|
Name |
Accession |
Description |
Interval |
E-value |
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1367-1698 |
6.72e-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: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1367 WLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPdyQSFWTFLHL 1446
Cdd:COG2956 11 WYFKGLNYLLNGQ------PDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDP--DRAEALLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1447 -ESTFEEKDYvcERMVEFLMGAAKREISDIlsfqllEALLFRVQLHIFTGRCQSALAVLQNALKLANDAIVAEYLktddr 1525
Cdd:COG2956 83 aQDYLKAGLL--DRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1526 clawLAYIHLiefnslpsklydpsnanpsrivntepfvmpwqaAQDvktNPDLLLAVFEDAVKACTDetltsgerievCL 1605
Cdd:COG2956 150 ----LAELYL---------------------------------EQG---DYDEAIEALEKALKLDPD-----------CA 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1606 PLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYhLCKFFIL 1685
Cdd:COG2956 179 RALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA-LADLLER 257
|
330
....*....|...
gi 90991706 1686 QDGGDKLLPVLRQ 1698
Cdd:COG2956 258 KEGLEAALALLER 270
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
826-1000 |
4.72e-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: 51.30 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 826 TKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSANRMFLKKLQEQIHRVQQR 905
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 906 VTIKKaltlkygEELARAKAVASKeLGKRKLEQDRLGPN------KMMRLDNSpISSPRKHSAELIAMEKRRLQKLEYEY 979
Cdd:COG4942 99 LEAQK-------EELAELLRALYR-LGRQPPLALLLSPEdfldavRRLQYLKY-LAPARREQAEELRADLAELAALRAEL 169
|
170 180
....*....|....*....|.
gi 90991706 980 ALKIQKLKEARALKAKEQQNL 1000
Cdd:COG4942 170 EAERAELEALLAELEEERAAL 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
737-1009 |
5.55e-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: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 737 LESMIKEARRTAEQASKpkvppKSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEM 816
Cdd:TIGR02168 710 LEEELEQLRKELEELSR-----QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 817 --------DGIGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSAN 888
Cdd:TIGR02168 785 eeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 889 RMFLKKLQEQIHRVQQRVtikkaltlkygEELARAKAVASKELGKRKLEQDRLGpNKMMRLDNSpisspRKHSAELIAME 968
Cdd:TIGR02168 865 EELIEELESELEALLNER-----------ASLEEALALLRSELEELSEELRELE-SKRSELRRE-----LEELREKLAQL 927
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 90991706 969 KRRLQKLEYEYALKIQKLKEARALKAKEQQNLVPVVEEEPE 1009
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
|
| zf-C3H1 |
pfam10650 |
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ... |
1188-1207 |
9.31e-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: 9.31e-06
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
742-1079 |
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 90991706 742 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRliKSDQLKTSSSSPANSDVEMDGIGR 821
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK--KADELKKAEELKKAEEKKKAEEAK 1570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 822 IAMVTKQVADAEAKLKKhKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKlTEQLQAAEKILSANRMFLKKLQEQihr 901
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEE--- 1645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 902 vqqrvtIKKALTLKYGEELARAKavasKELGKRKLEQDRLGPNKMMRLDNSpisspRKHSAELIAMEKRRLQKLEYEYAL 981
Cdd:PTZ00121 1646 ------KKKAEELKKAEEENKIK----AAEEAKKAEEDKKKAEEAKKAEED-----EKKAAEALKKEAEEAKKAEELKKK 1710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 982 KIQKLKEARALKAKEQQNLVPVVEEEPEFSVPQPSLHDLTQDKltldtEENDVDDEVLSGASRERRRSFLESNSFTKPNL 1061
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE-----EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
330
....*....|....*...
