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Conserved domains on  [gi|221468321|ref|NP_001137746|]
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sol narae, isoform C [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 ...
 313-542 2.20e-81

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


:

Pssm-ID: 239800  Cd Length: 220  Bit Score: 264.60  E-value: 2.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  313 IYPEVLVIVDYDGYRlHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIIISRGRDATPYLERNrvGRDAIDSAA 392
Cdd:cd04272     1 VYPELFVVVDYDHQS-EFFSNEQLIRYLAVMVNAANLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPI--NYGYIDAAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  393 ALTDMGKYLFRERRLPVYDIAVAITKLDMcrRTSAYGECNRGTAGFAYVGGACVVNkrlekvnSVAIIEDTGG-FSGIIV 471
Cdd:cd04272    78 TLENFNEYVKKKRDYFNPDVVFLVTGLDM--STYSGGSLQTGTGGYAYVGGACTEN-------RVAMGEDTPGsYYGVYT 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221468321  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 5.63e-20

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: 84.70  E-value: 5.63e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221468321   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 2.20e-81

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 264.60  E-value: 2.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  313 IYPEVLVIVDYDGYRlHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIIISRGRDATPYLERNrvGRDAIDSAA 392
Cdd:cd04272     1 VYPELFVVVDYDHQS-EFFSNEQLIRYLAVMVNAANLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPI--NYGYIDAAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  393 ALTDMGKYLFRERRLPVYDIAVAITKLDMcrRTSAYGECNRGTAGFAYVGGACVVNkrlekvnSVAIIEDTGG-FSGIIV 471
Cdd:cd04272    78 TLENFNEYVKKKRDYFNPDVVFLVTGLDM--STYSGGSLQTGTGGYAYVGGACTEN-------RVAMGEDTPGsYYGVYT 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221468321  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 5.63e-20

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: 84.70  E-value: 5.63e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221468321   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 1.39e-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: 71.25  E-value: 1.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321   375 TPYLERNrvGRDAIDSAAALTDMgkylfrERRLPVYDIAVAITKLDmcrrtsaygecNRGTAGFAYVGGACVVNKRlekv 454
Cdd:pfam13582   35 TPYTSSD--ALEILDELQEVNDT------RIGQYGYDLGHLFTGRD-----------GGGGGGIAYVGGVCNSGSK---- 91

                           90       100       110
                   ....*....|....*....|....*....|...
gi 221468321   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 2.20e-81

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 264.60  E-value: 2.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  313 IYPEVLVIVDYDGYRlHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIIISRGRDATPYLERNrvGRDAIDSAA 392
Cdd:cd04272     1 VYPELFVVVDYDHQS-EFFSNEQLIRYLAVMVNAANLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPI--NYGYIDAAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  393 ALTDMGKYLFRERRLPVYDIAVAITKLDMcrRTSAYGECNRGTAGFAYVGGACVVNkrlekvnSVAIIEDTGG-FSGIIV 471
Cdd:cd04272    78 TLENFNEYVKKKRDYFNPDVVFLVTGLDM--STYSGGSLQTGTGGYAYVGGACTEN-------RVAMGEDTPGsYYGVYT 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221468321  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 2.70e-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: 101.93  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  316 EVLVIVDYDGYRLHGGDNLQvkRYFISFWNGVDLRYR----------------LLKGPririsiaGIIISRGRDATPYLE 379
Cdd:cd04273     4 ETLVVADSKMVEFHHGEDLE--HYILTLMNIVASLYKdpslgnsinivvvrliVLEDE-------ESGLLISGNAQKSLK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  380 R-NRVGRDAIDSAAAltDMGKylfrerrlpvYDIAVAITKLDMCRRTSaygecNRGTAGFAYVGGACvvnkrlEKVNSVA 458
Cdd:cd04273    75 SfCRWQKKLNPPNDS--DPEH----------HDHAILLTRQDICRSNG-----NCDTLGLAPVGGMC------SPSRSCS 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  459 IIEDTgGFSGIIVAAHEVGHLLGAVHDGSPPpsylggpgaqRC--RWEDGYIMS-DLRHTERGFRWSACTVQSFHHFLNG 535
Cdd:cd04273   132 INEDT-GLSSAFTIAHELGHVLGMPHDGDGN----------SCgpEGKDGHIMSpTLGANTGPFTWSKCSRRYLTSFLDT 200


                  ....*..
gi 221468321  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 5.63e-20

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: 84.70  E-value: 5.63e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221468321   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 1.13e-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: 79.39  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  314 YPEVLVIVDYDGYRLHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIiisrgrdatpyLERNRvGRDAIDSAAA 393
Cdd:cd04267     2 EIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLRLGIRISLEG-----------LQILK-GEQFAPPIDS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  394 LTDMGKYLF---RERRLPVYDIAVAITKLDmcrrtsaYGECnrGTAGFAYVGGACvvnkrlEKVNSVAIIEDTGG-FSGI 469
Cdd:cd04267    70 DASNTLNSFsfwRAEGPIRHDNAVLLTAQD-------FIEG--DILGLAYVGSMC------NPYSSVGVVEDTGFtLLTA 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221468321  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 1.39e-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: 71.25  E-value: 1.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321   375 TPYLERNrvGRDAIDSAAALTDMgkylfrERRLPVYDIAVAITKLDmcrrtsaygecNRGTAGFAYVGGACVVNKRlekv 454
Cdd:pfam13582   35 TPYTSSD--ALEILDELQEVNDT------RIGQYGYDLGHLFTGRD-----------GGGGGGIAYVGGVCNSGSK---- 91

