|
Name |
Accession |
Description |
Interval |
E-value |
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1368-1699 |
7.04e-13 |
|
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: 71.30 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1368 WLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPdyQSFWTFLHL 1447
Cdd:COG2956 11 WYFKGLNYLLNGQ------PDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDP--DRAEALLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1448 -ESTFEEKDYvcERMVEFLMGAAKREISDIlsfqllEALLFRVQLHIFTGRCQSALAVLQNALKLANDAIVAEYLktddr 1526
Cdd:COG2956 83 aQDYLKAGLL--DRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1527 clawLAYIHLiefnslpsklydpsnanpsrivntepfvmpwqaAQDvktNPDLLLAVFEDAVKACTDetltsgerievCL 1606
Cdd:COG2956 150 ----LAELYL---------------------------------EQG---DYDEAIEALEKALKLDPD-----------CA 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1607 PLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYhLCKFFIL 1686
Cdd:COG2956 179 RALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA-LADLLER 257
|
330
....*....|...
gi 568967337 1687 QDGGDKLLPVLRQ 1699
Cdd:COG2956 258 KEGLEAALALLER 270
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
827-1001 |
4.94e-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: 50.92 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 827 TKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSANRMFLKKLQEQIHRVQQR 906
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 907 VTIKKaltlkygEELARAKAVASKeLGKRKLEQDRLGPN------KMMRLDNSpISSPRKHSAELIAMEKRRLQKLEYEY 980
Cdd:COG4942 99 LEAQK-------EELAELLRALYR-LGRQPPLALLLSPEdfldavRRLQYLKY-LAPARREQAEELRADLAELAALRAEL 169
|
170 180
....*....|....*....|.
gi 568967337 981 ALKIQKLKEARALKAKEQQNL 1001
Cdd:COG4942 170 EAERAELEALLAELEEERAAL 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
738-1010 |
5.70e-06 |
|
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: 51.60 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 738 LESMIKEARRTAEQASKpkvppKSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEM 817
Cdd:TIGR02168 710 LEEELEQLRKELEELSR-----QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 818 --------DGIGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSAN 889
Cdd:TIGR02168 785 eeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 890 RMFLKKLQEQIHRVQQRVtikkaltlkygEELARAKAVASKELGKRKLEQDRLGpNKMMRLDNSpisspRKHSAELIAME 969
Cdd:TIGR02168 865 EELIEELESELEALLNER-----------ASLEEALALLRSELEELSEELRELE-SKRSELRRE-----LEELREKLAQL 927
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568967337 970 KRRLQKLEYEYALKIQKLKEARALKAKEQQNLVPVVEEEPE 1010
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
|
| zf-C3H1 |
pfam10650 |
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ... |
1189-1208 |
9.32e-06 |
|
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger domain as it contains three conserved Cs and an H in the C-x8-C-x5-C-x3-H conformation typical of a zinc-finger.
Pssm-ID: 431418 Cd Length: 22 Bit Score: 43.72 E-value: 9.32e-06
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
743-1080 |
1.61e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 743 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRliKSDQLKTSSSSPANSDVEMDGIGR 822
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK--KADELKKAEELKKAEEKKKAEEAK 1570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 823 IAMVTKQVADAEAKLKKhKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKlTEQLQAAEKILSANRMFLKKLQEQihr 902
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEE--- 1645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 903 vqqrvtIKKALTLKYGEELARAKavasKELGKRKLEQDRLGPNKMMRLDNSpisspRKHSAELIAMEKRRLQKLEYEYAL 982
Cdd:PTZ00121 1646 ------KKKAEELKKAEEENKIK----AAEEAKKAEEDKKKAEEAKKAEED-----EKKAAEALKKEAEEAKKAEELKKK 1710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 983 KIQKLKEARALKAKEQQNLVPVVEEEPEFSVPQPSLHDLTQDKltldtEENDVDDEVLSGASRERRRSFLESNSFTKPNL 1062
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE-----EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
330
....*....|....*...