gi 90991706 1062 KHTDTPNKECINKLSKST 1079
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDI 1803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
743-1096 |
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 90991706 743 EARRTAEQASKPKVPPKseKENDPLRTPEA----LPEEKKMEYRLLKEEIANREKQRLIKSDQLKTSssspANSDVEMDG 818
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDK--KKADELKKAAAakkkADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK----AEEAKKAEE 1461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 819 IGRIAMVTKQVADAEAKLKKHKilliKDESVLKNLvlQEAKKK--ESVRNAEAKitKLTEQLQAAEKILSANRmfLKKLQ 896
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAK----KADEAKKKA--EEAKKKadEAKKAAEAK--KKADEAKKAEEAKKADE--AKKAE 1531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 897 E--QIHRVQQRVTIKKALTLKYGEELARAKAVASKELGKRKLEQDRLGPNK---MMRLDNSPISSPRKHSAELIAMEKRR 971
Cdd:PTZ00121 1532 EakKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 972 LQKLEyEYALKIQKLKEARALKAKEQQNLVPVVEEEPEfsvpqpslhdltQDKLTLDTEENDVDDEVLSGASRERRRSFL 1051
Cdd:PTZ00121 1612 AKKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK------------AEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 90991706 1052 ESNSFTKPNLKHTDTPNKECINKLSKSTVEKPELFLGLKIGELQK 1096
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
201-997 |
2.54e-05 |
|
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: 49.58 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 201 RKSSKSFGRSPSRKQNHSSKSENCAEETFEDLLLKYKQIQLELEciNKDEKLALSSKEETAQEdpKTLHLEDQTSTDNAS 280
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK--LQEEELKLLAKEEEELK--SELLKLERRKVDDEE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 281 ITKDPSKEVAPEEKTQVKTFQAFELKpLRQKLTLPGDKNRVKRGKDGTRQLSLKSSTtdASQGLEDKEQNLTRRLSASDI 360
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEEL-EKELKELEIKREAEEEEEEELEKLQEKLEQ--LEEELLAKKKLESERLSSAAK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 361 VSEKKLGEEEEELSelqlrllALQSASKKWQQKEQQVMKESKEKLTKTKTaQQKAKTSTKAHSAKKVSATAKQALRKQQT 440
Cdd:pfam02463 392 LKEEELELKSEEEK-------EAQLLLELARQLEDLLKEEKKEELEILEE-EEESIELKQGKLTEEKEELEKQELKLLKD 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 441 KAWKKLQQQKEQERQKEEDQRKHAEEEERRKREEEIRKirdLSNQEEQYNRFMKLVGGKRRARSKSSDPDLRRSLEKQSD 520
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK---ESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 521 SAGGIYQYDNYEEVAMDTDSETSSPAPSPVQPPFFPECSLGYFSSAPSVSLPPPAQVSSVPSLNQPYGEGLCVSLDPLPP 600
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 601 LPPLPPLPPEDPEQPPKPPFADEEEEEEMLLreellKSLASKRAFKpeETSSNSDPPSPPVLNNSQPLSRSNLSIVSINT 680
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKG-----VSLEEGLAEK--SEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 681 V-SQPRIQNPKFHRGPRLPRTVISLPKHKSVVVTLNDSDDSESDGEASKSTNSVFGG-LESMIKEARRTAEQASKPKVPP 758
Cdd:pfam02463 694 IlRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEeEEKSRLKKEEKEEEKSELSLKE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 759 KSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRLIK------SDQLKTSSSSPANSDVEMDGIGRIAMVTKQVADA 832
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEaelleeEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 833 EAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSANRMflkkLQEQIHRVQQRVTIKKAL 912
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL----LEEKENEIEERIKEEAEI 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 913 TLKYGEELARAKAVASKElgKRKLEQDRLGPNKMMRLDNSPISSPRKHSAELIaMEKRRLQKLEYEYALKIQKLKEARAL 992
Cdd:pfam02463 930 LLKYEEEPEELLLEEADE--KEKEENNKEEEEERNKRLLLAKEELGKVNLMAI-EEFEEKEERYNKDELEKERLEEEKKK 1006
|
....*
gi 90991706 993 KAKEQ 997
Cdd:pfam02463 1007 LIRAI 1011
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
736-1034 |
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 90991706 736 GLESMIKEARRTAEQaSKPKVPPKSEKENDPLRTPEALPEEKKMeyrLLKEEIANREKQRLIKSDqLKTSSSSPANSDVE 815
Cdd:pfam07888 77 ELESRVAELKEELRQ-SREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEED-IKTLTQRVLERETE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 816 MDGIG-RIAMVTKQVADAEAKLKKHKILLIKDESVLKNLV--LQEAKKKESVRNAEA-----KITKLTEQLQAAEKILSA 887
Cdd:pfam07888 152 LERMKeRAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSkeFQELRNSLAQRDTQVlqlqdTITTLTQKLTTAHRKEAE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 888 NRMFLKKL---QEQIHRVQQRVTIkkaltlkYGEELAraKAVASKELGKRKLEQDRLGPNKM----------MRLDNSPI 954
Cdd:pfam07888 232 NEALLEELrslQERLNASERKVEG-------LGEELS--SMAAQRDRTQAELHQARLQAAQLtlqladaslaLREGRARW 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 955 SSPRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAK--------EQQNLVPVVEEEPEFSVPQPSLHDLTQDKLT 1026
Cdd:pfam07888 303 AQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKlevelgreKDCNRVQLSESRRELQELKASLRVAQKEKEQ 382
|
....*...
