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Conserved domains on  [gi|1543644083|ref|WP_126260046|]
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LPXTG-anchored aggregation substance [Enterococcus faecalis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Agg_substance super family cl41491
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
1-1292 0e+00

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


The actual alignment was detected with superfamily member NF033875:

Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 2479.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083    1 MKQQTEVKKRFKTYKAKKRWVTAPILFIGVLGVVGLATDDVQAAELDTQPGTTTVQPDNPDPQVGSTTPKTAVSEEAAVQ 80
Cdd:NF033875     1 MKQQTEVKKRFKMYKAKKHWVVAPILFLGVLGVVGLATDNVQAAELDTQPGTTTVQPDNPDPQSGSETPKTAVSEEATVQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083   81 KDTTSQPTKVEEVVSSEVTTENTPVVENNTT------VSDETIGEAQPA-------EPIGKPTEIANPTASGNQATTIPK 147
Cdd:NF033875    81 KDTTSQPTKVEEVASEKNGAEQSSATPNDTTnaqqptVGAEKSAQEQPVvspettnEPLGQPTEVAPAENEANKSTSIPK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  148 EFTTPELDQVVAEAQKDPNITIVEKPAEDLGNVSSKDLDAKEKEVEQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAK 227
Cdd:NF033875   161 EFETPDVDKAVDEAKKDPNITVVEKPAEDLGNVSSKDLAAKEKEVDQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  228 NKAEKERYEKEVAEYNKHKNENGYVKEPVSKNLVFDQSVVTKDTKISSITGGKFIKAADFNKVNAGDSKDIFTKLRKDMA 307
Cdd:NF033875   241 NKAEKERYEKEVAEYNKHKNENGYVNEAISKNLVFDQSVVTKDTKISSIKGGKFIKATDFNKVNAGDSKDIFTKLSKDMG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  308 GKATGNFKNSFIKEVNLGSNGGYAVLLEKNKPVTVTYTGLNASYLGRKITKAEFVYELQSSPSQSGTLNAVFSNDPIITA 387
Cdd:NF033875   321 GKATGNFQNSFVKEANLGSNGGYAVLLEKNKPVTVTYTGLNASYLGRKITKAEFVYELQSSPSQSGTLNAVFSNDPIITA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  388 FIGTNRVNGKDVKTRLTIKFFDASGKEVLPDKDSPFAYALSSLNSSLTNKGGHAEFVSDFGANNAFKYINGSYVKKQADG 467
Cdd:NF033875   401 FVGTNNVNGKDVKTRLTIKFFDASGKEVLPDKDSPFAYALSSLNSSLTNKGGHAEFVSDFGANNAFKYINGSYVKKQADG 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  468 KFYSPEDIDYGTGPSGLKNSDWDAVGHKNAYFGSGVGLAN--GRISFSFGMTTKGKsNVPVSSAQWFAFSTNLNAKSITP 545
Cdd:NF033875   481 KFYSPEDIDYGTGPSGLKNSDWDAVGHKNAYFGSGVGLANtpGRISFSFGMTTKGK-NVPVSSAQWFAFSTNLNAKSIKP 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  546 YQEKGRFKQPEKATIEFNRYKANVVPVLVPNKEVTDGQKNINDLNVKRGDSLQYIVTGDTTELAKVDPKTVTKQGIRDTF 625
Cdd:NF033875   560 YQNKGNPKEPEKATIEFNRYKANVVPVLVPNKEVTDGQKNINDLNVKRGDSLQYIVTGDTTELAKVDPKTVTKQGIRDTF 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  626 DAEKVTIDLSKVKVYQADASLNEKDLKAVAAAINSGKAKDVTASYDLHLDQNTVTAMMKTNADGSVVLAMGYKYLLVLPF 705
Cdd:NF033875   640 DAEKVTIDLSKVKVYQADASLNEKDLKAVAAAINSGKAKDVTASYDLHLDQNTVTAMMKTNADGSVVLAMGYKYLLVLPF 719
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  706 LVKNVEGDFENTAVQLTNDGETVTNTVINHVPGSNPSKDVKADKNGTVGSVSLHDKDIPLQTKIYYEVKSSERPANYGGI 785
Cdd:NF033875   720 VVKNVEGDFENTAVQLTNDGETVTNTVINHVPGSNPSKDVKADKNGTVGSVSLHDKDIPLQTKIYYEVKSSERPANYGGI 799
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  786 TEEWGMNDVLDTTHDRFTGKWHAITNYDLKVGDKTLKAGTDISAYILLENKDNKDLTFTMNQALLAALNEGSNKVGKQAW 865
Cdd:NF033875   800 TEEWGMNDVLDTTHDRFTGKWHAITNYDLKVGDKTLKAGTDISAYILLENKDNKDLTFTMNQALLAALNEGSNKVGKQAW 879
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  866 SVYLEVERIKTGDVENTQTENYNKELVRSNTVVTHTPDDPKPTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYDKDF 945
Cdd:NF033875   880 SVYLEVERIKTGDVENTQTENYNKELVRSNTVVTHTPDDPKPTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYDKDF 959
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  946 AFDTVDLATGVSFFDDYDETKVTPIKDLLRVKDSKGVDITNQFTISWDDAKGTVTISAKDPQAFILAYGGQELRVTLPTK 1025
Cdd:NF033875   960 AFDTVDLATGVSFFDDYDETKVTPIKDLLRVKDSKGVDITNQFTISWDDAKGTVTISAKDPQAFILAHGGQELRVTLPTK 1039
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1026 VKADVSGNVYNSAEQNTFGQRIKTNTVVNHIPKVNPKKDVVIKVGDKQSQNGATIKLGEKFFYEFTSSDIPAEYVGVVEE 1105
Cdd:NF033875  1040 VKANVSGDVYNSAEQNTFGQRIKTNTVVNHIPKVNPKKDVVIKVGDKQSQNGATIKLGEKFFYEFTSSDIPAEYAGVVEE 1119
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1106 WSLSDKLDIKHDKFSGQWSVFANSNFVLADGTKVNKGDDISKLFTMTFEQGVVKITASQAFLDAMNLKENKNVAHSWKAF 1185
Cdd:NF033875  1120 WSISDKLDVKHDKFSGQWSVFANSNFVLADGTKVNKGDDISKLFTMTFEQGVVKITASQAFLDAMNLKENKNVAHSWKAF 1199
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1186 IGVERIAAGDVYNTIEESFNNEKIKTNTVVTHTPEKPQTPPEKTVIVPPTPKTPQAPVEPLVVEKASVVPELPQTGEKQN 1265
Cdd:NF033875  1200 IGVERIAAGDVYNTIEESFNNEKIKTNTVVTHTPEKPQTPPEKTVIVPPTPKTPQAPVEPLVVEKASVVPELPQTGEKQN 1279
                         1290      1300
                   ....*....|....*....|....*..
gi 1543644083 1266 VLLTVAGSLVTMLGLAGLGFKRRKETK 1292
Cdd:NF033875  1280 VLLTVAGSLAAMLGLAGLGFKRRKETK 1306
 
