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Conserved domains on  [gi|442624584|ref|NP_001261158|]
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sol narae, isoform F [Drosophila melanogaster]

Protein Classification

Graphical summary

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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 ...
 313-541 1.06e-81

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


:

Pssm-ID: 239800  Cd Length: 220  Bit Score: 256.89  E-value: 1.06e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 313 IYPEVLVIVDYDGYRlHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIIISRGRDATPYLERNrvGRDAIDSAA 392
Cdd:cd04272    1 VYPELFVVVDYDHQS-EFFSNEQLIRYLAVMVNAANLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPI--NYGYIDAAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 393 ALTDMGKYLFRERRLPVYDIAVAITKYDMcRRRKGGRCTKGTAGFAYVGGACVVNkrlekvnSVAIIEDTGG-FSGIIVA 471
Cdd:cd04272   78 TLENFNEYVKKKRDYFNPDVVFLVTGLDM-STYSGGSLQTGTGGYAYVGGACTEN-------RVAMGEDTPGsYYGVYTM 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442624584 472 AHEVGHLLGAVHDGSPPPSYLGG-PGAQRCRWEDGYIMSDLRHTERGFRWSACTVQSFHHFLNGDTATCLH 541
Cdd:cd04272  150 THELAHLLGAPHDGSPPPSWVKGhPGSLDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCLH 220
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 555-618 2.86e-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: 82.01  E-value: 2.86e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624584  555 PGTLLSLDAQCRRDRGTYACF---KDERVCAQLFCFDAQTGYCV-AYRPAAEGSACGNGYHCLDGRCT 618
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 ...
 313-541 1.06e-81

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 256.89  E-value: 1.06e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 313 IYPEVLVIVDYDGYRlHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIIISRGRDATPYLERNrvGRDAIDSAA 392
Cdd:cd04272    1 VYPELFVVVDYDHQS-EFFSNEQLIRYLAVMVNAANLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPI--NYGYIDAAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 393 ALTDMGKYLFRERRLPVYDIAVAITKYDMcRRRKGGRCTKGTAGFAYVGGACVVNkrlekvnSVAIIEDTGG-FSGIIVA 471
Cdd:cd04272   78 TLENFNEYVKKKRDYFNPDVVFLVTGLDM-STYSGGSLQTGTGGYAYVGGACTEN-------RVAMGEDTPGsYYGVYTM 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442624584 472 AHEVGHLLGAVHDGSPPPSYLGG-PGAQRCRWEDGYIMSDLRHTERGFRWSACTVQSFHHFLNGDTATCLH 541
Cdd:cd04272  150 THELAHLLGAPHDGSPPPSWVKGhPGSLDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCLH 220
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 555-618 2.86e-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: 82.01  E-value: 2.86e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624584  555 PGTLLSLDAQCRRDRGTYACF---KDERVCAQLFCFDAQTGYCV-AYRPAAEGSACGNGYHCLDGRCT 618
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFcpnGDEDVCSKLWCSNPGGSTCTtKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 375-484 5.02e-13

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: 66.24  E-value: 5.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584  375 TPYLERNrvGRDAIDSAAALTDMgkylfrERRLPVYDIAVAITKYDmcrrrkggrcTKGTAGFAYVGGACVVNKRlekvn 454
Cdd:pfam13582  35 TPYTSSD--ALEILDELQEVNDT------RIGQYGYDLGHLFTGRD----------GGGGGGIAYVGGVCNSGSK----- 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 442624584  455 sVAIIEDTG--GFSGIIVAAHEVGHLLGAVHD 484
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 ...
 313-541 1.06e-81

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 256.89  E-value: 1.06e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 313 IYPEVLVIVDYDGYRlHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIIISRGRDATPYLERNrvGRDAIDSAA 392
Cdd:cd04272    1 VYPELFVVVDYDHQS-EFFSNEQLIRYLAVMVNAANLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPI--NYGYIDAAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 393 ALTDMGKYLFRERRLPVYDIAVAITKYDMcRRRKGGRCTKGTAGFAYVGGACVVNkrlekvnSVAIIEDTGG-FSGIIVA 471
Cdd:cd04272   78 TLENFNEYVKKKRDYFNPDVVFLVTGLDM-STYSGGSLQTGTGGYAYVGGACTEN-------RVAMGEDTPGsYYGVYTM 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442624584 472 AHEVGHLLGAVHDGSPPPSYLGG-PGAQRCRWEDGYIMSDLRHTERGFRWSACTVQSFHHFLNGDTATCLH 541
Cdd:cd04272  150 THELAHLLGAPHDGSPPPSWVKGhPGSLDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCLH 220
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 316-541 5.08e-24