gi 90991706 1027 LDTEENDV 1034
Cdd:pfam07888 383 LQAEKQEL 390
|
|
| ACL4-like |
cd24142 |
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ... |
1620-1670 |
3.89e-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: 3.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 90991706 1620 RYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNP 1670
Cdd:cd24142 15 NFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
1353-1681 |
4.82e-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: 45.46 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1353 LEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVE 1432
Cdd:TIGR02917 556 LEKAAELNPQEIEPALALAQYYLGKGQ------LKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1433 YAPD-----------YQSF------WTFLHLESTFEEKDYVCERMVEFLMGAAKREISDILSFQLLE------ALLFRV- 1488
Cdd:TIGR02917 630 LQPDsalalllladaYAVMknyakaITSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQkqhpkaALGFELe 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1489 -QLHIFTGRCQSALAVLQNALKLANDAIVAEYL-----------KTDDRCLAWLAyihliefnslpsklyDPSNANPSRI 1556
Cdd:TIGR02917 710 gDLYLRQKDYPAAIQAYRKALKRAPSSQNAIKLhrallasgntaEAVKTLEAWLK---------------THPNDAVLRT 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1557 VNTEPFVMPWQAAQDVKtnpdlllaVFEDAVKACTDetltsgerievclplytNMIALHQL----LERYE-EAVELCTSL 1631
Cdd:TIGR02917 775 ALAELYLAQKDYDKAIK--------HYQTVVKKAPD-----------------NAVVLNNLawlyLELKDpRALEYAERA 829
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 90991706 1632 LESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCK 1681
Cdd:TIGR02917 830 LKLAPNIPAILDTLGWLLVEKGEADRALPLLRKAVNIAPEAAAIRYHLAL 879
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
1607-1660 |
6.40e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 37.37 E-value: 6.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90991706 1607 LYTNMIALHQLLERYEEAVELCTSLLESC--------PTNCQLLETLAALYLKTDRYDKARR 1660
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 ... |
1367-1698 |
6.72e-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: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1367 WLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPdyQSFWTFLHL 1446
Cdd:COG2956 11 WYFKGLNYLLNGQ------PDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDP--DRAEALLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1447 -ESTFEEKDYvcERMVEFLMGAAKREISDIlsfqllEALLFRVQLHIFTGRCQSALAVLQNALKLANDAIVAEYLktddr 1525
Cdd:COG2956 83 aQDYLKAGLL--DRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1526 clawLAYIHLiefnslpsklydpsnanpsrivntepfvmpwqaAQDvktNPDLLLAVFEDAVKACTDetltsgerievCL 1605
Cdd:COG2956 150 ----LAELYL---------------------------------EQG---DYDEAIEALEKALKLDPD-----------CA 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1606 PLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYhLCKFFIL 1685
Cdd:COG2956 179 RALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA-LADLLER 257
|
330
....*....|...
gi 90991706 1686 QDGGDKLLPVLRQ 1698
Cdd:COG2956 258 KEGLEAALALLER 270
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
1350-1444 |
1.26e-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: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1350 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1429
Cdd:COG4235 3 IARLRQALAANPNDAEGWLLLGRAYLRLGR------YDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLER 76
|
90
....*....|....*
gi 90991706 1430 AVEYAPDYQSFWTFL 1444
Cdd:COG4235 77 ALALDPDNPEALYLL 91
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
1566-1698 |
7.99e-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: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1566 WQAAQDVKTNPDLLLAVFEDAVKACTDETLTSGERIEVCLPLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETL 1645
Cdd:COG5010 15 LLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 90991706 1646 AALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCKFFILQDGGDKLLPVLRQ 1698
Cdd:COG5010 95 ALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQR 147
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1575-1700 |
9.59e-08 |
|
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: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1575 NPDLLLAVFEDAVKACTDEtltsgerievcLPLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDR 1654
Cdd:COG2956 23 QPDKAIDLLEEALELDPET-----------VEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGL 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 90991706 1655 YDKARRVWLTAFENNPQNAEIFYHLCKFFILQDGGDKLLPVLRQFV 1700
Cdd:COG2956 92 LDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLL 137
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1608-1698 |
2.31e-07 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 54.24 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1608 YTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCKFFILQD 1687
Cdd:COG0457 79 LNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLG 158
|
90
....*....|.
gi 90991706 1688 GGDKLLPVLRQ 1698
Cdd:COG0457 159 RYEEALELLEK 169
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1604-1690 |
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 90991706 1604 CLPLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCkfF 1683
Cdd:COG3914 111 NAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLG--N 188
|
....*..
gi 90991706 1684 ILQDGGD 1690
Cdd:COG3914 189 ALQDLGR 195
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1605-1690 |
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 90991706 1605 LPLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCkfFI 1684
Cdd:COG3914 146 AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLL--FA 223
|
....*.
gi 90991706 1685 LQDGGD 1690
Cdd:COG3914 224 LRQACD 229
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1608-1679 |
6.41e-07 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 52.70 E-value: 6.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90991706 1608 YTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHL 1679
Cdd:COG0457 45 LYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNL 116
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1604-1698 |
1.15e-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: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1604 CLPLYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCKFF 1683
Cdd:COG4783 3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82
|
90
....*....|....*
gi 90991706 1684 ILQDGGDKLLPVLRQ 1698
Cdd:COG4783 83 LKAGDYDEALALLEK 97
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1613-1723 |
1.22e-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: 52.42 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1613 ALHQLL-ERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCKFFILQDGGDK 1691
Cdd:COG2956 15 GLNYLLnGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDR 94
|
90 100 110
....*....|....*....|....*....|..