gi 568967337 1063 KHTDTPNKECINKLSKST 1080
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDI 1803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
744-1097 |
1.80e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 744 EARRTAEQASKPKVPPKseKENDPLRTPEA----LPEEKKMEYRLLKEEIANREKQRLIKSDQLKTSssspANSDVEMDG 819
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDK--KKADELKKAAAakkkADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK----AEEAKKAEE 1461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 820 IGRIAMVTKQVADAEAKLKKHKilliKDESVLKNLvlQEAKKK--ESVRNAEAKitKLTEQLQAAEKILSANRmfLKKLQ 897
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAK----KADEAKKKA--EEAKKKadEAKKAAEAK--KKADEAKKAEEAKKADE--AKKAE 1531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 898 E--QIHRVQQRVTIKKALTLKYGEELARAKAVASKELGKRKLEQDRLGPNK---MMRLDNSPISSPRKHSAELIAMEKRR 972
Cdd:PTZ00121 1532 EakKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 973 LQKLEyEYALKIQKLKEARALKAKEQQNLVPVVEEEPEfsvpqpslhdltQDKLTLDTEENDVDDEVLSGASRERRRSFL 1052
Cdd:PTZ00121 1612 AKKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK------------AEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568967337 1053 ESNSFTKPNLKHTDTPNKECINKLSKSTVEKPELFLGLKIGELQK 1097
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
737-1035 |
1.60e-04 |
|
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: 46.43 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 737 GLESMIKEARRTAEQaSKPKVPPKSEKENDPLRTPEALPEEKKMeyrLLKEEIANREKQRLIKSDqLKTSSSSPANSDVE 816
Cdd:pfam07888 77 ELESRVAELKEELRQ-SREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEED-IKTLTQRVLERETE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 817 MDGIG-RIAMVTKQVADAEAKLKKHKILLIKDESVLKNLV--LQEAKKKESVRNAEA-----KITKLTEQLQAAEKILSA 888
Cdd:pfam07888 152 LERMKeRAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSkeFQELRNSLAQRDTQVlqlqdTITTLTQKLTTAHRKEAE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 889 NRMFLKKL---QEQIHRVQQRVTIkkaltlkYGEELAraKAVASKELGKRKLEQDRLGPNKM----------MRLDNSPI 955
Cdd:pfam07888 232 NEALLEELrslQERLNASERKVEG-------LGEELS--SMAAQRDRTQAELHQARLQAAQLtlqladaslaLREGRARW 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 956 SSPRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAK--------EQQNLVPVVEEEPEFSVPQPSLHDLTQDKLT 1027
Cdd:pfam07888 303 AQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKlevelgreKDCNRVQLSESRRELQELKASLRVAQKEKEQ 382
|
....*...
gi 568967337 1028 LDTEENDV 1035
Cdd:pfam07888 383 LQAEKQEL 390
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
201-998 |
2.81e-04 |
|
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: 46.12 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 201 RKSSKSFGRSPSRKQNHSSKSENCAEETFEDLLLKYKQIQLELEciNKDEKLALSSKEETAQEdpKTLHLEDQTSTDNAS 280
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK--LQEEELKLLAKEEEELK--SELLKLERRKVDDEE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 281 ITKDPSKEVAPEEKTQVKTFQAFELKpLRQKLTLPGDKNRVKRGKDGTRQLSLKSSTtdASQGLEDKEQNLTRRLSASDI 360
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEEL-EKELKELEIKREAEEEEEEELEKLQEKLEQ--LEEELLAKKKLESERLSSAAK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 361 VSEKKLGEEEEELSelqlrllALQSASKKWQQKEQQVMKESKEKLTKTKTaQQKAKTSTKAHSAKKVSATAKQALRKQQT 440
Cdd:pfam02463 392 LKEEELELKSEEEK-------EAQLLLELARQLEDLLKEEKKEELEILEE-EEESIELKQGKLTEEKEELEKQELKLLKD 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 441 KAWKKLQQQKEQERQKEEDQRKHAEEEERRKREEEIRKirdLSNQEEQYNRFMKLVGGKRRARSKSSDPDLRRSLEKQSD 520
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK---ESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 521 SAGGIYQYDNYEEVAMDTDSETsspaAPSPVQPPFFPECSLGYFSSAPSVSLPPPAQVSSVPSLNQPYGEGLCVSLDPLP 600
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEE----RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 601 PLPPLPPLPPEDPEQPPKPPFADEEEEEEMLLREEllKSLASKRAFKpeETSSNSDPPSPPVLNNSQPLSRSNLSIVSIN 680
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG--VSLEEGLAEK--SEVKASLSELTKELLEIQELQEKAESELAKE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 681 TV-SQPRIQNPKFHRGPRLPRTVISLPKHKSVVVTLNDSDDSESDGEASKSTNSVFGG-LESMIKEARRTAEQASKPKVP 758
Cdd:pfam02463 693 EIlRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEeEEKSRLKKEEKEEEKSELSLK 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 759 PKSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRLIK------SDQLKTSSSSPANSDVEMDGIGRIAMVTKQVAD 832
Cdd:pfam02463 773 EKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEaelleeEQLLIEQEEKIKEEELEELALELKEEQKLEKLA 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 833 AEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSANRMflkkLQEQIHRVQQRVTIKKA 912
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL----LEEKENEIEERIKEEAE 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 913 LTLKYGEELARAKAVASKElgKRKLEQDRLGPNKMMRLDNSPISSPRKHSAELIaMEKRRLQKLEYEYALKIQKLKEARA 992
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADE--KEKEENNKEEEEERNKRLLLAKEELGKVNLMAI-EEFEEKEERYNKDELEKERLEEEKK 1005
|
....*.
gi 568967337 993 LKAKEQ 998
Cdd:pfam02463 1006 KLIRAI 1011
|
|
| ACL4-like |
cd24142 |
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ... |
1621-1671 |
3.90e-04 |
|
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.
