|
Name |
Accession |
Description |
Interval |
E-value |
| Streccoc_I_II |
NF033804 |
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ... |
3-832 |
0e+00 |
|
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.
Pssm-ID: 468188 [Multi-domain] Cd Length: 1552 Bit Score: 1121.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 3 NKKEVYGFRKSKVAKTLCGAVLGTALIAFADKAVFADEVTETTSTSTVEVATTGNPATNLAEAQGDMSQAAKESQAKAGS 82
Cdd:NF033804 1 KKKEVYGFRKSKVAKTLCGAVLGAALIAVADQQVFADEVTETTSTTNVEVTTTGNPATNLPEAQGEASQAAKESQAQAGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 83 KDSALPVEVSSADLDKAVADAKTAGVKVVQDETKDKGTATTATENAQKQDEIKSDYAKQAEEIKTSTEAYKKAAATHQAE 162
Cdd:NF033804 81 KDGALPVEVSSADLDKAVKDAKSAGVNVVQDETVDKGTATTATENAQKQTEIKSDYAKQAEEIKKTTEAYKKEVAAHQAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 163 TDKINAENKAADDKYQKDLKSHQEEVEKINTANATAKAEYEAKLAQYQKDLATVKKANEDSQQDYQNKLSAYQTELARVQ 242
Cdd:NF033804 161 TDKINAENKAAKDKYQKDLKAHQAEVEKINTANATAKAEYEAKLAQYQKDLAAVQKANEDSQADYQNKLSAYQTELARVQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 243 KANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELAR 322
Cdd:NF033804 241 KANAEAKEAYDKAVKENTAKNAALQAENEAIKQRNETAKANYEAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 323 VQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEADLVAVKQANATNETDYQTKLAAYQTEL 402
Cdd:NF033804 321 VQKANADAKAAYEKAVEENTAKNTAIQAENEAIKQRNAAAKATYEAALKQYEADLAAVKKANAANEADYQAKLAAYQTEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 403 ARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAKTDYEAKLAKYEADLAKYKKEFAAYTAALAE------- 475
Cdd:NF033804 401 ARVQKANADAKAAYEKAVEDNKAKNAALQAENEAIKQRNAAAKADYEAKLAKYQADLAKYKKDLAEYPAKLKAyedeqak 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 476 -------AESKKKQDGYLSEPRSQSLNFKSEPNAIRTIDPS----------------VHQYGQQELDalVKSWGISPTNP 532
Cdd:NF033804 481 ikaalaeLEKKKNEDGYLSEPSAQSLVYDSEPNAQLSLTTDgkllkasavdeafkkdTAQYGKKNLQ--LDNLNVTNLEQ 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 533 DRTKSTAYSYFNAINSNNTYAKLV------------LEKDKPVDVTYTGLKNSSFNGKKISKVVYTYTLKETGFNDGT-K 599
Cdd:NF033804 559 ADATTSSVELYGNIGDKSDWTTNVgnktevkwgsvlLERGQSVTATYTNLQNSYYNGKKISKIVYKYTVDPSSKFKNPgK 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 600 MTMFASSDPTVTAWYNDY------FTSTNINVKVKFYDEEGQLMNLTGGLVNFSSLNRgngsgaiDKDAIESVRNFNGRY 673
Cdd:NF033804 639 VWLGIFTDPTLGVFASAYtgqvekDTSIFIKNEFTFYDENGQPINFDNALLSVASLNR-------EHNSIEMAKDYTGTF 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 674 IPISGSSIkIHENNSAYADSSNAEKSL--GARWNT-------SEWDTTSSPNNWYGAIVGEITQSEISFNMA-------- 736
Cdd:NF033804 712 VKISGSSI-GEKNGMIYATETLNFKKGqgGSRWTMyknsqpgSGWDSSDAPNSWYGAGAISMSGPNNSVTVGaisatnvm 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 737 --------------SSKSGNIWFAFNSNINAIGVP-------TKPVAPTAPTQPMYETEKPLEPAPVAPTYENEPTPPVK 795
Cdd:NF033804 791 psdempavpgrdntEGKKPNIWYSLNGKIRAVNVPkitkekpTPPVAPTAPQAPTYEVEKPLEPAPVAPTYENEPTPPVK 870
|
890 900 910
....*....|....*....|....*....|....*..
gi 577038606 796 TPDQPEPSKPEEPKYETEKPLEPAPVAPSYENEPTPP 832
Cdd:NF033804 871 TPDQPEPSKPEEPTYETEKPLEPAPVAPTYENEPTPP 907
|
|
| GbpC |
pfam08363 |
Glucan-binding protein C; This domain is found in the Streptococcus Glucan-binding protein C ... |
477-748 |
5.22e-43 |
|
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: 156.98 E-value: 5.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 477 ESKKKQDGYLSEPRSQSLNFKSEPNAIRTIDpsvhqygqQELDALVKSWGISPTNPDRTKSTAYSYFNAinsnntyaklv 556
Cdd:pfam08363 1 EKHKNEEGYVSEALAQALVFDNEPQAQLSAN--------TRNQIITKGTALLGGYSKILQSTGFDVYDA----------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 557 LEKDKPVDVTYTGLKNSSFNGKKISKVVYTYTLKETGFNDGtKMTMFASSDPTVTAWYN------DYFTSTNINVKVKFY 630
Cdd:pfam08363 62 LKKGQPVSVTYTNLQNASYNGKKISKVEYDYTVLSSPAGTG-AVNLVLFNDPTETIFAGantgngDKNTDIEIRMVIKFY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 631 DEEGQLMNLTG---GLVNFSSLNRGNGSgaidkDAIESVRNFNGRYIPISGSSIKIHENNSAYADSSNAEKSLGARWN-T 706
Cdd:pfam08363 141 DEDGKEILFSKenaFVFSLSSLNHNDEN-----IHLEFVKDSTGKFVKINGSSVQVHGNGKIYSTGDNDYGTNGADLNlP 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 577038606 707 SEWDTTSSPNNWYGAIVGEITQSEISF---NMASSKSGNIWFAFN 748
Cdd:pfam08363 216 SGWDTVSAKNAYYGAGVSVTSGNRITFtfgQGDSNLPGSIWFALN 260
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
263-779 |
5.81e-26 |
|
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: 115.19 E-value: 5.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 263 NEALQAENEAIKqrneTAKANYDAAMKQYEADLAAIKKAKEDNDADYQAklAAYQTELARVQKANADA-KAAYEKAVEEN 341
Cdd:NF033875 59 NPDPQSGSETPK----TAVSEEATVQKDTTSQPTKVEEVASEKNGAEQS--SATPNDTTNAQQPTVGAeKSAQEQPVVSP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 342 TAKNNAIQAENEAIKQRNATAKST----------YDAAMKKYEADL-VAVKQANATNETDYQTK-LAAYQTELARVQKAN 409
Cdd:NF033875 133 ETTNEPLGQPTEVAPAENEANKSTsipkefetpdVDKAVDEAKKDPnITVVEKPAEDLGNVSSKdLAAKEKEVDQLQKEQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 410 ADAKAAyekavednkaKNAALKAENEEIKQRNAVAKTDYEAKLAKYEADLAKYKKEfaaytaalaeaeskKKQDGYLSEP 489
Cdd:NF033875 213 AKKIAQ----------QAAELKAKNEKIAKENAEIAAKNKAEKERYEKEVAEYNKH--------------KNENGYVNEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 490 RSQSLNFKSEP----------NAIRTIDPS----VHQYGQQELDALVKSWGISPTNPDRTKStaYSYFNAINSNNTYAkL 555
Cdd:NF033875 269 ISKNLVFDQSVvtkdtkissiKGGKFIKATdfnkVNAGDSKDIFTKLSKDMGGKATGNFQNS--FVKEANLGSNGGYA-V 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 556 VLEKDKPVDVTYTGLkNSSFNGKKISKVVYTYTLKETGFNDGTkMTMFASSDPTVTAwyndYFTSTNINVK-------VK 628
Cdd:NF033875 346 LLEKNKPVTVTYTGL-NASYLGRKITKAEFVYELQSSPSQSGT-LNAVFSNDPIITA----FVGTNNVNGKdvktrltIK 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 629 FYDEEGQLMNLTGGLVNFSSLNRGNGSGAIDKDAIESVRNF--NGRYIPISGSSIKIHENNSAYADSSNAEKSLGARWNT 706
Cdd:NF033875 420 FFDASGKEVLPDKDSPFAYALSSLNSSLTNKGGHAEFVSDFgaNNAFKYINGSYVKKQADGKFYSPEDIDYGTGPSGLKN 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 707 SEWDTTSSPNNWYGAIVGEI-TQSEISFNMASSKSGN-------IWFAFNSNINAIGVptkpvaptaptQPMYETEKPLE 778
Cdd:NF033875 500 SDWDAVGHKNAYFGSGVGLAnTPGRISFSFGMTTKGKnvpvssaQWFAFSTNLNAKSI-----------KPYQNKGNPKE 568
|
.
gi 577038606 779 P 779
Cdd:NF033875 569 P 569
|
|
| Adhesin_P1_N |
pfam18652 |
Adhesin P1 N-terminal domain; The cariogenic bacterium Streptococcus mutans uses adhesin P1 to ... |
80-184 |
7.34e-22 |
|
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: 91.27 E-value: 7.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 80 AGSKDSALPVEVSSADLDKAVADAKTAGVKVVQDETKDKGTATTATENAQKQDEIKSDYAKQAEEIKTSTEAYKKAAATH 159
Cdd:pfam18652 2 AGDSTGGIEVAVDATDLDQAVKEAKDAGVKVTQDPTVDKGTATTAEEAAAKKAEIKADYAKQVKEIKEATAKYKAKKAAY 81
|
90 100
....*....|....*....|....*
gi 577038606 160 QAETDKINAENKAADDKYQKDLKSH 184
Cdd:pfam18652 82 DKKYDKIKAKNKADKEKYDKDLAAY 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
67-483 |
3.01e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 67 GDMSQAAKESQAKAGSKDSALPVEVSSADLDKAVADAKTAGVKVVQDETKDKGTATTATENAQKQDEIKSDYAKQAEEIK 146
Cdd:PTZ00121 1109 GKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVR 1188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 147 TSTEAYKKAAATHQAETDKINAENKAADDKYQKDLKShQEEVEKINTANataKAEYEAKLAQYQKDLATVKKANEDSQQD 226
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKK-AEAVKKAEEAK---KDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 227 YQNKLSAYQTELARvqKANaEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANyDAAMKQYEADL---AAIKKAKE 303
Cdd:PTZ00121 1265 FARRQAAIKAEEAR--KAD-ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKkadAAKKKAEE 1340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 304 DNDADyQAKLAAYQTELARVQKANADAKAAyEKAVEENTAKNNAIQAENEAIKQRNATAKStydAAMKKYEADLVAvKQA 383
Cdd:PTZ00121 1341 AKKAA-EAAKAEAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEKKKADEAKKK---AEEDKKKADELK-KAA 1414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 384 NATNETDYQTKLAAYQTELARVQKANADAKAAYE---KAVEDNKAKNAALKAEN----EEIKQRNAVAKTDYEAKL---- 452
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEakkKAEEAKKAEEAKKKAEEakkaDEAKKKAEEAKKADEAKKkaee 1494
|
410 420 430
....*....|....*....|....*....|.