Name Accession Description Interval E-value
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
1-1292 0e+00

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 2479.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083    1 MKQQTEVKKRFKTYKAKKRWVTAPILFIGVLGVVGLATDDVQAAELDTQPGTTTVQPDNPDPQVGSTTPKTAVSEEAAVQ 80
Cdd:NF033875     1 MKQQTEVKKRFKMYKAKKHWVVAPILFLGVLGVVGLATDNVQAAELDTQPGTTTVQPDNPDPQSGSETPKTAVSEEATVQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083   81 KDTTSQPTKVEEVVSSEVTTENTPVVENNTT------VSDETIGEAQPA-------EPIGKPTEIANPTASGNQATTIPK 147
Cdd:NF033875    81 KDTTSQPTKVEEVASEKNGAEQSSATPNDTTnaqqptVGAEKSAQEQPVvspettnEPLGQPTEVAPAENEANKSTSIPK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  148 EFTTPELDQVVAEAQKDPNITIVEKPAEDLGNVSSKDLDAKEKEVEQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAK 227
Cdd:NF033875   161 EFETPDVDKAVDEAKKDPNITVVEKPAEDLGNVSSKDLAAKEKEVDQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  228 NKAEKERYEKEVAEYNKHKNENGYVKEPVSKNLVFDQSVVTKDTKISSITGGKFIKAADFNKVNAGDSKDIFTKLRKDMA 307
Cdd:NF033875   241 NKAEKERYEKEVAEYNKHKNENGYVNEAISKNLVFDQSVVTKDTKISSIKGGKFIKATDFNKVNAGDSKDIFTKLSKDMG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  308 GKATGNFKNSFIKEVNLGSNGGYAVLLEKNKPVTVTYTGLNASYLGRKITKAEFVYELQSSPSQSGTLNAVFSNDPIITA 387
Cdd:NF033875   321 GKATGNFQNSFVKEANLGSNGGYAVLLEKNKPVTVTYTGLNASYLGRKITKAEFVYELQSSPSQSGTLNAVFSNDPIITA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  388 FIGTNRVNGKDVKTRLTIKFFDASGKEVLPDKDSPFAYALSSLNSSLTNKGGHAEFVSDFGANNAFKYINGSYVKKQADG 467
Cdd:NF033875   401 FVGTNNVNGKDVKTRLTIKFFDASGKEVLPDKDSPFAYALSSLNSSLTNKGGHAEFVSDFGANNAFKYINGSYVKKQADG 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  468 KFYSPEDIDYGTGPSGLKNSDWDAVGHKNAYFGSGVGLAN--GRISFSFGMTTKGKsNVPVSSAQWFAFSTNLNAKSITP 545
Cdd:NF033875   481 KFYSPEDIDYGTGPSGLKNSDWDAVGHKNAYFGSGVGLANtpGRISFSFGMTTKGK-NVPVSSAQWFAFSTNLNAKSIKP 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  546 YQEKGRFKQPEKATIEFNRYKANVVPVLVPNKEVTDGQKNINDLNVKRGDSLQYIVTGDTTELAKVDPKTVTKQGIRDTF 625
Cdd:NF033875   560 YQNKGNPKEPEKATIEFNRYKANVVPVLVPNKEVTDGQKNINDLNVKRGDSLQYIVTGDTTELAKVDPKTVTKQGIRDTF 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  626 DAEKVTIDLSKVKVYQADASLNEKDLKAVAAAINSGKAKDVTASYDLHLDQNTVTAMMKTNADGSVVLAMGYKYLLVLPF 705
Cdd:NF033875   640 DAEKVTIDLSKVKVYQADASLNEKDLKAVAAAINSGKAKDVTASYDLHLDQNTVTAMMKTNADGSVVLAMGYKYLLVLPF 719
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  706 LVKNVEGDFENTAVQLTNDGETVTNTVINHVPGSNPSKDVKADKNGTVGSVSLHDKDIPLQTKIYYEVKSSERPANYGGI 785
Cdd:NF033875   720 VVKNVEGDFENTAVQLTNDGETVTNTVINHVPGSNPSKDVKADKNGTVGSVSLHDKDIPLQTKIYYEVKSSERPANYGGI 799
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  786 TEEWGMNDVLDTTHDRFTGKWHAITNYDLKVGDKTLKAGTDISAYILLENKDNKDLTFTMNQALLAALNEGSNKVGKQAW 865
Cdd:NF033875   800 TEEWGMNDVLDTTHDRFTGKWHAITNYDLKVGDKTLKAGTDISAYILLENKDNKDLTFTMNQALLAALNEGSNKVGKQAW 879
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  866 SVYLEVERIKTGDVENTQTENYNKELVRSNTVVTHTPDDPKPTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYDKDF 945
Cdd:NF033875   880 SVYLEVERIKTGDVENTQTENYNKELVRSNTVVTHTPDDPKPTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYDKDF 959
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  946 AFDTVDLATGVSFFDDYDETKVTPIKDLLRVKDSKGVDITNQFTISWDDAKGTVTISAKDPQAFILAYGGQELRVTLPTK 1025
Cdd:NF033875   960 AFDTVDLATGVSFFDDYDETKVTPIKDLLRVKDSKGVDITNQFTISWDDAKGTVTISAKDPQAFILAHGGQELRVTLPTK 1039
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1026 VKADVSGNVYNSAEQNTFGQRIKTNTVVNHIPKVNPKKDVVIKVGDKQSQNGATIKLGEKFFYEFTSSDIPAEYVGVVEE 1105
Cdd:NF033875  1040 VKANVSGDVYNSAEQNTFGQRIKTNTVVNHIPKVNPKKDVVIKVGDKQSQNGATIKLGEKFFYEFTSSDIPAEYAGVVEE 1119
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1106 WSLSDKLDIKHDKFSGQWSVFANSNFVLADGTKVNKGDDISKLFTMTFEQGVVKITASQAFLDAMNLKENKNVAHSWKAF 1185
Cdd:NF033875  1120 WSISDKLDVKHDKFSGQWSVFANSNFVLADGTKVNKGDDISKLFTMTFEQGVVKITASQAFLDAMNLKENKNVAHSWKAF 1199
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1186 IGVERIAAGDVYNTIEESFNNEKIKTNTVVTHTPEKPQTPPEKTVIVPPTPKTPQAPVEPLVVEKASVVPELPQTGEKQN 1265
Cdd:NF033875  1200 IGVERIAAGDVYNTIEESFNNEKIKTNTVVTHTPEKPQTPPEKTVIVPPTPKTPQAPVEPLVVEKASVVPELPQTGEKQN 1279
                         1290      1300
                   ....*....|....*....|....*..
gi 1543644083 1266 VLLTVAGSLVTMLGLAGLGFKRRKETK 1292
Cdd:NF033875  1280 VLLTVAGSLAAMLGLAGLGFKRRKETK 1306
GbpC pfam08363
Glucan-binding protein C; This domain is found in the Streptococcus Glucan-binding protein C ...
243-534 2.23e-70

