|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
144-702 |
2.40e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 144 KQQEARLRDQRQLIDVLRRQKKMLLDDIQrislEHDEKLSQLQQTVVGMELESKHVTGKCKQLLDLKSQMEHQLELRSTT 223
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELA----ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 224 LRSVTAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQYYQQ-KLKRESSMEIMHSYSMKFHEEINRKTSEIASLKN 302
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEaEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 303 SLNELQAELMLMSHMKEQCEEQQRQLEQLEFALQAQLLEETQLRQSNALKLEQVENLTISLASLQLDKEGLKENLGEAQK 382
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 383 TLKNLQQKVDILQKQYAEMCSLCQKTKQ-----QLELEKIEIAKMKQNGSLKESELMEKLKDYAAQCDELRKALAEAESR 457
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 458 IDVQIKKTEGWQVQ------------LKHNQATQTDLEDPILVQRIETLEQQLADVRSQKLHTVSLLQILLQQQEAKIKS 525
Cdd:COG1196 551 IVVEDDEVAAAAIEylkaakagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 526 TNEMEADWQQLLDALQATQSLEQEMRSELQHKTVELEHLNELFAGQNDELQKLQKLSQAQDEENRLELQLLKktfQENLK 605
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE---EEEER 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 606 INSAASINMQRLQGQVKSLLDEKEEIAREERKAVECLRSLGHVLEMETGRRLPHIKSWPQLAKILRKELRN-GRVNNRKA 684
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlGPVNLLAI 787
|
570
....*....|....*...
gi 24668309 685 EElpglkmkLAEISGRHQ 702
Cdd:COG1196 788 EE-------YEELEERYD 798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-504 |
3.17e-09 |
|
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: 60.84 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 220 RSTTLRSVTAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQYYQQKLKRESSMEIMHSysmKFHEEINRKTSEIAS 299
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA---RLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 300 LKNSLNELQAELmlmshmkeqcEEQQRQLEQLEFALQAQLLEETQLRQSNALKLEQVENLTISLASLQLDKEGLKENLGE 379
Cdd:TIGR02168 752 LSKELTELEAEI----------EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 380 AQKTLKNLQQKVDILQKQYAEMCSLCQKTKQQLELEKIEIAKMKQNGSLKESELMEKLKDYAAQcDELRKALAEAESRID 459
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL-EEALALLRSELEELS 900
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 24668309 460 VQIKKTEGWQVQLKHN-QATQTDLEDpiLVQRIETLEQQLADVRSQ 504
Cdd:TIGR02168 901 EELRELESKRSELRRElEELREKLAQ--LELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-413 |
2.22e-08 |
|
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: 58.14 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 148 ARLRDQRQLIDVLRRQKKMLLDDIQRISLEHDEKLSQLQQTVVGM-ELESK--HVTGKCKQLLDLKSQMEHQLELRSTTL 224
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEieELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 225 RSVTAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQYYQQKLKR----ESSMEIMHSYSMKFHEEINRKTSEIASL 300
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleelEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 301 KNSLNELQAELMLMSHMKEQCEEQQRQLEQlefaLQAQLLEETQLRQSNALKlEQVENLTISLASLQLDKEGLKENLGEA 380
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQ----EIEELLKKLEEAELKELQ-AELEELEEELEELQEELERLEEALEEL 466
|
250 260 270
....*....|....*....|....*....|...
gi 24668309 381 QKTLKNLQQKVDILQKQYAEMCSLCQKTKQQLE 413
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
204-503 |
1.26e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 204 KQLLDLKSQMEHQLElrSTTLRSVTAERdqLRQVIAELNETlqtQEHLLALKEQEFLD-LKQYYQQKLKRESSMEIMHSY 282
Cdd:TIGR02168 189 DRLEDILNELERQLK--SLERQAEKAER--YKELKAELREL---ELALLVLRLEELREeLEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 283 SMKFHEEINRKTSEIASLKNSLNELQAELM----LMSHMKEQCEEQQRQLEQLEFALQAQLLEETQLRQSNALKLEQVEN 358
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 359 LTISLASLQLDKEGLKENLGEAQKTLKNLQQKVDILQKQYAEMCSLCQKTKQQLELEKIEI--------------AKMKQ 424
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIerlearlerledrrERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 425 NGSLKESELME-KLKDYAAQCDELRKALAEAESRIDVQIKKTEGWQVQLKHNQATQTDLEDPI--LVQRIETLEQQLADV 501
Cdd:TIGR02168 422 EIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaqLQARLDSLERLQENL 501
|
..
