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Conserved domains on  [gi|2712540812|ref|WP_339687867|]
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zinc-dependent metalloprotease family protein [uncultured Nonlabens sp.]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
150-814 3.29e-29

Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443962 [Multi-domain]  Cd Length: 641  Bit Score: 124.55  E-value: 3.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 150 TQFVDSYTMNNSSVVVYKKMDLVDLGERWECHVEDDLGLRQGFAGPESPIDLKNANDGILRNFRLAISTTVEYSAFHWMR 229
Cdd:COG4935     1 GAAGGAGSTTGLAAAVLAAAAGTGSAATAEGGAASTATSAAVAGASAAAAAATAVGAGASSLAASAAAAAAAASGAAAGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 230 AGVSASALDADKRMAVMGAMVVTMTRNNFIYERDLSITMTFVANNDLLISIGFDNFSNTNPGAILGENQTAIDNTIGFAN 309
Cdd:COG4935    81 VDAAPAAATVVGAALGVVAVAGAGLAATASGAAAGAVAAAANGNTGAGPGSGGTGGGSGGAGAAAAAAALSAAGAAVGVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 310 YDIGHIFSTGGGGLASLASPCTNRKAQGVTGRGSPVGDPFDIDFVAHEIGHQMGAPHTFNGDAANCAGGNRSANSAYEPA 389
Cdd:COG4935   161 AVAGAAGGGGGVGVAAAVGVVLGAGLVADGGNGGGGAVAGGAAGGGGGGGGGGGLGGAAGGGGAGLAAAGGGGGGAAAAA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 390 SGTTIMAYAGICPPQNIQNNSDAYFHQTSLLRIFNNVFNGLSTCAQLNLTGNAAPSAIADADYTIPKGTPYRLVGNSTDP 469
Cdd:COG4935   241 AAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 470 DGTSTHTYTWEQFDLGPAGTPLENNVNGPLVRSFEGTDQKVRVIPKLEDIVAFGGNSTQWEKLPFATRPMNFVLTVRDND 549
Cdd:COG4935   321 GGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 550 SRGGQTDADLMTIQVDANAGPFSVTSPGNSGTVWRPNTTETITWNVAGTNANGVNTSNVNIILSTDSGRTFDTVLASNIP 629
Cdd:COG4935   401 VASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTGSAAGAAGGTTTATSGLASSTT 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 630 NTGSYDLLVPSGIVAPSCRLMVEGAGNIFFAINNVDFNINASVQTVCTTylSGALNTAIPDNNSNGLTSTINVPVTGDVA 709
Cdd:COG4935   481 AAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATF--SNTTDVAIPDNGPAGVTSTITVSGGGAVE 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 710 SIKVGLDISHTYISDMTVGISDPSSNNFALiWNRECANQDDLNATFEDGAaailcrqptvgnfapsstfsvFDNLPANGD 789
Cdd:COG4935   559 DVTVTVDITHTYRGDLVITLISPDGTTVVL-KNRSGGSADNINATFDVAN---------------------FSGESANGT 616
                         650       660
                  ....*....|....*....|....*
gi 2712540812 790 WALNIIDNAAQDTGALNSWSIEVCT 814
Cdd:COG4935   617 WTLRVVDTAGGDTGTLNSWSLTFTG 641
Por_Secre_tail pfam18962
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
832-906 7.61e-19

Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.


:

Pssm-ID: 436869 [Multi-domain]  Cd Length: 75  Bit Score: 81.50  E-value: 7.61e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2712540812 832 IYPNPSRGSFTILFDNASSNLVELDIFDLSGRYVFKKSyETYSSFNQNIDLKGVSSGMYLVQIKDGNRTITKKII 906
Cdd:pfam18962   1 IYPNPAKDVLNISLKNSNSSNLNISIYDILGKLVKSNS-KTNGNNTKTIDVSNLSSGIYFVKINSGNGSTTKKLI 74
 
Name Accession Description Interval E-value
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
150-814 3.29e-29

Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443962 [Multi-domain]  Cd Length: 641  Bit Score: 124.55  E-value: 3.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 150 TQFVDSYTMNNSSVVVYKKMDLVDLGERWECHVEDDLGLRQGFAGPESPIDLKNANDGILRNFRLAISTTVEYSAFHWMR 229
Cdd:COG4935     1 GAAGGAGSTTGLAAAVLAAAAGTGSAATAEGGAASTATSAAVAGASAAAAAATAVGAGASSLAASAAAAAAAASGAAAGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 230 AGVSASALDADKRMAVMGAMVVTMTRNNFIYERDLSITMTFVANNDLLISIGFDNFSNTNPGAILGENQTAIDNTIGFAN 309
Cdd:COG4935    81 VDAAPAAATVVGAALGVVAVAGAGLAATASGAAAGAVAAAANGNTGAGPGSGGTGGGSGGAGAAAAAAALSAAGAAVGVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 310 YDIGHIFSTGGGGLASLASPCTNRKAQGVTGRGSPVGDPFDIDFVAHEIGHQMGAPHTFNGDAANCAGGNRSANSAYEPA 389
Cdd:COG4935   161 AVAGAAGGGGGVGVAAAVGVVLGAGLVADGGNGGGGAVAGGAAGGGGGGGGGGGLGGAAGGGGAGLAAAGGGGGGAAAAA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 390 SGTTIMAYAGICPPQNIQNNSDAYFHQTSLLRIFNNVFNGLSTCAQLNLTGNAAPSAIADADYTIPKGTPYRLVGNSTDP 469
Cdd:COG4935   241 AAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 470 DGTSTHTYTWEQFDLGPAGTPLENNVNGPLVRSFEGTDQKVRVIPKLEDIVAFGGNSTQWEKLPFATRPMNFVLTVRDND 549
Cdd:COG4935   321 GGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 550 SRGGQTDADLMTIQVDANAGPFSVTSPGNSGTVWRPNTTETITWNVAGTNANGVNTSNVNIILSTDSGRTFDTVLASNIP 629
Cdd:COG4935   401 VASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTGSAAGAAGGTTTATSGLASSTT 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 630 NTGSYDLLVPSGIVAPSCRLMVEGAGNIFFAINNVDFNINASVQTVCTTylSGALNTAIPDNNSNGLTSTINVPVTGDVA 709
Cdd:COG4935   481 AAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATF--SNTTDVAIPDNGPAGVTSTITVSGGGAVE 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 710 SIKVGLDISHTYISDMTVGISDPSSNNFALiWNRECANQDDLNATFEDGAaailcrqptvgnfapsstfsvFDNLPANGD 789
Cdd:COG4935   559 DVTVTVDITHTYRGDLVITLISPDGTTVVL-KNRSGGSADNINATFDVAN---------------------FSGESANGT 616
                         650       660
                  ....*....|....*....|....*
gi 2712540812 790 WALNIIDNAAQDTGALNSWSIEVCT 814
Cdd:COG4935   617 WTLRVVDTAGGDTGTLNSWSLTFTG 641
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
248-367 1.44e-27

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: 108.23  E-value: 1.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 248 AMVVTMTRNNFIYERDLSITMTFVANndLLISIGFDNFSNTNPGAILGENQTAIDNTIGFANYDIGHIFST----GGGGL 323
Cdd:pfam13582   2 RIVSLVNRANTIYERDLGIRLQLAAI--IITTSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGrdggGGGGI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2712540812 324 ASLASPCTNRKAQGVTGRGSPVGDpFDIDFVAHEIGHQMGAPHT 367
Cdd:pfam13582  80 AYVGGVCNSGSKFGVNSGSGPVGD-TGADTFAHEIGHNFGLNHT 122
Por_Secre_tail pfam18962
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
832-906 7.61e-19

Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.


Pssm-ID: 436869 [Multi-domain]  Cd Length: 75  Bit Score: 81.50  E-value: 7.61e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2712540812 832 IYPNPSRGSFTILFDNASSNLVELDIFDLSGRYVFKKSyETYSSFNQNIDLKGVSSGMYLVQIKDGNRTITKKII 906
Cdd:pfam18962   1 IYPNPAKDVLNISLKNSNSSNLNISIYDILGKLVKSNS-KTNGNNTKTIDVSNLSSGIYFVKINSGNGSTTKKLI 74
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
797-908 1.89e-15

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 81.24  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 797 NAAQdtGALNSWSIEVCTLMVTP-------LSNESFELDNLSIYPNPSRGSFTILFDNASSNLVELDIFDLSGRYVFKKS 869
Cdd:NF038113  754 SASQ--GSSNSRSDQVEDFTVPPplanctsLATNEFGANKFIIYPNPAKGEIFISFSNKDSGEVKVKVYDINGRLVLSDK 831
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2712540812 870 YEtysSFNQN-IDLKGVSSGMYLVQIKDGNRTITKKIILE 908
Cdd:NF038113  832 VE---LTNTKtINTSGLQSGIYIVKIEGGSKSYTEKLIVK 868
Por_Secre_tail TIGR04183
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
832-908 4.56e-15

Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.