Glucan-binding protein C; This domain is found in the Streptococcus Glucan-binding protein C (GbpC) and also in surface protein antigen (Spa)-family proteins which show sequence similarity to GbpC.


Pssm-ID: 400594 [Multi-domain]  Cd Length: 260  Bit Score: 236.33  E-value: 2.23e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  243 NKHKNENGYVKEPVSKNLVFDQSVVTKdtkissitggkfikaadfnkVNAGDSKDIFTKlrkdmagkatGNFKNSFIKEV 322
Cdd:pfam08363    1 EKHKNEEGYVSEALAQALVFDNEPQAQ--------------------LSANTRNQIITK----------GTALLGGYSKI 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  323 NLGSNGGYAVLLEKNKPVTVTYTGL-NASYLGRKITKAEFVYELQSSPSQSGTLNAVFSNDPIITAFIGTNRVNGK---D 398
Cdd:pfam08363   51 LQSTGFDVYDALKKGQPVSVTYTNLqNASYNGKKISKVEYDYTVLSSPAGTGAVNLVLFNDPTETIFAGANTGNGDkntD 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  399 VKTRLTIKFFDASGKEVLPDKDSPFAYALSSLNSSLTNKggHAEFVSDFgaNNAFKYINGSYVKKQADGKFYSPEDIDYG 478
Cdd:pfam08363  131 IEIRMVIKFYDEDGKEILFSKENAFVFSLSSLNHNDENI--HLEFVKDS--TGKFVKINGSSVQVHGNGKIYSTGDNDYG 206
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1543644083  479 TGPSGLK-NSDWDAVGHKNAYFGSGVGLANG-RISFSFGMTTKGKsnvpvSSAQWFAF 534
Cdd:pfam08363  207 TNGADLNlPSGWDTVSAKNAYYGAGVSVTSGnRITFTFGQGDSNL-----PGSIWFAL 259
isopep_sspB_C2 TIGR04228
adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 ...
907-1057 2.09e-29

adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 in seed alignment) and Asn at 177 that form an intramolecular isopeptide bond. The Asp (or Glu) at position 59


Pssm-ID: 275068 [Multi-domain]  Cd Length: 173  Bit Score: 115.47  E-value: 2.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  907 PTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYdKDFAFDTVDLATGVSFFDDYDETKVTPIKDLLRVKDSKGVDITN 986
Cdd:TIGR04228    1 PTKKNTNDAGVNIDGKTVLPGSTNYYRLTWDLSQY-KGIKASKEAIAKGFGYVDDYDEEALTVDQDKITITDSNGKDVTG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  987 QFTIS---------------WDDAKGTVT-----ISAKDPQAFILAY--GGQELRVTLPTKVKADVSGNVY-NSAEQNTF 1043
Cdd:TIGR04228   80 LFTMYhvlsvkeapakvqaiLKAAGITPKgefqvWVAKDPQAFYKNYvqTGQNITIVLPMTVKKDKTGGKVeNTAYQIDF 159
                          170
                   ....*....|....
gi 1543644083 1044 GQRIKTNTVVNHIP 1057
Cdd:TIGR04228  160 GNGYETNTVTNNVP 173
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
153-244 1.26e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.08  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  153 ELDQVVAEAQKDpnitivekpAEDLGNVSS-KDLDAKEKEVEQLQKEQA---KKIAQQAAELKAKNEKIAKENAEIAAKN 228
Cdd:COG1579     67 EIEEVEARIKKY---------EEQLGNVRNnKEYEALQKEIESLKRRISdleDEILELMERIEELEEELAELEAELAELE 137
                           90
                   ....*....|....*....
gi 1543644083  229 K---AEKERYEKEVAEYNK 244
Cdd:COG1579    138 AeleEKKAELDEELAELEA 156
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
119-257 1.87e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 45.74  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  119 EAQPAEPigKPTEIANPTASGNQATTIPKEFTTPELDQVVAEAQKDPNITI--------VEKPAEDLGNVSSKDLDAKEK 190
Cdd:PRK13108   292 VDEALER--EPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVtdevaaesVVQVADRDGESTPAVEETSEA 369
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1543644083  191 EVEQLQKEQAKkiAQQAAELKAKNEKIAKENAEIAAKNKAEKERYEKEVAEYNKHKNENGYVKEPVS 257
Cdd:PRK13108   370 DIEREQPGDLA--GQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAV 434
 
Name Accession Description Interval E-value
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
1-1292 0e+00