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: 100.39  E-value: 5.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 316 EVLVIVDYDGYRLHGGDNLQvkRYFISFWNGVDLRYR----------------LLKGPririsiaGIIISRGRDATPYLE 379
Cdd:cd04273    4 ETLVVADSKMVEFHHGEDLE--HYILTLMNIVASLYKdpslgnsinivvvrliVLEDE-------ESGLLISGNAQKSLK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 380 R-NRVGRDAIDSAAAltDMGKylfrerrlpvYDIAVAITKYDMCRRRKggrcTKGTAGFAYVGGACvvnkrlEKVNSVAI 458
Cdd:cd04273   75 SfCRWQKKLNPPNDS--DPEH----------HDHAILLTRQDICRSNG----NCDTLGLAPVGGMC------SPSRSCSI 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 459 IEDTgGFSGIIVAAHEVGHLLGAVHDGSPPpsylggpgaqRC--RWEDGYIMS-DLRHTERGFRWSACTVQSFHHFLNGD 535
Cdd:cd04273  133 NEDT-GLSSAFTIAHELGHVLGMPHDGDGN----------SCgpEGKDGHIMSpTLGANTGPFTWSKCSRRYLTSFLDTG 201


                 ....*.
gi 442624584 536 TATCLH 541
Cdd:cd04273  202 DGNCLL 207
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 555-618 2.86e-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: 82.01  E-value: 2.86e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624584  555 PGTLLSLDAQCRRDRGTYACF---KDERVCAQLFCFDAQTGYCV-AYRPAAEGSACGNGYHCLDGRCT 618
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFcpnGDEDVCSKLWCSNPGGSTCTtKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 314-533 1.27e-16

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: 78.62  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 314 YPEVLVIVDYDGYRLHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIiisrgrdatpyLERNRvGRDAIDSAAA 393
Cdd:cd04267    2 EIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLRLGIRISLEG-----------LQILK-GEQFAPPIDS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 394 LTDMGKYLF---RERRLPVYDIAVAITKYDMCRrrkggrctKGTAGFAYVGGACvvnkrlEKVNSVAIIEDTGG-FSGII 469
Cdd:cd04267   70 DASNTLNSFsfwRAEGPIRHDNAVLLTAQDFIE--------GDILGLAYVGSMC------NPYSSVGVVEDTGFtLLTAL 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442624584 470 VAAHEVGHLLGAVHDGspppsylGGPGAQRCRWEDGYIMSDLRHTERGFRWSACTVQSFHHFLN 533
Cdd:cd04267  136 TMAHELGHNLGAEHDG-------GDELAFECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 375-484 5.02e-13

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: 66.24  E-value: 5.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584  375 TPYLERNrvGRDAIDSAAALTDMgkylfrERRLPVYDIAVAITKYDmcrrrkggrcTKGTAGFAYVGGACVVNKRlekvn 454
Cdd:pfam13582  35 TPYTSSD--ALEILDELQEVNDT------RIGQYGYDLGHLFTGRD----------GGGGGGIAYVGGVCNSGSK----- 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 442624584  455 sVAIIEDTG--GFSGIIVAAHEVGHLLGAVHD 484
Cdd:pfam13582  92 -FGVNSGSGpvGDTGADTFAHEIGHNFGLNHT 122
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 314-542 1.61e-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: 60.71  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 314 YPEVLVIVDYDGYRLHGGDNLQVKRYFISFWNGVDLRYR------LLKGpririsiagiiisrgrdatpyLE----RN-- 381
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRplnirvVLVG---------------------LEiwtdKDki 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 382 RVGRDAIDSAAALTDMGKYLFRERRlpVYDIAVAITKYDMcrrrkggrcTKGTAGFAYVGGACVVNkrlekvNSVAIIED 461
Cdd:cd04269   61 SVSGDAGETLNRFLDWKRSNLLPRK--PHDNAQLLTGRDF---------DGNTVGLAYVGGMCSPK------YSGGVVQD 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 462 ----TGGFSGIIvaAHEVGHLLGAVHDGSPPpsylggpgaqRCRwEDGYIMSdlRHTERG-FRWSACTVQSFHHFLNGDT 536
Cdd:cd04269  124 hsrnLLLFAVTM--AHELGHNLGMEHDDGGC----------TCG-RSTCIMA--PSPSSLtDAFSNCSYEDYQKFLSRGG 188