gi 24668309 502 RS 503
Cdd:TIGR02168 502 EG 503
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
142-718 |
4.75e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 142 EAKQQEARLRDQRQLIDVLRRQKKMLLDDIQRISLEHDEKLsQLQQTVVGMELESKHVTGKCKQLLDLKSQMEHQLELrs 221
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEI-QENKDLIKENNATRHLCNLLKETCARSAEKTKKYEY-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 222 ttlrsvtaERDQLRQVIAELNETLQtqEHLLALKEQEFLDLKQYYQQKLKRESSMEIMHSYSMKFHEEINRKTSEIASLK 301
Cdd:pfam05483 177 --------EREETRQVYMDLNNNIE--KMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 302 NSLNELQAELMLMSHMKEQCEEQQRQLEQlEFALQAQLLEETQLRQSNALKleQVENLTISLASLQLDKEGLKENLGEAQ 381
Cdd:pfam05483 247 IQITEKENKMKDLTFLLEESRDKANQLEE-KTKLQDENLKELIEKKDHLTK--ELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 382 KTLKNLQQKVD---------------ILQKQYAEMCS---LCQKTKQQLE--LEKIEIAKMKQNGSLKESELMEKLK-DY 440
Cdd:pfam05483 324 KTICQLTEEKEaqmeelnkakaahsfVVTEFEATTCSleeLLRTEQQRLEknEDQLKIITMELQKKSSELEEMTKFKnNK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 441 AAQCDELRKALAEAESRIDvQIKKTEGWQVQLKHNQATQTDLEDPiLVQRIETLEQQLADVRSQKLHTVSLLQILLQQQE 520
Cdd:pfam05483 404 EVELEELKKILAEDEKLLD-EKKQFEKIAEELKGKEQELIFLLQA-REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 521 AKIKSTNEMEADWQQLLDAlqatqslEQEMRSELQHKTVELE-HLNELFAGQNDELQKLQKLSQAQDEENRL--ELQLLK 597
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLE-------NKELTQEASDMTLELKkHQEDIINCKKQEERMLKQIENLEEKEMNLrdELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 598 KTFQENlkinsaasinmqrlQGQVKSLLDEKEEIAR-------EERKAVECLRSLGHVLEMETGRRLPHIKSWPQLAKIL 670
Cdd:pfam05483 555 EEFIQK--------------GDEVKCKLDKSEENARsieyevlKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 24668309 671 RKE--LRNGRVN------NRKAEELPGLKMKLAEISGRHQQALSKIKCLEHTLVME 718
Cdd:pfam05483 621 KKKgsAENKQLNayeikvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-712 |
1.19e-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: 49.28 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 358 NLTISLASLQLDKEGLKENLGEAQKTLKNLQQKVDILQKQYAEMCSLCQKTKQQLELEKIEIAKMKQngslkeselmeKL 437
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA-----------EV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 438 KDYAAQCDELRKALAEAESRIDVQIKKTEGWQVQLKHNQATQTDLEDPI--LVQRIETLEQQLADVRSQklhtVSLLQIL 515
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeqLKEELKALREALDELRAE----LTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 516 LQQQEAKIKSTNEMEADWQQLLDALQATQSLEQEMRSELQHktvELEHLNELFAGQNDELQKLQKLSQAQDE---ENRLE 592
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA---EIEELEELIEELESELEALLNERASLEEalaLLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 593 LQLLKKTFQENLKINSAASINMQRLQGQVKSLLDEKEEIAREERKAVECLRSLGHVLEMETGRRLPHIKSWPQLAKILRK 672
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24668309 673 ELRN-----GRVNNRKAEELPGLKMKLAEISGRHQQALSKIKCLE 712
Cdd:TIGR02168 976 RLENkikelGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
230-731 |
1.30e-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: 49.20 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 230 ERDQLRQVIAELNETLQTqehLLALKEQEflDLKQYYQQKLKRESSMEIMHSYS--MKFHEEINRKTSEIASLKNSLNEL 307
Cdd:pfam02463 181 ETENLAELIIDLEELKLQ---ELKLKEQA--KKALEYYQLKEKLELEEEYLLYLdyLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 308 QAELMlmshMKEQCEEQQRQLEQLEFALQAQLLEETQLRQSNALKLEQVENLTISLASLQLDKE--GLKENLGEAQKTLK 385
Cdd:pfam02463 256 SKQEI----EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKlkESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 386 NLQQKVDILQKQYAEMcslcQKTKQQLELEKIEIAKMKQNGSLKESELMEKLKDYAAQCDELRKALAEAESRIDVQIKKT 465
Cdd:pfam02463 332 KEKEEIEELEKELKEL----EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 466 EGWQVQLKHNQATQTDLEDPILVQRIETLEQQLADVRSQKLhtVSLLQILLQQQEAKIKSTNEMEADWQQLLDALQATQS 545
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE--EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 546 LEQEMRSELQHKTVELEHLNELFAGQNDELQKLQKLSQAQDEENRLELQLLKKTfqenlKINSAASINMQRLQGQVKSLL 625
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE-----NYKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 626 DEKEEIAREERKAVECLRSLGHVLEMETGRRLPHIKSWPQLAKILRKELRNG--RVNNRKAEELPGLKMKLAEISGRHQQ 703
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATleADEDDKRAKVVEGILKDTELTKLKES 640
|
490 500
....*....|....*....|....*...
