|
Name |
Accession |
Description |
Interval |
E-value |
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
43-726 |
0e+00 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 573.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 43 AGKIAGAGLLFVGGGIGGTILYAKWDSHFRESVEKTIPYSDKLFGMVLGSAPYTVPlpkKPIQSGPLKISSVSEVMTDSE 122
Cdd:pfam09731 4 FGKFFVALVLIVGVGYGGVVLYAYKDDNFRDFFEEYIPYGEEVVLYALGEDPPLAP---KPKTFRPLQPSVVSAVTGESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 123 LPMAQTQETNGDTPASAASTgaaqiisAAGDPAPEVEHEDTINTECPNTDEGTStfvtAALAKSLEDALNQTATVTRQTI 202
Cdd:pfam09731 81 EPKEEKKQVKIPRQSGVSSE-------VAEEEKEATKDAAEAKAQLPKSEQEKE----KALEEVLKEAISKAESATAVAK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 203 TAQNAAVQAVKAHSSTLKTAMDNSEIAGEKKSAQWRTVEGALKErrkavdeaadallkakeeleKMKTIIEDAKKREIAG 282
Cdd:pfam09731 150 EAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAE--------------------KLKEVINLAKQSEEEA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 283 ATPYITAAEEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDFRKELDSITPDITPGWKGMSIsdlagtLSTD 362
Cdd:pfam09731 210 APPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNL------LSND 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 363 DLNALIAHAHRRIDQLNRELAQQKATEKQHIELALERQKlEEKRAFDSAVAKALEHHRS----EIQAEQDRKVEEVRDAM 438
Cdd:pfam09731 284 DLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQK-EELDKLAEELSARLEEVRAadeaQLRLEFEREREEIRESY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 439 ENEMRTQLRRQAAAHTDHLRDVLKVQEQELKFEFEQclqrleeeadpwncsqfDLSEKLSEQElefhrrsqeqmDNFTLD 518
Cdd:pfam09731 363 EEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQ-----------------DIKEKVEEER-----------AGRLLK 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 519 INTAYARLRGIEQAVQSHAVAEEEARKAHQLWLSVEALKYSMKTSSAEMPTIPLGSAVEAIRVSCSDNEFTQALTAAIPP 598
Cdd:pfam09731 415 LNELLANLKGLEKATSSHSEVEDENRKAQQLWLAVEALRSTLEDGSADSRPRPLVRELKALKELASDDEVVKAALASLPE 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 599 ESLTRGVYSEETLRARFYAVQKLAGRVAMIDETKNSLYQYFLSYLQSLLLFPPKQlkppAELYPEDINTFKLLSYASYCI 678
Cdd:pfam09731 495 EAYQRGVYTEAALRERFRRVAKEVRKVSLIDPEGAGLLSHALSYLLSKLMFKPKQ----GEADPAGDDVESILARAEYYL 570
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1958769463 679 EHGDLELAAKFVNQLKGESRRVAQDWLKEARMTLETKQIVEILTTYAS 726
Cdd:pfam09731 571 EEGDLDSAAREMNSLKGWSKKLASDWLKEARRRLEVQQALELLQAEAA 618
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
205-557 |
3.69e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 205 QNAAVQAVKAHSS-TLKTAMDNSEIAGEKKSAQWRTVEGALK--ERRKAVDEAADALLKAKEELEKMKTIIEDAK----- 276
Cdd:PTZ00121 1268 RQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKkaaea 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 277 -KREIAGATPYITAAEEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDfRKELDSITPDITPGWKGMSISDL 355
Cdd:PTZ00121 1348 aKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED-KKKADELKKAAAAKKKADEAKKK 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 356 AGTLSTDDLNALIAHAHRRIDQLNR--------ELAQQKATEKQHIELAleRQKLEEKRAFDSAVAKALEHHRSEIQ--- 424
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKkaeeakkaEEAKKKAEEAKKADEA--KKKAEEAKKADEAKKKAEEAKKKADEakk 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 425 -------------AEQDRKVEEVRDAMENEMRTQLRR-QAAAHTDHLRDVLKVQEQELKFEFEQclQRLEEEADPWNCSQ 490
Cdd:PTZ00121 1505 aaeakkkadeakkAEEAKKADEAKKAEEAKKADEAKKaEEKKKADELKKAEELKKAEEKKKAEE--AKKAEEDKNMALRK 1582
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769463 491 FDLSEKLSEqelefhRRSQEQMDNFTLDINTAYARLRGIEQAvqshAVAEEEARKAHQLWLSVEALK 557
Cdd:PTZ00121 1583 AEEAKKAEE------ARIEEVMKLYEEEKKMKAEEAKKAEEA----KIKAEELKKAEEEKKKVEQLK 1639
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-549 |
1.45e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 208 AVQAVKAHssTLKTAMDnsEIAGEKKSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKTIIEDAKKReiagatpyI 287
Cdd:COG1196 209 AEKAERYR--ELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE--------L 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 288 TAAEEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDFRKELDSITpditpgwkgMSISDLAGTLSTDDLNAL 367
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE---------EELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 368 IAHAHRRIDQLNRELAQQKATEKQHIELALERQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKVEEVRDAMENEMRTQLR 447
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 448 RQAAAHTDHLRDVLKVQEQELKFEFEQCLQRLEEEAdpwncsqfDLSEKLSEQELEfhrrsQEQMDNFTLDINTAYARLR 527
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE--------LLAELLEEAALL-----EAALAELLEELAEAAARLL 494
|
330 340
....*....|....*....|..