Pssm-ID: 467942 [Multi-domain] Cd Length: 306 Bit Score: 44.54 E-value: 3.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568967337 1621 RYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNP 1671
Cdd:cd24142 15 NFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
1354-1682 |
5.03e-04 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 45.07 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1354 LEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVE 1433
Cdd:TIGR02917 556 LEKAAELNPQEIEPALALAQYYLGKGQ------LKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1434 YAPD-----------YQSF------WTFLHLESTFEEKDYVCERMVEFLMGAAKREISDILSFQLLE------ALLFRV- 1489
Cdd:TIGR02917 630 LQPDsalalllladaYAVMknyakaITSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQkqhpkaALGFELe 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1490 -QLHIFTGRCQSALAVLQNALKLANDAIVAEYL-----------KTDDRCLAWLAyihliefnslpsklyDPSNANPSRI 1557
Cdd:TIGR02917 710 gDLYLRQKDYPAAIQAYRKALKRAPSSQNAIKLhrallasgntaEAVKTLEAWLK---------------THPNDAVLRT 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1558 VNTEPFVMPWQAAQDVKtnpdlllaVFEDAVKACTDetltsgerievclplytNMIALHQL----LERYE-EAVELCTSL 1632
Cdd:TIGR02917 775 ALAELYLAQKDYDKAIK--------HYQTVVKKAPD-----------------NAVVLNNLawlyLELKDpRALEYAERA 829
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568967337 1633 LESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCK 1682
Cdd:TIGR02917 830 LKLAPNIPAILDTLGWLLVEKGEADRALPLLRKAVNIAPEAAAIRYHLAL 879
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
1608-1661 |
6.53e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 37.37 E-value: 6.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967337 1608 LYTNMIALHQLLERYEEAVELCTSLLESC--------PTNCQLLETLAALYLKTDRYDKARR 1661
Cdd:pfam13424 5 ALNNLAAVLRRLGRYDEALELLEKALEIArrllgpdhPLTATTLLNLGRLYLELGRYEEALE 66
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1368-1699 |
7.04e-13 |
|
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: 71.30 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1368 WLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPdyQSFWTFLHL 1447
Cdd:COG2956 11 WYFKGLNYLLNGQ------PDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDP--DRAEALLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1448 -ESTFEEKDYvcERMVEFLMGAAKREISDIlsfqllEALLFRVQLHIFTGRCQSALAVLQNALKLANDAIVAEYLktddr 1526
Cdd:COG2956 83 aQDYLKAGLL--DRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1527 clawLAYIHLiefnslpsklydpsnanpsrivntepfvmpwqaAQDvktNPDLLLAVFEDAVKACTDetltsgerievCL 1606
Cdd:COG2956 150 ----LAELYL---------------------------------EQG---DYDEAIEALEKALKLDPD-----------CA 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1607 PLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYhLCKFFIL 1686
Cdd:COG2956 179 RALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA-LADLLER 257
|
330
....*....|...
gi 568967337 1687 QDGGDKLLPVLRQ 1699
Cdd:COG2956 258 KEGLEAALALLER 270
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
1351-1445 |
1.31e-10 |
|
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: 60.79 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1351 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1430
Cdd:COG4235 3 IARLRQALAANPNDAEGWLLLGRAYLRLGR------YDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLER 76
|
90
....*....|....*
gi 568967337 1431 AVEYAPDYQSFWTFL 1445
Cdd:COG4235 77 ALALDPDNPEALYLL 91
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
1567-1699 |
8.47e-09 |
|
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: 56.51 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1567 WQAAQDVKTNPDLLLAVFEDAVKACTDETLTSGERIEVCLPLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETL 1646
Cdd:COG5010 15 LLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568967337 1647 AALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCKFFILQDGGDKLLPVLRQ 1699
Cdd:COG5010 95 ALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQR 147
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1576-1701 |
1.03e-07 |
|
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: 55.51 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1576 NPDLLLAVFEDAVKACTDEtltsgerievcLPLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDR 1655
Cdd:COG2956 23 QPDKAIDLLEEALELDPET-----------VEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGL 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568967337 1656 YDKARRVWLTAFENNPQNAEIFYHLCKFFILQDGGDKLLPVLRQFV 1701
Cdd:COG2956 92 LDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLL 137
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1609-1699 |
2.40e-07 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 53.86 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1609 YTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCKFFILQD 1688
Cdd:COG0457 79 LNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLG 158
|
90
....*....|.
gi 568967337 1689 GGDKLLPVLRQ 1699
Cdd:COG0457 159 RYEEALELLEK 169
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1605-1691 |
4.65e-07 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 55.00 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1605 CLPLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCkfF 1684
Cdd:COG3914 111 NAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLG--N 188
|
....*..
gi 568967337 1685 ILQDGGD 1691
Cdd:COG3914 189 ALQDLGR 195
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1606-1691 |
4.81e-07 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 55.00 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1606 LPLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCkfFI 1685
Cdd:COG3914 146 AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLL--FA 223
|
....*.
gi 568967337 1686 LQDGGD 1691
Cdd:COG3914 224 LRQACD 229
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1609-1680 |
6.71e-07 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 52.70 E-value: 6.71e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967337 1609 YTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHL 1680
Cdd:COG0457 45 LYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNL 116
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1605-1699 |
1.22e-06 |
|
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: 49.81 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1605 CLPLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCKFF 1684
Cdd:COG4783 3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82
|
90
....*....|....*
gi 568967337 1685 ILQDGGDKLLPVLRQ 1699
Cdd:COG4783 83 LKAGDYDEALALLEK 97
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1614-1724 |
1.26e-06 |
|
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: 52.04 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1614 ALHQLL-ERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCKFFILQDGGDK 1692
Cdd:COG2956 15 GLNYLLnGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDR 94
|
90 100 110
....*....|....*....|....*....|..