gi 24668309 704 ALSKIKCLEHTLVMERARFEASDSGKST 731
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEKSEVKASL 668
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-332 |
3.49e-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: 47.74 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 47 RQELLRTRSEVQRLLKSEQWYKQELKSQKHSRLQTLERLYAQERKYLMENQKLQQESIRLHTQCATLEKQQEQGSPFSPG 126
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 127 SSPFKAD-----SESHDSSFEAKQQEARLRDQRQLIDVLRRQKKMLLDDIQRISLEhdekLSQLQQTVVGMELESKHVTG 201
Cdd:TIGR02168 805 LDELRAEltllnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEELESELEALLN 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 202 KCKQLLDLKSQMEHQLELRSTTLRSVTAERDQLRQVIAELNEtlqtQEHLLALKEQEFLDLKQYYQQKLKRESSMEIMH- 280
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE----KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEa 956
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24668309 281 --------SYSMKFHEEINRKTSEIASLKN----SLNELQAELMLMSHMKEQCEEQQRQLEQLE 332
Cdd:TIGR02168 957 ealenkieDDEEEARRRLKRLENKIKELGPvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
422-634 |
5.15e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 422 MKQNGSLKESELMEKLKDYAAQCDELRKALAEAESRIdVQIKKTegwqvqlkhNQATQTDLEDPILVQRIETLEQQLADV 501
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAAL-EEFRQK---------NGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 502 RSQKlhtvsllqillQQQEAKIKSTNEMEADWQQLLDALQATQSLeQEMRSELQHKTVELEHLNELFAGQNDELQKLQKl 581
Cdd:COG3206 232 RAEL-----------AEAEARLAALRAQLGSGPDALPELLQSPVI-QQLRAQLAELEAELAELSARYTPNHPDVIALRA- 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24668309 582 sqaqdEENRLELQLLkktfQENLKINSAASINMQRLQGQVKSLLDEKEEIARE 634
Cdd:COG3206 299 -----QIAALRAQLQ----QEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-499 |
7.29e-05 |
|
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: 46.60 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 231 RDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQYYQQKLKRESSMEIMHSYSMKFHEEINRKTSEIASLKNSLNELQAE 310
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 311 LMLMSHMKEQCEEQQRQLEQLEFALQAQLLEEtQLRQSNALKL---EQVENLTISLASLQLDKEGLKENLGEAQKTLKNL 387
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHS-RIPEIQAELSkleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 388 QQKVDILQKQYAEMCslcqktkQQLELEKIEIAKMKQ---NGSLKESELMEKLKDYAAQCDELRKALAEAESRIDvQIKk 464
Cdd:TIGR02169 839 QEQRIDLKEQIKSIE-------KEIENLNGKKEELEEeleELEAALRDLESRLGDLKKERDELEAQLRELERKIE-ELE- 909
|
250 260 270
....*....|....*....|....*....|....*
gi 24668309 465 tegWQVQLKHNQATQTDLEDPILVQRIETLEQQLA 499
Cdd:TIGR02169 910 ---AQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
288-767 |
8.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 288 EEINRKTSEIASLKNSLNELQAELMLMSHMKEQCEEQQRQLEQLEFALQAQLLEETQLRQSNALKLEQVENLtislASLQ 367
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK----AEEA 1469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 368 LDKEGLKENLGEAQKTlKNLQQKVDILQKQYAEMCSLCQKTKQQLELEKIEIAKMKQngSLKESELMEKlKDYAAQCDEL 447
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD--EAKKAEEAKK-ADEAKKAEEK 1545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 448 RKAlaeAESRIDVQIKKTEgwqvQLKHNQATQTDLEDPILVQRIETLEQQLADVRSQKLHTVSLLQILLQQQEAKIKSTN 527
Cdd:PTZ00121 1546 KKA---DELKKAEELKKAE----EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 528 EMEAdwqqlldalqatqslEQEMRSELQHKTVElehlnELFAGQNDELQKLQKLSQAQdEENRLELQLLKKTFQENLKIN 607
Cdd:PTZ00121 1619 KIKA---------------EELKKAEEEKKKVE-----QLKKKEAEEKKKAEELKKAE-EENKIKAAEEAKKAEEDKKKA 1677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 608 SAAsinmqRLQGQVKSLLDEKEEIAREERKAVECLRSlghvLEMETGRRLPHIKSWPQLAKILRKEL-RNGRVNNRKAEE 686
Cdd:PTZ00121 1678 EEA-----KKAEEDEKKAAEALKKEAEEAKKAEELKK----KEAEEKKKAEELKKAEEENKIKAEEAkKEAEEDKKKAEE 1748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 687 L---PGLKMKLAEISGRHQQALSKIKCLEHTLVME-------RARFEASDSGKSTASNTP--QEPAHEVANLIDDYKKLV 754
Cdd:PTZ00121 1749 AkkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeldeedeKRRMEVDKKIKDIFDNFAniIEGGKEGNLVINDSKEME 1828
|
490
....*....|...