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 2479.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083    1 MKQQTEVKKRFKTYKAKKRWVTAPILFIGVLGVVGLATDDVQAAELDTQPGTTTVQPDNPDPQVGSTTPKTAVSEEAAVQ 80
Cdd:NF033875     1 MKQQTEVKKRFKMYKAKKHWVVAPILFLGVLGVVGLATDNVQAAELDTQPGTTTVQPDNPDPQSGSETPKTAVSEEATVQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083   81 KDTTSQPTKVEEVVSSEVTTENTPVVENNTT------VSDETIGEAQPA-------EPIGKPTEIANPTASGNQATTIPK 147
Cdd:NF033875    81 KDTTSQPTKVEEVASEKNGAEQSSATPNDTTnaqqptVGAEKSAQEQPVvspettnEPLGQPTEVAPAENEANKSTSIPK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  148 EFTTPELDQVVAEAQKDPNITIVEKPAEDLGNVSSKDLDAKEKEVEQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAK 227
Cdd:NF033875   161 EFETPDVDKAVDEAKKDPNITVVEKPAEDLGNVSSKDLAAKEKEVDQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  228 NKAEKERYEKEVAEYNKHKNENGYVKEPVSKNLVFDQSVVTKDTKISSITGGKFIKAADFNKVNAGDSKDIFTKLRKDMA 307
Cdd:NF033875   241 NKAEKERYEKEVAEYNKHKNENGYVNEAISKNLVFDQSVVTKDTKISSIKGGKFIKATDFNKVNAGDSKDIFTKLSKDMG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  308 GKATGNFKNSFIKEVNLGSNGGYAVLLEKNKPVTVTYTGLNASYLGRKITKAEFVYELQSSPSQSGTLNAVFSNDPIITA 387
Cdd:NF033875   321 GKATGNFQNSFVKEANLGSNGGYAVLLEKNKPVTVTYTGLNASYLGRKITKAEFVYELQSSPSQSGTLNAVFSNDPIITA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  388 FIGTNRVNGKDVKTRLTIKFFDASGKEVLPDKDSPFAYALSSLNSSLTNKGGHAEFVSDFGANNAFKYINGSYVKKQADG 467
Cdd:NF033875   401 FVGTNNVNGKDVKTRLTIKFFDASGKEVLPDKDSPFAYALSSLNSSLTNKGGHAEFVSDFGANNAFKYINGSYVKKQADG 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  468 KFYSPEDIDYGTGPSGLKNSDWDAVGHKNAYFGSGVGLAN--GRISFSFGMTTKGKsNVPVSSAQWFAFSTNLNAKSITP 545
Cdd:NF033875   481 KFYSPEDIDYGTGPSGLKNSDWDAVGHKNAYFGSGVGLANtpGRISFSFGMTTKGK-NVPVSSAQWFAFSTNLNAKSIKP 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  546 YQEKGRFKQPEKATIEFNRYKANVVPVLVPNKEVTDGQKNINDLNVKRGDSLQYIVTGDTTELAKVDPKTVTKQGIRDTF 625
Cdd:NF033875   560 YQNKGNPKEPEKATIEFNRYKANVVPVLVPNKEVTDGQKNINDLNVKRGDSLQYIVTGDTTELAKVDPKTVTKQGIRDTF 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  626 DAEKVTIDLSKVKVYQADASLNEKDLKAVAAAINSGKAKDVTASYDLHLDQNTVTAMMKTNADGSVVLAMGYKYLLVLPF 705
Cdd:NF033875   640 DAEKVTIDLSKVKVYQADASLNEKDLKAVAAAINSGKAKDVTASYDLHLDQNTVTAMMKTNADGSVVLAMGYKYLLVLPF 719
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  706 LVKNVEGDFENTAVQLTNDGETVTNTVINHVPGSNPSKDVKADKNGTVGSVSLHDKDIPLQTKIYYEVKSSERPANYGGI 785
Cdd:NF033875   720 VVKNVEGDFENTAVQLTNDGETVTNTVINHVPGSNPSKDVKADKNGTVGSVSLHDKDIPLQTKIYYEVKSSERPANYGGI 799
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  786 TEEWGMNDVLDTTHDRFTGKWHAITNYDLKVGDKTLKAGTDISAYILLENKDNKDLTFTMNQALLAALNEGSNKVGKQAW 865
Cdd:NF033875   800 TEEWGMNDVLDTTHDRFTGKWHAITNYDLKVGDKTLKAGTDISAYILLENKDNKDLTFTMNQALLAALNEGSNKVGKQAW 879
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  866 SVYLEVERIKTGDVENTQTENYNKELVRSNTVVTHTPDDPKPTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYDKDF 945
Cdd:NF033875   880 SVYLEVERIKTGDVENTQTENYNKELVRSNTVVTHTPDDPKPTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYDKDF 959
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  946 AFDTVDLATGVSFFDDYDETKVTPIKDLLRVKDSKGVDITNQFTISWDDAKGTVTISAKDPQAFILAYGGQELRVTLPTK 1025
Cdd:NF033875   960 AFDTVDLATGVSFFDDYDETKVTPIKDLLRVKDSKGVDITNQFTISWDDAKGTVTISAKDPQAFILAHGGQELRVTLPTK 1039
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1026 VKADVSGNVYNSAEQNTFGQRIKTNTVVNHIPKVNPKKDVVIKVGDKQSQNGATIKLGEKFFYEFTSSDIPAEYVGVVEE 1105
Cdd:NF033875  1040 VKANVSGDVYNSAEQNTFGQRIKTNTVVNHIPKVNPKKDVVIKVGDKQSQNGATIKLGEKFFYEFTSSDIPAEYAGVVEE 1119
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1106 WSLSDKLDIKHDKFSGQWSVFANSNFVLADGTKVNKGDDISKLFTMTFEQGVVKITASQAFLDAMNLKENKNVAHSWKAF 1185
Cdd:NF033875  1120 WSISDKLDVKHDKFSGQWSVFANSNFVLADGTKVNKGDDISKLFTMTFEQGVVKITASQAFLDAMNLKENKNVAHSWKAF 1199
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1186 IGVERIAAGDVYNTIEESFNNEKIKTNTVVTHTPEKPQTPPEKTVIVPPTPKTPQAPVEPLVVEKASVVPELPQTGEKQN 1265
Cdd:NF033875  1200 IGVERIAAGDVYNTIEESFNNEKIKTNTVVTHTPEKPQTPPEKTVIVPPTPKTPQAPVEPLVVEKASVVPELPQTGEKQN 1279
                         1290      1300
                   ....*....|....*....|....*..
gi 1543644083 1266 VLLTVAGSLVTMLGLAGLGFKRRKETK 1292
Cdd:NF033875  1280 VLLTVAGSLAAMLGLAGLGFKRRKETK 1306
GbpC pfam08363
Glucan-binding protein C; This domain is found in the Streptococcus Glucan-binding protein C ...
243-534 2.23e-70

Glucan-binding protein C; This domain is found in the Streptococcus Glucan-binding protein C (GbpC) and also in surface protein antigen (Spa)-family proteins which show sequence similarity to GbpC.