gi 568967337 1693 LLPVLRQFVGsffkpgfEKYSNVDLFRYLLNI 1724
Cdd:COG2956 95 AEELLEKLLE-------LDPDDAEALRLLAEI 119
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1351-1521 |
1.45e-06 |
|
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: 52.04 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1351 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1430
Cdd:COG2956 96 EELLEKLLELDPDDAEALRLLAEIYEQEGD------WEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1431 AVEYAPDYQSFWTFL-HLEstFEEKDYvcERMVEFLMGAAKREISDilsfqlLEALLFRVQLHIFTGRCQSALAVLQNAL 1509
Cdd:COG2956 170 ALKLDPDCARALLLLaELY--LEQGDY--EEAIAALERALEQDPDY------LPALPRLAELYEKLGDPEEALELLRKAL 239
|
170
....*....|..
gi 568967337 1510 KLANDAIVAEYL 1521
Cdd:COG2956 240 ELDPSDDLLLAL 251
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1609-1680 |
2.27e-06 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 51.16 E-value: 2.27e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967337 1609 YTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHL 1680
Cdd:COG0457 11 YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNL 82
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1610-1680 |
2.30e-06 |
|
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: 49.03 E-value: 2.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967337 1610 TNMIALHQL------LERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHL 1680
Cdd:COG4783 36 DNPEAFALLgeillqLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRL 112
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1351-1536 |
3.55e-06 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 50.39 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1351 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1430
Cdd:COG0457 62 LADYEQALELDPDDAEALNNLGLALQALGR------YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYER 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1431 AVEYAPDYQSFWT----FLHLESTFEEKDYVCERMVEFLMGAAKREISDILSFQLLEALLFRVQLHIFTGRCQSALAVLQ 1506
Cdd:COG0457 136 ALELDPDDADALYnlgiALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILT 215
|
170 180 190
....*....|....*....|....*....|
gi 568967337 1507 NALKLANDAIVAEYLKTDDRCLAWLAYIHL 1536
Cdd:COG0457 216 LAALAELLLLALALLLALRLAALALYQYRA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
827-1001 |
4.94e-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: 50.92 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 827 TKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSANRMFLKKLQEQIHRVQQR 906
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 907 VTIKKaltlkygEELARAKAVASKeLGKRKLEQDRLGPN------KMMRLDNSpISSPRKHSAELIAMEKRRLQKLEYEY 980
Cdd:COG4942 99 LEAQK-------EELAELLRALYR-LGRQPPLALLLSPEdfldavRRLQYLKY-LAPARREQAEELRADLAELAALRAEL 169
|
170 180
....*....|....*....|.
gi 568967337 981 ALKIQKLKEARALKAKEQQNL 1001
Cdd:COG4942 170 EAERAELEALLAELEEERAAL 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
738-1010 |
5.70e-06 |
|
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: 51.60 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 738 LESMIKEARRTAEQASKpkvppKSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEM 817
Cdd:TIGR02168 710 LEEELEQLRKELEELSR-----QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 818 --------DGIGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSAN 889
Cdd:TIGR02168 785 eeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 890 RMFLKKLQEQIHRVQQRVtikkaltlkygEELARAKAVASKELGKRKLEQDRLGpNKMMRLDNSpisspRKHSAELIAME 969
Cdd:TIGR02168 865 EELIEELESELEALLNER-----------ASLEEALALLRSELEELSEELRELE-SKRSELRRE-----LEELREKLAQL 927
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568967337 970 KRRLQKLEYEYALKIQKLKEARALKAKEQQNLVPVVEEEPE 1010
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
|
| zf-C3H1 |
pfam10650 |
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ... |
1189-1208 |
9.32e-06 |
|
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger domain as it contains three conserved Cs and an H in the C-x8-C-x5-C-x3-H conformation typical of a zinc-finger.
Pssm-ID: 431418 Cd Length: 22 Bit Score: 43.72 E-value: 9.32e-06
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1351-1438 |
1.39e-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: 46.72 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1351 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1430
Cdd:COG4783 58 IVLLHEALELDPDEPEARLNLGLALLKAGD------YDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEK 131
|
....*...
gi 568967337 1431 AVEYAPDY 1438
Cdd:COG4783 132 ALELDPDD 139
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
743-1080 |
1.61e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 743 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRliKSDQLKTSSSSPANSDVEMDGIGR 822
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK--KADELKKAEELKKAEEKKKAEEAK 1570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 823 IAMVTKQVADAEAKLKKhKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKlTEQLQAAEKILSANRMFLKKLQEQihr 902
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEE--- 1645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 903 vqqrvtIKKALTLKYGEELARAKavasKELGKRKLEQDRLGPNKMMRLDNSpisspRKHSAELIAMEKRRLQKLEYEYAL 982
Cdd:PTZ00121 1646 ------KKKAEELKKAEEENKIK----AAEEAKKAEEDKKKAEEAKKAEED-----EKKAAEALKKEAEEAKKAEELKKK 1710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 983 KIQKLKEARALKAKEQQNLVPVVEEEPEFSVPQPSLHDLTQDKltldtEENDVDDEVLSGASRERRRSFLESNSFTKPNL 1062
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE-----EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
330
....*....|....*...