gi 90991706 1692 LLPVLRQFVGsffkpgfEKYSNVDLFRYLLNI 1723
Cdd:COG2956 95 AEELLEKLLE-------LDPDDAEALRLLAEI 119
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1350-1520 |
1.40e-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: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1350 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1429
Cdd:COG2956 96 EELLEKLLELDPDDAEALRLLAEIYEQEGD------WEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1430 AVEYAPDYQSFWTFL-HLEstFEEKDYvcERMVEFLMGAAKREISDilsfqlLEALLFRVQLHIFTGRCQSALAVLQNAL 1508
Cdd:COG2956 170 ALKLDPDCARALLLLaELY--LEQGDY--EEAIAALERALEQDPDY------LPALPRLAELYEKLGDPEEALELLRKAL 239
|
170
....*....|..
gi 90991706 1509 KLANDAIVAEYL 1520
Cdd:COG2956 240 ELDPSDDLLLAL 251
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1608-1679 |
2.20e-06 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 51.16 E-value: 2.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90991706 1608 YTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHL 1679
Cdd:COG0457 11 YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNL 82
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1609-1679 |
2.23e-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: 2.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90991706 1609 TNMIALHQL------LERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHL 1679
Cdd:COG4783 36 DNPEAFALLgeillqLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRL 112
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1350-1535 |
3.36e-06 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 50.39 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1350 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1429
Cdd:COG0457 62 LADYEQALELDPDDAEALNNLGLALQALGR------YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYER 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1430 AVEYAPDYQSFWT----FLHLESTFEEKDYVCERMVEFLMGAAKREISDILSFQLLEALLFRVQLHIFTGRCQSALAVLQ 1505
Cdd:COG0457 136 ALELDPDDADALYnlgiALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILT 215
|
170 180 190
....*....|....*....|....*....|
gi 90991706 1506 NALKLANDAIVAEYLKTDDRCLAWLAYIHL 1535
Cdd:COG0457 216 LAALAELLLLALALLLALRLAALALYQYRA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
826-1000 |
4.72e-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: 51.30 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 826 TKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSANRMFLKKLQEQIHRVQQR 905
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 906 VTIKKaltlkygEELARAKAVASKeLGKRKLEQDRLGPN------KMMRLDNSpISSPRKHSAELIAMEKRRLQKLEYEY 979
Cdd:COG4942 99 LEAQK-------EELAELLRALYR-LGRQPPLALLLSPEdfldavRRLQYLKY-LAPARREQAEELRADLAELAALRAEL 169
|
170 180
....*....|....*....|.
gi 90991706 980 ALKIQKLKEARALKAKEQQNL 1000
Cdd:COG4942 170 EAERAELEALLAELEEERAAL 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
737-1009 |
5.55e-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: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 737 LESMIKEARRTAEQASKpkvppKSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEM 816
Cdd:TIGR02168 710 LEEELEQLRKELEELSR-----QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 817 --------DGIGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSAN 888
Cdd:TIGR02168 785 eeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 889 RMFLKKLQEQIHRVQQRVtikkaltlkygEELARAKAVASKELGKRKLEQDRLGpNKMMRLDNSpisspRKHSAELIAME 968
Cdd:TIGR02168 865 EELIEELESELEALLNER-----------ASLEEALALLRSELEELSEELRELE-SKRSELRRE-----LEELREKLAQL 927
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 90991706 969 KRRLQKLEYEYALKIQKLKEARALKAKEQQNLVPVVEEEPE 1009
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
|
| zf-C3H1 |
pfam10650 |
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ... |
1188-1207 |
9.31e-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: 9.31e-06
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1350-1437 |
1.31e-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: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1350 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1429
Cdd:COG4783 58 IVLLHEALELDPDEPEARLNLGLALLKAGD------YDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEK 131
|
....*...
gi 90991706 1430 AVEYAPDY 1437
Cdd:COG4783 132 ALELDPDD 139
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
742-1079 |
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 90991706 742 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRliKSDQLKTSSSSPANSDVEMDGIGR 821
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK--KADELKKAEELKKAEEKKKAEEAK 1570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 822 IAMVTKQVADAEAKLKKhKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKlTEQLQAAEKILSANRMFLKKLQEQihr 901
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEE--- 1645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 902 vqqrvtIKKALTLKYGEELARAKavasKELGKRKLEQDRLGPNKMMRLDNSpisspRKHSAELIAMEKRRLQKLEYEYAL 981
Cdd:PTZ00121 1646 ------KKKAEELKKAEEENKIK----AAEEAKKAEEDKKKAEEAKKAEED-----EKKAAEALKKEAEEAKKAEELKKK 1710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 982 KIQKLKEARALKAKEQQNLVPVVEEEPEFSVPQPSLHDLTQDKltldtEENDVDDEVLSGASRERRRSFLESNSFTKPNL 1061
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE-----EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
330
....*....|....*...