                 ....*.
gi 442624584 537 ATCLHN 542
Cdd:cd04269  189 GQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 434-544 4.00e-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: 4.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584  434 TAGFAYVGGACvvnkrlEKVNSVAIIED----TGGFSGIIvaAHEVGHLLGAVHDGSPPPSYlggpgaqrCRWEDGYIMS 509
Cdd:pfam01421 102 TVGAAYVGGMC------SLEYSGGVNEDhsknLESFAVTM--AHELGHNLGMQHDDFNGGCK--------CPPGGGCIMN 165

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 442624584  510 DLRHTERGFRWSACTVQSFHHFLNGDTATCLHNAP 544
Cdd:pfam01421 166 PSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 405-509 6.61e-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: 6.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584  405 RRLPVYDIAVAITKYDMCRRRKGGRCTKGTAGFAYVGGACvvNKRLEKVNSVAIIEDTGGFSG-------IIVAAHEVGH 477
Cdd:pfam13574  57 RRLNFLSQWRGEQDYCLAHLVTMGTFSGGELGLAYVGQIC--QKGASSPKTNTGLSTTTNYGSfnyptqeWDVVAHEVGH 134

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 442624584  478 LLGAVHDgsPPPSYLGGPGAQRC---RWEDG---YIMS 509
Cdd:pfam13574 135 NFGATHD--CDGSQYASSGCERNaatSVCSAngsFIMN 170
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 387-535 3.61e-07

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 51.08  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584  387 AIDSAAALTDMGKYLFRERRLPV-YDIAVAITKYdmcrrrkggRCTKGTAGFAYVGGACVVNKRLEKVNSVAIIEDtgGF 465
Cdd:pfam13583  68 ADCSGGDLGNWRLATLTSWRDSLnYDLAYLTLMT---------GPSGQNVGVAWVGALCSSARQNAKASGVARSRD--EW 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442624584  466 SgiiVAAHEVGHLLGAVHD---GSPPPSYlggpgaQRCRWEDGYIMSdLRHTERGFRWSACTVQSFHHFLNGD 535
Cdd:pfam13583 137 D---IFAHEIGHTFGAVHDcssQGEGLSS------STEDGSGQTIMS-YASTASQTAFSPCTIRNINGNPCSQ 199
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 425-532 1.27e-06

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: 48.67  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584 425 RKGGRCTKGTAGFAYVGGACvvnkrlEKVNSVAIIEDT--GGFSGIIVAAHEVGHLLGAVHDGSP-----PPSYLGGPGA 497
Cdd:cd00203   58 VTRQDFDGGTGGWAYLGRVC------DSLRGVGVLQDNqsGTKEGAQTIAHELGHALGFYHDHDRkdrddYPTIDDTLNA 131

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 442624584 498 qrCRWEDGYIMS--DLRHT-ERGFRWSACTVQSFHHFL 532
Cdd:cd00203  132 --EDDDYYSVMSytKGSFSdGQRKDFSQCDIDQINKLY 167
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
433-509 5.71e-06

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 47.41  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624584  433 GTAGFAYVGGAC------VVNKRLEKVNSVAiiedtGGFSGIIVAAHEVGHLLGAVHD--------GSPPPSYLGGPGAQ 498
Cdd:pfam13688 102 SGGGLAWLGQLCnsgsagSVSTRVSGNNVVV-----STATEWQVFAHEIGHNFGAVHDcdsstssqCCPPSNSTCPAGGR 176

                          90
                  ....*....|.
gi 442624584  499 rcrwedgYIMS 509
Cdd:pfam13688 177 -------YIMN 180
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 470-540 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 442624584 470 VAAHEVGHLLGAVHDGSPPPSYLGGPGAQR--------CRWEDGYIMSDlrHTERGF-RWSACTVQSFHHFL--NGDTAT 538
Cdd:cd04271  148 VFAHEIGHTFGAVHDCTSGTCSDGSVGSQQccplststCDANGQYIMNP--SSSSGItEFSPCTIGNICSLLgrNPVRTS 225


                 ..
gi 442624584 539 CL 540
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.
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