Pssm-ID: 400594 [Multi-domain]  Cd Length: 260  Bit Score: 236.33  E-value: 2.23e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  243 NKHKNENGYVKEPVSKNLVFDQSVVTKdtkissitggkfikaadfnkVNAGDSKDIFTKlrkdmagkatGNFKNSFIKEV 322
Cdd:pfam08363    1 EKHKNEEGYVSEALAQALVFDNEPQAQ--------------------LSANTRNQIITK----------GTALLGGYSKI 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  323 NLGSNGGYAVLLEKNKPVTVTYTGL-NASYLGRKITKAEFVYELQSSPSQSGTLNAVFSNDPIITAFIGTNRVNGK---D 398
Cdd:pfam08363   51 LQSTGFDVYDALKKGQPVSVTYTNLqNASYNGKKISKVEYDYTVLSSPAGTGAVNLVLFNDPTETIFAGANTGNGDkntD 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  399 VKTRLTIKFFDASGKEVLPDKDSPFAYALSSLNSSLTNKggHAEFVSDFgaNNAFKYINGSYVKKQADGKFYSPEDIDYG 478
Cdd:pfam08363  131 IEIRMVIKFYDEDGKEILFSKENAFVFSLSSLNHNDENI--HLEFVKDS--TGKFVKINGSSVQVHGNGKIYSTGDNDYG 206
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1543644083  479 TGPSGLK-NSDWDAVGHKNAYFGSGVGLANG-RISFSFGMTTKGKsnvpvSSAQWFAF 534
Cdd:pfam08363  207 TNGADLNlPSGWDTVSAKNAYYGAGVSVTSGnRITFTFGQGDSNL-----PGSIWFAL 259
Antigen_C pfam16364
Cell surface antigen C-terminus; This repeated domain is found at the C-terminus of cell ...
1060-1219 7.25e-41

Cell surface antigen C-terminus; This repeated domain is found at the C-terminus of cell surface antigens. In the Streptococcus mutans antigen I/II there are three repeats of this domain, a cleft between the first two of these forms a binding site for the human salivary agglutinin (SAG).


Pssm-ID: 435302 [Multi-domain]  Cd Length: 171  Bit Score: 148.32  E-value: 7.25e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1060 NPKKDVVIKVGDkQSQNGATIKLGEKFFYEFTSSDIPAEY-VGVVEEWSLSDKLDIKHDKFSGQWSVFANSNFVLADGTK 1138
Cdd:pfam16364    1 NPSKDVVVEVGG-DSIDGKSVYLNSLFLYRLDSSVLPANRaYPKVTEWSIVDQYDPKHDQYTGQWAVYATRDLTLADGSV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083 1139 VNK--------GDDISK---LFTMTFEQ-GVVKITASQAFLDAMNLKENKNVAhsWKAFIGVERIAAGD-VYNTIEESFN 1205
Cdd:pfam16364   80 IAAkgqriagsGFDATAygdLFTVTYDNeGHLTITATADYLKLVSADSAFEAA--WRAYVQFKRIAAGDrVENTFTETVN 157
                          170
                   ....*....|....
gi 1543644083 1206 NEKIKTNTVVTHTP 1219
Cdd:pfam16364  158 GQPRKSNTVTTHTP 171
Antigen_C pfam16364
Cell surface antigen C-terminus; This repeated domain is found at the C-terminus of cell ...
740-902 8.92e-33

Cell surface antigen C-terminus; This repeated domain is found at the C-terminus of cell surface antigens. In the Streptococcus mutans antigen I/II there are three repeats of this domain, a cleft between the first two of these forms a binding site for the human salivary agglutinin (SAG).


Pssm-ID: 435302 [Multi-domain]  Cd Length: 171  Bit Score: 125.21  E-value: 8.92e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  740 NPSKDVKAdkngTVGSVSLHDKDIPLQTKIYYEVKSSERPANYG-GITEEWGMNDVLDTTHDRFTGKWHAITNYDL---- 814
Cdd:pfam16364    1 NPSKDVVV----EVGGDSIDGKSVYLNSLFLYRLDSSVLPANRAyPKVTEWSIVDQYDPKHDQYTGQWAVYATRDLtlad 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  815 -----KVGDKTLKAGTDISAYILL---ENKDNKDLTFTMNQALLAALNEGSNKvgKQAWSVYLEVERIKTGD-VENTQTE 885
Cdd:pfam16364   77 gsviaAKGQRIAGSGFDATAYGDLftvTYDNEGHLTITATADYLKLVSADSAF--EAAWRAYVQFKRIAAGDrVENTFTE 154
                          170
                   ....*....|....*..
gi 1543644083  886 NYNKELVRSNTVVTHTP 902
Cdd:pfam16364  155 TVNGQPRKSNTVTTHTP 171
AgI_II_C2 pfam17998
Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the ...
907-1052 4.62e-30

Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the C-terminal region found in antigen I/II type adhesin protein AspA from S. pyogenes. Together with C3, these two domains form an elongated structure, each domain adopts the DEv-IgG fold. Similar to the classical IgG folds, it is comprised of two major antiparallel beta-sheets, designated ABED and CFG. For the C2-domain, there are two additional strands on the CFG sheet. Furthermore, sheets ABED and CFG are interconnected by several cross-connecting loops and one alpha-helix (DH1). The side chains of D982 and N996 in the C2-domain are involved in hydrogen bonding with the side chains of R1264 and N1295 in the C3 domain. Main chain hydrogen bonding can also be observed between S992 in C2 and N1189/G1191 in C3, furthermore stabilizing the interaction between the domains. The C2 domain contains one bound metal ion, modeled as Ca2+, and both the C2- and C3-domains are stabilized by conserved isopeptide bonds, which connect the beta-sheets of the central DEv-IgG motifs.Other members of this family include Major cell-surface adhesin PAc from Streptococcus mutans and SspB from Streptococcus gordonii.