gi 24668309 755 QQTANETCRPRNS 767
Cdd:PTZ00121 1829 DSAIKEVADSKNM 1841
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-637 |
1.10e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 69 QELKSQKHSRLQTLERLYAQERKYLMENQKLQQESIRLHTQCATLEKQQEqgspfspgsspfkadseshdssfEAKQQEA 148
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE-----------------------ELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 149 RLRDQRQLIDVLRRQKKMLLDDIQRISLEHDEKLSQLQQtvvgmeleskhvtgkckQLLDLKSQMEHQLELRSTTLRSVT 228
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE-----------------ALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 229 AERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQYYQQKLKRESSMEIMHSYSMKFHEEINRKTSEIASLKNSLNELQ 308
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 309 AELMLMSHMKEQCEEQQRQLEQLEfALQAQLLEETQLRQSNALKLEQVENLTISLASLQLDKEGLKENLGEAQKTLKNLQ 388
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 389 QKVDILQKQYAEMCSLCQKTKQQLELEKIEIAKMKQNGSLKESELMEKLKDYAAQCDELRKALAEAESRIDVQIKKTEGW 468
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 469 QVQLKHNQATQTDLEDPILVQRIETLEQQLAdvRSQKLHTVSLLQILLQQQEAKIKSTNEMEADWQQLLDALQATQSLEQ 548
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAG--GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 549 EMRSELQHKTVELEHLNELFAGQndELQKLQKLSQAQDEENRLELQLLKKTFQENLKINSAASiNMQRLQGQVKSL---- 624
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQ--LEAEREELLEELLEEEELLEEEALEELPEPPDLEELER-ELERLEREIEALgpvn 783
|
570
....*....|....*.
gi 24668309 625 ---LDEKEEIarEERK 637
Cdd:COG1196 784 llaIEEYEEL--EERY 797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-459 |
1.13e-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: 45.82 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 38 EPDQSIFLVRQELLRTRSEVQRLLKSEQWYKQELKSQKHSrlqtLERLYAQERKYLMENQKLQQESIRLHTQCATLEKQQ 117
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 118 EQGSpfspgsspfkadseshdssfeakQQEARLRDQRQLIDVLRRQKKMLLDDIQRISLEHDEKLSQLQQTVvgmelesk 197
Cdd:TIGR02168 743 EQLE-----------------------ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-------- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 198 hvtgkckqlldlkSQMEHQLELRSTTLRSVTAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLkqyyQQKLKRESsme 277
Cdd:TIGR02168 792 -------------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL----EEQIEELS--- 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 278 imhsysmkfhEEINRKTSEIASLKNSLNELQAELMLMSHMKEQCEEQQRQLEQLEFALQAQLLE-ETQLRQSNALKLEqv 356
Cdd:TIGR02168 852 ----------EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRElESKRSELRRELEE-- 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 357 enLTISLASLQLDKEGLKENLGEAQKTLKNLQQKV-DILQKQYAEMCSLCQKTKQQLELEKIEIAKMkqnG-----SLKE 430
Cdd:TIGR02168 920 --LREKLAQLELRLEGLEVRIDNLQERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKEL---GpvnlaAIEE 994
|
410 420 430
....*....|....*....|....*....|
gi 24668309 431 -SELMEKLKDYAAQCDELRKALAEAESRID 459
Cdd:TIGR02168 995 yEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
44-432 |
1.51e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 44 FLVRQELLRTR------SEVQRLLKSEQWYKQELKSQKHSRLQTLERLY---AQERKYLMENQKLQQESIRLHTQCATLE 114