gi 1958769463 528 GIEQAVQSHAVAEEEARKAHQL 549
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLL 516
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-535 |
4.97e-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: 50.44 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 211 AVKAHSSTLKTamdNSEIagEKKSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKTIIEDaKKREIAGATPYITAA 290
Cdd:TIGR02168 665 SAKTNSSILER---RREI--EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 291 EEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDFRKELDSITPDITPGWKGMSISDLAGTLSTDDLNALIAH 370
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 371 AHRRIDQLNRELAQQKATEKQHIELALERQKLEEKRAFDSAV-----------AKALEHHrSEIQAEQDRKVEEVRDAME 439
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieeleelieelESELEAL-LNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 440 NEM---------RTQLRRQAAAHTDHLRDvLKVQEQELKFEFEQCLQRLEEEAdpwncsqfdlseKLSEQELEfhrrsqE 510
Cdd:TIGR02168 898 ELSeelreleskRSELRRELEELREKLAQ-LELRLEGLEVRIDNLQERLSEEY------------SLTLEEAE------A 958
|
330 340
....*....|....*....|....*
gi 1958769463 511 QMDNFTLDINTAYARLRGIEQAVQS 535
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKE 983
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
368-482 |
4.17e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.87 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 368 IAHAHRRIDQLNRELAQQKATEKQHIELA-LERQKLEEKRAFdsavakaLEHHRSEIQAEQDRKVEEVRDAMENEMRTQL 446
Cdd:cd16269 182 EAEAILQADQALTEKEKEIEAERAKAEAAeQERKLLEEQQRE-------LEQKLEDQERSYEEHLRQLKEKMEEERENLL 254
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958769463 447 RRQAAAhtdhLRDVLKVQEQELKFEFEQCLQRLEEE 482
Cdd:cd16269 255 KEQERA----LESKLKEQEALLEEGFKEQAELLQEE 286
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
43-726 |
0e+00 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 573.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 43 AGKIAGAGLLFVGGGIGGTILYAKWDSHFRESVEKTIPYSDKLFGMVLGSAPYTVPlpkKPIQSGPLKISSVSEVMTDSE 122
Cdd:pfam09731 4 FGKFFVALVLIVGVGYGGVVLYAYKDDNFRDFFEEYIPYGEEVVLYALGEDPPLAP---KPKTFRPLQPSVVSAVTGESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 123 LPMAQTQETNGDTPASAASTgaaqiisAAGDPAPEVEHEDTINTECPNTDEGTStfvtAALAKSLEDALNQTATVTRQTI 202
Cdd:pfam09731 81 EPKEEKKQVKIPRQSGVSSE-------VAEEEKEATKDAAEAKAQLPKSEQEKE----KALEEVLKEAISKAESATAVAK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 203 TAQNAAVQAVKAHSSTLKTAMDNSEIAGEKKSAQWRTVEGALKErrkavdeaadallkakeeleKMKTIIEDAKKREIAG 282
Cdd:pfam09731 150 EAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAE--------------------KLKEVINLAKQSEEEA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 283 ATPYITAAEEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDFRKELDSITPDITPGWKGMSIsdlagtLSTD 362
Cdd:pfam09731 210 APPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNL------LSND 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 363 DLNALIAHAHRRIDQLNRELAQQKATEKQHIELALERQKlEEKRAFDSAVAKALEHHRS----EIQAEQDRKVEEVRDAM 438
Cdd:pfam09731 284 DLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQK-EELDKLAEELSARLEEVRAadeaQLRLEFEREREEIRESY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 439 ENEMRTQLRRQAAAHTDHLRDVLKVQEQELKFEFEQclqrleeeadpwncsqfDLSEKLSEQElefhrrsqeqmDNFTLD 518
Cdd:pfam09731 363 EEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQ-----------------DIKEKVEEER-----------AGRLLK 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 519 INTAYARLRGIEQAVQSHAVAEEEARKAHQLWLSVEALKYSMKTSSAEMPTIPLGSAVEAIRVSCSDNEFTQALTAAIPP 598
Cdd:pfam09731 415 LNELLANLKGLEKATSSHSEVEDENRKAQQLWLAVEALRSTLEDGSADSRPRPLVRELKALKELASDDEVVKAALASLPE 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 599 ESLTRGVYSEETLRARFYAVQKLAGRVAMIDETKNSLYQYFLSYLQSLLLFPPKQlkppAELYPEDINTFKLLSYASYCI 678
Cdd:pfam09731 495 EAYQRGVYTEAALRERFRRVAKEVRKVSLIDPEGAGLLSHALSYLLSKLMFKPKQ----GEADPAGDDVESILARAEYYL 570
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1958769463 679 EHGDLELAAKFVNQLKGESRRVAQDWLKEARMTLETKQIVEILTTYAS 726