Pssm-ID: 465609 [Multi-domain]  Cd Length: 180  Bit Score: 117.96  E-value: 4.62e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  907 PTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYDKDFAFDTvdLATGVSFFDDYDETKVTPIKDLLRV-KDSKGVDIT 985
Cdd:pfam17998    1 PTKTVTNENGVSIDGKTVLRGDTLYYRVTLDLTQYKGIAAYDV--IRKGFGIVDDYDEEYLTVDAATIKViDDATGKDVT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  986 NQFTISWDDAKGTVT-------------------------------ISAKDPQAFILAY--GGQELRVTLPTKVKADVSG 1032
Cdd:pfam17998   79 GKFNIQVRDGVVYAFaktvdslvpatgevqgdpqpadlkpygafqvFDALDPPAFDQTYlqKGQTYTLVLPMTVKKDVDG 158
                          170       180
                   ....*....|....*....|..
gi 1543644083 1033 --NVYNSAEQNTFGQRIKTNTV 1052
Cdd:pfam17998  159 ggTIENTAYQVDFGNGYVTNTV 180
isopep_sspB_C2 TIGR04228
adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 ...
907-1057 2.09e-29

adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 in seed alignment) and Asn at 177 that form an intramolecular isopeptide bond. The Asp (or Glu) at position 59


Pssm-ID: 275068 [Multi-domain]  Cd Length: 173  Bit Score: 115.47  E-value: 2.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  907 PTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYdKDFAFDTVDLATGVSFFDDYDETKVTPIKDLLRVKDSKGVDITN 986
Cdd:TIGR04228    1 PTKKNTNDAGVNIDGKTVLPGSTNYYRLTWDLSQY-KGIKASKEAIAKGFGYVDDYDEEALTVDQDKITITDSNGKDVTG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  987 QFTIS---------------WDDAKGTVT-----ISAKDPQAFILAY--GGQELRVTLPTKVKADVSGNVY-NSAEQNTF 1043
Cdd:TIGR04228   80 LFTMYhvlsvkeapakvqaiLKAAGITPKgefqvWVAKDPQAFYKNYvqTGQNITIVLPMTVKKDKTGGKVeNTAYQIDF 159
                          170
                   ....*....|....
gi 1543644083 1044 GQRIKTNTVVNHIP 1057
Cdd:TIGR04228  160 GNGYETNTVTNNVP 173
AgI_II_C2 pfam17998
Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the ...
575-732 1.64e-20

Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the C-terminal region found in antigen I/II type adhesin protein AspA from S. pyogenes. Together with C3, these two domains form an elongated structure, each domain adopts the DEv-IgG fold. Similar to the classical IgG folds, it is comprised of two major antiparallel beta-sheets, designated ABED and CFG. For the C2-domain, there are two additional strands on the CFG sheet. Furthermore, sheets ABED and CFG are interconnected by several cross-connecting loops and one alpha-helix (DH1). The side chains of D982 and N996 in the C2-domain are involved in hydrogen bonding with the side chains of R1264 and N1295 in the C3 domain. Main chain hydrogen bonding can also be observed between S992 in C2 and N1189/G1191 in C3, furthermore stabilizing the interaction between the domains. The C2 domain contains one bound metal ion, modeled as Ca2+, and both the C2- and C3-domains are stabilized by conserved isopeptide bonds, which connect the beta-sheets of the central DEv-IgG motifs.Other members of this family include Major cell-surface adhesin PAc from Streptococcus mutans and SspB from Streptococcus gordonii.


Pssm-ID: 465609 [Multi-domain]  Cd Length: 180  Bit Score: 90.22  E-value: 1.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  575 PNKEVTDG-QKNINDLNVKRGDSLQYIVTGDTTELAKVDPKTVTKQ--GIRDTFDAEKVTIDLSKVKVyqadaslnekdl 651
Cdd:pfam17998    1 PTKTVTNEnGVSIDGKTVLRGDTLYYRVTLDLTQYKGIAAYDVIRKgfGIVDDYDEEYLTVDAATIKV------------ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  652 kavaaaINSGKAKDVTASYDLHLDQNTVTAMMKTN-----ADGSV-----------------------------VLAMGY 697
Cdd:pfam17998   69 ------IDDATGKDVTGKFNIQVRDGVVYAFAKTVdslvpATGEVqgdpqpadlkpygafqvfdaldppafdqtYLQKGQ 142
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1543644083  698 KYLLVLPFLVK---NVEGDFENTAVQLTNDGETVTNTV 732
Cdd:pfam17998  143 TYTLVLPMTVKkdvDGGGTIENTAYQVDFGNGYVTNTV 180
Adhesin_P1_N pfam18652
Adhesin P1 N-terminal domain; The cariogenic bacterium Streptococcus mutans uses adhesin P1 to ...
137-242 6.19e-20

Adhesin P1 N-terminal domain; The cariogenic bacterium Streptococcus mutans uses adhesin P1 to adhere to tooth surfaces, extracellular matrix components, and other bacteria. The N terminus forms a stabilizing scaffold by wrapping behind the base of P1's elongated stalk and physically 'locking' it into place. It is suggested that the N-terminal has such a pronounced impact on P1 immunogenicity, antigenicity, folding, stability, and adherent function.


Pssm-ID: 465829 [Multi-domain]  Cd Length: 106  Bit Score: 86.26  E-value: 6.19e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  137 ASGNQATTIPKEFTTPELDQVVAEAqKDPNITIVEKPAEDLGNVSSKD-LDAKEKEVEQLQKEQAKKIAQQAAELKAKNE 215
Cdd:pfam18652    1 QAGDSTGGIEVAVDATDLDQAVKEA-KDAGVKVTQDPTVDKGTATTAEeAAAKKAEIKADYAKQVKEIKEATAKYKAKKA 79
                           90       100
                   ....*....|....*....|....*..
gi 1543644083  216 KIAKENAEIAAKNKAEKERYEKEVAEY 242
Cdd:pfam18652   80 AYDKKYDKIKAKNKADKEKYDKDLAAY 106
isopep_sspB_C2 TIGR04228
adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 ...
575-737 3.90e-09

adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 in seed alignment) and Asn at 177 that form an intramolecular isopeptide bond. The Asp (or Glu) at position 59