gi 90991706 1062 KHTDTPNKECINKLSKST 1079
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDI 1803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
743-1096 |
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 90991706 743 EARRTAEQASKPKVPPKseKENDPLRTPEA----LPEEKKMEYRLLKEEIANREKQRLIKSDQLKTSssspANSDVEMDG 818
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDK--KKADELKKAAAakkkADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK----AEEAKKAEE 1461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 819 IGRIAMVTKQVADAEAKLKKHKilliKDESVLKNLvlQEAKKK--ESVRNAEAKitKLTEQLQAAEKILSANRmfLKKLQ 896
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAK----KADEAKKKA--EEAKKKadEAKKAAEAK--KKADEAKKAEEAKKADE--AKKAE 1531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 897 E--QIHRVQQRVTIKKALTLKYGEELARAKAVASKELGKRKLEQDRLGPNK---MMRLDNSPISSPRKHSAELIAMEKRR 971
Cdd:PTZ00121 1532 EakKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 972 LQKLEyEYALKIQKLKEARALKAKEQQNLVPVVEEEPEfsvpqpslhdltQDKLTLDTEENDVDDEVLSGASRERRRSFL 1051
Cdd:PTZ00121 1612 AKKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK------------AEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 90991706 1052 ESNSFTKPNLKHTDTPNKECINKLSKSTVEKPELFLGLKIGELQK 1096
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
201-997 |
2.54e-05 |
|
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: 49.58 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 201 RKSSKSFGRSPSRKQNHSSKSENCAEETFEDLLLKYKQIQLELEciNKDEKLALSSKEETAQEdpKTLHLEDQTSTDNAS 280
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK--LQEEELKLLAKEEEELK--SELLKLERRKVDDEE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 281 ITKDPSKEVAPEEKTQVKTFQAFELKpLRQKLTLPGDKNRVKRGKDGTRQLSLKSSTtdASQGLEDKEQNLTRRLSASDI 360
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEEL-EKELKELEIKREAEEEEEEELEKLQEKLEQ--LEEELLAKKKLESERLSSAAK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 361 VSEKKLGEEEEELSelqlrllALQSASKKWQQKEQQVMKESKEKLTKTKTaQQKAKTSTKAHSAKKVSATAKQALRKQQT 440
Cdd:pfam02463 392 LKEEELELKSEEEK-------EAQLLLELARQLEDLLKEEKKEELEILEE-EEESIELKQGKLTEEKEELEKQELKLLKD 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 441 KAWKKLQQQKEQERQKEEDQRKHAEEEERRKREEEIRKirdLSNQEEQYNRFMKLVGGKRRARSKSSDPDLRRSLEKQSD 520
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK---ESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 521 SAGGIYQYDNYEEVAMDTDSETSSPAPSPVQPPFFPECSLGYFSSAPSVSLPPPAQVSSVPSLNQPYGEGLCVSLDPLPP 600
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 601 LPPLPPLPPEDPEQPPKPPFADEEEEEEMLLreellKSLASKRAFKpeETSSNSDPPSPPVLNNSQPLSRSNLSIVSINT 680
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKG-----VSLEEGLAEK--SEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 681 V-SQPRIQNPKFHRGPRLPRTVISLPKHKSVVVTLNDSDDSESDGEASKSTNSVFGG-LESMIKEARRTAEQASKPKVPP 758
Cdd:pfam02463 694 IlRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEeEEKSRLKKEEKEEEKSELSLKE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 759 KSEKENDPLRTPEALPEEKKMEYRLLKEEIANREKQRLIK------SDQLKTSSSSPANSDVEMDGIGRIAMVTKQVADA 832
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEaelleeEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 833 EAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSANRMflkkLQEQIHRVQQRVTIKKAL 912
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL----LEEKENEIEERIKEEAEI 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 913 TLKYGEELARAKAVASKElgKRKLEQDRLGPNKMMRLDNSPISSPRKHSAELIaMEKRRLQKLEYEYALKIQKLKEARAL 992
Cdd:pfam02463 930 LLKYEEEPEELLLEEADE--KEKEENNKEEEEERNKRLLLAKEELGKVNLMAI-EEFEEKEERYNKDELEKERLEEEKKK 1006
|
....*
gi 90991706 993 KAKEQ 997
Cdd:pfam02463 1007 LIRAI 1011
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1612-1700 |
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 90991706 1612 IALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCKFFILQDGGDK 1691
Cdd:COG3914 85 ALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEE 164
|
....*....
gi 90991706 1692 LLPVLRQFV 1700
Cdd:COG3914 165 AIAALRRAL 173
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1350-1444 |
2.71e-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: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1350 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1429
Cdd:COG4783 24 EALLEKALELDPDNPEAFALLGEILLQLGD------LDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEK 97
|
90
....*....|....*
gi 90991706 1430 AVEYAPDYQSFWTFL 1444
Cdd:COG4783 98 ALKLDPEHPEAYLRL 112
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1350-1441 |
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 90991706 1350 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1429
Cdd:COG3914 98 LALYRRALALNPDNAEALFNLGNLLLALGR------LEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRR 171
|
90
....*....|..
gi 90991706 1430 AVEYAPDYQSFW 1441
Cdd:COG3914 172 ALELDPDNAEAL 183
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1350-1537 |
2.85e-05 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 47.69 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1350 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1429
Cdd:COG0457 28 IEDYEKALELDPDDAEALYNLGLAYLRLGR------YEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1430 AVEYAPDYQSFWTFLHLeSTFEEKDYvcERMVEFLMGAAKREISDIlsfqllEALLFRVQLHIFTGRCQSALAVLQNALK 1509
Cdd:COG0457 102 ALELDPDDAEALYNLGL-ALLELGRY--DEAIEAYERALELDPDDA------DALYNLGIALEKLGRYEEALELLEKLEA 172
|
170 180
....*....|....*....|....*...