Pssm-ID: 275036 [Multi-domain]  Cd Length: 72  Bit Score: 70.51  E-value: 4.56e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2712540812 832 IYPNPSRGSFTILFDNASSNlVELDIFDLSGRYVFKKSyetySSFNQNIDLKGVSSGMYLVQIKDGNRTITKKIILE 908
Cdd:TIGR04183   1 IYPNPAKGTLIIILLSSSGK-VKVEIYDLSGKLVKKTT----LNNSNSIDLSNLSSGVYIVKITTGNGTITKKIIKK 72
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
277-397 2.01e-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: 51.75  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 277 LISIGFDNFSNTNPGAILGENQTAI--DNTIGFANYDighiFSTGGGGLASLASPCTNRKAQGVTGRGSPVGDPFDIDFv 354
Cdd:cd00203    26 LILIAMQIWRDYLNIRFVLVGVEIDkaDIAILVTRQD----FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTI- 100
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2712540812 355 AHEIGHQMGAPHTFnGDAANCAGGNRSANSAYEPASGTTIMAY 397
Cdd:cd00203   101 AHELGHALGFYHDH-DRKDRDDYPTIDDTLNAEDDDYYSVMSY 142
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
441-602 1.39e-04

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 45.80  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812  441 NAAPSAIADADYTIPKGTPYRLVGNSTDPDGtSTHTYTWEQFDlGPAGTpLENnvngplvrsfEGTDQKVRVIPKLEdiv 520
Cdd:NF038112  1280 NRAPVAVAGAPATVDERSTVTLDGSGTDADG-DALTYAWTQTS-GPAVT-LTG----------ATTATATFTAPEVT--- 1343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812  521 afggnstqweklpfATRPMNFVLTVRDndsrGGQTDADLMTIQV-DANAGPfsVTSPGNSGTVwrpNTTETITWNVAGTN 599
Cdd:NF038112  1344 --------------ADTQLTFTLTVSD----GTASATDTVTVTVrNVNRAP--VANAGADQTV---DERSTVTLSGSATD 1400

                   ...
gi 2712540812  600 ANG 602
Cdd:NF038112  1401 PDG 1403
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
441-570 1.45e-03

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 42.72  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812  441 NAAPSAIADADYTIPKGTPYRLVGNSTDPDGtSTHTYTWEQfdlgpagtplennVNGPLVrSFEGTDQKVrvipklediV 520
Cdd:NF038112  1467 NRAPVAHAGESITVDEGSTVTLDASATDPDG-DTLTYAWTQ-------------VAGPSV-TLTGADSAK---------L 1522
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2712540812  521 AFGGNSTQweklpfATRPMNFVLTVRDNDsrgGQTDADLMTIQV-DANAGP 570
Cdd:NF038112  1523 TFTAPEVS------ADTTLTFSLTVTDGS---GSSGPVVVTVTVkNVNRAP 1564
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
441-489 8.72e-03

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 40.03  E-value: 8.72e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2712540812  441 NAAPSAIADADYTIPKGTPYRLVGNSTDPDGTsTHTYTWEQFDlGPAGT 489
Cdd:NF038112  1373 NRAPVANAGADQTVDERSTVTLSGSATDPDGD-ALTYAWTQTA-GPTVT 1419
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
296-369 8.81e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 37.72  E-value: 8.81e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2712540812  296 ENQTAIDNTIGFANYDIG----HIFSTGGGGLASLASPCTNRkaqGVtgrgspvgdpfdidfVAHEIGHQMGAPHTFN 369
Cdd:smart00235  44 ERTGTADIYISFGSGDSGctlsHAGRPGGDQHLSLGNGCINT---GV---------------AAHELGHALGLYHEQS 103
 
Name Accession Description Interval E-value
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
150-814 3.29e-29

Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443962 [Multi-domain]  Cd Length: 641  Bit Score: 124.55  E-value: 3.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 150 TQFVDSYTMNNSSVVVYKKMDLVDLGERWECHVEDDLGLRQGFAGPESPIDLKNANDGILRNFRLAISTTVEYSAFHWMR 229
Cdd:COG4935     1 GAAGGAGSTTGLAAAVLAAAAGTGSAATAEGGAASTATSAAVAGASAAAAAATAVGAGASSLAASAAAAAAAASGAAAGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 230 AGVSASALDADKRMAVMGAMVVTMTRNNFIYERDLSITMTFVANNDLLISIGFDNFSNTNPGAILGENQTAIDNTIGFAN 309
Cdd:COG4935    81 VDAAPAAATVVGAALGVVAVAGAGLAATASGAAAGAVAAAANGNTGAGPGSGGTGGGSGGAGAAAAAAALSAAGAAVGVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 310 YDIGHIFSTGGGGLASLASPCTNRKAQGVTGRGSPVGDPFDIDFVAHEIGHQMGAPHTFNGDAANCAGGNRSANSAYEPA 389
Cdd:COG4935   161 AVAGAAGGGGGVGVAAAVGVVLGAGLVADGGNGGGGAVAGGAAGGGGGGGGGGGLGGAAGGGGAGLAAAGGGGGGAAAAA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 390 SGTTIMAYAGICPPQNIQNNSDAYFHQTSLLRIFNNVFNGLSTCAQLNLTGNAAPSAIADADYTIPKGTPYRLVGNSTDP 469
Cdd:COG4935   241 AAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 470 DGTSTHTYTWEQFDLGPAGTPLENNVNGPLVRSFEGTDQKVRVIPKLEDIVAFGGNSTQWEKLPFATRPMNFVLTVRDND 549
Cdd:COG4935   321 GGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 550 SRGGQTDADLMTIQVDANAGPFSVTSPGNSGTVWRPNTTETITWNVAGTNANGVNTSNVNIILSTDSGRTFDTVLASNIP 629
Cdd:COG4935   401 VASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTGSAAGAAGGTTTATSGLASSTT 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 630 NTGSYDLLVPSGIVAPSCRLMVEGAGNIFFAINNVDFNINASVQTVCTTylSGALNTAIPDNNSNGLTSTINVPVTGDVA 709
Cdd:COG4935   481 AAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATF--SNTTDVAIPDNGPAGVTSTITVSGGGAVE 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 710 SIKVGLDISHTYISDMTVGISDPSSNNFALiWNRECANQDDLNATFEDGAaailcrqptvgnfapsstfsvFDNLPANGD 789
Cdd:COG4935   559 DVTVTVDITHTYRGDLVITLISPDGTTVVL-KNRSGGSADNINATFDVAN---------------------FSGESANGT 616
                         650       660
                  ....*....|....*....|....*
gi 2712540812 790 WALNIIDNAAQDTGALNSWSIEVCT 814
Cdd:COG4935   617 WTLRVVDTAGGDTGTLNSWSLTFTG 641
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
248-367 1.44e-27

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: 108.23  E-value: 1.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 248 AMVVTMTRNNFIYERDLSITMTFVANndLLISIGFDNFSNTNPGAILGENQTAIDNTIGFANYDIGHIFST----GGGGL 323
Cdd:pfam13582   2 RIVSLVNRANTIYERDLGIRLQLAAI--IITTSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGrdggGGGGI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2712540812 324 ASLASPCTNRKAQGVTGRGSPVGDpFDIDFVAHEIGHQMGAPHT 367
Cdd:pfam13582  80 AYVGGVCNSGSKFGVNSGSGPVGD-TGADTFAHEIGHNFGLNHT 122
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
244-401 4.91e-20

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: 88.84  E-value: 4.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 244 AVMGAMVVTMTRNNFIYERD-LSITMTFVANNDLLI----SIGFDNFSNTNPgaILGENQTAIDNTIGFANYDIGHI--- 315
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPDdININGGLVNPGEIPAttsaSDSGNNYCNSPT--TIVRRLNFLSQWRGEQDYCLAHLvtm 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 316 --FSTGGGGLASLASPCtNRKAQGV---------TGRGSPVGDPFDIDFVAHEIGHQMGAPHTFNGDAANCAGGNRSANS 384
Cdd:pfam13574  80 gtFSGGELGLAYVGQIC-QKGASSPktntglsttTNYGSFNYPTQEWDVVAHEVGHNFGATHDCDGSQYASSGCERNAAT 158
                         170
                  ....*....|....*..
gi 2712540812 385 AYEPASGTTIMAYAGIC 401
Cdd:pfam13574 159 SVCSANGSFIMNPASKS 175
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
209-401 7.15e-20