                           90       100       110
                   ....*....|....*....|....*....|...
gi 221468321   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 1.06e-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: 62.25  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  314 YPEVLVIVDYDGYRLHGGDNLQVKRYFISFWNGVDLRYR------LLKGpririsiagiiisrgrdatpyLE----RN-- 381
Cdd:cd04269     2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRplnirvVLVG---------------------LEiwtdKDki 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  382 RVGRDAIDSAAALTDMGKYLFRERRlpVYDIAVAITKLDMcrrtsaygecNRGTAGFAYVGGACVVNkrlekvNSVAIIE 461
Cdd:cd04269    61 SVSGDAGETLNRFLDWKRSNLLPRK--PHDNAQLLTGRDF----------DGNTVGLAYVGGMCSPK------YSGGVVQ 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  462 D----TGGFSGIIvaAHEVGHLLGAVHDGSPPpsylggpgaqRCRwEDGYIMSdlRHTERG-FRWSACTVQSFHHFLNGD 536
Cdd:cd04269   123 DhsrnLLLFAVTM--AHELGHNLGMEHDDGGC----------TCG-RSTCIMA--PSPSSLtDAFSNCSYEDYQKFLSRG 187


                  ....*..
gi 221468321  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 4.01e-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: 57.70  E-value: 4.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321   435 TAGFAYVGGACvvnkrlEKVNSVAIIED----TGGFSGIIvaAHEVGHLLGAVHDGSPPPSYlggpgaqrCRWEDGYIMS 510
Cdd:pfam01421  102 TVGAAYVGGMC------SLEYSGGVNEDhsknLESFAVTM--AHELGHNLGMQHDDFNGGCK--------CPPGGGCIMN 165

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 221468321   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 3.45e-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: 3.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321   429 GECNRGTAGFAYVGGACvvNKRLEKVNSVAIIEDTGGFSG-------IIVAAHEVGHLLGAVHDgsPPPSYLGGPGAQRC 501
Cdd:pfam13574   80 GTFSGGELGLAYVGQIC--QKGASSPKTNTGLSTTTNYGSfnyptqeWDVVAHEVGHNFGATHD--CDGSQYASSGCERN 155

                           90
                   ....*....|....*
gi 221468321   502 ---RWEDG---YIMS 510
Cdd:pfam13574  156 aatSVCSAngsFIMN 170
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 428-533 5.04e-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: 50.98  E-value: 5.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  428 YGECNRGTAGFAYVGGACvvnkrlEKVNSVAIIEDT--GGFSGIIVAAHEVGHLLGAVHDGSP-----PPSYLGGPGAqr 500
Cdd:cd00203    60 RQDFDGGTGGWAYLGRVC------DSLRGVGVLQDNqsGTKEGAQTIAHELGHALGFYHDHDRkdrddYPTIDDTLNA-- 131

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 221468321  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 3.38e-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: 3.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321   387 AIDSAAALTDMGKYLFRERRLPV-YDIAVAITKldmcrrtsaYGEcNRGTAGFAYVGGACVVNKRLEKVNSVAIIEDtgG 465
Cdd:pfam13583   68 ADCSGGDLGNWRLATLTSWRDSLnYDLAYLTLM---------TGP-SGQNVGVAWVGALCSSARQNAKASGVARSRD--E 135

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221468321   466 FSgiiVAAHEVGHLLGAVHD---GSPPPSYlggpgaQRCRWEDGYIMSdLRHTERGFRWSACTVQSFHHFLNGD 536
Cdd:pfam13583  136 WD---IFAHEIGHTFGAVHDcssQGEGLSS------STEDGSGQTIMS-YASTASQTAFSPCTIRNINGNPCSQ 199
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
431-510 6.41e-06

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 48.18  E-value: 6.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321   431 CNRGTAGFAYVGGAC------VVNKRLEKVNSVAiiedtGGFSGIIVAAHEVGHLLGAVHD--------GSPPPSYLGGP 496
Cdd:pfam13688   99 TNCSGGGLAWLGQLCnsgsagSVSTRVSGNNVVV-----STATEWQVFAHEIGHNFGAVHDcdsstssqCCPPSNSTCPA 173

                           90
                   ....*....|....
gi 221468321   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 3.64e-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: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221468321  471 VAAHEVGHLLGAVHDGSPPPSYLGGPGAQR--------CRWEDGYIMSDlrHTERGF-RWSACTVQSFHHFL--NGDTAT 539
Cdd:cd04271   148 VFAHEIGHTFGAVHDCTSGTCSDGSVGSQQccplststCDANGQYIMNP--SSSSGItEFSPCTIGNICSLLgrNPVRTS 225


                  ..
gi 221468321  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.
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