gi 90991706 1510 LANDAIVAEYLKTDDRCLAWLAYIHLIE 1537
Cdd:COG0457 173 AALAALLAAALGEAALALAAAEVLLALL 200
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
1607-1670 |
3.20e-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: 3.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90991706 1607 LYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNP 1670
Cdd:COG5010 90 LYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
832-1048 |
4.36e-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: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 832 AEAKLKKHKILLIKDESVLKNLVLQEAKKKEsvrnAEAKITKLTEQLQAAEKILSANRMFLKKLQEQIHRVQQRVTIKKA 911
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 912 LTLKYGEELARAKAvASKELGKRKLEQDRLGPNKMMRLDNspissprkHSAELIAMEKrRLQKLEYEYALKIQKLKEARA 991
Cdd:COG1196 296 ELARLEQDIARLEE-RRRELEERLEELEEELAELEEELEE--------LEEELEELEE-ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90991706 992 LKAKEQQNLVPVVEEepefsvpqpsLHDLTQDKLTLDTEENDVDDEVLSGASRERRR 1048
Cdd:COG1196 366 ALLEAEAELAEAEEE----------LEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
1350-1435 |
5.46e-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: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1350 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1429
Cdd:COG5010 74 LALLEQALQLDPNNPELYYNLALLYSRSGD------KDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQR 147
|
....*.
gi 90991706 1430 AVEYAP 1435
Cdd:COG5010 148 ALGTSP 153
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
1614-1700 |
6.54e-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: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1614 LHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRvWLTAFENNPQNAEIFYHLCKFFILQDGGDKLL 1693
Cdd:COG3063 1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEAL 79
|
....*..
gi 90991706 1694 PVLRQFV 1700
Cdd:COG3063 80 AYLERAL 86
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
1608-1670 |
1.27e-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: 1.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90991706 1608 YTNMIALHQLLERYEEAVELcTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNP 1670
Cdd:COG3063 29 LNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
736-1034 |
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 90991706 736 GLESMIKEARRTAEQaSKPKVPPKSEKENDPLRTPEALPEEKKMeyrLLKEEIANREKQRLIKSDqLKTSSSSPANSDVE 815
Cdd:pfam07888 77 ELESRVAELKEELRQ-SREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEED-IKTLTQRVLERETE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 816 MDGIG-RIAMVTKQVADAEAKLKKHKILLIKDESVLKNLV--LQEAKKKESVRNAEA-----KITKLTEQLQAAEKILSA 887
Cdd:pfam07888 152 LERMKeRAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSkeFQELRNSLAQRDTQVlqlqdTITTLTQKLTTAHRKEAE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 888 NRMFLKKL---QEQIHRVQQRVTIkkaltlkYGEELAraKAVASKELGKRKLEQDRLGPNKM----------MRLDNSPI 954
Cdd:pfam07888 232 NEALLEELrslQERLNASERKVEG-------LGEELS--SMAAQRDRTQAELHQARLQAAQLtlqladaslaLREGRARW 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 955 SSPRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAK--------EQQNLVPVVEEEPEFSVPQPSLHDLTQDKLT 1026
Cdd:pfam07888 303 AQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKlevelgreKDCNRVQLSESRRELQELKASLRVAQKEKEQ 382
|
....*...
gi 90991706 1027 LDTEENDV 1034
Cdd:pfam07888 383 LQAEKQEL 390
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1364-1513 |
2.13e-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: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1364 VQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPDYQSFWTF 1443
Cdd:COG4783 4 AEALYALAQALLLAGD------YDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLN 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1444 LhLESTFEEKDYvcERMVEFLMGAAKREISDILSFQLLEALLFRvqlhifTGRCQSALAVLQNALKLAND 1513
Cdd:COG4783 78 L-GLALLKAGDY--DEALALLEKALKLDPEHPEAYLRLARAYRA------LGRPDEAIAALEKALELDPD 138
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
1350-1436 |
2.26e-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: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1350 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNvLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1429
Cdd:COG3063 12 EEYYEKALELDPDNADALNNLGLLLLEQGR------YDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLER 84
|
....*..
gi 90991706 1430 AVEYAPD 1436
Cdd:COG3063 85 ALELDPS 91
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
1567-1674 |
3.36e-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: 42.69 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1567 QAAQDVKTNPD-----LLLAV-------FEDAVKACTDETLTSGERIEVclplYTNMIALHQLLERYEEAVELCTSLLES 1634
Cdd:COG4235 5 RLRQALAANPNdaegwLLLGRaylrlgrYDEALAAYEKALRLDPDNADA----LLDLAEALLAAGDTEEAEELLERALAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 90991706 1635 CPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAE 1674
Cdd:COG4235 81 DPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAP 120
|
|
| ACL4-like |
cd24142 |
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ... |
1620-1670 |
3.89e-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: 3.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 90991706 1620 RYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNP 1670
Cdd:cd24142 15 NFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1360-1519 |
4.67e-04 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 43.84 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1360 NPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPDYqs 1439
Cdd:COG0457 4 DPDDAEAYNNLGLAYRRLGR------YEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1440 FWTFLHLESTFEE-KDYvcERMVEFLMGAAKREISDIlsfqllEALLFRVQLHIFTGRCQSALAVLQNALKLANDAIVAE 1518
Cdd:COG0457 76 AEALNNLGLALQAlGRY--EEALEDYDKALELDPDDA------EALYNLGLALLELGRYDEAIEAYERALELDPDDADAL 147
|
.