gi 568967337 1063 KHTDTPNKECINKLSKST 1080
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDI 1803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
744-1097 |
1.80e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 744 EARRTAEQASKPKVPPKseKENDPLRTPEA----LPEEKKMEYRLLKEEIANREKQRLIKSDQLKTSssspANSDVEMDG 819
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDK--KKADELKKAAAakkkADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK----AEEAKKAEE 1461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 820 IGRIAMVTKQVADAEAKLKKHKilliKDESVLKNLvlQEAKKK--ESVRNAEAKitKLTEQLQAAEKILSANRmfLKKLQ 897
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAK----KADEAKKKA--EEAKKKadEAKKAAEAK--KKADEAKKAEEAKKADE--AKKAE 1531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 898 E--QIHRVQQRVTIKKALTLKYGEELARAKAVASKELGKRKLEQDRLGPNK---MMRLDNSPISSPRKHSAELIAMEKRR 972
Cdd:PTZ00121 1532 EakKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 973 LQKLEyEYALKIQKLKEARALKAKEQQNLVPVVEEEPEfsvpqpslhdltQDKLTLDTEENDVDDEVLSGASRERRRSFL 1052
Cdd:PTZ00121 1612 AKKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK------------AEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568967337 1053 ESNSFTKPNLKHTDTPNKECINKLSKSTVEKPELFLGLKIGELQK 1097
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1613-1701 |
2.62e-05 |
|
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: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1613 IALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCKFFILQDGGDK 1692
Cdd:COG3914 85 ALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEE 164
|
....*....
gi 568967337 1693 LLPVLRQFV 1701
Cdd:COG3914 165 AIAALRRAL 173
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1351-1445 |
2.82e-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: 45.95 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1351 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1430
Cdd:COG4783 24 EALLEKALELDPDNPEAFALLGEILLQLGD------LDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEK 97
|
90
....*....|....*
gi 568967337 1431 AVEYAPDYQSFWTFL 1445
Cdd:COG4783 98 ALKLDPEHPEAYLRL 112
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1351-1442 |
2.83e-05 |
|
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: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1351 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1430
Cdd:COG3914 98 LALYRRALALNPDNAEALFNLGNLLLALGR------LEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRR 171
|
90
....*....|..
gi 568967337 1431 AVEYAPDYQSFW 1442
Cdd:COG3914 172 ALELDPDNAEAL 183
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1351-1538 |
2.93e-05 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 47.69 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1351 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1430
Cdd:COG0457 28 IEDYEKALELDPDDAEALYNLGLAYLRLGR------YEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1431 AVEYAPDYQSFWTFLHLeSTFEEKDYvcERMVEFLMGAAKREISDIlsfqllEALLFRVQLHIFTGRCQSALAVLQNALK 1510
Cdd:COG0457 102 ALELDPDDAEALYNLGL-ALLELGRY--DEAIEAYERALELDPDDA------DALYNLGIALEKLGRYEEALELLEKLEA 172
|
170 180
....*....|....*....|....*...
gi 568967337 1511 LANDAIVAEYLKTDDRCLAWLAYIHLIE 1538
Cdd:COG0457 173 AALAALLAAALGEAALALAAAEVLLALL 200
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
1608-1671 |
3.33e-05 |
|
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: 46.11 E-value: 3.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967337 1608 LYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNP 1671
Cdd:COG5010 90 LYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
833-1049 |
4.51e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 833 AEAKLKKHKILLIKDESVLKNLVLQEAKKKEsvrnAEAKITKLTEQLQAAEKILSANRMFLKKLQEQIHRVQQRVTIKKA 912
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 913 LTLKYGEELARAKAvASKELGKRKLEQDRLGPNKMMRLDNspissprkHSAELIAMEKrRLQKLEYEYALKIQKLKEARA 992
Cdd:COG1196 296 ELARLEQDIARLEE-RRRELEERLEELEEELAELEEELEE--------LEEELEELEE-ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967337 993 LKAKEQQNLVPVVEEepefsvpqpsLHDLTQDKLTLDTEENDVDDEVLSGASRERRR 1049
Cdd:COG1196 366 ALLEAEAELAEAEEE----------LEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
1351-1436 |
5.72e-05 |
|
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: 45.34 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1351 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1430
Cdd:COG5010 74 LALLEQALQLDPNNPELYYNLALLYSRSGD------KDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQR 147
|
....*.
gi 568967337 1431 AVEYAP 1436
Cdd:COG5010 148 ALGTSP 153
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
1615-1701 |
6.61e-05 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 43.62 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1615 LHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRvWLTAFENNPQNAEIFYHLCKFFILQDGGDKLL 1694
Cdd:COG3063 1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEAL 79
|
....*..