gi 577038606 453 AKYEADLAKYKKEFAAYTAALAEAESKKKQD 483
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-461 |
7.47e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 139 AKQAEEIKTSTEAYKKAAATHQaetdkinaenkaaDDKYQKDLKSHQEEVEKINTANATAKAEY---EAKLAQYQKDLAT 215
Cdd:COG1196 212 AERYRELKEELKELEAELLLLK-------------LRELEAELEELEAELEELEAELEELEAELaelEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 216 VKKANEDSQQDYQNkLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQYEADL 295
Cdd:COG1196 279 LELELEEAQAEEYE-LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 296 AAIKKAKEDndadyQAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEA 375
Cdd:COG1196 358 AELAEAEEA-----LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 376 DLVAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAKTDYEAKLAKY 455
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
....*.
gi 577038606 456 EADLAK 461
Cdd:COG1196 513 ALLLAG 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-460 |
3.78e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 138 YAKQAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKYQKDLKSHQEEVEKINTANAtAKAEYEAKLAQYQKDLAtvk 217
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA-EEYELLAELARLEQDIA--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 218 kANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNEtAKANYDAAMKQYEADLAA 297
Cdd:COG1196 306 -RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE-ALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 298 IKKAKEDNDADyQAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAmkkyEADL 377
Cdd:COG1196 384 LAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL----EEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 378 VAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAKTDYEAKLAKYEA 457
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
...
gi 577038606 458 DLA 460
Cdd:COG1196 539 ALE 541
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
114-499 |
5.59e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 114 ETKDKGTATTATENAQKQDEI-KSDYAKQAEEIKTSTEAYKKAAATHQAETDKINAENKaaddKYQKDLKSHQEEVEKIN 192
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR----KFEEARMAHFARRQAAI 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 193 TANATAKAEyEAKLAQYQKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAK---EAYEKAVKENTEKNEALQAE 269
Cdd:PTZ00121 1273 KAEEARKAD-ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkkaDAAKKKAEEAKKAAEAAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 270 NEAIKQRNETAKANYDAAMKQYEADL----AAIKKAKEDNDADYQAKLAAYQTELARVQKANADAKAAYEKAVEENTAKN 345
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKkkadAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 346 NAIQAENEAIKQRNATAKSTYDAAMKKYEAdlvAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKA 425
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEE---AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038606 426 KNAALKAENEEIKQRNAVAKTDYEAKLAK--YEADLAKYKKEFAAYTAALAEAESKKKQDGYLSEPRSQSLNFKSE 499
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-483 |
2.51e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 101 ADAKTAGVKVVQDETKDKGT-ATTATENAQKQDEIKSDYAKQAEEIKTSTEAyKKAAATHQAETDKINAENKAADDKYQK 179
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEeAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK-KKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 180 ---DLKSHQEEVEKinTANATAKAEYEAKLAQYQKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAV 256
Cdd:PTZ00121 1399 kaeEDKKKADELKK--AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 257 KENTEKNEALQAENEA--IKQRNETAKANYDAAMKQYEADLA-------AIKKAKEDNDADyQAKLAAYQTELARVQKAN 327
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAeeAKKKADEAKKAAEAKKKADEAKKAeeakkadEAKKAEEAKKAD-EAKKAEEKKKADELKKAE 1555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 328 ADAKAAYEKAVEE-NTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEADLVAVKQANATNETDYQT----KLAAYQTEL 402
Cdd:PTZ00121 1556 ELKKAEEKKKAEEaKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelkKAEEEKKKV 1635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 403 ARVQKANADAKAAYE---KAVEDNKAKNAALKAENEEIKQRNAVAKTDYEAKLAKYEADLAKYKKEFAAYTAALAEAESK 479
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEelkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
....
gi 577038606 480 KKQD 483
Cdd:PTZ00121 1716 KKAE 1719
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
105-483 |
1.24e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 105 TAGVKVVQDETKDKgtATTATENAQKQDEIKSDYAKQAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKYQKDLKSH 184
Cdd:PTZ00121 1082 DAKEDNRADEATEE--AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 185 QEEVEKINTANataKAEyEAKLAQYQKDLATVKKANEDSQQDYQNKLSAYQ--TELARVQKANAEAKEAYEKAVKENTEK 262
Cdd:PTZ00121 1160 AEDARKAEEAR---KAE-DAKKAEAARKAEEVRKAEELRKAEDARKAEAARkaEEERKAEEARKAEDAKKAEAVKKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 263 NEALQAENEAIKQRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAayqtelaRVQKANADAKAAYEKAVEENT 342
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE-------EKKKADEAKKAEEKKKADEAK 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 343 AKNNAIQAENEAiKQRNATAKSTYDAAMKKYE----ADLVAVKQANATNETDYQTKLAAYQTELaRVQKANADAKAAYEK 418
Cdd:PTZ00121 1309 KKAEEAKKADEA-KKKAEEAKKKADAAKKKAEeakkAAEAAKAEAEAAADEAEAAEEKAEAAEK-KKEEAKKKADAAKKK 1386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038606 419 AVEDNKAKNAALKAEneEIKQRNAVAKTDYEAKlaKYEADLAKYKKEFAAYTAALAEAESKKKQD 483
Cdd:PTZ00121 1387 AEEKKKADEAKKKAE--EDKKKADELKKAAAAK--KKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
198-460 |
9.91e-11 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 65.35 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 198 AKAEYEAKLAQYQKD----LATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAI 273
Cdd:PRK05035 451 AKARFEARQARLEREkaarEARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQA 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 274 KQRNETAKANYDAAMKQyEADLAAIKKAKedndadyqAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENE 353
Cdd:PRK05035 531 RARQAEKQAAAAADPKK-AAVAAAIARAK--------AKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASA 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 354 AikqrNATAKSTYDAAMKKYEAdlvAVKQANAtnetdyqtkLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAE 433
Cdd:PRK05035 602 E----PEEQVAEVDPKKAAVAA---AIARAKA---------KKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQA 665
|
250 260
....*....|....*....|....*..
gi 577038606 434 NEEIKQRNAVAKTDYEAKLAKYEADLA 460
Cdd:PRK05035 666 NAEPEEAEDPKKAAVAAAIARAKAKKA 692
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
94-429 |
1.32e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 94 ADLDKAVADAKTAGVKVVQDETKDKGTATTATENAQKQDEIKSDY-AKQAEEIKTSTEAYKKAAATHQAETDKINAENKA 172
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 173 ADDKYQKD-LKSHQEEVEKINTANATAKAEYEAKLAQYQKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEA 251
Cdd:COG1196 319 EELEEELAeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 252 yEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAyQTELARVQKANADAK 331
Cdd:COG1196 399 -AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL-LELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 332 AAYEKAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEADLVAVKQANATNETDYQTKLAAYqTELARVQKANAD 411
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-LAAALQNIVVED 555
|
330
....*....|....*...
gi 577038606 412 AKAAyEKAVEDNKAKNAA 429
Cdd:COG1196 556 DEVA-AAAIEYLKAAKAG 572
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
261-463 |
3.12e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 57.27 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 261 EKNEALQAENEaiKQRNETAKANYDAamKQY------EADLAAIKKAKEDNDADYQAKLAAYQTELARVQKANADAKAAY 334
Cdd:PRK05035 434 AKAEIRAIEQE--KKKAEEAKARFEA--RQArlerekAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIK 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 335 EKAVEENTAKNNAIQAENEAIKQRNATA---------KSTYDAAMKKYEADLVAVKQANATNETDYQTKLAAYQTELARV 405
Cdd:PRK05035 510 AGARPDNSAVIAAREARKAQARARQAEKqaaaaadpkKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARA 589
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038606 406 ------QKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAKTDYEA---KLAKYEADLAKYK 463
Cdd:PRK05035 590 kakkaaQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPvdpRKAAVAAAIARAK 656
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
144-339 |
3.79e-08 |
|
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: 54.93 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 144 EIKTSTEAYKKAAATHQAETDKINAENKAAddkyQKDLKSHQEEVEKINTANATAKAEYE---AKLAQYQKDLATVKKAN 220
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEIEeveARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 221 EdsqqdyqnkLSAYQTELARVQKANAEAkeayEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQYEADLAAIKK 300
Cdd:COG1579 90 E---------YEALQKEIESLKRRISDL----EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 577038606 301 AkedndadyQAKLAAYQTELArvQKANADAKAAYEKAVE 339
Cdd:COG1579 157 E--------LEELEAEREELA--AKIPPELLALYERIRK 185
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
128-442 |
5.68e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 128 AQKQDEIKSDYAKQAEEIKtsteaykkaaathqaetdkinaenkaaddkyqkdlkshQEEVEKintanatAKAEYEAKLA 207
Cdd:PRK05035 440 AIEQEKKKAEEAKARFEAR--------------------------------------QARLER-------EKAAREARHK 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 208 QyqkdlATVKKANEDsqqdyQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAA 287
Cdd:PRK05035 475 K-----AAEARAAKD-----KDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAAD 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 288 MKQyEADLAAIKKAKedndadyqAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNATA---KS 364
Cdd:PRK05035 545 PKK-AAVAAAIARAK--------AKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVdpkKA 615
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038606 365 TYDAAMKKYEADLVAVKQANATNETDyQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNA 442
Cdd:PRK05035 616 AVAAAIARAKAKKAEQQANAEPEEPV-DPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKA 692
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-482 |
6.79e-08 |
|
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: 56.61 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 176 KYQkDLKSHQEEVEKinTANATAKAEYEAKLAQYQKDLATVkkanEDSQQDYQNKLSAYQTELARvqkANAEAKEAYEKA 255
Cdd:TIGR02169 212 RYQ-ALLKEKREYEG--YELLKEKEALERQKEAIERQLASL----EEELEKLTEEISELEKRLEE---IEQLLEELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 256 VKENTEKNEALQAENEAIKQRNETAKANYDAAMKQYEADLAAIKKAKEDNDAdYQAKLAAYQTELARVQKAnadaKAAYE 335
Cdd:TIGR02169 282 KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK-LLAEIEELEREIEEERKR----RDKLT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 336 KAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEaDLVAVKQANATNETDYQTKLAAYQTELARVQKANADAKAA 415
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038606 416 YEKAVEDNKAKNAALKAENEEIKQRNAVaKTDYEAKLAKYEADLAKYKKEFAAYTAALAEAESKKKQ 482
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLAAD-LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
|
| strep_RK_lipo |
TIGR03726 |
putative cross-wall-targeting lipoprotein signal; The YSIRK signal domain targets proteins to ... |
8-39 |
1.43e-07 |
|
putative cross-wall-targeting lipoprotein signal; The YSIRK signal domain targets proteins to the cross-wall, or septum, of dividing Gram-positive bacterial. Lipoprotein signal motifs direct a characteristic N-terminal cleavage and lipid modification for membrane anchoring. This Streptococcal-only signal peptide variant appears to be a hybrid between the two, likely directing protein targeting of nascent surface lipoproteins to the cross-wall. Nearly all members of this family have the characteristic LPXTG cell wall anchor signal at the C-terminus.