gi 90991706 1519 Y 1519
Cdd:COG0457 148 Y 148
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
1353-1681 |
4.82e-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: 45.46 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1353 LEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVE 1432
Cdd:TIGR02917 556 LEKAAELNPQEIEPALALAQYYLGKGQ------LKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1433 YAPD-----------YQSF------WTFLHLESTFEEKDYVCERMVEFLMGAAKREISDILSFQLLE------ALLFRV- 1488
Cdd:TIGR02917 630 LQPDsalalllladaYAVMknyakaITSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQkqhpkaALGFELe 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1489 -QLHIFTGRCQSALAVLQNALKLANDAIVAEYL-----------KTDDRCLAWLAyihliefnslpsklyDPSNANPSRI 1556
Cdd:TIGR02917 710 gDLYLRQKDYPAAIQAYRKALKRAPSSQNAIKLhrallasgntaEAVKTLEAWLK---------------THPNDAVLRT 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 1557 VNTEPFVMPWQAAQDVKtnpdlllaVFEDAVKACTDetltsgerievclplytNMIALHQL----LERYE-EAVELCTSL 1631
Cdd:TIGR02917 775 ALAELYLAQKDYDKAIK--------HYQTVVKKAPD-----------------NAVVLNNLawlyLELKDpRALEYAERA 829
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 90991706 1632 LESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHLCK 1681
Cdd:TIGR02917 830 LKLAPNIPAILDTLGWLLVEKGEADRALPLLRKAVNIAPEAAAIRYHLAL 879
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
743-1007 |
7.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 743 EARRTAEQASKPKVPPKSEKENdplRTPEALPEEKKMEYRLLKEEIANRekqrliKSDQLKTSSSSPANSDVEMDGIGRI 822
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKK------KADAAKKKAEEKKKADEAKKKAEED 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 823 AMVTKQVADAEAKLKKHKILLIKDESVLKnlvLQEAKKK-ESVRNAEAKITKLTEQLQAAEKILSANRMflKKLQEQIHR 901
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKK---ADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEA--KKADEAKKK 1478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 902 VQQRvtiKKALTLKYGEELARAKA--VASKELGKRKLEQDRLGPNKMMRLDNSPISSPRKHSAELIAMEKRRLQKL---- 975
Cdd:PTZ00121 1479 AEEA---KKADEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkae 1555
|
250 260 270
....*....|....*....|....*....|..
gi 90991706 976 EYEYALKIQKLKEARalKAKEQQNLVPVVEEE 1007
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAK--KAEEDKNMALRKAEE 1585
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
819-1081 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 819 IGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILS---------ANR 889
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSireiscqqhTLT 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 890 MFLKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKElgkRKLEQDRLGPNKMMRLDNSPISSPRKHSAELIA--- 966
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQcek 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 967 MEKRRLQKLEYEYALKIQKLK----------------EARALKAKEQQNLVPVVEEEPE--------FSVPQPSLHDLTQ 1022
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQLQtkeqihlqetrkkavvLARLLELQEEPCPLCGSCIHPNparqdidnPGPLTRRMQRGEQ 535
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90991706 1023 DKLTLDTEENDVDDEVLSgaSRERRRSF---LESNSFTKPNLKHTDTPNKECINKLSKSTVE 1081
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 ... |
742-1069 |
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 90991706 742 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKMEYRLLKEEIA------NREKQRLIKSDQLKTSSSSPANSDVE 815
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKllakeeEELKSELLKLERRKVDDEEKLKESEK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 816 MDG--IGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSANRMF-- 891
Cdd:pfam02463 322 EKKkaEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELks 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 892 --LKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKELGKRKLEQDRLGPNKMMRLDNSPISSPRKHSAELIAMEK 969
Cdd:pfam02463 402 eeEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 970 RRLQKLEyeyALKIQKLKEARalkAKEQQNLVPVVEEEPEFSVPQPSLHDLTQDKLTlDTEENDVDDEVLSGASRERRRS 1049
Cdd:pfam02463 482 LQEQLEL---LLSRQKLEERS---QKESKARSGLKVLLALIKDGVGGRIISAHGRLG-DLGVAVENYKVAISTAVIVEVS 554
|
330 340
....*....|....*....|
gi 90991706 1050 FLESNSFTKPNLKHTDTPNK 1069
Cdd:pfam02463 555 ATADEVEERQKLVRALTELP 574
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
776-998 |
1.57e-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: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 776 EKKMEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEmdgigrIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVL 855
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELE------ELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 856 QEAKKKEsvRNAEAKITKLTEQLQAAEKILSANRMFLKKLQEQIHRVQQRVtikkaltLKYGEELARAKAVASKELGKRK 935
Cdd:COG1196 284 EEAQAEE--YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL-------EELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90991706 936 LEQDRLgpnkmmrldnspisspRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAKEQQ 998
Cdd:COG1196 355 EAEAEL----------------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
1614-1679 |
2.50e-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: 2.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90991706 1614 LHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEIFYHL 1679
Cdd:COG4235 26 AYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLL 91
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
738-925 |
3.10e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 738 ESMIKEARRTAEQASKpkvppksekendplrtpEALPEEKKmEYRLLKEEIANREKQRLIKSDQLKtsssspansdvemd 817
Cdd:PRK12704 41 KRILEEAKKEAEAIKK-----------------EALLEAKE-EIHKLRNEFEKELRERRNELQKLE-------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 818 gigriamvtKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKL-TEQLQAAEKI--LS---ANRMF 891
Cdd:PRK12704 89 ---------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERIsgLTaeeAKEIL 159
|
170 180 190
....*....|....*....|....*....|....
gi 90991706 892 LKKLQEQIhRVQQRVTIKKAltlkygEELARAKA 925
Cdd:PRK12704 160 LEKVEEEA-RHEAAVLIKEI------EEEAKEEA 186
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1607-1672 |
4.80e-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: 4.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90991706 1607 LYTNMIALHQLLERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQN 1672
Cdd:COG4783 74 ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
1607-1660 |
6.40e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 37.37 E-value: 6.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90991706 1607 LYTNMIALHQLLERYEEAVELCTSLLESC--------PTNCQLLETLAALYLKTDRYDKARR 1660
Cdd:pfam13424 5 ALNNLAAVLRRLGRYDEALELLEKALEIArrllgpdhPLTATTLLNLGRLYLELGRYEEALE 66
|
|
| TPR_19 |
pfam14559 |
Tetratricopeptide repeat; |
1619-1675 |
7.30e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 434038 [Multi-domain] Cd Length: 65 Bit Score: 36.79 E-value: 7.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 90991706 1619 ERYEEAVELCTSLLESCPTNCQLLETLAALYLKTDRYDKARRVWLTAFENNPQNAEI 1675
Cdd:pfam14559 2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRY 58
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
834-992 |
7.41e-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: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 834 AKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTE-QLQAAEKILSANRMFLKKLQEQIHRVQQRVT----- 907
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEkLSEAEDMLACEQHALLRKLQPEQDLQDVRLHlqqcs 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 908 --IKKALTLKYGEELA------RAKAVASKELGKRKLEQDRLGPNKM--------------------MRLDNSPISSPRK 959
Cdd:TIGR00618 639 qeLALKLTALHALQLTltqervREHALSIRVLPKELLASRQLALQKMqsekeqltywkemlaqcqtlLRELETHIEEYDR 718
|
170 180 190
....*....|....*....|....*....|...
gi 90991706 960 HSAELIAMEKRRLQKLEYEYALKIQKLKEARAL 992
Cdd:TIGR00618 719 EFNEIENASSSLGSDLAAREDALNQSLKELMHQ 751
|
|
| TPR_19 |
pfam14559 |
Tetratricopeptide repeat; |
1350-1407 |
7.75e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 434038 [Multi-domain] Cd Length: 65 Bit Score: 36.79 E-value: 7.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 90991706 1350 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIW 1407
Cdd:pfam14559 8 LELLEQALAEDPDNAEARLGLAEALLALGR------LDEAEALLAALPAADPDDPRYA 59
|
|
| TPR_14 |
pfam13428 |
Tetratricopeptide repeat; |
1364-1413 |
8.48e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 463874 [Multi-domain] Cd Length: 44 Bit Score: 35.86 E-value: 8.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 90991706 1364 VQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRL 1413
Cdd:pfam13428 1 PEALLALARALLALGD------PDEALALLERALALDPDDPEAWLALAQL 44
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
775-1027 |
9.78e-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: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 775 EEKKMEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEMDGIGRiamvTKQVADAEAKLKKHKILLIKDEsvLKNLV 854
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES----KLDELAEELAELEEKLEELKEE--LESLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 855 LQEAKKKESVRNAEAKITKLTEQLQAAekilsANRMFLKKLQEQIHRVQQRVtikkaltlkYGEELARAKAVASKELGKR 934
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETL-----RSKVAQLELQIASLNNEIER---------LEARLERLEDRRERLQQEI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90991706 935 KLEQDRLGPNKMMRLdnspissprkhsAELIAMEKRRLQKLEYEYALKIQKLKEARALKAKEQQNLVPVVEEEPEFSVPQ 1014
Cdd:TIGR02168 424 EELLKKLEEAELKEL------------QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
250
....*....|...
gi 90991706 1015 PSLHDLTQDKLTL 1027
Cdd:TIGR02168 492 DSLERLQENLEGF 504
|
|
|