gi 568967337 1695 PVLRQFV 1701
Cdd:COG3063 80 AYLERAL 86
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
1609-1671 |
1.28e-04 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 42.85 E-value: 1.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967337 1609 YTNMIALHQLLERYEEAVELcTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNP 1671
Cdd:COG3063 29 LNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
737-1035 |
1.60e-04 |
|
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: 46.43 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 737 GLESMIKEARRTAEQaSKPKVPPKSEKENDPLRTPEALPEEKKMeyrLLKEEIANREKQRLIKSDqLKTSSSSPANSDVE 816
Cdd:pfam07888 77 ELESRVAELKEELRQ-SREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEED-IKTLTQRVLERETE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 817 MDGIG-RIAMVTKQVADAEAKLKKHKILLIKDESVLKNLV--LQEAKKKESVRNAEA-----KITKLTEQLQAAEKILSA 888
Cdd:pfam07888 152 LERMKeRAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSkeFQELRNSLAQRDTQVlqlqdTITTLTQKLTTAHRKEAE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 889 NRMFLKKL---QEQIHRVQQRVTIkkaltlkYGEELAraKAVASKELGKRKLEQDRLGPNKM----------MRLDNSPI 955
Cdd:pfam07888 232 NEALLEELrslQERLNASERKVEG-------LGEELS--SMAAQRDRTQAELHQARLQAAQLtlqladaslaLREGRARW 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 956 SSPRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAK--------EQQNLVPVVEEEPEFSVPQPSLHDLTQDKLT 1027
Cdd:pfam07888 303 AQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKlevelgreKDCNRVQLSESRRELQELKASLRVAQKEKEQ 382
|
....*...
gi 568967337 1028 LDTEENDV 1035
Cdd:pfam07888 383 LQAEKQEL 390
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1365-1514 |
2.15e-04 |
|
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: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1365 VQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPDYQSFWTF 1444
Cdd:COG4783 4 AEALYALAQALLLAGD------YDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLN 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1445 LhLESTFEEKDYvcERMVEFLMGAAKREISDILSFQLLEALLFRvqlhifTGRCQSALAVLQNALKLAND 1514
Cdd:COG4783 78 L-GLALLKAGDY--DEALALLEKALKLDPEHPEAYLRLARAYRA------LGRPDEAIAALEKALELDPD 138
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
1351-1437 |
2.37e-04 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 42.08 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1351 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNvLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1430
Cdd:COG3063 12 EEYYEKALELDPDNADALNNLGLLLLEQGR------YDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLER 84
|
....*..
gi 568967337 1431 AVEYAPD 1437
Cdd:COG3063 85 ALELDPS 91
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
201-998 |
2.81e-04 |
|
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: 46.12 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 201 RKSSKSFGRSPSRKQNHSSKSENCAEETFEDLLLKYKQIQLELEciNKDEKLALSSKEETAQEdpKTLHLEDQTSTDNAS 280
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK--LQEEELKLLAKEEEELK--SELLKLERRKVDDEE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 281 ITKDPSKEVAPEEKTQVKTFQAFELKpLRQKLTLPGDKNRVKRGKDGTRQLSLKSSTtdASQGLEDKEQNLTRRLSASDI 360
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEEL-EKELKELEIKREAEEEEEEELEKLQEKLEQ--LEEELLAKKKLESERLSSAAK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 361 VSEKKLGEEEEELSelqlrllALQSASKKWQQKEQQVMKESKEKLTKTKTaQQKAKTSTKAHSAKKVSATAKQALRKQQT 440
Cdd:pfam02463 392 LKEEELELKSEEEK-------EAQLLLELARQLEDLLKEEKKEELEILEE-EEESIELKQGKLTEEKEELEKQELKLLKD 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 441 KAWKKLQQQKEQERQKEEDQRKHAEEEERRKREEEIRKirdLSNQEEQYNRFMKLVGGKRRARSKSSDPDLRRSLEKQSD 520
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK---ESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 521 SAGGIYQYDNYEEVAMDTDSETsspaAPSPVQPPFFPECSLGYFSSAPSVSLPPPAQVSSVPSLNQPYGEGLCVSLDPLP 600
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEE----RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 601 PLPPLPPLPPEDPEQPPKPPFADEEEEEEMLLREEllKSLASKRAFKpeETSSNSDPPSPPVLNNSQPLSRSNLSIVSIN 680
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG--VSLEEGLAEK--SEVKASLSELTKELLEIQELQEKAESELAKE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 681 TV-SQPRIQNPKFHRGPRLPRTVISLPKHKSVVVTLNDSDDSESDGEASKSTNSVFGG-LESMIKEARRTAEQASKPKVP 758
Cdd:pfam02463 693 EIlRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEeEEKSRLKKEEKEEEKSELSLK 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 759 PKSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRLIK------SDQLKTSSSSPANSDVEMDGIGRIAMVTKQVAD 832
Cdd:pfam02463 773 EKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEaelleeEQLLIEQEEKIKEEELEELALELKEEQKLEKLA 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 833 AEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSANRMflkkLQEQIHRVQQRVTIKKA 912
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL----LEEKENEIEERIKEEAE 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 913 LTLKYGEELARAKAVASKElgKRKLEQDRLGPNKMMRLDNSPISSPRKHSAELIaMEKRRLQKLEYEYALKIQKLKEARA 992
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADE--KEKEENNKEEEEERNKRLLLAKEELGKVNLMAI-EEFEEKEERYNKDELEKERLEEEKK 1005
|
....*.
gi 568967337 993 LKAKEQ 998
Cdd:pfam02463 1006 KLIRAI 1011
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
1568-1675 |
3.63e-04 |
|
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: 42.30 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1568 QAAQDVKTNPD-----LLLAV-------FEDAVKACTDETLTSGERIEVclplYTNMIALHQLLERYEEAVELCTSLLES 1635
Cdd:COG4235 5 RLRQALAANPNdaegwLLLGRaylrlgrYDEALAAYEKALRLDPDNADA----LLDLAEALLAAGDTEEAEELLERALAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568967337 1636 CPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAE 1675
Cdd:COG4235 81 DPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAP 120
|
|
| ACL4-like |
cd24142 |
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ... |
1621-1671 |
3.90e-04 |
|
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.