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 88.24  E-value: 7.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 209 LRNFRLAISTTVEYSAFHwmragvsasalDADkrmAVMGAMVVTMTRNNFIYERDLSITMTFVAnndllISIGFDNFSNT 288
Cdd:pfam13688   2 TRTVALLVAADCSYVAAF-----------GGD---AAQANIINMVNTASNVYERDFNISLGLVN-----LTISDSTCPYT 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 289 NPGAILGENQTAIDNTIGF------ANYDIGHIFS---TGGGGLASLASPCTNRKAQGVTGRGSP----VGDPFDIDFVA 355
Cdd:pfam13688  63 PPACSTGDSSDRLSEFQDFsawrgtQNDDLAYLFLmtnCSGGGLAWLGQLCNSGSAGSVSTRVSGnnvvVSTATEWQVFA 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2712540812 356 HEIGHQMGAPHTFNGDAAN--CAGGNrsansAYEPASGTTIMAYAGIC 401
Cdd:pfam13688 143 HEIGHNFGAVHDCDSSTSSqcCPPSN-----STCPAGGRYIMNPSSSP 185
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
210-414 5.21e-19

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: 86.13  E-value: 5.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 210 RNFRLAISTTVEYSAFHWMRAGVSAsaldadkrmavmgAMVVTMTRNNFIYERDLSITMTFVANNDLLISIG-FDNF-SN 287
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSVDELRA-------------NINATVTTANEVYGRDFNVSLALISDRDVIYTDSsTDSFnAD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 288 TNPGAILGENQTAIDNTIGFANYDIGHIF-----STGGGGLASLASPCT----NRKAQGVtgrgSPVGDPFDIdfVAHEI 358
Cdd:pfam13583  70 CSGGDLGNWRLATLTSWRDSLNYDLAYLTlmtgpSGQNVGVAWVGALCSsarqNAKASGV----ARSRDEWDI--FAHEI 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2712540812 359 GHQMGAPHTfngdaanCAGGNRSANSAYEPASGTTIMAYAGICPPQNIQNNSDAYF 414
Cdd:pfam13583 144 GHTFGAVHD-------CSSQGEGLSSSTEDGSGQTIMSYASTASQTAFSPCTIRNI 192
Por_Secre_tail pfam18962
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
832-906 7.61e-19

Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.


Pssm-ID: 436869 [Multi-domain]  Cd Length: 75  Bit Score: 81.50  E-value: 7.61e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2712540812 832 IYPNPSRGSFTILFDNASSNLVELDIFDLSGRYVFKKSyETYSSFNQNIDLKGVSSGMYLVQIKDGNRTITKKII 906
Cdd:pfam18962   1 IYPNPAKDVLNISLKNSNSSNLNISIYDILGKLVKSNS-KTNGNNTKTIDVSNLSSGIYFVKINSGNGSTTKKLI 74
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
797-908 1.89e-15

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 81.24  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 797 NAAQdtGALNSWSIEVCTLMVTP-------LSNESFELDNLSIYPNPSRGSFTILFDNASSNLVELDIFDLSGRYVFKKS 869
Cdd:NF038113  754 SASQ--GSSNSRSDQVEDFTVPPplanctsLATNEFGANKFIIYPNPAKGEIFISFSNKDSGEVKVKVYDINGRLVLSDK 831
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2712540812 870 YEtysSFNQN-IDLKGVSSGMYLVQIKDGNRTITKKIILE 908
Cdd:NF038113  832 VE---LTNTKtINTSGLQSGIYIVKIEGGSKSYTEKLIVK 868
Por_Secre_tail TIGR04183
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
832-908 4.56e-15

Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.


Pssm-ID: 275036 [Multi-domain]  Cd Length: 72  Bit Score: 70.51  E-value: 4.56e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2712540812 832 IYPNPSRGSFTILFDNASSNlVELDIFDLSGRYVFKKSyetySSFNQNIDLKGVSSGMYLVQIKDGNRTITKKIILE 908
Cdd:TIGR04183   1 IYPNPAKGTLIIILLSSSGK-VKVEIYDLSGKLVKKTT----LNNSNSIDLSNLSSGVYIVKITTGNGTITKKIIKK 72
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
708-810 1.89e-07

Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein convertases is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain.