Cdd:COG5022 758 RYLRRRYLQALkrikkiQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLgsrKEYRSYLACIIKLQKTIKREKKLRETEE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 115 KQqeqgspfspgsspFKADSESHDSSFEaKQQEARLRDQRQLIDVLRRQKKMLLDDIQRISLEHDE---KLSQLQQtvVG 191
Cdd:COG5022 838 VE-------------FSLKAEVLIQKFG-RSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIdvkSISSLKL--VN 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 192 MELESKHVTGKCKQLLDLKSQMEHQLELrSTTLRSVTAERDQLRQVIAElnetLQTQEHLLALKEQEfldlkqyyqQKLK 271
Cdd:COG5022 902 LELESEIIELKKSLSSDLIENLEFKTEL-IARLKKLLNNIDLEEGPSIE----YVKLPELNKLHEVE---------SKLK 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 272 RES-SMEIMHSYSMKFHEEINRKTSEIASLKNSLNELQAELMLMSHMKEQCEEQQRQLEQLEFALQAQLLEETQLRQSNA 350
Cdd:COG5022 968 ETSeEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKP 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 351 LKlEQVENLTISLASLQLDKEGLK--ENLGEAQKTLKNLQQKVDILQKQYAEmcSLCQKTKQQLELEK----IEIAKMKQ 424
Cdd:COG5022 1048 LQ-KLKGLLLLENNQLQARYKALKlrRENSLLDDKQLYQLESTENLLKTINV--KDLEVTNRNLVKPAnvlqFIVAQMIK 1124
|
....*...
gi 24668309 425 NGSLKESE 432
Cdd:COG5022 1125 LNLLQEIS 1132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
323-730 |
1.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 323 EQQRQLEQLEFALQAQLLEETQLRQSNALKLEQVENLTislaSLQLDKEGLKENLGEAQKTLKNLQ-QKVDILQKqyAEM 401
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE----EIRKFEEARMAHFARRQAAIKAEEaRKADELKK--AEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 402 CSLCQKTKQQLELEKIEIAKMKQNGSLKESELMEKLKDYAAQCDELRKALAEAESRIDVQIKKTEGWQVQLK--HNQATQ 479
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEA 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 480 TDLEDPILVQRIETLEQQLADVR-----SQKLHTVSLLQILLQQQEAKIKSTNEMEADWQQLLDALQATQSLEQEMRSEL 554
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEKKkadeaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE 1448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 555 QHKTVELEHLNELFAGQNDELQKLQKLSQAQDEENRLElQLLKKTFQENLKINSAASINMQRLQGQVKSLLDEK---EEI 631
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkkaDEA 1527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 632 AR-EERKAVECLRSLGHVLEMETGRRLPHIKSWPQLAKI--LRKELRNGRVNNRKAEELPGLKMKLAEISGRHQQALSKI 708
Cdd:PTZ00121 1528 KKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAeeAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
410 420
....*....|....*....|..
gi 24668309 709 KClEHTLVMERARFEASDSGKS 730
Cdd:PTZ00121 1608 KA-EEAKKAEEAKIKAEELKKA 1628
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
204-439 |
1.90e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 204 KQLLDLKSQMEHQLelrsTTLRSVTAERDQLRQVIAELNETLQT-QEHLLALKEQEFLDLKQYYQQKLK-RESSMEIMHS 281
Cdd:TIGR04523 253 TQLNQLKDEQNKIK----KQLSEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQKEQDWNKELKSELKnQEKKLEEIQN 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 282 YSMKFHEEINRKTSEIASLKNSLNELQAElmlMSHMKEQCEEQQRQLEQLEFALQAQLLEETQL--------------RQ 347
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESE---NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLesqindleskiqnqEK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 348 SNALKLEQVENLTISLASLQLDKEGLKENLGEAQKTLKNLQQKVDILQKQYAEMCSLCQKTKQQLELEKIEIAKMKQNGS 427
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE 485
|
250
....*....|..