Pssm-ID: 467942 [Multi-domain] Cd Length: 306 Bit Score: 44.54 E-value: 3.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568967337 1621 RYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNP 1671
Cdd:cd24142 15 NFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1361-1520 |
4.98e-04 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 43.84 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1361 NPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPDYqs 1440
Cdd:COG0457 4 DPDDAEAYNNLGLAYRRLGR------YEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1441 FWTFLHLESTFEE-KDYvcERMVEFLMGAAKREISDIlsfqllEALLFRVQLHIFTGRCQSALAVLQNALKLANDAIVAE 1519
Cdd:COG0457 76 AEALNNLGLALQAlGRY--EEALEDYDKALELDPDDA------EALYNLGLALLELGRYDEAIEAYERALELDPDDADAL 147
|
.
gi 568967337 1520 Y 1520
Cdd:COG0457 148 Y 148
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
1354-1682 |
5.03e-04 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 45.07 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1354 LEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVE 1433
Cdd:TIGR02917 556 LEKAAELNPQEIEPALALAQYYLGKGQ------LKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1434 YAPD-----------YQSF------WTFLHLESTFEEKDYVCERMVEFLMGAAKREISDILSFQLLE------ALLFRV- 1489
Cdd:TIGR02917 630 LQPDsalalllladaYAVMknyakaITSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQkqhpkaALGFELe 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1490 -QLHIFTGRCQSALAVLQNALKLANDAIVAEYL-----------KTDDRCLAWLAyihliefnslpsklyDPSNANPSRI 1557
Cdd:TIGR02917 710 gDLYLRQKDYPAAIQAYRKALKRAPSSQNAIKLhrallasgntaEAVKTLEAWLK---------------THPNDAVLRT 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 1558 VNTEPFVMPWQAAQDVKtnpdlllaVFEDAVKACTDetltsgerievclplytNMIALHQL----LERYE-EAVELCTSL 1632
Cdd:TIGR02917 775 ALAELYLAQKDYDKAIK--------HYQTVVKKAPD-----------------NAVVLNNLawlyLELKDpRALEYAERA 829
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568967337 1633 LESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCK 1682
Cdd:TIGR02917 830 LKLAPNIPAILDTLGWLLVEKGEADRALPLLRKAVNIAPEAAAIRYHLAL 879
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
744-1008 |
7.16e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 744 EARRTAEQASKPKVPPKSEKENdplRTPEALPEEKKMEYRLLKEEIANRekqrliKSDQLKTSSSSPANSDVEMDGIGRI 823
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKK------KADAAKKKAEEKKKADEAKKKAEED 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 824 AMVTKQVADAEAKLKKHKILLIKDESVLKnlvLQEAKKK-ESVRNAEAKITKLTEQLQAAEKILSANRMflKKLQEQIHR 902
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKK---ADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEA--KKADEAKKK 1478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 903 VQQRvtiKKALTLKYGEELARAKA--VASKELGKRKLEQDRLGPNKMMRLDNSPISSPRKHSAELIAMEKRRLQKL---- 976
Cdd:PTZ00121 1479 AEEA---KKADEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkae 1555
|
250 260 270
....*....|....*....|....*....|..
gi 568967337 977 EYEYALKIQKLKEARalKAKEQQNLVPVVEEE 1008
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAK--KAEEDKNMALRKAEE 1585
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
820-1082 |
1.06e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 820 IGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILS---------ANR 890
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSireiscqqhTLT 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 891 MFLKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKElgkRKLEQDRLGPNKMMRLDNSPISSPRKHSAELIA--- 967
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQcek 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 968 MEKRRLQKLEYEYALKIQKLK----------------EARALKAKEQQNLVPVVEEEPE--------FSVPQPSLHDLTQ 1023
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQLQtkeqihlqetrkkavvLARLLELQEEPCPLCGSCIHPNparqdidnPGPLTRRMQRGEQ 535
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967337 1024 DKLTLDTEENDVDDEVLSgaSRERRRSF---LESNSFTKPNLKHTDTPNKECINKLSKSTVE 1082
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTS--ERKQRASLkeqMQEIQQSFSILTQCDNRSKEDIPNLQNITVR 595
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
743-1070 |
1.06e-03 |
|
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: 44.19 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 743 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKMEYRLLKEEIA------NREKQRLIKSDQLKTSSSSPANSDVE 816
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKllakeeEELKSELLKLERRKVDDEEKLKESEK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 817 MDG--IGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSANRMF-- 892
Cdd:pfam02463 322 EKKkaEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELks 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 893 --LKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKELGKRKLEQDRLGPNKMMRLDNSPISSPRKHSAELIAMEK 970
Cdd:pfam02463 402 eeEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 971 RRLQKLEyeyALKIQKLKEARalkAKEQQNLVPVVEEEPEFSVPQPSLHDLTQDKLTlDTEENDVDDEVLSGASRERRRS 1050
Cdd:pfam02463 482 LQEQLEL---LLSRQKLEERS---QKESKARSGLKVLLALIKDGVGGRIISAHGRLG-DLGVAVENYKVAISTAVIVEVS 554
|
330 340
....*....|....*....|
gi 568967337 1051 FLESNSFTKPNLKHTDTPNK 1070
Cdd:pfam02463 555 ATADEVEERQKLVRALTELP 574
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
777-999 |
1.61e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 777 EKKMEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEmdgigrIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVL 856
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELE------ELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 857 QEAKKKEsvRNAEAKITKLTEQLQAAEKILSANRMFLKKLQEQIHRVQQRVtikkaltLKYGEELARAKAVASKELGKRK 936
Cdd:COG1196 284 EEAQAEE--YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL-------EELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967337 937 LEQDRLgpnkmmrldnspisspRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAKEQQ 999
Cdd:COG1196 355 EAEAEL----------------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
1615-1680 |
2.52e-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: 39.99 E-value: 2.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967337 1615 LHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHL 1680
Cdd:COG4235 26 AYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLL 91
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
739-926 |
3.21e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 739 ESMIKEARRTAEQASKpkvppksekendplrtpEALPEEKKmEYRLLKEEIANREKQRLIKSDQLKtsssspansdvemd 818
Cdd:PRK12704 41 KRILEEAKKEAEAIKK-----------------EALLEAKE-EIHKLRNEFEKELRERRNELQKLE-------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 819 gigriamvtKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKL-TEQLQAAEKI--LS---ANRMF 892
Cdd:PRK12704 89 ---------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERIsgLTaeeAKEIL 159
|
170 180 190
....*....|....*....|....*....|....