Pssm-ID: 460225 [Multi-domain]  Cd Length: 86  Bit Score: 49.57  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 708 VASIKVGLDISHTYISDMTVGISDPSSNNFALIWNRecaNQDDLNATFEDGaaailcrqptvgnfapssTFSV--FDNLP 785
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRR---GGDTSSAGFLDW------------------TFMSvhHWGER 59
                          90       100
                  ....*....|....*....|....*
gi 2712540812 786 ANGDWALNIIDNAAQDTGALNSWSI 810
Cdd:pfam01483  60 AEGTWTLEVTDTAPGDTGTLNSWQL 84
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
277-397 2.01e-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: 51.75  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 277 LISIGFDNFSNTNPGAILGENQTAI--DNTIGFANYDighiFSTGGGGLASLASPCTNRKAQGVTGRGSPVGDPFDIDFv 354
Cdd:cd00203    26 LILIAMQIWRDYLNIRFVLVGVEIDkaDIAILVTRQD----FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTI- 100
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2712540812 355 AHEIGHQMGAPHTFnGDAANCAGGNRSANSAYEPASGTTIMAY 397
Cdd:cd00203   101 AHELGHALGFYHDH-DRKDRDDYPTIDDTLNAEDDDYYSVMSY 142
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
441-602 1.39e-04

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 45.80  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812  441 NAAPSAIADADYTIPKGTPYRLVGNSTDPDGtSTHTYTWEQFDlGPAGTpLENnvngplvrsfEGTDQKVRVIPKLEdiv 520
Cdd:NF038112  1280 NRAPVAVAGAPATVDERSTVTLDGSGTDADG-DALTYAWTQTS-GPAVT-LTG----------ATTATATFTAPEVT--- 1343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812  521 afggnstqweklpfATRPMNFVLTVRDndsrGGQTDADLMTIQV-DANAGPfsVTSPGNSGTVwrpNTTETITWNVAGTN 599
Cdd:NF038112  1344 --------------ADTQLTFTLTVSD----GTASATDTVTVTVrNVNRAP--VANAGADQTV---DERSTVTLSGSATD 1400

                   ...
gi 2712540812  600 ANG 602
Cdd:NF038112  1401 PDG 1403
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
322-398 2.73e-04

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: 42.79  E-value: 2.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2712540812 322 GLASLASPCTNRKAQGVTGRGSPvgdPFDIDFV-AHEIGHQMGAPHtfngDAANCAGGNRSANSAYepasgttIMAYA 398
Cdd:cd04267   107 GLAYVGSMCNPYSSVGVVEDTGF---TLLTALTmAHELGHNLGAEH----DGGDELAFECDGGGNY-------IMAPV 170
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
317-433 1.19e-03

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 41.18  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812 317 STGGGGLASLASPCT-NRKAQGVTGRGSPVGdpfdIDFVAHEIGHQMGAPHTFNGDAANCAGGNRSANSayePASGTTIM 395
Cdd:cd04272   115 QTGTGGYAYVGGACTeNRVAMGEDTPGSYYG----VYTMTHELAHLLGAPHDGSPPPSWVKGHPGSLDC---PWDDGYIM 187
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2712540812 396 AYAgicppqniQNNSDAYFHQTSLLRIFNNVFNGLS-TC 433
Cdd:cd04272   188 SYV--------VNGERQYRFSQCSQRQIRNVFRRLGaSC 218
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
441-570 1.45e-03

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 42.72  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2712540812  441 NAAPSAIADADYTIPKGTPYRLVGNSTDPDGtSTHTYTWEQfdlgpagtplennVNGPLVrSFEGTDQKVrvipklediV 520
Cdd:NF038112  1467 NRAPVAHAGESITVDEGSTVTLDASATDPDG-DTLTYAWTQ-------------VAGPSV-TLTGADSAK---------L 1522
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2712540812  521 AFGGNSTQweklpfATRPMNFVLTVRDNDsrgGQTDADLMTIQV-DANAGP 570
Cdd:NF038112  1523 TFTAPEVS------ADTTLTFSLTVTDGS---GSSGPVVVTVTVkNVNRAP 1564
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
441-489 8.72e-03

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 40.03  E-value: 8.72e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2712540812  441 NAAPSAIADADYTIPKGTPYRLVGNSTDPDGTsTHTYTWEQFDlGPAGT 489
Cdd:NF038112  1373 NRAPVANAGADQTVDERSTVTLSGSATDPDGD-ALTYAWTQTA-GPTVT 1419
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
296-369 8.81e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 37.72  E-value: 8.81e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2712540812  296 ENQTAIDNTIGFANYDIG----HIFSTGGGGLASLASPCTNRkaqGVtgrgspvgdpfdidfVAHEIGHQMGAPHTFN 369
Cdd:smart00235  44 ERTGTADIYISFGSGDSGctlsHAGRPGGDQHLSLGNGCINT---GV---------------AAHELGHALGLYHEQS 103
 
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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