gi 24668309 428 LKESELMEKLKD 439
Cdd:TIGR04523 486 QKQKELKSKEKE 497
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
127-448 |
2.14e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 127 SSPFKADSESHDSSFEAKQQEARLRDQ---RQLIDV----------LRRQKKMLLDDIQRISLE---HDEKLSQLQQTVV 190
Cdd:pfam15921 287 ASSARSQANSIQSQLEIIQEQARNQNSmymRQLSDLestvsqlrseLREAKRMYEDKIEELEKQlvlANSELTEARTERD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 191 GMELESKHVTGKCKQLLDLKSQMEHQLELRST---------TLRSVTAerDQLRQVIAELNETLQTQEHLL-ALKEQEFL 260
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEqnkrlwdrdTGNSITI--DHLRRELDDRNMEVQRLEALLkAMKSECQG 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 261 DLKQYYQQKLKRESSMEIMHSYSMKFHEeinrkTSEIasLKNSLNELQAELMLMSHMKEQCEEQQRQLEQLEFALQAQLL 340
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLES-----TKEM--LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 341 EETQLRQSNALKLEQVENLTIS---LASLQLDKEGLKENLGEAQKTLKNLQQKVDILQK---QYAEMCSLCQKTKQQL-- 412
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgQHGRTAGAMQVEKAQLek 597
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24668309 413 -------ELEKIEIAKMKQNGSLKESEL------MEKLKDYAAQCDELR 448
Cdd:pfam15921 598 eindrrlELQEFKILKDKKDAKIRELEArvsdleLEKVKLVNAGSERLR 646
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
319-549 |
2.23e-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: 44.37 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 319 EQCEEQQRQLEQLEFALQAQLLEETQLRQSNALKLEQVENLTISLASLQLDKEGLKENLGEAQKTLKNLQQKVDILQKQ- 397
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 398 ------YAEMCSLCQKTKQQLELEKIeiakMKQNGSLKESELMEKLKDYAAQCDELRKALAEAESRIDVQIKKTEGWQVQ 471
Cdd:COG4942 100 eaqkeeLAELLRALYRLGRQPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24668309 472 LKHNQATQtdledpilvqriETLEQQLADVRSQKLHTVSLLQILLQQQEAKIKSTNEMEADWQQLLDALQATQSLEQE 549
Cdd:COG4942 176 LEALLAEL------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
214-454 |
5.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 214 EHQLELRST--TLRSVTAERDQLRQVIAELNETLQTQEHLLALKEQEfldlKQYYQQKLKRESSMEIMHSYSMKFHE-EI 290
Cdd:COG4913 215 EYMLEEPDTfeAADALVEHFDDLERAHEALEDAREQIELLEPIRELA----ERYAAARERLAELEYLRAALRLWFAQrRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 291 NRKTSEIASLKNSLNELQAELMLMSHMKEQCEEQQRQLE---------QLEfALQAQLLEETQLRQSNALKLEQVENLTI 361
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggdRLE-QLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 362 SL-ASLQLDKEGLKENLGEAQKTLKNLQQKVDILQKQYAEMCSLCQKTKQQL-ELEKiEIAKMKQNGSlkeselmeklkD 439
Cdd:COG4913 370 ALgLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELrELEA-EIASLERRKS-----------N 437
|
250
....*....|....*
gi 24668309 440 YAAQCDELRKALAEA 454
Cdd:COG4913 438 IPARLLALRDALAEA 452
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
47-644 |
6.70e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 47 RQELLRTRSEVQRLL----KSEQWYKQELKSQKHSRLQTLERLYAQERKY-LMENQ--KLQQESIRLHTQCATLEKQQEq 119
Cdd:COG4913 241 HEALEDAREQIELLEpireLAERYAAARERLAELEYLRAALRLWFAQRRLeLLEAEleELRAELARLEAELERLEARLD- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 120 gspfspgsspfkadseshdssfEAKQQEARLRDQR-----QLIDVLRRQKKML---LDDIQRISLEHDEKLSQLQQTVVG 191
Cdd:COG4913 320 ----------------------ALREELDELEAQIrgnggDRLEQLEREIERLereLEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 192 MEleskhvtgkcKQLLDLKSQMEHQLELRSTTLRSVTAERDQLRQVIAELNETLQTqehllalKEQEFLDLKQyyqqklk 271
Cdd:COG4913 378 SA----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIASLER------- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 272 RESSMeimHSYSMKFHEEINRKTSEIASlknslnELQ--AELMlmsHMKEQCEEQQRQLEQL-------------EFALQ 336
Cdd:COG4913 434 RKSNI---PARLLALRDALAEALGLDEA------ELPfvGELI---EVRPEEERWRGAIERVlggfaltllvppeHYAAA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 337 AQLLEETQLRQsnALKLEQVENLTISLASLQLDKEGLKENL----GEAQKTLKNLqqkvdiLQKQYAEMCslCQkTKQQL 412