Pssm-ID: 274751 [Multi-domain] Cd Length: 34 Bit Score: 48.13 E-value: 1.43e-07
10 20 30
....*....|....*....|....*....|...
gi 577038606 8 YGFRKSKVAKTLCGAVLGTALIAFADKA-VFAD 39
Cdd:TIGR03726 1 YGFRKSKKYKTLCGAVLGTTVTAATAGTvVHAD 33
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
128-349 |
4.07e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.80 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 128 AQKQDEIKSDYAKQAEEIKtsteAYKKAAATHQAETDKINAENKAADDKYQKDLKSHQEEVEKINTANATA--KAEYEAK 205
Cdd:PRK05035 478 EARAAKDKDAVAAALARVK----AKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADpkKAAVAAA 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 206 LAQYQKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKqRNETAKANYD 285
Cdd:PRK05035 554 IARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIA-RAKAKKAEQQ 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038606 286 AAMKQYEAD-------LAAIKKAKedndadyqAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQ 349
Cdd:PRK05035 633 ANAEPEEPVdprkaavAAAIARAK--------ARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-440 |
5.37e-07 |
|
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 138 YAKQAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKyQKDLKSHQEEVEKINTANATAKAEYEAKLAQYQKDLATVK 217
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKA-LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 218 KANEDSQQDYQNkLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQYeadlaa 297
Cdd:TIGR02168 740 AEVEQLEERIAQ-LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL------ 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 298 ikKAKEDNDADYQAKLAAYQTELARVQKANADAkaayekavEENTAKNNAIQAENEAikqrnatAKSTYDAAMKKYEADL 377
Cdd:TIGR02168 813 --TLLNEEAANLRERLESLERRIAATERRLEDL--------EEQIEELSEDIESLAA-------EIEELEELIEELESEL 875
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038606 378 VAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKaKNAALKAENEEIKQR 440
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE-KLAQLELRLEGLEVR 937
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
175-419 |
6.01e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 175 DKYQKD-LKSHQEEVEKINTANATAKAEYEAKLAQYQKDLATVKKAN-----EDSQQDYQNKLSAYQTELARVQKANAEA 248
Cdd:COG3206 159 EAYLEQnLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 249 KEAYEKAVKENTEKNEALQAENE-----AIKQRNETAKANYDAAMKQYEADLAAIKKAkedndadyQAKLAAYQTEL-AR 322
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSARYTPNHPDVIAL--------RAQIAALRAQLqQE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 323 VQKANADAKAAYEKAveenTAKNNAIQAENEAIKQRNATakstydaaMKKYEADLVAVKQanatnetDYQTKLAAYQTEL 402
Cdd:COG3206 311 AQRILASLEAELEAL----QAREASLQAQLAQLEARLAE--------LPELEAELRRLER-------EVEVARELYESLL 371
|
250
....*....|....*..
gi 577038606 403 ARVQKANADAKAAYEKA 419
Cdd:COG3206 372 QRLEEARLAEALTVGNV 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
126-464 |
6.44e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 126 ENAQKQDEIK---SDYAKQAEEIKTSTeAYKkAAATHQAETDKINAENKAADdkYQKDLKSHQEEVEKINTAnATAKAEY 202
Cdd:PRK04863 241 ENRMTLEAIRvtqSDRDLFKHLITEST-NYV-AADYMRHANERRVHLEEALE--LRRELYTSRRQLAAEQYR-LVEMARE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 203 EAKLAQYQKDLATVKKANEDSQQ------DYQNKLSAYQTELARVQKANAEAKEayekAVKENTEKNEALQAENEAIKQR 276
Cdd:PRK04863 316 LAELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQADLEELEERLEEQNE----VVEEADEQQEENEARAEAAEEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 277 NETAK---ANY----DAAMK---QYEADLAAIKKAKE---------DNDADYQAKLAAYQTELA--------RVQKANAd 329
Cdd:PRK04863 392 VDELKsqlADYqqalDVQQTraiQYQQAVQALERAKQlcglpdltaDNAEDWLEEFQAKEQEATeellsleqKLSVAQA- 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 330 AKAAYEKA----------VEENTAKNNAIQAENEAIKQRNATAKstydaamkkyeadLVAVKQANATNETDYQTKLAAYQ 399
Cdd:PRK04863 471 AHSQFEQAyqlvrkiageVSRSEAWDVARELLRRLREQRHLAEQ-------------LQQLRMRLSELEQRLRQQQRAER 537
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038606 400 --TELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRnavaKTDYEAKLAKYEADLAKYKK 464
Cdd:PRK04863 538 llAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER----RMALRQQLEQLQARIQRLAA 600
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
194-426 |
8.99e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 194 ANATAKAEYEAKLAQYQKDLATVKK---ANEDSQQDYQNKLSAYQTELA----RVQKANAEAKEAyEKAVKENTEKNEAL 266
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKelaALKKEEKALLKQLAALERRIAalarRIRALEQELAAL-EAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 267 QAENEAikQRNETAKANYDAAMKQYEADLAAIKKAKEDNDA----DYQAKLAAYQTELARVQKANADAKAAYEKAVEENT 342
Cdd:COG4942 96 RAELEA--QKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 343 AKNNAIQAENEAIKQRNATAKSTYDAAMKKYEADLVAVKQANATNETDYQTklaaYQTELARVQKANAD-AKAAYEKAVE 421
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE----LEALIARLEAEAAAaAERTPAAGFA 249
|
....*
gi 577038606 422 DNKAK 426
Cdd:COG4942 250 ALKGK 254
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
112-431 |
1.24e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 112 QDETKDKGTATTATENAQKQdeiksdYAKQAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKYQK---DLKSHQEEV 188
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEH------YLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDmtlELKKHQEDI 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 189 EKINTANATAKAEYEA---KLAQYQKDLATVKKANEDSQQDYQNKLSAYQtELARVQKANAEAKEAYEKAVK-------- 257
Cdd:pfam05483 523 INCKKQEERMLKQIENleeKEMNLRDELESVREEFIQKGDEVKCKLDKSE-ENARSIEYEVLKKEKQMKILEnkcnnlkk 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 258 --ENTEKN-EALQAENEAIKQRN--ETAKAN-YDAAMKQYEADLAAIKKAKEDNDADYQAKLA----AYQTELARVQKAN 327
Cdd:pfam05483 602 qiENKNKNiEELHQENKALKKKGsaENKQLNaYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAK 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 328 ADAKAAYEKAVEENTAKNNAIqAENEAIKQRNataKSTYDAAMKKYEADLVAVK---QANATNETDYQTKLAAYQTELAR 404
Cdd:pfam05483 682 AIADEAVKLQKEIDKRCQHKI-AEMVALMEKH---KHQYDKIIEERDSELGLYKnkeQEQSSAKAALEIELSNIKAELLS 757
|
330 340
....*....|....*....|....*..
gi 577038606 405 VQKANADAKAAYEKAVEDNKAKNAALK 431
Cdd:pfam05483 758 LKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
240-443 |
1.31e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.35 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 240 RVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQyeadlaaiKKAKEDndadyQAKLAAYQTE 319
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ--------KKQAEE-----AAKQAALKQK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 320 LARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAMKKY---EADLVAVKQANATNETDYQTKLA 396
Cdd:PRK09510 133 QAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaeaEAAAKAAAEAKKKAEAEAKKKAA 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577038606 397 AYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAV 443
Cdd:PRK09510 213 AEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
250-463 |
1.50e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 250 EAYekaVKENTE-KNEALQAENEAIKQRNETAKANYDAAmkqyEADLAAIKKAKEDNDADYQAK-----LAAYQTELARV 323
Cdd:COG3206 159 EAY---LEQNLElRREEARKALEFLEEQLPELRKELEEA----EAALEEFRQKNGLVDLSEEAKlllqqLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 324 QKANADAKAAYEKAVEENTAKNNAIQAENE-----AIKQRNATAKSTYDAAMKKYEADLVAVKQANAtnetdyqtKLAAY 398
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSARYTPNHPDVIALRA--------QIAAL 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038606 399 QTEL-ARVQKANADAKAAYEKAvednKAKNAALKAENEEIKQRNAVA----------KTDYEAKLAKYEADLAKYK 463
Cdd:COG3206 304 RAQLqQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELpeleaelrrlEREVEVARELYESLLQRLE 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
141-369 |
2.19e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 141 QAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKY---QKDLKSHQEEVEKINTANATAKAEYEAKLAQYQKDLATVK 217
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 218 KANED-----------------SQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETA 280
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 281 KANYDAAMKQYEADLAAIKKAKedndADYQAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNA 360
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQL----AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
....*....
gi 577038606 361 TAKSTYDAA 369
Cdd:COG3883 253 GAAGAAAGS 261
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
128-453 |
2.20e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.51 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 128 AQKQDEIKSDYAKQAEEIKT--STEAYKKAAATHQAETDKI-NAENKAADDKYQKDLKSHQEEVEKINTANATAKAEYEA 204
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQelKLKEQAKKALEYYQLKEKLeLEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 205 KLAQYQKDLATVKK--ANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKA 282
Cdd:pfam02463 259 EIEKEEEKLAQVLKenKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 283 NYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRN--- 359
Cdd:pfam02463 339 ELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARqle 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 360 --ATAKSTYDAAMKKYEADLVAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEI 437
Cdd:pfam02463 419 dlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
330
....*....|....*.