Cdd:pfam09731 571 EEGDLDSAAREMNSLKGWSKKLASDWLKEARRRLEVQQALELLQAEAA 618
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
205-557 |
3.69e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 205 QNAAVQAVKAHSS-TLKTAMDNSEIAGEKKSAQWRTVEGALK--ERRKAVDEAADALLKAKEELEKMKTIIEDAK----- 276
Cdd:PTZ00121 1268 RQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKkaaea 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 277 -KREIAGATPYITAAEEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDfRKELDSITPDITPGWKGMSISDL 355
Cdd:PTZ00121 1348 aKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED-KKKADELKKAAAAKKKADEAKKK 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 356 AGTLSTDDLNALIAHAHRRIDQLNR--------ELAQQKATEKQHIELAleRQKLEEKRAFDSAVAKALEHHRSEIQ--- 424
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKkaeeakkaEEAKKKAEEAKKADEA--KKKAEEAKKADEAKKKAEEAKKKADEakk 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 425 -------------AEQDRKVEEVRDAMENEMRTQLRR-QAAAHTDHLRDVLKVQEQELKFEFEQclQRLEEEADPWNCSQ 490
Cdd:PTZ00121 1505 aaeakkkadeakkAEEAKKADEAKKAEEAKKADEAKKaEEKKKADELKKAEELKKAEEKKKAEE--AKKAEEDKNMALRK 1582
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769463 491 FDLSEKLSEqelefhRRSQEQMDNFTLDINTAYARLRGIEQAvqshAVAEEEARKAHQLWLSVEALK 557
Cdd:PTZ00121 1583 AEEAKKAEE------ARIEEVMKLYEEEKKMKAEEAKKAEEA----KIKAEELKKAEEEKKKVEQLK 1639
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-549 |
1.45e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 208 AVQAVKAHssTLKTAMDnsEIAGEKKSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKTIIEDAKKReiagatpyI 287
Cdd:COG1196 209 AEKAERYR--ELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE--------L 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 288 TAAEEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDFRKELDSITpditpgwkgMSISDLAGTLSTDDLNAL 367
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE---------EELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 368 IAHAHRRIDQLNRELAQQKATEKQHIELALERQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKVEEVRDAMENEMRTQLR 447
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 448 RQAAAHTDHLRDVLKVQEQELKFEFEQCLQRLEEEAdpwncsqfDLSEKLSEQELEfhrrsQEQMDNFTLDINTAYARLR 527
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE--------LLAELLEEAALL-----EAALAELLEELAEAAARLL 494
|
330 340
....*....|....*....|..
gi 1958769463 528 GIEQAVQSHAVAEEEARKAHQL 549
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLL 516
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-549 |
3.16e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 181 AALAKSLEDALNQTATVTRQtitAQNAAVQAVKAHSSTLKTAMDNSEIAGEKKSAQWRTVEGALK--ERRKAVDEA---A 255
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKK---AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAkkkA 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 256 DALLKAKEELEKM---KTIIEDAKKR--EIAGATPYITAAEEKlhsmivdldsvvKKVQAAQSEAKVVSQYHELVVQARD 330
Cdd:PTZ00121 1401 EEDKKKADELKKAaaaKKKADEAKKKaeEKKKADEAKKKAEEA------------KKADEAKKKAEEAKKAEEAKKKAEE 1468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 331 dfRKELDSITPDITPGWKGmsisdlagtlstDDLNALIAHAHRRIDQLNR-ELAQQKATEKQHIE---LALERQKLEEKR 406
Cdd:PTZ00121 1469 --AKKADEAKKKAEEAKKA------------DEAKKKAEEAKKKADEAKKaAEAKKKADEAKKAEeakKADEAKKAEEAK 1534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 407 AFDSAvAKALEHHRSE--IQAEQDRKVEEVRDA----MENEMRTQLRRQA----AAHTDHLRDVLKVQEQELKFEFEQcL 476
Cdd:PTZ00121 1535 KADEA-KKAEEKKKADelKKAEELKKAEEKKKAeeakKAEEDKNMALRKAeeakKAEEARIEEVMKLYEEEKKMKAEE-A 1612
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769463 477 QRLEEEADPwncsqfdlSEKLSEQELEfhRRSQEQMDNFTLDINTAYARLRGIEQ-----AVQSHAVAEEEARKAHQL 549
Cdd:PTZ00121 1613 KKAEEAKIK--------AEELKKAEEE--KKKVEQLKKKEAEEKKKAEELKKAEEenkikAAEEAKKAEEDKKKAEEA 1680
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-535 |
4.97e-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: 50.44 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 211 AVKAHSSTLKTamdNSEIagEKKSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKTIIEDaKKREIAGATPYITAA 290
Cdd:TIGR02168 665 SAKTNSSILER---RREI--EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 291 EEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDFRKELDSITPDITPGWKGMSISDLAGTLSTDDLNALIAH 370
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 371 AHRRIDQLNRELAQQKATEKQHIELALERQKLEEKRAFDSAV-----------AKALEHHrSEIQAEQDRKVEEVRDAME 439
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieeleelieelESELEAL-LNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 440 NEM---------RTQLRRQAAAHTDHLRDvLKVQEQELKFEFEQCLQRLEEEAdpwncsqfdlseKLSEQELEfhrrsqE 510
Cdd:TIGR02168 898 ELSeelreleskRSELRRELEELREKLAQ-LELRLEGLEVRIDNLQERLSEEY------------SLTLEEAE------A 958
|
330 340
....*....|....*....|....*
gi 1958769463 511 QMDNFTLDINTAYARLRGIEQAVQS 535
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKE 983
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-463 |
5.44e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 198 TRQTITAQNAAVQAVKAHSSTLKTAmdnseiagekkSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKTIIEDAKK 277
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAAL-----------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 278 R----EIAGATPYITAAEEKLHSmiVDLDSVVKKVQA------AQSEAKVVSQYHELV--------------------VQ 327
Cdd:COG4913 735 RleaaEDLARLELRALLEERFAA--ALGDAVERELREnleeriDALRARLNRAEEELEramrafnrewpaetadldadLE 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 328 ARDDFRKELDSITPDITPG-----------WKGMSISDLAGTLSTDdlnalIAHAHRRIDQLNRELAQQKATEKQHIELA 396
Cdd:COG4913 813 SLPEYLALLDRLEEDGLPEyeerfkellneNSIEFVADLLSKLRRA-----IREIKERIDPLNDSLKRIPFGPGRYLRLE 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769463 397 LERQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKVEEVRDAMEnemrtQLRRQAAAHTDH-LRDVLKV 463
Cdd:COG4913 888 ARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIE-----RLRSEEEESDRRwRARVLDV 950
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
150-549 |
9.83e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 150 AAGDPAPEVEHEDTINTECPNTDEGTSTFVTAALAKSLEDALNQTATVTRQTITAQNAAVQAVKAHSSTLKTAMDNSEIA 229
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 230 GEKKSAQWRTVEGALK--ERRKAVDEA---ADALLKAKEELEKM---KTIIEDAKKREIAGATPYITAAEEKLHSMIVDL 301
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKkaEEAKKADEAkkkAEEAKKKADEAKKAaeaKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 302 DSVVKKVQAAQSEAKVvsQYHELVVQARDDFRKELDsitpditpgwKGMSISDlagtlstddlnaliAHAHRRIDQlNRE 381
Cdd:PTZ00121 1542 AEEKKKADELKKAEEL--KKAEEKKKAEEAKKAEED----------KNMALRK--------------AEEAKKAEE-ARI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 382 LAQQKATEKQHIELALERQKLEEKRAFDSAVAKALEHHRSEIQ-----AEQDRKVEEVRDAME-NEMRT-QLRRQAAAHT 454
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQlkkkeAEEKKKAEELKKAEEeNKIKAaEEAKKAEEDK 1674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 455 DHLRDVLKVQEQELKFEfEQCLQRLEEEADPWNCSQFDLSEKLSEQELefhRRSQEQmdnftldintayaRLRGIEQAVQ 534
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAA-EALKKEAEEAKKAEELKKKEAEEKKKAEEL---KKAEEE-------------NKIKAEEAKK 1737
|
410
....*....|....*
gi 1958769463 535 ShavAEEEARKAHQL 549
Cdd:PTZ00121 1738 E---AEEDKKKAEEA 1749
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
376-548 |
1.49e-05 |
|
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: 48.81 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 376 DQLNRELAQQKATEKQHIELALERQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKVEEVRDAMENEMRTQLRRQAAAhtd 455
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA--- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 456 HLRDVLKVQEQElkfEFEQCLQRLEEEADPWNCSQFDLSEKLSEQ-ELEFHRRSQEQMDNFTLDINTAYARLRGIEQAVQ 534
Cdd:TIGR00618 333 HVKQQSSIEEQR---RLLQTLHSQEIHIRDAHEVATSIREISCQQhTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ 409
|
170
....*....|....
gi 1958769463 535 SHAVAEEEARKAHQ 548
Cdd:TIGR00618 410 ATIDTRTSAFRDLQ 423
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
180-535 |
1.88e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 180 TAALAKSLEDALNQTATVTRQTITAQNAAVQAVKAHSSTLKTAMdnseiagekkSAQWRTVEGALKERRKAVDEAADAL- 258
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK----------QAYWQVVEGALDAQLALLKAAIAARr 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 259 LKAKEELEKMKTiiedAKKREIAGATPyitaAEEKLHSMIVDLDSVVKKV-QAAQSEAKVVSQ---YHELVVQARDDFRK 334
Cdd:pfam12128 743 SGAKAELKALET----WYKRDLASLGV----DPDVIAKLKREIRTLERKIeRIAVRRQEVLRYfdwYQETWLQRRPRLAT 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 335 ELDSITpditpgwkgMSISDLagtlsTDDLNALIAHAHRRIDQLNRELaqqKATEKQHIELALERQKLeekRAFDSAVAK 414
Cdd:pfam12128 815 QLSNIE---------RAISEL-----QQQLARLIADTKLRRAKLEMER---KASEKQQVRLSENLRGL---RCEMSKLAT 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 415 ALEHHRSE----IQAEQDRKVEEVRDAMENEM---RTQLRRQAAAHTDH-----------LRDVLKVQ--EQELKFEFEQ 474
Cdd:pfam12128 875 LKEDANSEqaqgSIGERLAQLEDLKLKRDYLSesvKKYVEHFKNVIADHsgsglaetwesLREEDHYQndKGIRLLDYRK 954
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769463 475 CLQRLEEEADPwncsqfdlsekLSEQELEFHRrsqEQMDNFTLDINTAYARLRGIEQAVQS 535
Cdd:pfam12128 955 LVPYLEQWFDV-----------RVPQSIMVLR---EQVSILGVDLTEFYDVLADFDRRIAS 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
245-557 |
1.91e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 245 KERRKAVDEAA----------DALLK---AKEELEKMKTII--------------EDAKK-----------------REI 280
Cdd:COG1196 155 EERRAIIEEAAgiskykerkeEAERKleaTEENLERLEDILgelerqleplerqaEKAERyrelkeelkeleaelllLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 281 AGATPYITAAEEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDFRKELDSITpditpgwkgMSISDLAGTLs 360
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL---------AELARLEQDI- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 361 tDDLNALIAHAHRRIDQLNRELAQQKATEKQH--------IELALERQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKVE 432
Cdd:COG1196 305 -ARLEERRRELEERLEELEEELAELEEELEELeeeleeleEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 433 EVRDAMENEMRTQLRRQAAAHTDHLRDVLKVQEQELKFEFEQCLQRLEEEADpwncsQFDLSEKLSEQELEFHRRSQEQM 512
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-----EEEEEEEALEEAAEEEAELEEEE 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958769463 513 DNFTLDINTAYARLRGIEQAVQshAVAEEEARKAHQLWLSVEALK 557
Cdd:COG1196 459 EALLELLAELLEEAALLEAALA--ELLEELAEAAARLLLLLEAEA 501
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
362-548 |
3.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 362 DDLNAL---IAHAHRRIDQL-----NRELAQQKATEKQHIELALERQKLEEKRAFDSAVAKALEHHRSEIQAEQDRK--V 431
Cdd:COG4913 235 DDLERAheaLEDAREQIELLepireLAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELerL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 432 EEVRDAMENEmRTQLRRQAAAHTDHLRDVLKVQEQELKFEFEQCLQRLEEEADpwNCSQFDLSEKLSEQEL-EFHRRSQE 510
Cdd:COG4913 315 EARLDALREE-LDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA--LLAALGLPLPASAEEFaALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958769463 511 QMDNFTldintayARLRGIEQAVQSHAVAEEEARKAHQ 548
Cdd:COG4913 392 LLEALE-------EELEALEEALAEAEAALRDLRRELR 422
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-625 |
9.19e-05 |
|
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: 46.20 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 256 DALLKAKEEleKMKTIIEDAkkreiAGATPYIT---AAEEKLHSMIVDLDSVV-------KKVQAAQSEAKVVSQYHELV 325
Cdd:TIGR02168 147 SEIIEAKPE--ERRAIFEEA-----AGISKYKErrkETERKLERTRENLDRLEdilneleRQLKSLERQAEKAERYKELK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 326 VQarddfrkeldsitpditpgwkgmsISDLAGTLSTDDLNALIAHAHRR---IDQLNREL----AQQKATEKQHIELALE 398
Cdd:TIGR02168 220 AE------------------------LRELELALLVLRLEELREELEELqeeLKEAEEELeeltAELQELEEKLEELRLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 399 RQKLEEK-----RAFDSAVAK--ALEHHRSEIQAEQDR---KVEEVRDAMENEMRTQLRRQAAAHTdhlrdvLKVQEQEL 468
Cdd:TIGR02168 276 VSELEEEieelqKELYALANEisRLEQQKQILRERLANlerQLEELEAQLEELESKLDELAEELAE------LEEKLEEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 469 KFEFEQCLQRLEEEADPWncsqFDLSEKLSEQELEFHRRS------QEQMDNFTLDINTAYARLrgiEQAVQSHAVAEEE 542
Cdd:TIGR02168 350 KEELESLEAELEELEAEL----EELESRLEELEEQLETLRskvaqlELQIASLNNEIERLEARL---ERLEDRRERLQQE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 543 ARKAHQLWLSVEALKYSMKTSSAEMPTIPLGSAVEAI--RVSCSDNEFTQALTAaippesLTRGVYSEETLRARFYAVQK 620
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLeeALEELREELEEAEQA------LDAAERELAQLQARLDSLER 496
|
....*
gi 1958769463 621 LAGRV 625
Cdd:TIGR02168 497 LQENL 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
254-483 |
1.42e-04 |
|
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: 44.75 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 254 AADALLKAKEELEKMKTIIEdAKKREIAGATPYITAAEEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDFR 333
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 334 KELDSITPDITP----GWKGMSISDLAGTLSTDDLNALIAHAhRRIDQLNRELAQQ-KATEKQHIELALERQKLEEKRAF 408
Cdd:COG4942 97 AELEAQKEELAEllraLYRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREQaEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769463 409 DSAVAKALEHHRSEIQAEQDRKveevrdameNEMRTQLRRQAAAHTDHLRDvLKVQEQELkfefEQCLQRLEEEA 483
Cdd:COG4942 176 LEALLAELEEERAALEALKAER---------QKLLARLEKELAELAAELAE-LQQEAEEL----EALIARLEAEA 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
275-545 |
1.48e-04 |
|
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: 45.43 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 275 AKKREIAGATPYITAAEEKLHsmivdldsvvkkvqAAQSEAKVVSQYHELVVQARDDFRKELDSITPDItpgwkgmsisd 354
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIA--------------ELEKALAELRKELEELEEELEQLRKELEELSRQI----------- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 355 lagtlstDDLNALIAHAHRRIDQLNRELAQQKATEKqhiELALERQKLEEKRAFDSAVAKALEHHRseiqAEQDRKVEEV 434
Cdd:TIGR02168 729 -------SALRKDLARLEAEVEQLEERIAQLSKELT---ELEAEIEELEERLEEAEEELAEAEAEI----EELEAQIEQL 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 435 RDAMENEmRTQLRRQAAAHTDHLRDVLKVQE--QELKFEFEQCLQRLEEEADPWNcsqfDLSEKLSEQELEfHRRSQEQM 512
Cdd:TIGR02168 795 KEELKAL-REALDELRAELTLLNEEAANLRErlESLERRIAATERRLEDLEEQIE----ELSEDIESLAAE-IEELEELI 868
|
250 260 270
....*....|....*....|....*....|...
gi 1958769463 513 DNFTLDINTAYARLRGIEQAVQSHAVAEEEARK 545
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSE 901
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
397-510 |
4.26e-04 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 41.58 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 397 LERQKLEE------KRAFDSAVAKALEHHRSEIQAEQDRKVEEVRDAMENEMRTQL--RRQAAAHTDHLRD--------- 459
Cdd:pfam15346 3 AESKLLEEetarrvEEAVAKRVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELerEREAELEEERRKEeeerkkree 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958769463 460 --------VLKVQEQELKFEFEQCL-----QRLEEEAdpwncsqfdlsEKLSEQELEFHRRSQE 510
Cdd:pfam15346 83 lerileenNRKIEEAQRKEAEERLAmleeqRRMKEER-----------QRREKEEEEREKREQQ 135
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
373-557 |
1.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 373 RRIDQLNRELAQQKATEKQHIELALERQKLEEKRAfdsAVAKALEHHRSEIqaEQDRKVEEVRDAMENemRTQLRRQAAA 452
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE---ELEAELEELREEL--EKLEKLLQLLPLYQE--LEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 453 HTDHLRDvLKVQEQELKfEFEQCLQRLEEEADPWNCSQFDLSEKLSEQELEFHRRSQEQMDNFTLDINTAYARLRGIEQA 532
Cdd:COG4717 144 LPERLEE-LEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180
....*....|....*....|....*
gi 1958769463 533 VQSHAVAEEEARKAHQLWLSVEALK 557
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLK 246
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
380-570 |
1.15e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 380 RELAQQKATEKQHIELA-LERQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKVEEVRDAMENEMRTqlRRQAAAHTDHLR 458
Cdd:pfam17380 438 RRLEEERAREMERVRLEeQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE--RKQAMIEEERKR 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 459 DVL-KVQEQELKFEFEQCLQRLEEEadpwncsqfdlsEKLSEQELEFHRRSQEQMDNFTLDINTAYARLRgiEQAVQSHA 537
Cdd:pfam17380 516 KLLeKEMEERQKAIYEEERRREAEE------------ERRKQQEMEERRRIQEQMRKATEERSRLEAMER--EREMMRQI 581
|
170 180 190
....*....|....*....|....*....|....*
gi 1958769463 538 VAEEEARKAHQLWLSVEALK--YSMKTSSAEMPTI 570
Cdd:pfam17380 582 VESEKARAEYEATTPITTIKpiYRPRISEYQPPDV 616
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
362-547 |
1.94e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 362 DDLNALIAHAHRRIDQLNRELAQQKAtekqhiELALERQKLEEKRAFDSAVAKALEHHRSEIQ------AEQDRKVEEVR 435
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQ------EEEKLKERLEELEEDLSSLEQEIENVKSELKeleariEELEEDLHKLE 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 436 DAMENEMRTQLRRQAAAHTDHLRDVLK-VQEQELKF-EFEQCLQRLEEEAdpwncsqfDLSEKLSEQELEFHRRSQEQMD 513
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQAELSKLEEeVSRIEARLrEIEQKLNRLTLEK--------EYLEKEIQELQEQRIDLKEQIK 850
|
170 180 190
....*....|....*....|....*....|....
gi 1958769463 514 NFTLDINTAYARLRGIEQAVQSHAVAEEEARKAH 547
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
180-480 |
1.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 180 TAALAKS-LEDALNQTATVTRQTITAQNAAVQAVKAHSSTLKTAMdNSEIAGEKKSAqwRTVEGALKERRKAVDEAADAL 258
Cdd:PRK02224 296 DDLLAEAgLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAH-NEEAESLREDA--DDLEERAEELREEAAELESEL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 259 LKAKEELEKMKTIIEDAKKReiagatpyITAAEEKLHSMIVDLDSVvkkvqaaqseakvvSQYHELVVQARDDFRKELDS 338
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEE--------IEELRERFGDAPVDLGNA--------------EDFLEELREERDELREREAE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 339 ITPDITPGWK-----------------GMSISDLAGTLSTDDlnaliahAHRRIDQLNRELAQQKATE----------KQ 391
Cdd:PRK02224 431 LEATLRTARErveeaealleagkcpecGQPVEGSPHVETIEE-------DRERVEELEAELEDLEEEVeeveerleraED 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 392 HIELALERQKLEEKRafdSAVAKALEHHRSEIQAEQDRkVEEVR---DAMENEMRTQLRRQAAAH--TDHLRDVLKVQEQ 466
Cdd:PRK02224 504 LVEAEDRIERLEERR---EDLEELIAERRETIEEKRER-AEELReraAELEAEAEEKREAAAEAEeeAEEAREEVAELNS 579
|
330
....*....|....
gi 1958769463 467 ELKfEFEQCLQRLE 480
Cdd:PRK02224 580 KLA-ELKERIESLE 592
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
362-556 |
2.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 362 DDLNALIAHAHRRIDQLNRELAQQKATEKQHIELALERQKLEEKRAFDSAVAKALEHHRSEIQAEQ-----DRKVEEVRD 436
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelaelPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 437 AME--NEMRTQLRRQAAAHTDhLRDVLKVQEQELKFEFEQCLQRLEEEADpwncsqfDLSEKLSEQELEFHRRSQEqmdn 514
Cdd:COG4717 154 RLEelRELEEELEELEAELAE-LQEELEELLEQLSLATEEELQDLAEELE-------ELQQRLAELEEELEEAQEE---- 221
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958769463 515 ftldINTAYARLRGIEQAVQSHAvAEEEARKAHQLWLSVEAL 556
Cdd:COG4717 222 ----LEELEEELEQLENELEAAA-LEERLKEARLLLLIAAAL 258
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
204-557 |
2.30e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 204 AQNAAVQAVKAHSSTLKTAMDNSEIAGEKKSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKTI---IEDAKKREI 280
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIarkAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 281 AGATPYITAAEEKLHSMIVDLDSVVKKVQAAQsEAKVVSQYHElvVQARDDFRKELDSitpditpgwkgmsisdlagtls 360
Cdd:PTZ00121 1169 ARKAEDAKKAEAARKAEEVRKAEELRKAEDAR-KAEAARKAEE--ERKAEEARKAEDA---------------------- 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 361 tddlnaliahahRRIDQLNR-ELAQQKATEKQHIElalERQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKVEEVRDAME 439
Cdd:PTZ00121 1224 ------------KKAEAVKKaEEAKKDAEEAKKAE---EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 440 NEMRTQLRR-QAAAHTDHLR---------DVLKVQEQELKFEFEQCLQRLEE--EADPWNCSQFDLSEKLSEQELEFHRR 507
Cdd:PTZ00121 1289 KKKADEAKKaEEKKKADEAKkkaeeakkaDEAKKKAEEAKKKADAAKKKAEEakKAAEAAKAEAEAAADEAEAAEEKAEA 1368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958769463 508 SQEQMDNFTLDINTAYARLRGIEQAVQSHAVAEEEARKAHQLWLSVEALK 557
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-481 |
2.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 248 RKAVDEAADALLKAKEELEKMKTIIEDAK-KREIAGATPYITAAEEKLHSMIVDLDSVVKKVQAAQSEAKVvsqyhELVV 326
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAReQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL-----ELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 327 QARDDFRKELDSITPDItpgwkgmsisdlagtlstDDLNALIAHAHRRIDQLNRELAQQKATEKQHIELALERQKLEEKR 406
Cdd:COG4913 295 AELEELRAELARLEAEL------------------ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769463 407 AfdSAVAKALEHHRSEIQAEQDRKVEEVRDAMEN--EMRTQLRRQAAAHTDHLRDvLKVQEQELKFEFEQCLQRLEE 481
Cdd:COG4913 357 R--ERRRARLEALLAALGLPLPASAEEFAALRAEaaALLEALEEELEALEEALAE-AEAALRDLRRELRELEAEIAS 430
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
368-482 |
4.17e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.87 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 368 IAHAHRRIDQLNRELAQQKATEKQHIELA-LERQKLEEKRAFdsavakaLEHHRSEIQAEQDRKVEEVRDAMENEMRTQL 446
Cdd:cd16269 182 EAEAILQADQALTEKEKEIEAERAKAEAAeQERKLLEEQQRE-------LEQKLEDQERSYEEHLRQLKEKMEEERENLL 254
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958769463 447 RRQAAAhtdhLRDVLKVQEQELKFEFEQCLQRLEEE 482
Cdd:cd16269 255 KEQERA----LESKLKEQEALLEEGFKEQAELLQEE 286
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
240-434 |
5.09e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 240 VEGALKERRKAVDEAADALLKAKEELEKMKTIIEDAkKREIAgatpyitaaeeKLHSMIVDLDSVVKKVQAAQSEAKVVS 319
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIK-----------RLELEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 320 QYHELvvqarddfRKELDSITPDItpgwkgmsisdlagtlstDDLNALIAHAHRRIDQLNRELAQQKAtekqhiELALER 399
Cdd:COG1579 90 EYEAL--------QKEIESLKRRI------------------SDLEDEILELMERIEELEEELAELEA------ELAELE 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958769463 400 QKLEEKRA-FDSAVAKaLEHHRSEIQAEQDRKVEEV 434
Cdd:COG1579 138 AELEEKKAeLDEELAE-LEAELEELEAEREELAAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
181-480 |
7.15e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 181 AALAKSLEDALNQTATVTRQTITAQNAAVQAVKAHSSTLKTAMDNSEIAG----EKKSAQWRTVEGAL-------KERRK 249
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaALLLAGLRGLAGAVavligveAAYEA 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 250 AVDEAADALLKAK--EELEKMKTIIEDAKKREIAGAT--PYITAAEEKLHSMIVDLDSVVKKVQAAQSEAkvvsQYHELV 325
Cdd:COG1196 539 ALEAALAAALQNIvvEDDEVAAAAIEYLKAAKAGRATflPLDKIRARAALAAALARGAIGAAVDLVASDL----READAR 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 326 VQARDDFRKELDSITPDITPGWKGMSISDLAGTLSTDDLNALIAH----AHRRIDQLNRELAQQKATEKQHIELALERQK 401
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGgsltGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 402 LEEKRAFDSAvAKALEHHRSEIQAEQDRKVEEVRDAMENEMRTQLRRQAAAHTDHLRDV---------LKVQEQELKfEF 472
Cdd:COG1196 695 LEEALLAEEE-EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAleelpeppdLEELERELE-RL 772
|
....*...
gi 1958769463 473 EQCLQRLE 480
Cdd:COG1196 773 EREIEALG 780
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
290-525 |
7.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 290 AEEKLHSMIVDLDSVVKKVQAAQSEAKVVSQYHELVVQARDDFRKELDSITPDItpgwkgmsisDLAGtlstddlnalia 369
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI----------DVAS------------ 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 370 hAHRRIDQLNRELA--------------QQKATEKQHIELALERQKLEEKRAfdsAVAKALEHHRSEIQAEQDRkVEEVR 435
Cdd:COG4913 666 -AEREIAELEAELErldassddlaaleeQLEELEAELEELEEELDELKGEIG---RLEKELEQAEEELDELQDR-LEAAE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 436 DAMENEMRTQL--RRQAA---AHTDHLRDVLKVQEQELKFEFEQCLQRLEE------EADPWNCSQFDLS---------- 494
Cdd:COG4913 741 DLARLELRALLeeRFAAAlgdAVERELRENLEERIDALRARLNRAEEELERamrafnREWPAETADLDADleslpeylal 820
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958769463 495 -EKLSEQEL-----EFHRRSQEQMDNFTLDINTAYAR 525
Cdd:COG4913 821 lDRLEEDGLpeyeeRFKELLNENSIEFVADLLSKLRR 857
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
477-727 |
8.03e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 38.88 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 477 QRLEE-EADPWNCSQFD-LSEKLSEQELEFHRRSQEQMDnftLDINTAYARLRGIEQAVQSHAVAEEEARKAHQLWLSVE 554
Cdd:COG4223 21 QRLAAlEAAPAAAAATAaLEARLAALRAALAAAREAVAA---AAAAALEARLAALEAKAAAPEAEAAAAARAAALALAAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 555 ALKYSMKTSSaemptiPLGSAVEAIRVSCSDNEFTQALTAAippesLTRGVYSEETLRARFYAVQKLAGRVAMIDETKNS 634
Cdd:COG4223 98 ALRAAVERGQ------PFAAELAALEALAPDAPALAALAAF-----AATGVPTLAALRAEFPAAARAALAAARAPEADAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769463 635 LYQYFLSYLQSLLlfppkQLKPPAElyPEDINTFKLLSYASYCIEHGDLELAAKFVNQLKGESRRVAQDWLKEARMTLET 714
Cdd:COG4223 167 WLDRLLAFARSLV-----TVRRVGP--VEGDDPDAILARAEAALAAGDLAGALAELEALPEAAQAAAAPWIAKAEARLAA 239
|
250
....*....|...
gi 1958769463 715 KQIVEILTTYASA 727
Cdd:COG4223 240 DAALQALAAQALA 252
|
|
|