Cdd:COG4913 502 LRWVNRLHLRG--RLVYERVRTGLPDPERPRLDPDSLAGKLdfkpHPFRAWLEAE------LGRRFDYVC--VD-SPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 413 ELEKIEIAK---MKQNGSLKE--------SELM------EKLKDYAAQCDELRKALAEAESRIDVQIKKTEGWQVQLKHN 475
Cdd:COG4913 571 RRHPRAITRagqVKGNGTRHEkddrrrirSRYVlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 476 QATQTDLEDPIlvqRIETLEQQLADVRSQKlhtvsllqillqqqeAKIKSTNemeADWQQLLDALQATQSLEQEMRSELQ 555
Cdd:COG4913 651 QRLAEYSWDEI---DVASAEREIAELEAEL---------------ERLDASS---DDLAALEEQLEELEAELEELEEELD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 556 HKTVELEHLNELFAGQNDELQKLQ-KLSQAQDEENRLELQLLKKTFQENLKINSAASInMQRLQGQVKSLldeKEEIARE 634
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQdRLEAAEDLARLELRALLEERFAAALGDAVEREL-RENLEERIDAL---RARLNRA 785
|
650
....*....|
gi 24668309 635 ERKAVECLRS 644
Cdd:COG4913 786 EEELERAMRA 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
47-279 |
7.80e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 47 RQELLRTRSEVQRLLKSeqwyKQELKSQKHSRLQTLERLYAQERKYLMENQKLQQESIRLHTQCATLEKQQEQgspfspg 126
Cdd:COG1196 287 QAEEYELLAELARLEQD----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE------- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 127 sspfkADSESHDSSFEAKQQEARLRDQRQLIDVLRRQKKMLLDDIqrisLEHDEKLSQLQQTVVGMELESKHVTGKCKQL 206
Cdd:COG1196 356 -----AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA----AELAAQLEELEEAEEALLERLERLEEELEEL 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24668309 207 LDLKSQMEHQLELRSTTLRSVTAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQYYQQKLKRESSMEIM 279
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
177-431 |
8.36e-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: 42.44 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 177 EHDEKLSQLQQTVVGMELESKHVTGKCKQLLDLKSQMEHQLELRSTTLRSVTAERDQLRQVIAELNETLQTQEHLLALKE 256
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 257 QEFLDLKQYYQQKLKRESSMEIMHSysmkfheeinrktseiaslkNSLNELQAELMLMSH----MKEQCEEQQRQLEQLE 332
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSP--------------------EDFLDAVRRLQYLKYlapaRREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 333 fALQAQLleETQLRQSNALKLEQVEnltiSLASLQLDKEGLKENLGEAQKTLKNLQQKVDILQKQYAEMcslcQKTKQQL 412
Cdd:COG4942 164 -ALRAEL--EAERAELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL----EALIARL 232
|
250
....*....|....*....
gi 24668309 413 ELEKIEIAKMKQNGSLKES 431
Cdd:COG4942 233 EAEAAAAAERTPAAGFAAL 251
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
229-636 |
8.73e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 229 AERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQYYQQKLKRESSMEIMHsysmkfheeinrktsEIASlkNSLNELQ 308
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDY---------------QAAS--DHLNLVQ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 309 AELMLmshmKEQCEEQQRQLEQLEFALQAQLleetqlrqsnalklEQVENLTISLASLQLDKEGLKENLGEAQKTLKNLQ 388
Cdd:COG3096 341 TALRQ----QEKIERYQEDLEELTERLEEQE--------------EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 389 QKVDILQK---QYAEMCSLCQKTKQQLELEKIEIAKMK--------QNGSLKES--ELMEKLKDYAAQCDELRKALaEAE 455
Cdd:COG3096 403 QALDVQQTraiQYQQAVQALEKARALCGLPDLTPENAEdylaafraKEQQATEEvlELEQKLSVADAARRQFEKAY-ELV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 456 SRIDVQIKKTEGWQVQlkhNQATQTDLEDPILVQRIETLEQQLADVRsQKLHtvsLLQILLQQQEAKIKSTN-------- 527
Cdd:COG3096 482 CKIAGEVERSQAWQTA---RELLRRYRSQQALAQRLQQLRAQLAELE-QRLR---QQQNAERLLEEFCQRIGqqldaaee 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 528 --EMEADWQQLLDALQATQSLEQEMRSELQHktvELEHLNelfagqndelQKLQKLSQ-------AQDEENRLELQLlkk 598
Cdd:COG3096 555 leELLAELEAQLEELEEQAAEAVEQRSELRQ---QLEQLR----------ARIKELAArapawlaAQDALERLREQS--- 618
|
410 420 430
....*....|....*....|....*....|....*...