gi 577038606 438 KQRNAVAKTDYEAKLA 453
Cdd:pfam02463 499 SQKESKARSGLKVLLA 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
64-387 |
2.21e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 64 EAQGDMSQAAKESQAKAGSKDSALPVEVSSADLDKAVADAKTAGvKVVQDETKDKGTATTATENAQKQDEI-KSDYAKQA 142
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELKKAEELKKAEEKkKAEEAKKA 1572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 143 EEIKTSteAYKKAAATHQAETDKINAENKA-ADDKYQKDLKSHQEEVEKINTANATAKAEYEAKLAQYQKDLA-TVKKAN 220
Cdd:PTZ00121 1573 EEDKNM--ALRKAEEAKKAEEARIEEVMKLyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeEKKKAE 1650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 221 EDSQQDYQNKLSAyqTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQYEadlaaIKK 300
Cdd:PTZ00121 1651 ELKKAEEENKIKA--AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE-----LKK 1723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 301 AKEDNDADYQAKLAAYQTELARVQKANADA----KAAYEKAVEENTAKNNAIQAE---NEAIKQRNATAKSTYDAAMKKY 373
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkKIAHLKKEEEKKAEEIRKEKEaviEEELDEEDEKRRMEVDKKIKDI 1803
|
330
....*....|....
gi 577038606 374 EADLVAVKQANATN 387
Cdd:PTZ00121 1804 FDNFANIIEGGKEG 1817
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-440 |
2.23e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 127 NAQKQDEIKSDYAKQAEEIKTSTEAYKKAAATHQAETDKINAENKAAD-DKYQKDLKSHQEEvekintanatakaeyeak 205
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEySWDEIDVASAERE------------------ 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 206 LAQYQKDLATVKKANEDsqqdyqnklsayqteLARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYD 285
Cdd:COG4913 670 IAELEAELERLDASSDD---------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 286 AAmkqyeadLAAIKKAKEDNDADYQAKLAAyqtelARVQKANADAKAAYEKAVEENTAKNNaiQAENEAIKQRNAtAKST 365
Cdd:COG4913 735 RL-------EAAEDLARLELRALLEERFAA-----ALGDAVERELRENLEERIDALRARLN--RAEEELERAMRA-FNRE 799
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577038606 366 YDAAMKKYEADLVAVkqanatneTDYQTKLAAYQTE-LARVQkanADAKAAYEKAVEDNKAK-NAALKAENEEIKQR 440
Cdd:COG4913 800 WPAETADLDADLESL--------PEYLALLDRLEEDgLPEYE---ERFKELLNENSIEFVADlLSKLRRAIREIKER 865
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
160-361 |
2.27e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 160 QAETDKIN------AENKAAddkyQKDLKSHQEEVEKINTANATAK------AEYEAKLAQYQKDLATVKKAN-EDSQQD 226
Cdd:PRK11281 42 QAQLDALNkqklleAEDKLV----QQDLEQTLALLDKIDRQKEETEqlkqqlAQAPAKLRQAQAELEALKDDNdEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 227 Y--------QNKLSAYQTELARVQKANAEA-------KEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQY 291
Cdd:PRK11281 118 LstlslrqlESRLAQTLDQLQNAQNDLAEYnsqlvslQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 292 EADLAAI-------KKAKEDNDA---------DY-QAKLAAYQTELARVQKA-NADAKAAYEKAVEE--NTAKNNAIQaE 351
Cdd:PRK11281 198 QAEQALLnaqndlqRKSLEGNTQlqdllqkqrDYlTARIQRLEHQLQLLQEAiNSKRLTLSEKTVQEaqSQDEAARIQ-A 276
|
250
....*....|
gi 577038606 352 NEAIKQRNAT 361
Cdd:PRK11281 277 NPLVAQELEI 286
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-466 |
3.21e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 259 NTEKNEALQAENEAIKQRNETAKANY---DAAMKQYEADLAAIKKAKEDNDAD-----YQAKLAAYQTELARVQKANADA 330
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSWDEidvasAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 331 KAAyEKAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEADLVAVKQANATNETDYQTKLAAYQTELArVQKANA 410
Cdd:COG4913 688 AAL-EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL-GDAVER 765
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038606 411 DAKAAYEKAVEDNKAKNAalKAENEEIKQRNAVAKT----------------DYEAKLAKYEAD-LAKYKKEF 466
Cdd:COG4913 766 ELRENLEERIDALRARLN--RAEEELERAMRAFNREwpaetadldadleslpEYLALLDRLEEDgLPEYEERF 836
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
216-460 |
8.90e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 216 VKKANEDSQ-QDYQ-----NKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEaikQRNEtAKANYDAAMK 289
Cdd:PHA02562 176 IRELNQQIQtLDMKidhiqQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIE---ELTD-ELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 290 QYEADLAAIKKAKedndADYQAKLAAYQTELArvqkanadakaAYEKAVEENTAKNNAIQAEN--EAIKQRNATAKSTYD 367
Cdd:PHA02562 252 DPSAALNKLNTAA----AKIKSKIEQFQKVIK-----------MYEKGGVCPTCTQQISEGPDriTKIKDKLKELQHSLE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 368 AAMKKYEADLVAVKQANA--TNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKqrnAVAK 445
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNEqsKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD---KIVK 393
|
250
....*....|....*
gi 577038606 446 TDYEAKLAKYEADLA 460
Cdd:PHA02562 394 TKSELVKEKYHRGIV 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
121-336 |
9.06e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 121 ATTATENAQKQDEIKSDYAKQAEEIKTSTEAYKKAAATHQAETDKINAENKAADdKYQKDLKSHQEEVEKINTANATAKA 200
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 201 EYEAKLAQYQKDLATVKKANE---------------------------DSQQDYQNKLSAYQTELARVQKANAEAKEAYE 253
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 254 KAVKENTEKNEALQAEneaiKQRNETAKANYDAAMKQYEADLAAIKKAKEdndaDYQAKLAAYQTELARVQKANADAKAA 333
Cdd:COG4942 178 ALLAELEEERAALEAL----KAERQKLLARLEKELAELAAELAELQQEAE----ELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 577038606 334 YEK 336
Cdd:COG4942 250 ALK 252
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
201-466 |
9.07e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.45 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 201 EYEAKLAQYQKDLatvkKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETA 280
Cdd:pfam12128 601 ELRERLDKAEEAL----QSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 281 KanydaamKQYEADLAAIKKAKEDNDADYQAKLAAYQTELarvqKANADAKAAYEKAVEEntAKNNAIQAENEAIKQRNA 360
Cdd:pfam12128 677 K-------DSANERLNSLEAQLKQLDKKHQAWLEEQKEQK----REARTEKQAYWQVVEG--ALDAQLALLKAAIAARRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 361 TAKSTYDAAMKKYEADLvAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQr 440
Cdd:pfam12128 744 GAKAELKALETWYKRDL-ASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIER- 821
|
250 260
....*....|....*....|....*.
gi 577038606 441 navAKTDYEAKLAKYEADLAKYKKEF 466
Cdd:pfam12128 822 ---AISELQQQLARLIADTKLRRAKL 844
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
179-370 |
1.36e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 179 KDLKSHQEEVEK----------INTANAT-AKAEYEAKLAQYQKDLATVKKAnEDSQQDYQNKLSAYQTELARVQKANAE 247
Cdd:COG4913 235 DDLERAHEALEDareqiellepIRELAERyAAARERLAELEYLRAALRLWFA-QRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 248 AKEAYEKAVKE-----------NTEKNEALQAENEAIKQRNETAK---ANYDAAMKQYEADLAAIKKAKEDNDADYQAKL 313
Cdd:COG4913 314 LEARLDALREEldeleaqirgnGGDRLEQLEREIERLERELEERErrrARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577038606 314 AAYQTELARVQKANADAKAAYEKAVEENTAknnaIQAENEAIKQRnataKSTYDAAM 370
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRE----LEAEIASLERR----KSNIPARL 442
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-461 |
1.50e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 249 KEAYEKAVKEnTEKNEALqaenEAIKQRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELARVQKANA 328
Cdd:COG4913 238 ERAHEALEDA-REQIELL----EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 329 DAKAAYEKAVEENTAKNNAIQAEN----EAIKQRNATAKSTYDAAMKK---YEADLVAVKQANATNETDY---QTKLAAY 398
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEERERRrarLEALLAALGLPLPASAEEFaalRAEAAAL 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038606 399 QTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRnavaKTDYEAKLAKYEADLAK 461
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR----KSNIPARLLALRDALAE 451
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
189-372 |
1.50e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.33 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 189 EKINTAN-ATAKAEYEAKLAQYQKDLATvKKANEDSQQDYQNKlsayqtELARVQKANAEAKEAYEKAVKENTEKNEALQ 267
Cdd:COG2268 196 EIIRDARiAEAEAERETEIAIAQANREA-EEAELEQEREIETA------RIAEAEAELAKKKAEERREAETARAEAEAAY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 268 AENEAIKQRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAA--YQTElarvQKANADAKAAYEKAveentakn 345
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAekQAAE----AEAEAEAEAIRAKG-------- 336
|
170 180
....*....|....*....|....*..
gi 577038606 346 naiQAENEAIKQRNATAKSTYDAAMKK 372
Cdd:COG2268 337 ---LAEAEGKRALAEAWNKLGDAAILL 360
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
55-304 |
3.00e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 47.70 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 55 TGNPATNLAEAQGDMSQAAKESQAKAGSKDSALP------VEVSSADLDKAVADAKTAGVKVVQDETKDKGTATTATE-- 126
Cdd:NF033838 134 TLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPtntyktLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAkv 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 127 -----NAQKQDEIKSDYAKQAEEIKTSTEAYKKAAATHQAET---DKINAENK-------AADDKYQKDLKSHQEEVEKI 191
Cdd:NF033838 214 eskkaEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATseqDKPKRRAKrgvlgepATPDKKENDAKSSDSSVGEE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 192 NTANATAKAEYEAKLAQYQKDLATvKKANEDSQQDYQN-KLSAYQTELARVQKANAEAKEAYEKAVKE------NTEKNE 264
Cdd:NF033838 294 TLPSPSLKPEKKVAEAEKKVEEAK-KKAKDQKEEDRRNyPTNTYKTLELEIAESDVKVKEAELELVKEeakeprNEEKIK 372
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 577038606 265 ALQAENE---AIKQRNETAKANYDAAMKQYEADLAAIKKAKED 304
Cdd:NF033838 373 QAKAKVEskkAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEK 415
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
121-464 |
3.10e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 47.66 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 121 ATTATENAQKQDEIKSDYAKQAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKYQKDLKSHQEEVEKINTANATAKA 200
Cdd:COG4995 122 LALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAALALLALLLAALAAALAAAAAALALL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 201 EYEAKLAQYQKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETA 280
Cdd:COG4995 202 LALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 281 KANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNA 360
Cdd:COG4995 282 LAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALAL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 361 TAKSTYDAAmkKYEADLVAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEI--- 437
Cdd:COG4995 362 ALLAALLLL--LAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIeyi 439
|
330 340
....*....|....*....|....*....
gi 577038606 438 --KQRNAVAKTDYEAKLAKYEADLAKYKK 464
Cdd:COG4995 440 ilPDRLYAFVQLYQLLIAPIEAELPGIKR 468
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
228-437 |
3.22e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 228 QNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQYEADLAAikkAKEDNDA 307
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAA---AKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 308 DYQAKLAAYQTELArVQKANADAKAayeKAVEENTAKnnaiqAENEAIKQRNATAKSTYDA-AMKKYEADLVAVKQANAT 386
Cdd:PRK09510 146 KAKAEAEAKRAAAA-AKKAAAEAKK---KAEAEAAKK-----AAAEAKKKAEAEAAAKAAAeAKKKAEAEAKKKAAAEAK 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577038606 387 NETDYQTKLAAyqtelarvQKANADAKAAYEKAVEDNKAKNAALKAENEEI 437
Cdd:PRK09510 217 KKAAAEAKAAA--------AKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
241-445 |
4.06e-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: 46.76 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 241 VQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRN-ETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTE 319
Cdd:TIGR02794 43 VDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEaEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 320 LARvQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEADLVAVKQANATNETD--------Y 391
Cdd:TIGR02794 123 EAK-AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEeakakaeaA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577038606 392 QTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAK 445
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGA 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
128-326 |
5.14e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 128 AQKQDEIKSDYAKQAEEIKTSTEAYKKAAATHQAETDKINAENKaaddkyQKDLKSHQEEVEKI-NTANATAKAEYEAKL 206
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE------ELQLEELEQEIAALlAEAGVEDEEELRAAL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 207 AQYQKDLATVKKANEDSQQdYQNKLSAYQTELARVQKANAEAK-EAYEKAVKENTEKNEALQAENEAIKQRNETAKAN-- 283
Cdd:COG4717 392 EQAEEYQELKEELEELEEQ-LEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDge 470
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577038606 284 YDAAMKQYEadlaaIKKAKEDNDADYQAKLAAYQTELARVQKA 326
Cdd:COG4717 471 LAELLQELE-----ELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
215-450 |
6.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 215 TVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIkqrnETAKANYDAAMKQYEAD 294
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI----AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 295 LAAIKKAKEDND-----------ADYQAKLAAYQTELARVQKANADAKAAyEKAVEENTAKNNAIQAENEAIKQRNATAK 363
Cdd:COG3883 92 ARALYRSGGSVSyldvllgsesfSDFLDRLSALSKIADADADLLEELKAD-KAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 364 STYDAAMKKYEADLVAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAV 443
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
....*..
gi 577038606 444 AKTDYEA 450
Cdd:COG3883 251 AAGAAGA 257
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
82-194 |
7.31e-05 |
|
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: 46.63 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 82 SKDSALPVEVSSADLDKAVADAKT-AGVKVVQDETKDKGT------ATTATENAQKQDEIKSDYAKQAEEIKTSTEAYKK 154
Cdd:NF033875 153 NKSTSIPKEFETPDVDKAVDEAKKdPNITVVEKPAEDLGNvsskdlAAKEKEVDQLQKEQAKKIAQQAAELKAKNEKIAK 232
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 577038606 155 aaathqaETDKINAENKAADDKYQKDL---KSHQEEVEKINTA 194
Cdd:NF033875 233 -------ENAEIAAKNKAEKERYEKEVaeyNKHKNENGYVNEA 268
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
760-832 |
7.60e-05 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 45.06 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 760 PVAPTAPTQPMYETE-------KPLEPAPVA-PTYENEPTPPVKTPDQPEPSKPEEPKYEtEKPLEPAPVAPSYENEPTP 831
Cdd:PRK10819 61 PQAVQPPPEPVVEPEpepepipEPPKEAPVViPKPEPKPKPKPKPKPKPVKKVEEQPKRE-VKPVEPRPASPFENTAPAR 139
|
.
gi 577038606 832 P 832
Cdd:PRK10819 140 P 140
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
763-832 |
7.66e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.62 E-value: 7.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 763 PTAPTQPMYETEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPEEPKYETEKPLEPAPVAPSYEnEPTPP 832
Cdd:PRK10263 768 PQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQ-QPQQP 836
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
113-315 |
7.82e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.95 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 113 DETKDKGTATTATENAQKQdeiksdyAKQAEEIKtstEAYKKAAATHQAETDKINAENKAADDKYQKdlkshqEEVEKIN 192
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQ-------AAEQERLK---QLEKERLAAQEQKKQAEEAAKQAALKQKQA------EEAAAKA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 193 TANATAKAEYEAKLAQyqkdlATVKKANEDSQQdyqnklsayQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEA 272
Cdd:PRK09510 142 AAAAKAKAEAEAKRAA-----AAAKKAAAEAKK---------KAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577038606 273 IKQRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAA 315
Cdd:PRK09510 208 KKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKA 250
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
178-367 |
8.31e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.95 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 178 QKDLKSHQEEVEKINTANATAKAEYEAKLAQYQKDLATVKKA--NEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKA 255
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAaqEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 256 VKENTEKNEALQAENEAIKQRNETAKANYDAAMKQyEADLAAIKKAKEDNDADYQAKLAAYQTELARvQKANADAKAAYE 335
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKK-KAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK-KKAAAEAKAAAA 228
|
170 180 190
....*....|....*....|....*....|..
gi 577038606 336 KAVEENTAKNNAIQAENEAIKQRNATAKSTYD 367
Cdd:PRK09510 229 KAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
217-397 |
9.56e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 217 KKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQYEAdla 296
Cdd:PRK09510 82 KKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAA--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 297 AIKKAKEDNDADYQAKLAAYQTELARvQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEAD 376
Cdd:PRK09510 159 AAKKAAAEAKKKAEAEAAKKAAAEAK-KKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAA 237
|
170 180
....*....|....*....|.
gi 577038606 377 LVAVKQANATNETDYQTKLAA 397
Cdd:PRK09510 238 AEKAAAAKAAEKAAAAKAAAE 258
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
136-440 |
1.04e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 136 SDYAKQAEEIKTSTEAYKKAAATHQAETDKINAEnkaaddkyQKDLKSHQEEVEKINTANATAKAEYEAKLAQYQKDLAT 215
Cdd:COG3096 271 ADYMRHANERRELSERALELRRELFGARRQLAEE--------QYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 216 VKKanedsqqdyQNKLSAYQTELARVQKANAEAKEayekAVKENTEKNEALQAENEAIKQRNETAK---ANYDAAMK--- 289
Cdd:COG3096 343 LRQ---------QEKIERYQEDLEELTERLEEQEE----VVEEAAEQLAEAEARLEAAEEEVDSLKsqlADYQQALDvqq 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 290 ----QYEADLAAIKKAKE---------DNDADYQAKLAAYQTELARV-----QKAN--ADAKAAYEKA----------VE 339
Cdd:COG3096 410 traiQYQQAVQALEKARAlcglpdltpENAEDYLAAFRAKEQQATEEvleleQKLSvaDAARRQFEKAyelvckiageVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 340 ENTAKNNAIQA-----ENEAIKQRNATAKSTYDAAMKKYEADLVAVKQANATN-----ETDYQTKLAAYQTEL-ARVQKA 408
Cdd:COG3096 490 RSQAWQTARELlrryrSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCqrigqQLDAAEELEELLAELeAQLEEL 569
|
330 340 350
....*....|....*....|....*....|..
gi 577038606 409 NADAKAAYEKAVEdnkaknaaLKAENEEIKQR 440
Cdd:COG3096 570 EEQAAEAVEQRSE--------LRQQLEQLRAR 593
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
757-832 |
1.08e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038606 757 PTKPVAPTAPtqPMYETEKPlepaPVAPTYENEPTPPVKTPDQPEPSKPEEPKYETEKPLEPAPVAPsyenEPTPP 832
Cdd:PHA03247 2872 AAKPAAPARP--PVRRLARP----AVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP----PPPPP 2937
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
285-482 |
1.09e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 285 DAAMKQYEADLAAIKKAKEDNDADY---QAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNAT 361
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELdalQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 362 AKSTyDAAMKKYEADLVAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRN 441
Cdd:COG3883 95 LYRS-GGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 577038606 442 AVAKTDYEAKLAKYEADLAKYKKEFAAYTAALAEAESKKKQ 482
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
143-455 |
1.15e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 143 EEIKTSTEAYKKAAAtHQAETD---KINAENKAADDKYQKDLKSHQEEVEKINTANATAKAEYEAKLAQYQKDLATVKKA 219
Cdd:pfam13868 32 KRIKAEEKEEERRLD-EMMEEErerALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 220 NEDSQQDYQNKLS---AYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAEneaiKQRNEtakanydaamKQYEADLA 296
Cdd:pfam13868 111 QEEDQAEAEEKLEkqrQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKE----KAERE----------EEREAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 297 AIKKAKEDNdadyQAKLAAYQtELARVQKANADAKAAyEKAVEENTAKN--NAIQAENEAIKQRNATAKSTYDAAMKKYE 374
Cdd:pfam13868 177 EIEEEKERE----IARLRAQQ-EKAQDEKAERDELRA-KLYQEEQERKErqKEREEAEKKARQRQELQQAREEQIELKER 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 375 ADLVAVKQANATNET---DYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAKTDYEAK 451
Cdd:pfam13868 251 RLAEEAEREEEEFERmlrKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRER 330
|
....
gi 577038606 452 LAKY 455
Cdd:pfam13868 331 IEEE 334
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
129-297 |
1.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 129 QKQDEIKSDYAKQAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKYQKDLKSHQEEVEKIntanatakaeyEAKLAQ 208
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEER-----------ERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 209 YQKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNE---ALQAENEAIKQRnetaKANYD 285
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelrELEAEIASLERR----KSNIP 439
|
170
....*....|..
gi 577038606 286 AAMKQYEADLAA 297
Cdd:COG4913 440 ARLLALRDALAE 451
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
137-404 |
1.77e-04 |
|
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: 44.45 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 137 DYAKQAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKYQKDLKSHQEEVEKINTANATAKAEYEAKLAQYQKdlatv 216
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQ----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 217 KKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKentEKNEALQAENEAIKQRNETAKANYDAAMKQYEADLA 296
Cdd:TIGR02794 119 KQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAK---AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 297 AIKKAKEdndadyqAKLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNATAKSTyDAAMKKYEAD 376
Cdd:TIGR02794 196 AKAEAAK-------AKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAA-GSEVDKYAAI 267
|
250 260
....*....|....*....|....*...