gi 568967337 893 LKKLQEQIhRVQQRVTIKKAltlkygEELARAKA 926
Cdd:PRK12704 160 LEKVEEEA-RHEAAVLIKEI------EEEAKEEA 186
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1608-1673 |
4.95e-03 |
|
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: 39.40 E-value: 4.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967337 1608 LYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQN 1673
Cdd:COG4783 74 ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
1608-1661 |
6.53e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 37.37 E-value: 6.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967337 1608 LYTNMIALHQLLERYEEAVELCTSLLESC--------PTNCQLLETLAALYLKTDRYDKARR 1661
Cdd:pfam13424 5 ALNNLAAVLRRLGRYDEALELLEKALEIArrllgpdhPLTATTLLNLGRLYLELGRYEEALE 66
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
835-993 |
7.42e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 835 AKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTE-QLQAAEKILSANRMFLKKLQEQIHRVQQRVT----- 908
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEkLSEAEDMLACEQHALLRKLQPEQDLQDVRLHlqqcs 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 909 --IKKALTLKYGEELA------RAKAVASKELGKRKLEQDRLGPNKM--------------------MRLDNSPISSPRK 960
Cdd:TIGR00618 639 qeLALKLTALHALQLTltqervREHALSIRVLPKELLASRQLALQKMqsekeqltywkemlaqcqtlLRELETHIEEYDR 718
|
170 180 190
....*....|....*....|....*....|...
gi 568967337 961 HSAELIAMEKRRLQKLEYEYALKIQKLKEARAL 993
Cdd:TIGR00618 719 EFNEIENASSSLGSDLAAREDALNQSLKELMHQ 751
|
|
| TPR_19 |
pfam14559 |
Tetratricopeptide repeat; |
1620-1676 |
7.60e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 434038 [Multi-domain] Cd Length: 65 Bit Score: 36.79 E-value: 7.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967337 1620 ERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEI 1676
Cdd:pfam14559 2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRY 58
|
|
| TPR_19 |
pfam14559 |
Tetratricopeptide repeat; |
1351-1408 |
8.22e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 434038 [Multi-domain] Cd Length: 65 Bit Score: 36.79 E-value: 8.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568967337 1351 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIW 1408
Cdd:pfam14559 8 LELLEQALAEDPDNAEARLGLAEALLALGR------LDEAEALLAALPAADPDDPRYA 59
|
|
| TPR_14 |
pfam13428 |
Tetratricopeptide repeat; |
1365-1414 |
8.91e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 463874 [Multi-domain] Cd Length: 44 Bit Score: 35.86 E-value: 8.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568967337 1365 VQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRL 1414
Cdd:pfam13428 1 PEALLALARALLALGD------PDEALALLERALALDPDDPEAWLALAQL 44
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
776-1028 |
9.95e-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: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 776 EEKKMEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEMDGIGRiamvTKQVADAEAKLKKHKILLIKDEsvLKNLV 855
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES----KLDELAEELAELEEKLEELKEE--LESLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 856 LQEAKKKESVRNAEAKITKLTEQLQAAekilsANRMFLKKLQEQIHRVQQRVtikkaltlkYGEELARAKAVASKELGKR 935
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETL-----RSKVAQLELQIASLNNEIER---------LEARLERLEDRRERLQQEI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967337 936 KLEQDRLGPNKMMRLdnspissprkhsAELIAMEKRRLQKLEYEYALKIQKLKEARALKAKEQQNLVPVVEEEPEFSVPQ 1015
Cdd:TIGR02168 424 EELLKKLEEAELKEL------------QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
250
....*....|...
gi 568967337 1016 PSLHDLTQDKLTL 1028
Cdd:TIGR02168 492 DSLERLQENLEGF 504
|
|
| |