Pssm-ID: 275068 [Multi-domain]  Cd Length: 173  Bit Score: 57.31  E-value: 3.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  575 PNKEVTDGQ-KNINDLNVKRGDSLQYIVTGDTTELA--KVDPKTVTK-QGIRDTFDAEKVTIDLSKVKVYQADAslnekd 650
Cdd:TIGR04228    1 PTKKNTNDAgVNIDGKTVLPGSTNYYRLTWDLSQYKgiKASKEAIAKgFGYVDDYDEEALTVDQDKITITDSNG------ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  651 lKAVAAAINSGKAKDVTASYDlhlDQNTVTAMMKTNADGSVVLAM--------------GYKYLLVLPFLVKNVE--GDF 714
Cdd:TIGR04228   75 -KDVTGLFTMYHVLSVKEAPA---KVQAILKAAGITPKGEFQVWVakdpqafyknyvqtGQNITIVLPMTVKKDKtgGKV 150
                          170       180
                   ....*....|....*....|...
gi 1543644083  715 ENTAVQLTNDGETVTNTVINHVP 737
Cdd:TIGR04228  151 ENTAYQIDFGNGYETNTVTNNVP 173
Gram_pos_anchor pfam00746
LPXTG cell wall anchor motif;
1249-1292 3.45e-08

LPXTG cell wall anchor motif;


Pssm-ID: 366278 [Multi-domain]  Cd Length: 43  Bit Score: 50.62  E-value: 3.45e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1543644083 1249 EKASVVPELPQTGEKQNVLLTVAGSLVtMLGLAGLGFKRRKETK 1292
Cdd:pfam00746    1 AKKSKKKTLPKTGENSNIFLTAAGLLA-LLGGLLLLVKRRKKEK 43
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
99-248 8.55e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 55.62  E-value: 8.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083   99 TTENTPVvENNTTVSDETIGEAQPAEPIGKPTEIANPTASGNQATTIPKEFTTPELDQ-VVAEAQKDPNItivEKPAEDL 177
Cdd:TIGR02794   26 SVKPEPG-GGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKqRAAEQARQKEL---EQRAAAE 101
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1543644083  178 GNVSSKDLDAKEKEVEQLQKEQAKkiAQQAAELKAKNEKIAKENAEIAAKNKAEKERYEKEVAEyNKHKNE 248
Cdd:TIGR02794  102 KAAKQAEQAAKQAEEKQKQAEEAK--AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAE-AKKKAE 169
KxYKxGKxW_sig pfam19258
KxYKxGKxW signal peptide; This entry represents a novel form of signal peptide that occurs as ...
6-44 1.51e-07

KxYKxGKxW signal peptide; This entry represents a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK signal peptide.


Pssm-ID: 466014 [Multi-domain]  Cd Length: 41  Bit Score: 48.64  E-value: 1.51e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1543644083    6 EVKKRFKTYKAKKRWVTAPILFIGVLGVVGLATDDVQAA 44
Cdd:pfam19258    1 ERKTHYKMYKSGKHWVFAGITTLGLGLGLLGGTTAAAAD 39
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
153-244 1.26e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.08  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  153 ELDQVVAEAQKDpnitivekpAEDLGNVSS-KDLDAKEKEVEQLQKEQA---KKIAQQAAELKAKNEKIAKENAEIAAKN 228
Cdd:COG1579     67 EIEEVEARIKKY---------EEQLGNVRNnKEYEALQKEIESLKRRISdleDEILELMERIEELEEELAELEAELAELE 137
                           90
                   ....*....|....*....
gi 1543644083  229 K---AEKERYEKEVAEYNK 244
Cdd:COG1579    138 AeleEKKAELDEELAELEA 156
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
1256-1290 1.58e-06

LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other]


Pssm-ID: 273478 [Multi-domain]  Cd Length: 34  Bit Score: 45.54  E-value: 1.58e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1543644083 1256 ELPQTGEKQNVLLTVAGslVTMLGLAGLGFKRRKE 1290
Cdd:TIGR01167    1 KLPKTGESGNSLLLLLG--LLLLGLGGLLLRKRKK 33
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
191-248 4.86e-05

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 44.17  E-value: 4.86e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  191 EVEQLQ--KEQAKKIAQQAAELKAKNEKIAKENAEIAAKNKAEKERYEKEVAEYNKHKNE 248
Cdd:pfam07926   55 DIKALQalREELNELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEKRIED 114
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
85-253 4.89e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.15  E-value: 4.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083   85 SQPTKVEEVVSSeVTTENTPVVENNTTVSDETIGEAQPAEPIGKPTEIANPTASGNQAttiPKEFTTPELDQVVAEA--- 161
Cdd:TIGR02794   29 PEPGGGAEIIQA-VLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRA---AEQARQKELEQRAAAEkaa 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  162 ----QKDPNITIVEKPAEDLGNVSSKDLDAK-EKEVEQLQKEQAKKiaQQAAELKAKNEKIAKENAEIAAKN-----KAE 231
Cdd:TIGR02794  105 kqaeQAAKQAEEKQKQAEEAKAKQAAEAKAKaEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEAKKKaeaeaKAK 182
                          170       180
                   ....*....|....*....|..
gi 1543644083  232 KERYEKEVAEYNKHKNENGYVK 253
Cdd:TIGR02794  183 AEAEAKAKAEEAKAKAEAAKAK 204
KxYKxGKxW TIGR03715
KxYKxGKxW signal peptide; This model describes a novel form of signal peptide that occurs as ...
8-30 8.91e-05

KxYKxGKxW signal peptide; This model describes a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK and PEP-CTERM forms of signal peptide. This domain tends to occur on long, low-complexity (usually Serine-rich and heavily glycosylated) proteins of the Firmicutes, and (as with YSIRK) the majority of these proteins have the LPXTG cell wall-anchoring motif at the C-terminus.


Pssm-ID: 274741 [Multi-domain]  Cd Length: 23  Bit Score: 40.45  E-value: 8.91e-05
                           10        20
                   ....*....|....*....|...
gi 1543644083    8 KKRFKTYKAKKRWVTAPILFIGV 30
Cdd:TIGR03715    1 KKRYKMYKSGKHWVFAGIATLAL 23
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
119-257 1.87e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 45.74  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  119 EAQPAEPigKPTEIANPTASGNQATTIPKEFTTPELDQVVAEAQKDPNITI--------VEKPAEDLGNVSSKDLDAKEK 190
Cdd:PRK13108   292 VDEALER--EPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVtdevaaesVVQVADRDGESTPAVEETSEA 369
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1543644083  191 EVEQLQKEQAKkiAQQAAELKAKNEKIAKENAEIAAKNKAEKERYEKEVAEYNKHKNENGYVKEPVS 257
Cdd:PRK13108   370 DIEREQPGDLA--GQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAV 434
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
187-249 3.27e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.86  E-value: 3.27e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1543644083  187 AKEKEVEQLQKEQAKKIAQQAAELKAKNE-----KIAKENAE---IAAKNKAEKERYEKEVAEYNKHKNEN 249
Cdd:COG2268    287 EREREIELQEKEAEREEAELEADVRKPAEaekqaAEAEAEAEaeaIRAKGLAEAEGKRALAEAWNKLGDAA 357
rne PRK10811
ribonuclease E; Reviewed
18-176 4.20e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 45.03  E-value: 4.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083   18 KRWVTAPILFIGVLGVVGLATDDVQAAE--LDTQPGTTTVQPDNPDPQV--GSTTPKTAVSEEAAVQKDTTSQPTKVEEV 93
Cdd:PRK10811   840 KVWIRYPVVRPQDVQVEEQREAEEVQVQpvVAEVPVAAAVEPVVSAPVVeaVAEVVEEPVVVAEPQPEEVVVVETTHPEV 919
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083   94 VSSEVTTENTPVVENNTTVSDETIGEAQPA-EPIGKPTEIANPTASGNQATTIPKEFTTPELDQVVAEAQKDPNITIVEK 172
Cdd:PRK10811   920 IAAPVTEQPQVITESDVAVAQEVAEHAEPVvEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEP 999

                   ....
gi 1543644083  173 PAED 176
Cdd:PRK10811  1000 EVAP 1003
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
173-237 7.87e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 7.87e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1543644083  173 PAEDLGNVSSKDLDAKEKEVEQLQKEQAK----------KIAQQAAELKAKNEKIAKENAEIAAKNKAEKERYEK 237
Cdd:COG3883     13 FADPQIQAKQKELSELQAELEAAQAELDAlqaeleelneEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
187-241 8.40e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.26  E-value: 8.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1543644083  187 AKEKEVEQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAKNKAEKERYEKEVAE 241
Cdd:PRK09510   160 AKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAE 214
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
189-243 1.81e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.52  E-value: 1.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1543644083  189 EKEVEQLQkEQAKKIAQQAAELKAKNEKIAkenaEIAAKNKAEKERYEKEVAEYN 243
Cdd:pfam20492   40 EEERRQAE-EEAERLEQKRQEAEEEKERLE----ESAEMEAEEKEQLEAELAEAQ 89
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
180-248 2.33e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 2.33e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1543644083  180 VSSKDLDAKEKEVEQLQKEQAK---KIAQQAAELKAKNEKIAKENAEIaAKNKAEKERYEKEVAEYNKHKNE 248
Cdd:TIGR02169  713 DASRKIGEIEKEIEQLEQEEEKlkeRLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKLEEALND 783
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
185-244 3.45e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 3.45e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1543644083  185 LDAKEKEVEQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAKnKAEKERYEKEV-----AEYNK 244
Cdd:COG1579    119 IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL-EAEREELAAKIppellALYER 182
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
171-241 5.17e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 5.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1543644083  171 EKPAEDLGNVSSKDLDAKEKEvEQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAKNKAEKERYEKEVAE 241
Cdd:PRK09510   153 AKRAAAAAKKAAAEAKKKAEA-EAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAE 222
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
187-241 5.44e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 5.44e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1543644083  187 AKEKEVEQLQKEQAKKIAQQAAELKAKNEkiAKENAEIAAKNKAEKERYEKEVAE 241
Cdd:PRK09510   124 AKQAALKQKQAEEAAAKAAAAAKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAA 176
Nnf1 pfam03980
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ...
153-220 5.57e-03

Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is associated with the spindle poles and forms part of a kinetochore subcomplex called MIND.


Pssm-ID: 461118  Cd Length: 103  Bit Score: 37.61  E-value: 5.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1543644083  153 ELDQVVAEAQK-----DPNITIVEKPAEDLgnVSSKDLDAKEKEVEQLQKEQAKkiaqqaaeLKAKNEKIAKE 220
Cdd:pfam03980   37 ELDELIEEAKErreegEGPAWRPSVPPEEL--IRAHLAPYKQKQLEQLNARLQK--------LEAENAALAEE 99
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
184-255 7.17e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 7.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1543644083  184 DLDAKEKEVEQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAKNKAEKERYEKEVAEYN-----KHKNENGYVKEP 255
Cdd:COG0542    412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEeiqelKEELEQRYGKIP 488
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
159-241 7.96e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.21  E-value: 7.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  159 AEAQKDPNITIVEKPAEDLGNVSSKDLDAKEKEVEQLQKEQAKKIAqqAAELKAKNEKIAKENAEIA-AKNKAEKERYEK 237
Cdd:TIGR02794  130 AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA--EAEAKAKAEAEAKAKAEEAkAKAEAAKAKAAA 207

                   ....
gi 1543644083  238 EVAE 241
Cdd:TIGR02794  208 EAAA 211
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
188-241 8.03e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.24  E-value: 8.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1543644083  188 KEKEVEQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAKnKAEKERyEKEVAE 241
Cdd:COG2268    210 RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK-KAEERR-EAETAR 261
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
155-244 8.75e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.24  E-value: 8.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543644083  155 DQVVAEAQKDPNITIVEKpAEdlgnvSSKDLdAKEKEVEQLQKEQAKKIAQQAAEL-KAKNEKIAKENAEIAAKNK---- 229
Cdd:COG2268    222 EAEEAELEQEREIETARI-AE-----AEAEL-AKKKAEERREAETARAEAEAAYEIaEANAEREVQRQLEIAEREReiel 294
                           90
                   ....*....|....*
gi 1543644083  230 AEKERyEKEVAEYNK 244
Cdd:COG2268    295 QEKEA-EREEAELEA 308
 
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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