gi 577038606 377 LVAVKQANATNETDYQTKLAAYQTELAR 404
Cdd:TIGR02794 268 IQQAIQQNLYDDPSFRGKTCRLRIRLAP 295
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
223-402 |
2.43e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 223 SQQDYQNKLSAYQTelarvQKANaeakEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAA---MKQYEADLAAIK 299
Cdd:PRK11281 37 TEADVQAQLDALNK-----QKLL----EAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQApakLRQAQAELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 300 KakeDND------------ADYQAKLAAYQTELARVQKANADAKA-------AYEKAVEENTAKNNAIQAENEAIKQRNA 360
Cdd:PRK11281 108 D---DNDeetretlstlslRQLESRLAQTLDQLQNAQNDLAEYNSqlvslqtQPERAQAALYANSQRLQQIRNLLKGGKV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 577038606 361 TAKSTYDAAMKKYEADLVAVKQANatnetDYQTKLAAYQTEL 402
Cdd:PRK11281 185 GGKALRPSQRVLLQAEQALLNAQN-----DLQRKSLEGNTQL 221
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
762-832 |
3.28e-04 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 43.07 E-value: 3.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038606 762 APTAPTQPMYETEKPLEPAPVAPtyENEPTPPVKTPDQPEPSKPEEPKYETEKPLEPAPVAPSYENEPTPP 832
Cdd:PRK11633 77 AGDAAAPSLDPATVAPPNTPVEP--EPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAPKPEPKPVVEEKAAP 145
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
198-337 |
3.97e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.57 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 198 AKAEYEAKLAQYQ---KDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAkeayeKAVKENTEKNEALQAENEAIK 274
Cdd:pfam00529 66 QLAKAQAQVARLQaelDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQL-----AQAQIDLARRRVLAPIGGISR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577038606 275 QRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELARVQKANADAKAAYEKA 337
Cdd:pfam00529 141 ESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLA 203
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
140-466 |
4.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 140 KQAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKYQKDLKSHQEEVEKINTANATAKAEY---EAKLAQYQKDLATV 216
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELeeaQEELEELEEELEQL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 217 KKANEDSQQdyQNKLSAYQ-----------------------------------------TELARVQKANAEAKEAYEKA 255
Cdd:COG4717 233 ENELEAAAL--EERLKEARlllliaaallallglggsllsliltiagvlflvlgllallfLLLAREKASLGKEAEELQAL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 256 VKENTEKNEALQaenEAIKQRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELARV-QKANADAKAAY 334
Cdd:COG4717 311 PALEELEEEELE---ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlAEAGVEDEEEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 335 EKAVEEntaknnaiQAENEAIKQRNATAKSTYDAAMKKYEADLvavkqaNATNETDYQTKLAAYQTELArvqkanadaka 414
Cdd:COG4717 388 RAALEQ--------AEEYQELKEELEELEEQLEELLGELEELL------EALDEEELEEELEELEEELE----------- 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 577038606 415 AYEKAVEDNKAKNAALKAENEEIKQRNAVAKTdyEAKLAKYEADLAKYKKEF 466
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGELAEL--LQELEELKAELRELAEEW 492
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
292-465 |
4.14e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 292 EADLAAIKKAK--EDNDADYQAKLAAYQTELARVQKANADAkAAYEKAVEENTAKNNAIQAENEAIKQRNAT-AKSTYDA 368
Cdd:PRK11281 42 QAQLDALNKQKllEAEDKLVQQDLEQTLALLDKIDRQKEET-EQLKQQLAQAPAKLRQAQAELEALKDDNDEeTRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 369 A-MKKYEADLVAV--KQANATNE-TDYQTKLAAYQTELARVQKANADAKAAYEKAvednkakNAALKAENEEIKQRNAVA 444
Cdd:PRK11281 121 LsLRQLESRLAQTldQLQNAQNDlAEYNSQLVSLQTQPERAQAALYANSQRLQQI-------RNLLKGGKVGGKALRPSQ 193
|
170 180
....*....|....*....|.
gi 577038606 445 KTDYEAKLAKYEADLAKYKKE 465
Cdd:PRK11281 194 RVLLQAEQALLNAQNDLQRKS 214
|
|
| YfgM |
COG2976 |
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ... |
182-345 |
4.50e-04 |
|
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms];
Pssm-ID: 442215 [Multi-domain] Cd Length: 207 Bit Score: 42.15 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 182 KSHQEEvekintANATAKAEYEAKLAQYQ-KDLATVKKANEDSQQDYQNKLSAYQT--ELARVQ---KANAEAKEAYEKA 255
Cdd:COG2976 43 QSYQES------QAEEASALYEQLLEALAaGDAAAAAAAAEKLIDDYGGTAYAALAalLLAKAAvdaGDLDKAAAQLQWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 256 VKENteKNEALQAeneAIKQRnetaKANYDAAMKQYEADLAAIKKAKednDADYQAKLAAYQTELARVQKANADAKAAYE 335
Cdd:COG2976 117 LDNA--KDPALKA---LARLR----LARVLLAQKKYDEALATLDAVK---PEAFAALYAELRGDILLAQGDKAEARAAYQ 184
|
170
....*....|
gi 577038606 336 KAVEENTAKN 345
Cdd:COG2976 185 KALAALPEDA 194
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
286-480 |
4.67e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 286 AAMKQYEADLAAIKKAKEDNDADyQAKLAAYQTE-LARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNATAKS 364
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEAR-QARLEREKAArEARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 365 TYDAAMKKYEADLVAVKQANATNETDyqtklaayqtelarvqKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVA 444
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAA----------------AAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPK 578
|
170 180 190
....*....|....*....|....*....|....*.
gi 577038606 445 KTDYEAKLAKYEADLAKYKKEFAAYTAALAEAESKK 480
Cdd:PRK05035 579 KAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKK 614
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
204-327 |
5.72e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 204 AKLAQYQKDLATVKKANEDSQQD---YQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQ-RNET 279
Cdd:PRK09039 60 SQIAELADLLSLERQGNQDLQDSvanLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARaLAQV 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 577038606 280 AKANYD-AAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTEL--ARVQKAN 327
Cdd:PRK09039 140 ELLNQQiAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvALAQRVQ 190
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
186-483 |
5.91e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 186 EEVEKINTANATAKAEYEAKLAQYQKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVK--ENTEKN 263
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGkaEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 264 EALQAE-----NEAIKQRNETAKAN----------YDAAMKQYEADLAAIKKAKEDNDADYQAKLA--AYQTELAR---- 322
Cdd:PTZ00121 1107 ETGKAEearkaEEAKKKAEDARKAEearkaedarkAEEARKAEDAKRVEIARKAEDARKAEEARKAedAKKAEAARkaee 1186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 323 VQKANADAKAAYEKAVEENTAKNNAIQAEN--EAIKQRNATAKSTYDAAMKKYEADLVAVKQANATNETDYQTKLAAYQT 400
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEERKAEEarKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 401 ELARVQKANADAKAAYEKAVEDNKAKNAALKAEN----EEIKQRNAVAKTDYEAKL----AKYEADLAKYKKEFAAYTAA 472
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKKADEAKKAEEkkkaDEAKKKAEEAKKADEAKKkaeeAKKKADAAKKKAEEAKKAAE 1346
|
330
....*....|.
gi 577038606 473 LAEAESKKKQD 483
Cdd:PTZ00121 1347 AAKAEAEAAAD 1357
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
150-410 |
5.99e-04 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 43.44 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 150 EAYKKAAATHQAETDKINAENKAADDKYQKDLKSHQEEVEkintANATAKAEYEAKLAQYQKDLAtvkkANEDSQQDYQN 229
Cdd:COG3914 46 LLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAA----LLLQALGRYEEALALYRRALA----LNPDNAEALFN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 230 KLSAYQtelarVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNetakaNYDAAMKQYEadlAAIKKAKEDNDADY 309
Cdd:COG3914 118 LGNLLL-----ALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG-----RLEEAIAALR---RALELDPDNAEALN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 310 QakLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEADLVAVkQANATNET 389
Cdd:COG3914 185 N--LGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEELLAALARGPSELSPF-ALLYLPDD 261
|
250 260
....*....|....*....|.
gi 577038606 390 DYQTKLAAYQTELARVQKANA 410
Cdd:COG3914 262 DPAELLALARAWAQLVAAAAA 282
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
71-286 |
6.81e-04 |
|
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: 42.91 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 71 QAAKESQAKAGSKDSAlPVEVSSADLDKAVADAKTAGVKVVQDETKDKGTATTATENAQKQDEIKSDYAKQAEEIKTSTE 150
Cdd:TIGR02794 51 QANRIQQQKKPAAKKE-QERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 151 AYKKAAATHQAETDKI-NAENKAADD---KYQKDLKSHQEEVEKINTANATAKAEYEAKlAQYQKDLATVKKANEDSQQD 226
Cdd:TIGR02794 130 AEAKAKAEAEAERKAKeEAAKQAEEEakaKAAAEAKKKAEEAKKKAEAEAKAKAEAEAK-AKAEEAKAKAEAAKAKAAAE 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 227 YQNKlsayqtelARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDA 286
Cdd:TIGR02794 209 AAAK--------AEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| PHA03308 |
PHA03308 |
transcriptional regulator ICP4; Provisional |
766-824 |
6.91e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 165563 [Multi-domain] Cd Length: 1463 Bit Score: 43.64 E-value: 6.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038606 766 PTQPMYETEKPL-EPAPVAPtyENEPTPPVKTPDQP-EPSKPEEPKYET----EKPLEPAPVAPS 824
Cdd:PHA03308 830 PAVPETDRDNPLlPPCPITP--EGPPCPPREEPQQPqEPQEPQSPSFHIseigEALFHSTPVSPT 892
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
167-440 |
7.89e-04 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 42.41 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 167 NAENKAADDKYQKDLKSHQEEVE-KINTANA-TAKAEYEAKLAQYQKDLAtvkkANEDSQQdyqnklsaYQTELARVQKA 244
Cdd:COG2956 21 NGQPDKAIDLLEEALELDPETVEaHLALGNLyRRRGEYDRAIRIHQKLLE----RDPDRAE--------ALLELAQDYLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 245 N---AEAKEAYEKAVKENTEKNEALQaeneaikqrnetAKANYDAAMKQYEADLAAIKKAKEDNDADyqaklAAYQTELA 321
Cdd:COG2956 89 AgllDRAEELLEKLLELDPDDAEALR------------LLAEIYEQEGDWEKAIEVLERLLKLGPEN-----AHAYCELA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 322 RVQKANAD---AKAAYEKAVEEN--TAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEADL-VAVKQANATNETDYQTKL 395
Cdd:COG2956 152 ELYLEQGDydeAIEALEKALKLDpdCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLpALPRLAELYEKLGDPEEA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 577038606 396 AAYQTELARvQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQR 440
Cdd:COG2956 232 LELLRKALE-LDPSDDLLLALADLLERKEGLEAALALLERQLRRH 275
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
756-831 |
7.99e-04 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 42.83 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 756 VPTKPVAPTAPTQPMYETEKP-LEPAPVAPTYENEPTPPVKTPD---QPEPSKPE-EPKYETEKP-LEPAPVAPSYENEP 829
Cdd:NF033839 332 VKPQPEKPKPEVKPQLETPKPeVKPQPEKPKPEVKPQPEKPKPEvkpQPETPKPEvKPQPEKPKPeVKPQPEKPKPEVKP 411
|
..
gi 577038606 830 TP 831
Cdd:NF033839 412 QP 413
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
757-833 |
8.28e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 42.87 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 757 PTKPVAPTAPTQ-PMYETEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPE---EPKYETEKPLE-------PAPVAPSY 825
Cdd:PRK14950 365 APQPAKPTAAAPsPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRpvaPPVPHTPESAPkltraaiPVDEKPKY 444
|
....*...
gi 577038606 826 ENEPTPPE 833
Cdd:PRK14950 445 TPPAPPKE 452
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
757-832 |
8.29e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 8.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577038606 757 PTKPVAPTAPTQPmyeteKPLEPAPVAPtyenEPTPPVKTPDQPEPskPEEPKYETEKPLEPAPVAPSYENEPTPP 832
Cdd:PHA03247 2905 PERPPQPQAPPPP-----QPQPQPPPPP----QPQPPPPPPPRPQP--PLAPTTDPAGAGEPSGAVPQPWLGALVP 2969
|
|
| YfgM |
COG2976 |
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ... |
274-428 |
8.96e-04 |
|
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms];
Pssm-ID: 442215 [Multi-domain] Cd Length: 207 Bit Score: 41.38 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 274 KQRNETAKANYDAAMKQYEA-DLAAIKKAKEDNDADY----QAKLAAYQteLARVQ---KANADAKAAYEKAVEEntAKN 345
Cdd:COG2976 47 ESQAEEASALYEQLLEALAAgDAAAAAAAAEKLIDDYggtaYAALAALL--LAKAAvdaGDLDKAAAQLQWVLDN--AKD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 346 NAIQAeneAIKQRNATAKstydAAMKKYEAdlvAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKA 425
Cdd:COG2976 123 PALKA---LARLRLARVL----LAQKKYDE---ALATLDAVKPEAFAALYAELRGDILLAQGDKAEARAAYQKALAALPE 192
|
...
gi 577038606 426 KNA 428
Cdd:COG2976 193 DAP 195
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
185-463 |
1.16e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 185 QEEVEKINTANATAKAEYEAKLAQYQKDLATVKKANEDSQQDyQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNE 264
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREK-HEELEEKYKELSASSEELSEEKDALLAQRAAHEARIR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 265 ALQAENEAIKQRNETAKANYDAaMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELARVQKANADAKAAYEK-------- 336
Cdd:pfam07888 133 ELEEDIKTLTQRVLERETELER-MKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQrdtqvlql 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 337 --AVEENTAKNNAIQ---AENEAIKQRNATAKSTYDAAMKKYEA---DL-VAVKQANATNETDYQTKLAAYQTELA---- 403
Cdd:pfam07888 212 qdTITTLTQKLTTAHrkeAENEALLEELRSLQERLNASERKVEGlgeELsSMAAQRDRTQAELHQARLQAAQLTLQlada 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038606 404 ----RVQKAN-ADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAKTDYEaklaKYEADLAKYK 463
Cdd:pfam07888 292 slalREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE----KLEVELGREK 352
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
180-482 |
1.17e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 180 DLKSHQEEVEKINTANATAKAEYEAKL----AQYQKDLATVKKANEDSQQDYQNKLSAYQTEL--ARVQKANA-EAKEAY 252
Cdd:pfam01576 696 EMKTQLEELEDELQATEDAKLRLEVNMqalkAQFERDLQARDEQGEEKRRQLVKQVRELEAELedERKQRAQAvAAKKKL 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 253 EKAVKE-NTEKNEALQAENEAIKQRNETakanyDAAMKQYEADLAAIKKAKEDNDA----------DYQAKLAAYQTELA 321
Cdd:pfam01576 776 ELDLKElEAQIDAANKGREEAVKQLKKL-----QAQMKDLQRELEEARASRDEILAqskesekklkNLEAELLQLQEDLA 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 322 RVQKANADAKAAYEKAVEE---NTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEADLVAVKQANATNETdyqtklaaY 398
Cdd:pfam01576 851 ASERARRQAQQERDELADEiasGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQ--------L 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 399 QTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAKTDYEAKLAKYEADLAKYKKEFAAYTAALAEAES 478
Cdd:pfam01576 923 TTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEK 1002
|
....
gi 577038606 479 KKKQ 482
Cdd:pfam01576 1003 KLKE 1006
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
281-493 |
1.40e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 281 KANYDAAMKQYEADLAAiKKA---KEDNDADYQAKLAAYQTELARVQKANADAKAAYEKAVEEN-TAKNNAIQAENEAIK 356
Cdd:NF012221 1541 SQQADAVSKHAKQDDAA-QNAladKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNgQAQRDAILEESRAVT 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 357 QRNATAKSTYDAAMKkyeadlvavkQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAAlkaenEE 436
Cdd:NF012221 1620 KELTTLAQGLDALDS----------QATYAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQRHVD-----NQ 1684
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577038606 437 IKQRNAVAKTDY-----EAKLAKYEADL--AKYKKEFAAYTAALAEAESKK-KQDGYLSEPRSQS 493
Cdd:NF012221 1685 QKVKDAVAKSEAgvaqgEQNQANAEQDIddAKADAEKRKDDALAKQNEAQQaESDANAAANDAQS 1749
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
140-483 |
2.42e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 140 KQAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKYQKDLKSHQEEVEKINTANATAKAEYEAKLAQYQKDLATVKKA 219
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 220 NEDSQQDyQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRnETAKANYDAAMKQYEADLAAIK 299
Cdd:COG4372 86 NEQLQAA-QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL-QSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 300 KAKEDNDADYQAKLAAYQTELARVQKANADAKAAYEKAVEENTAKN-----NAIQAENEAIKQRNATAKSTYDAAMKKYE 374
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIeslprELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 375 ADLVAVKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAKTDYEAKLAK 454
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330 340
....*....|....*....|....*....
gi 577038606 455 YEADLAKYKKEFAAYTAALAEAESKKKQD 483
Cdd:COG4372 324 LAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
157-350 |
2.50e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 157 ATHQAETDKINAENKAADDKYQ----------KDLKSHQEEV---------EKINTANA-----TAKAEYEAKLAQYQKD 212
Cdd:PHA02562 198 KTYNKNIEEQRKKNGENIARKQnkydelveeaKTIKAEIEELtdellnlvmDIEDPSAAlnklnTAAAKIKSKIEQFQKV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 213 LATVKKANE---DSQQ--DYQNKLSAYQTELARVQKANAEAKEAYEKAVKENTEKNEALQAENEaIKQRNETAKANYDAA 287
Cdd:PHA02562 278 IKMYEKGGVcptCTQQisEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE-LKNKISTNKQSLITL 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038606 288 MKQYEADLAAIKKAKEDNdADYQAKLAAYQTELARVQKANAD-AKAAYEKAVEENTAKNNAIQA 350
Cdd:PHA02562 357 VDKAKKVKAAIEELQAEF-VDNAEELAKLQDELDKIVKTKSElVKEKYHRGIVTDLLKDSGIKA 419
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
282-440 |
2.69e-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: 40.29 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 282 ANYDAAMKQYEADLAAIKK---AKEDNDADYQAKLAAYQTELARVQKANADAKAAYEKAVEE--------NTAKNN---- 346
Cdd:COG1579 13 QELDSELDRLEHRLKELPAelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeqlGNVRNNkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 347 AIQAENEAIKQRNATAKSTYDAAMKKYEAdlvavkqanatnetdYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAK 426
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEE---------------LEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....
gi 577038606 427 NAALKAENEEIKQR 440
Cdd:COG1579 158 LEELEAEREELAAK 171
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
129-303 |
2.73e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 129 QKQDEIKSDYAKQAEEIKTSTEAYKKAAATHQAEtdkinaENKAADDKYQKDLKSHQEEVEKIntanatakaeyEAKLAQ 208
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKE------EIHKLRNEFEKELRERRNELQKL-----------EKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 209 YQKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAYEKAVKEnTEKNEALQAEnEAIKQ--RNETAKANYDA 286
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE-LERISGLTAE-EAKEIllEKVEEEARHEA 171
|
170 180
....*....|....*....|.
gi 577038606 287 A--MKQYE--ADLAAIKKAKE 303
Cdd:PRK12704 172 AvlIKEIEeeAKEEADKKAKE 192
|
|
| Ribonuc_P_40 |
pfam08584 |
Ribonuclease P 40kDa (Rpp40) subunit; The tRNA processing enzyme ribonuclease P (RNase P) ... |
538-599 |
2.74e-03 |
|
Ribonuclease P 40kDa (Rpp40) subunit; The tRNA processing enzyme ribonuclease P (RNase P) consists of an RNA molecule and at least eight protein subunits. Subunits hpop1, Rpp21, Rpp29, Rpp30, Rpp38, and Rpp40 (this entry) are involved in extensive, but weak, protein-protein interactions in the holoenzyme complex.
Pssm-ID: 462526 Cd Length: 277 Bit Score: 40.38 E-value: 2.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038606 538 TAYSYFNAINSNNTYA-----KLVLEKDKPvdvTY--TGL--KNSSFNGKKISKVVYTYTLKETGFNDGTK 599
Cdd:pfam08584 19 YALSYNTRIDSDNVVAllpngTLILSLDKD---TYerLGLegKPSRFGGRKKQRYVVELDLRDPSFLPGKK 86
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
239-354 |
2.96e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 41.01 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 239 ARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQ--RNETAKANYDAAMKQYEADLAAIK----KAKEDN---DADY 309
Cdd:PRK12472 190 ARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASlrKLERAKARADAELKRADKALAAAKtdeaKARAEErqqKAAQ 269
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 577038606 310 QAKLAAYQTELAR--VQKANADAKAAYEKAVEENTAKNNAIQAENEA 354
Cdd:PRK12472 270 QAAEAATQLDTAKadAEAKRAAAAATKEAAKAAAAKKAETAKAATDA 316
|
|
| FAP |
pfam07174 |
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ... |
745-832 |
3.00e-03 |
|
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.
Pssm-ID: 429334 Cd Length: 301 Bit Score: 40.68 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 745 FAFNSNINAIGVPTKPVAPTAPTQPmyeTEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPEEPkyetekplEPAPVAPs 824
Cdd:pfam07174 31 VALPAVAHADPEPAPPPPSTATAPP---APPPPPPAPAAPAPPPPPAAPNAPNAPPPPADPNAP--------PPPPADP- 98
|
....*...
gi 577038606 825 yeNEPTPP 832
Cdd:pfam07174 99 --NAPPPP 104
|
|
| THOC7 |
pfam05615 |
Tho complex subunit 7; The Tho complex is involved in transcription elongation and mRNA export ... |
205-298 |
3.01e-03 |
|
Tho complex subunit 7; The Tho complex is involved in transcription elongation and mRNA export from the nucleus.
Pssm-ID: 461692 [Multi-domain] Cd Length: 135 Bit Score: 38.79 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 205 KLAQYQKDLATVKKANEDSQQDYQNKLSAYQTELAR---VQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAK 281
Cdd:pfam05615 27 RFLKLCNSLDSTPEEIQALREDLLLDLAAFELSIEKsqlLAEANERERENYEAEKEEIEEEIEAVREEIEELKERLEEAK 106
|
90
....*....|....*..
gi 577038606 282 ANYDAAMKqYEADLAAI 298
Cdd:pfam05615 107 RTRKNREE-YDALAEKI 122
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
64-440 |
3.36e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 64 EAQGDMSQAAKESQAKAGSKD-SALPVEVSSADLDKAVADAKTAGVKVVQDETKDKGTATTATENAQKQDEIKSDYAKQA 142
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 143 EEIKTSTEAYKKAAATHQAETDKINAENKAADDKYQ------KDLKSHQEEV--------EKINTANATAK------AEY 202
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvdlGNAEDFLEELreerdelrEREAELEATLRtarervEEA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 203 EAKLA--------QYQKDLATVKKANEDSQQ--DYQNKLSAYQTELARVQKANAEAKEAYEKA-----VKENTEKNEALQ 267
Cdd:PRK02224 446 EALLEagkcpecgQPVEGSPHVETIEEDRERveELEAELEDLEEEVEEVEERLERAEDLVEAEdrierLEERREDLEELI 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 268 AENEA-IKQRNETA------KANYDAAMKQYEADLAAIKKAKEDND---ADYQAKLAAYQTELARVQK--ANADAKAAYE 335
Cdd:PRK02224 526 AERREtIEEKRERAeelrerAAELEAEAEEKREAAAEAEEEAEEAReevAELNSKLAELKERIESLERirTLLAAIADAE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 336 KAVEENTAKNNAIQAENEAIKQRNATAKSTYDAAMKKYEADLVAVKQANATNETDYQTKLAAYQTELaRVQKANADAKAA 415
Cdd:PRK02224 606 DEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDEL-REERDDLQAEIG 684
|
410 420
....*....|....*....|....*
gi 577038606 416 yekAVEDNKAKNAALKAENEEIKQR 440
Cdd:PRK02224 685 ---AVENELEELEELRERREALENR 706
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
756-831 |
4.08e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 40.52 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 756 VPTKPVAPTAPTQPMYETEKP-LEPAPVAPTYENEPTPPVKTPD-QPEPSKPE-EPKYETEKP---LEPAPVAPSYENEP 829
Cdd:NF033839 387 VKPQPEKPKPEVKPQPEKPKPeVKPQPEKPKPEVKPQPEKPKPEvKPQPEKPKpEVKPQPEKPkpeVKPQPETPKPEVKP 466
|
..
gi 577038606 830 TP 831
Cdd:NF033839 467 QP 468
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
239-353 |
4.20e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.03 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 239 ARVQKANAEAKEAYEKAVKENTEKNEALQAENEAIKQRNETAKANYDAAMKQYEADLAAIKK---AKEDNDaDYQAKLAA 315
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKgavSQQELD-EARAALDA 159
|
90 100 110
....*....|....*....|....*....|....*...
gi 577038606 316 YQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENE 353
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAA 197
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
757-825 |
4.25e-03 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 39.60 E-value: 4.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577038606 757 PTKPVAPTAPTQPMYETEKPLEPAPVAPTyenePTPPVKTPDQPEPSKPEEPKYETEKPLE--PAPVAPSY 825
Cdd:PRK11633 84 SLDPATVAPPNTPVEPEPAPVEPPKPKPV----EKPKPKPKPQQKVEAPPAPKPEPKPVVEekAAPTGKAY 150
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
125-305 |
4.88e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 125 TENAQKQDEIKSDYAKQAEEIKTSTEAYKKAAATHQAETDKINAENKAADDKYQKDLKSHQ--EEVEKINTANATAKAEY 202
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKqaEEAAAKAAAAAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 203 EAKLAQY--QKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAK-----EAYEKAVKENTEKNEALQAENEAIKQ 275
Cdd:PRK09510 152 EAKRAAAaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKkkaeaEAKKKAAAEAKKKAAAEAKAAAAKAA 231
|
170 180 190
....*....|....*....|....*....|
gi 577038606 276 RNETAKANYDAAMKQYEADLAAIKKAKEDN 305
Cdd:PRK09510 232 AEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
108-460 |
4.94e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 108 VKVVQDETKDKGTATTATENAQKQDEIK----SDYAKQAEEIKTSTEAYKKAAATHQAE-------TDKINAENKAADDK 176
Cdd:COG5185 186 LGLLKGISELKKAEPSGTVNSIKESETGnlgsESTLLEKAKEIINIEEALKGFQDPESEledlaqtSDKLEKLVEQNTDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 177 YQKDLKSHQEEVEKINTANATAKAEYEA---KLAQYQKDLATVKKANEDSQQDYQNKLSAYQTELAR-VQKANAEAKEAY 252
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENtkeKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKReTETGIQNLTAEI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 253 EKAVKENTEKNEALQAENEAI--KQRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELARVQKANADA 330
Cdd:COG5185 346 EQGQESLTENLEAIKEEIENIvgEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEEL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 331 KAAYEKAVEENTAKNNAIqaeNEAIKQRNATAKSTYDAAMKKYEADLVAVKQANATNETDYQTKLAAYQTELARVQKANA 410
Cdd:COG5185 426 QRQIEQATSSNEEVSKLL---NELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLE 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577038606 411 DAKAAYEKAVE---------DNKAKNAALKAENEEIKQRN-----AVAKTDYEAKLAKYEADLA 460
Cdd:COG5185 503 KLRAKLERQLEgvrskldqvAESLKDFMRARGYAHILALEnlipaSELIQASNAKTDGQAANLR 566
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
305-406 |
5.57e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 39.93 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 305 NDADYQAKLAAYQTELARVQKANADAKAAYEKAveentaknnaiqaenEAIKQRNATAKSTYDAAMKKYEADLVAVKQAN 384
Cdd:COG0845 55 DPPDLQAALAQAQAQLAAAQAQLELAKAELERY---------------KALLKKGAVSQQELDQAKAALDQAQAALAAAQ 119
|
90 100
....*....|....*....|..
gi 577038606 385 AtnetdyqtKLAAYQTELARVQ 406
Cdd:COG0845 120 A--------ALEQARANLAYTT 133
|
|
| PRK14948 |
PRK14948 |
DNA polymerase III subunit gamma/tau; |
748-825 |
5.69e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237862 [Multi-domain] Cd Length: 620 Bit Score: 40.33 E-value: 5.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577038606 748 NSNINAIGVPTKPVAPTAPTQPMYETEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPEEPKYETEKPLEPAPVAPSY 825
Cdd:PRK14948 362 SAFISEIANASAPANPTPAPNPSPPPAPIQPSAPKTKQAATTPSPPPAKASPPIPVPAEPTEPSPTPPANAANAPPSL 439
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
312-464 |
6.05e-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: 39.14 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 312 KLAAYQTELARVQKANADAKAAYEKAVEENTAKNNAIQAENEAIKQ------RNATAKSTYDAAMKKYEADLVAV---KQ 382
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlekeikRLELEIEEVEARIKKYEEQLGNVrnnKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 383 ANA-TNETDYQTK--------LAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAKTDYEAKLA 453
Cdd:COG1579 91 YEAlQKEIESLKRrisdledeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
170
....*....|..
gi 577038606 454 KYEADL-AKYKK 464
Cdd:COG1579 171 KIPPELlALYER 182
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
756-831 |
6.31e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 40.14 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 756 VPTKPVAPTAPTQPMYETEKP-LEPAPVAPTYENEPTPPVKTPD-QPEPSKPE-EPKYETEKP---LEPAPVAPSYENEP 829
Cdd:NF033839 398 VKPQPEKPKPEVKPQPEKPKPeVKPQPEKPKPEVKPQPEKPKPEvKPQPEKPKpEVKPQPETPkpeVKPQPEKPKPEVKP 477
|
..
gi 577038606 830 TP 831
Cdd:NF033839 478 QP 479
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
199-304 |
6.49e-03 |
|
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: 37.62 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 199 KAEYEAKLAQYQKDLATVKKANEDSQQDYQNKLSAYQTELARVQKANAEAKEAyEKAVKENTEKNEALQAENEAIKQRNE 278
Cdd:pfam07926 17 AADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELNEL-KAEIAELKAEAESAKAELEESEESWE 95
|
90 100
....*....|....*....|....*.
gi 577038606 279 TAKanydaamKQYEADLAAIKKAKED 304
Cdd:pfam07926 96 EQK-------KELEKELSELEKRIED 114
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
300-431 |
9.22e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 39.32 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 300 KAKEDNDADYQAKLAAYQTELARVQKANADAKAAYekaveentaknnaiqaeneaikqrnATAKSTYDAAMKKYEADLVA 379
Cdd:TIGR04320 250 PNPPNSLAALQAKLATAQADLAAAQTALNTAQAAL-------------------------TSAQTAYAAAQAALATAQKE 304
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 577038606 380 VKQANATNETDYQTKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALK 431
Cdd:TIGR04320 305 LANAQAQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
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|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
255-450 |
9.97e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.09 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 255 AVKENTEKNEALqaENEAIKQRNE-TAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQTELARVQKANADAKAA 333
Cdd:COG2268 175 AITDLEDENNYL--DALGRRKIAEiIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577038606 334 YEKAVEENTAKNNAIQAENEAIKQRnatakstydaamkkyeadlvAVKQANATNETDYQTKLAAYQTELAR-------VQ 406
Cdd:COG2268 253 ERREAETARAEAEAAYEIAEANAER--------------------EVQRQLEIAEREREIELQEKEAEREEaeleadvRK 312
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 577038606 407 KANADAKAAYEKAVEDNKAKNAALKAENEEIKQRNAVAKTDYEA 450
Cdd:COG2268 313 PAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDA 356
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