVGGACvvnkrlEKVNSVAIIED----TGGFSGIIvaAHEVGHLLGAVHDGSPPPSYlggpgaqrCRWEDGYIMS 510
Cdd:pfam01421 102 TVGAAYVGGMC------SLEYSGGVNEDhsknLESFAVTM--AHELGHNLGMQHDDFNGGCK--------CPPGGGCIMN 165

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 78707567   511 DLRHTERGFRWSACTVQSFHHFLNGDTATCLHNAP 545
Cdd:pfam01421 166 PSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 429-510 1.83e-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: 372637  Cd Length: 193  Bit Score: 51.86  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567   429 GECNRGTAGFAYVGGACvvNKRLEKVNSVAIIEDTGGFSG-------IIVAAHEVGHLLGAVHDgsPPPSYLGGPGAQRC 501
Cdd:pfam13574  80 GTFSGGELGLAYVGQIC--QKGASSPKTNTGLSTTTNYGSfnyptqeWDVVAHEVGHNFGATHD--CDGSQYASSGCERN 155

                          90
                  ....*....|....*
gi 78707567   502 ---RWEDG---YIMS 510
Cdd:pfam13574 156 aatSVCSAngsFIMN 170
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 428-533 7.82e-07

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: 49.44  E-value: 7.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 428 YGECNRGTAGFAYVGGACvvnkrlEKVNSVAIIEDT--GGFSGIIVAAHEVGHLLGAVHDGSP-----PPSYLGGPGAqr 500
Cdd:cd00203  60 RQDFDGGTGGWAYLGRVC------DSLRGVGVLQDNqsGTKEGAQTIAHELGHALGFYHDHDRkdrddYPTIDDTLNA-- 131

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 78707567 501 CRWEDGYIMS--DLRHT-ERGFRWSACTVQSFHHFL 533
Cdd:cd00203 132 EDDDYYSVMSytKGSFSdGQRKDFSQCDIDQINKLY 167
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 387-536 1.82e-06

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 49.15  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567   387 AIDSAAALTDMGKYLFRERRLPV-YDIAVAITKldmcrrtsaYGEcNRGTAGFAYVGGACVVNKRLEKVNSVAIIEDtgG 465
Cdd:pfam13583  68 ADCSGGDLGNWRLATLTSWRDSLnYDLAYLTLM---------TGP-SGQNVGVAWVGALCSSARQNAKASGVARSRD--E 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78707567   466 FSgiiVAAHEVGHLLGAVHD---GSPPPSYlggpgaQRCRWEDGYIMSdLRHTERGFRWSACTVQSFHHFLNGD 536
Cdd:pfam13583 136 WD---IFAHEIGHTFGAVHDcssQGEGLSS------STEDGSGQTIMS-YASTASQTAFSPCTIRNINGNPCSQ 199
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
431-510 4.32e-06

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 47.80  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567   431 CNRGTAGFAYVGGAC------VVNKRLEKVNSVAiiedtGGFSGIIVAAHEVGHLLGAVHD--------GSPPPSYLGGP 496
Cdd:pfam13688  99 TNCSGGGLAWLGQLCnsgsagSVSTRVSGNNVVV-----STATEWQVFAHEIGHNFGAVHDcdsstssqCCPPSNSTCPA 173

                          90
                  ....*....|....
gi 78707567   497 GAQrcrwedgYIMS 510
Cdd:pfam13688 174 GGR-------YIMN 180
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 471-541 1.93e-03

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: 40.10  E-value: 1.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707567 471 VAAHEVGHLLGAVHDGSPPPSYLGGPGAQR--------CRWEDGYIMSDlrHTERGF-RWSACTVQSFHHFL--NGDTAT 539
Cdd:cd04271 148 VFAHEIGHTFGAVHDCTSGTCSDGSVGSQQccplststCDANGQYIMNP--SSSSGItEFSPCTIGNICSLLgrNPVRTS 225


                ..
gi 78707567 540 CL 541
Cdd:cd04271 226 CL 227
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH