|
Name |
Accession |
Description |
Interval |
E-value |
| SHNi-TPR |
pfam10516 |
SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted ... |
542-579 |
4.64e-09 |
|
SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted form of TPR repeat.
Pssm-ID: 402238 [Multi-domain] Cd Length: 38 Bit Score: 52.45 E-value: 4.64e-09
10 20 30
....*....|....*....|....*....|....*...
gi 27262628 542 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAH 579
Cdd:pfam10516 1 ADVYDLLGEISLENENFPQAVTDLRKALELREELLPPE 38
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
540-616 |
5.53e-08 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 50.46 E-value: 5.53e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262628 540 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 616
Cdd:pfam13424 1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
542-644 |
1.36e-06 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 49.91 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 542 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRllaethyqLGLAYGYNSQYDEAVAQFSKSIEVIEN-RMAV 620
Cdd:COG4785 107 AEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLN--------RGIALYYLGRYELAIADLEKALELDPNdPERA 178
|
90 100
....*....|....*....|....
gi 27262628 621 LNEQVKEAEgssAEYKKEIEELKE 644
Cdd:COG4785 179 LWLYLAERK---LDPEKALALLLE 199
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
542-612 |
8.71e-06 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 49.22 E-value: 8.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262628 542 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllaetHYQLGLAYGYNSQYDEAVAQFSKSIE 612
Cdd:COG3914 146 AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEA--------LNNLGNALQDLGRLEEAIAAYRRALE 208
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
216-516 |
2.23e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 44.99 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 216 GAAPEGPNEAEVTSGKPEQEVPDAEEEKSVSGTDVQ--EECREKGGQEKQGEVivsieekPKEVSEEQPVVTlEKQGTAV 293
Cdd:TIGR00927 633 GDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEqeGETETKGENESEGEI-------PAERKGEQEGEG-EIEAKEA 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 294 EVEAESLDPTVKPVDVGGDEPEEKVVTSENEAGKAVLEQLVGQEvppAEESPEVTTEAAEASAVEAGSEVSEKPGQEApv 373
Cdd:TIGR00927 705 DHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGE---AEGKHEVETEGDRKETEHEGETEAEGKEDED-- 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 374 lpkdgavngpsvvgdqtpiEPQTSIERLTETKDGSGLEEKVRAKLVPSQEETKLSVEESEAAGDGVDTKVAQGATEKSPE 453
Cdd:TIGR00927 780 -------------------EGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAE 840
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262628 454 DKVQIAANEETQEREEQMKEGEETEGSEEDDKENDKTEEMpndsvlENKSLQENEEEEIGNLE 516
Cdd:TIGR00927 841 NQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEE------EEEEEEEEENEEPLSLE 897
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-516 |
2.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 141 EELREQVYDAMGEKEEAKKTEDKSLAKPETDKEQDSEMEKGGREdmdISKSAEEPQEKvdltlDWLTETSEEAKGGA--- 217
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---AKKKAEEKKKA-----DEAKKKAEEDKKKAdel 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 218 --APEGPNEAEVTSGKPEQEVPDAEEEKSVSGTDVQEECREKGGQEKQGEVIVSIEEKPKEVSEEQPVVTLEKQGTAVEV 295
Cdd:PTZ00121 1411 kkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 296 EAESLDPTVKPVDVGGDEPEEKVVTSENEAGKAVLEQLVGQEVPPAEESPEvtTEAAEASAVEAGSEVSEKPGQEAPVLP 375
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKKKADELKKAEELKKAEEKKKAEE 1568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 376 KDGAVNGPSVVGDQTPIEPQTSIERLTETKDGSGLEEKVRAKLVPSQEETKLSVEE----------SEAAGDGVDTKVAQ 445
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaeeekkkVEQLKKKEAEEKKK 1648
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262628 446 GATEKSPEDKVQIAANEETQEREEQMKEGEETEGSEEDDKENDKTEEMPNDSVLENKSLQENEEEEIGNLE 516
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
|
| TPR |
smart00028 |
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
584-616 |
2.23e-03 |
|
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.
Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 36.27 E-value: 2.23e-03
10 20 30
....*....|....*....|....*....|...
gi 27262628 584 AETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 616
Cdd:smart00028 1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33
|
|
| PRK02603 |
PRK02603 |
photosystem I assembly protein Ycf3; Provisional |
524-622 |
3.03e-03 |
|
photosystem I assembly protein Ycf3; Provisional
Pssm-ID: 179448 [Multi-domain] Cd Length: 172 Bit Score: 39.27 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 524 LAKIIFK----RQETKEAQLY-----AAQAHlklGEvsvesenYVQAVEEFQSCLNLQEqylEAHDRllAETHYQLGLAY 594
Cdd:PRK02603 18 MADLILKilpiNKKAKEAFVYyrdgmSAQAD---GE-------YAEALENYEEALKLEE---DPNDR--SYILYNMGIIY 82
|
90 100
....*....|....*....|....*...
gi 27262628 595 GYNSQYDEAVAQFSKSIEVIENRMAVLN 622
Cdd:PRK02603 83 ASNGEHDKALEYYHQALELNPKQPSALN 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
376-676 |
3.05e-03 |
|
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: 41.20 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 376 KDGAVNGPSVVGDQTPIEPQTSIERLTETKDgsGLEEKVRAKlvpSQEETKLSVEESEAAGDGVDT-KVAQGATEKSPED 454
Cdd:TIGR02168 657 PGGVITGGSAKTNSSILERRREIEELEEKIE--ELEEKIAEL---EKALAELRKELEELEEELEQLrKELEELSRQISAL 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 455 KVQIAANEETQEREEQMKEGEETEGSEEDDK--ENDKTEEMPNDSVLENKSLQENEEEEIGNLELAWdmldlakiifkrq 532
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEieELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL------------- 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 533 ETKEAQLYAAQAhlKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIE 612
Cdd:TIGR02168 799 KALREALDELRA--ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262628 613 VIENRMAVLNEQVKEAEgssAEYKKEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVE 676
Cdd:TIGR02168 877 ALLNERASLEEALALLR---SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SHNi-TPR |
pfam10516 |
SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted ... |
542-579 |
4.64e-09 |
|
SHNi-TPR; SHNi-TPR family members contain a reiterated sequence motif that is an interrupted form of TPR repeat.
Pssm-ID: 402238 [Multi-domain] Cd Length: 38 Bit Score: 52.45 E-value: 4.64e-09
10 20 30
....*....|....*....|....*....|....*...
gi 27262628 542 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAH 579
Cdd:pfam10516 1 ADVYDLLGEISLENENFPQAVTDLRKALELREELLPPE 38
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
540-616 |
5.53e-08 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 50.46 E-value: 5.53e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262628 540 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 616
Cdd:pfam13424 1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
542-644 |
1.36e-06 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 49.91 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 542 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRllaethyqLGLAYGYNSQYDEAVAQFSKSIEVIEN-RMAV 620
Cdd:COG4785 107 AEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLN--------RGIALYYLGRYELAIADLEKALELDPNdPERA 178
|
90 100
....*....|....*....|....
gi 27262628 621 LNEQVKEAEgssAEYKKEIEELKE 644
Cdd:COG4785 179 LWLYLAERK---LDPEKALALLLE 199
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
499-612 |
6.31e-06 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 47.99 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 499 LENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYlea 578
Cdd:COG4785 30 LFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDL--- 106
|
90 100 110
....*....|....*....|....*....|....
gi 27262628 579 hdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIE 612
Cdd:COG4785 107 -----AEAYNNRGLAYLLLGDYDAALEDFDRALE 135
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
542-612 |
8.71e-06 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 49.22 E-value: 8.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262628 542 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllaetHYQLGLAYGYNSQYDEAVAQFSKSIE 612
Cdd:COG3914 146 AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEA--------LNNLGNALQDLGRLEEAIAAYRRALE 208
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
516-648 |
9.15e-05 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 43.26 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 516 ELAWDMLDLAKIIFKRQETKEAQLYA----------AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllae 585
Cdd:COG4783 2 ACAEALYALAQALLLAGDYDEAEALLekaleldpdnPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEA------- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262628 586 tHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNE--QVKEAEGSSAEYKKEIEELKELLPE 648
Cdd:COG4783 75 -RLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRlaRAYRALGRPDEAIAALEKALELDPD 138
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
513-646 |
9.64e-05 |
|
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: 45.11 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 513 GNLELAWDMLDLAKIIFkrQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHdRLLAETHYQLGl 592
Cdd:COG2956 49 GNLYRRRGEYDRAIRIH--QKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEAL-RLLAEIYEQEG- 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 27262628 593 aygynsQYDEAVAQFSKSIEVIENRMAVLNEQVKEAEGSSaEYKKEIEELKELL 646
Cdd:COG2956 125 ------DWEKAIEVLERLLKLGPENAHAYCELAELYLEQG-DYDEAIEALEKAL 171
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
542-612 |
1.15e-04 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 44.61 E-value: 1.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262628 542 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYleahdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIE 612
Cdd:COG0457 8 AEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD--------AEALYNLGLAYLRLGRYEEALADYEQALE 70
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
216-516 |
2.23e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 44.99 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 216 GAAPEGPNEAEVTSGKPEQEVPDAEEEKSVSGTDVQ--EECREKGGQEKQGEVivsieekPKEVSEEQPVVTlEKQGTAV 293
Cdd:TIGR00927 633 GDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEqeGETETKGENESEGEI-------PAERKGEQEGEG-EIEAKEA 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 294 EVEAESLDPTVKPVDVGGDEPEEKVVTSENEAGKAVLEQLVGQEvppAEESPEVTTEAAEASAVEAGSEVSEKPGQEApv 373
Cdd:TIGR00927 705 DHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGE---AEGKHEVETEGDRKETEHEGETEAEGKEDED-- 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 374 lpkdgavngpsvvgdqtpiEPQTSIERLTETKDGSGLEEKVRAKLVPSQEETKLSVEESEAAGDGVDTKVAQGATEKSPE 453
Cdd:TIGR00927 780 -------------------EGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAE 840
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262628 454 DKVQIAANEETQEREEQMKEGEETEGSEEDDKENDKTEEMpndsvlENKSLQENEEEEIGNLE 516
Cdd:TIGR00927 841 NQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEE------EEEEEEEEENEEPLSLE 897
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
501-646 |
4.02e-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: 43.18 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 501 NKSLQENEEEEIGNLELAWD-----MLDLAKIIFKRQETKEAqlYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQY 575
Cdd:COG2956 66 QKLLERDPDRAEALLELAQDylkagLLDRAEELLEKLLELDP--DDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPEN 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262628 576 leahdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNE--QVKEAEGssaEYKKEIEELKELL 646
Cdd:COG2956 144 --------AHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLlaELYLEQG---DYEEAIAALERAL 205
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
514-661 |
5.75e-04 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 42.30 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 514 NLELAWDMLDLAKIIFKRQETKEA-QLYA---------AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYleahdrll 583
Cdd:COG0457 72 DPDDAEALNNLGLALQALGRYEEAlEDYDkaleldpddAEALYNLGLALLELGRYDEAIEAYERALELDPDD-------- 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262628 584 AETHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNEQVKEAEGSSAEYKKEIEELKELLPEIREKIEDAKESQR 661
Cdd:COG0457 144 ADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAE 221
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
491-622 |
6.85e-04 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 43.06 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 491 EEMPNDSVLENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEA-QLYA---------AQAHLKLGEVSVESENYVQ 560
Cdd:COG3914 51 LAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEAlALYRralalnpdnAEALFNLGNLLLALGRLEE 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262628 561 AVEEFQSCLNLQEQYLEAHdrllaethYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLN 622
Cdd:COG3914 131 ALAALRRALALNPDFAEAY--------LNLGEALRRLGRLEEAIAALRRALELDPDNAEALN 184
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
542-646 |
6.86e-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: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 542 AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHdRLLAETHYQLGLaygynsqYDEAVAQFSKSIEVIENRMAVL 621
Cdd:COG2956 42 VEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEAL-LELAQDYLKAGL-------LDRAEELLEKLLELDPDDAEAL 113
|
90 100
....*....|....*....|....*..
gi 27262628 622 NEQVK--EAEGssaEYKKEIEELKELL 646
Cdd:COG2956 114 RLLAEiyEQEG---DWEKAIEVLERLL 137
|
|
| TPR_1 |
pfam00515 |
Tetratricopeptide repeat; |
584-616 |
1.64e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 36.63 E-value: 1.64e-03
10 20 30
....*....|....*....|....*....|...
gi 27262628 584 AETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 616
Cdd:pfam00515 1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-516 |
2.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 141 EELREQVYDAMGEKEEAKKTEDKSLAKPETDKEQDSEMEKGGREdmdISKSAEEPQEKvdltlDWLTETSEEAKGGA--- 217
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---AKKKAEEKKKA-----DEAKKKAEEDKKKAdel 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 218 --APEGPNEAEVTSGKPEQEVPDAEEEKSVSGTDVQEECREKGGQEKQGEVIVSIEEKPKEVSEEQPVVTLEKQGTAVEV 295
Cdd:PTZ00121 1411 kkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 296 EAESLDPTVKPVDVGGDEPEEKVVTSENEAGKAVLEQLVGQEVPPAEESPEvtTEAAEASAVEAGSEVSEKPGQEAPVLP 375
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKKKADELKKAEELKKAEEKKKAEE 1568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 376 KDGAVNGPSVVGDQTPIEPQTSIERLTETKDGSGLEEKVRAKLVPSQEETKLSVEE----------SEAAGDGVDTKVAQ 445
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaeeekkkVEQLKKKEAEEKKK 1648
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262628 446 GATEKSPEDKVQIAANEETQEREEQMKEGEETEGSEEDDKENDKTEEMPNDSVLENKSLQENEEEEIGNLE 516
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
|
| TPR |
smart00028 |
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
584-616 |
2.23e-03 |
|
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.
Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 36.27 E-value: 2.23e-03
10 20 30
....*....|....*....|....*....|...
gi 27262628 584 AETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 616
Cdd:smart00028 1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
518-628 |
2.53e-03 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 38.83 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 518 AWDMLdlAKIIFKRQETKEA-QLYA---------AQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAhdrllaetH 587
Cdd:COG4235 19 GWLLL--GRAYLRLGRYDEAlAAYEkalrldpdnADALLDLAEALLAAGDTEEAEELLERALALDPDNPEA--------L 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 27262628 588 YQLGLAYGYNSQYDEAVAQFSKSIEVIEN--RMAVLNEQVKEA 628
Cdd:COG4235 89 YLLGLAAFQQGDYAEAIAAWQKLLALLPAdaPARLLEASIAEA 131
|
|
| PRK02603 |
PRK02603 |
photosystem I assembly protein Ycf3; Provisional |
524-622 |
3.03e-03 |
|
photosystem I assembly protein Ycf3; Provisional
Pssm-ID: 179448 [Multi-domain] Cd Length: 172 Bit Score: 39.27 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 524 LAKIIFK----RQETKEAQLY-----AAQAHlklGEvsvesenYVQAVEEFQSCLNLQEqylEAHDRllAETHYQLGLAY 594
Cdd:PRK02603 18 MADLILKilpiNKKAKEAFVYyrdgmSAQAD---GE-------YAEALENYEEALKLEE---DPNDR--SYILYNMGIIY 82
|
90 100
....*....|....*....|....*...
gi 27262628 595 GYNSQYDEAVAQFSKSIEVIENRMAVLN 622
Cdd:PRK02603 83 ASNGEHDKALEYYHQALELNPKQPSALN 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
376-676 |
3.05e-03 |
|
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: 41.20 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 376 KDGAVNGPSVVGDQTPIEPQTSIERLTETKDgsGLEEKVRAKlvpSQEETKLSVEESEAAGDGVDT-KVAQGATEKSPED 454
Cdd:TIGR02168 657 PGGVITGGSAKTNSSILERRREIEELEEKIE--ELEEKIAEL---EKALAELRKELEELEEELEQLrKELEELSRQISAL 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 455 KVQIAANEETQEREEQMKEGEETEGSEEDDK--ENDKTEEMPNDSVLENKSLQENEEEEIGNLELAWdmldlakiifkrq 532
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEieELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL------------- 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 533 ETKEAQLYAAQAhlKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIE 612
Cdd:TIGR02168 799 KALREALDELRA--ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262628 613 VIENRMAVLNEQVKEAEgssAEYKKEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVE 676
Cdd:TIGR02168 877 ALLNERASLEEALALLR---SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
524-644 |
3.55e-03 |
|
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: 40.10 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 524 LAKIIFKRQETKEAQLYAAQA----------HLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRlLAETHYQLGla 593
Cdd:COG2956 150 LAELYLEQGDYDEAIEALEKAlkldpdcaraLLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPR-LAELYEKLG-- 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 27262628 594 ygynsQYDEAVAQFSKSIEVIENRMAVLN--EQVKEAEGSSAEYKKEIEELKE 644
Cdd:COG2956 227 -----DPEEALELLRKALELDPSDDLLLAlaDLLERKEGLEAALALLERQLRR 274
|
|
| CpoB |
COG1729 |
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
540-609 |
3.73e-03 |
|
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 37.66 E-value: 3.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 540 YAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQyleahDRLLAETHYQLGLAYGYNSQYDEAVAQFSK 609
Cdd:COG1729 28 LAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPD-----SPKAPDALLKLGLSYLELGDYDKARATLEE 92
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
498-640 |
6.26e-03 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 38.02 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 498 VLENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYle 577
Cdd:COG5010 10 LPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNN-- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262628 578 ahdrllAETHYQLGLAYGYNSQYDEAVAQFSKSIE------VIENRMAVLNEQVKEAEGSSAEYKKEIE 640
Cdd:COG5010 88 ------PELYYNLALLYSRSGDKDEAKEYYEKALAlspdnpNAYSNLAALLLSLGQDDEAKAALQRALG 150
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
457-679 |
9.35e-03 |
|
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: 39.65 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 457 QIAANEETQEREEQMKEGEETEGSEEDDKENDKTEEMPNDSVLENKSLqENEEEEIGNLELAWDMLDLAKIIFKRQETKE 536
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL-ARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262628 537 AQlYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIEN 616
Cdd:TIGR02168 767 EE-RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262628 617 RMAVLNEQVKEAEGssaeykkEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVESST 679
Cdd:TIGR02168 846 QIEELSEDIESLAA-------EIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
|
| |