gi 24668309 599 tfQENLKINSAASINMQRLQGQVKSLLDEKEEIAREER 636
Cdd:COG3096 619 --GEALADSQEVTAAMQQLLEREREATVERDELAARKQ 654
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
151-724 |
1.07e-03 |
|
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: 42.90 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 151 RDQRQLIDVLRRQKKmLLDDIQRISLEHDeKLSQLQQTVVGMELESKHVTGkckQLLDLKSQMEHQLELRSTTLRSVTAE 230
Cdd:pfam12128 217 RLNRQQVEHWIRDIQ-AIAGIMKIRPEFT-KLQQEFNTLESAELRLSHLHF---GYKSDETLIASRQEERQETSAELNQL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 231 ----RDQLRQVIAELNETLQTQEHLLALKEQEF----LDLKQYYQ---QKLKRESSMEimhsysMKFHEEINRKTSEIAS 299
Cdd:pfam12128 292 lrtlDDQWKEKRDELNGELSAADAAVAKDRSELealeDQHGAFLDadiETAAADQEQL------PSWQSELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 300 LKNSLNELQAEL-MLMSHMKEQC---------------EEQQRQLEQLEFALQAQlleETQLRqsnalkleqvENLTISL 363
Cdd:pfam12128 366 LTGKHQDVTAKYnRRRSKIKEQNnrdiagikdklakirEARDRQLAVAEDDLQAL---ESELR----------EQLEAGK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 364 ASLQLDKEGLKENLGEAQ----------KTLKNLQQKVDILQKQYAEMCSlCQKTKQQLELEKIEIAKMKQNGSLKESEL 433
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKlrlnqatatpELLLQLENFDERIERAREEQEA-ANAEVERLQSELRQARKRRDQASEALRQA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 434 MEKLKDYAAQCDELRKAL-AEAESRIDVQIKKTEGWQVQLKHNQAT----QTDLeDPILVQRIETLEQQLADVRsqkLHt 508
Cdd:pfam12128 512 SRRLEERQSALDELELQLfPQAGTLLHFLRKEAPDWEQSIGKVISPellhRTDL-DPEVWDGSVGGELNLYGVK---LD- 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 509 vsllqILLQQQEAKIKSTNEMEADWQQLLDALQATQSLEQEMRSELQHKTVELEHLN--ELFAG---QNDELQKLQKLSQ 583
Cdd:pfam12128 587 -----LKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASreETFARtalKNARLDLRRLFDE 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 584 AQDEENRLELQLLKKTFQENLKINSAASiNMQRLQGQVKSLLDEKEEIAREER-------KAVECLRS--LGHVLEMETG 654
Cdd:pfam12128 662 KQSEKDKKNKALAERKDSANERLNSLEA-QLKQLDKKHQAWLEEQKEQKREARtekqaywQVVEGALDaqLALLKAAIAA 740
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24668309 655 RRLPHIKSWPQLAKILRKELR----NGRVNNRKAEELPGLKMKLAEISGRHQQALSKIKCLEHTLVMERARFEA 724
Cdd:pfam12128 741 RRSGAKAELKALETWYKRDLAslgvDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
225-453 |
1.94e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 225 RSVTAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQYYQqklkressmeimhsySMKFHEEINRKTSEIASLKNSL 304
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG---------------LVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 305 NELQAELmlmshmkeqcEEQQRQLEQLEFALQAQLLEETQLRQSnalklEQVENLTISLASLQLDKEGLKENLGEAQKTL 384
Cdd:COG3206 229 AEARAEL----------AEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24668309 385 KNLQQKVDILQKQYAemcslcQKTKQQLELEKIEIAKMKQngslKESELMEKLKDYAAQCDELRKALAE 453
Cdd:COG3206 294 IALRAQIAALRAQLQ------QEAQRILASLEAELEALQA----REASLQAQLAQLEARLAELPELEAE 352
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
247-466 |
2.81e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.38 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 247 TQEHLL--ALKEQeFLDLKQYYQQKLKRESSME-IMHSYSM--KFHEE--INRKTSEIASLKNSLNELQAELMLMSHMKE 319
Cdd:PLN03229 500 SQDQLMhpVLMEK-IEKLKDEFNKRLSRAPNYLsLKYKLDMlnEFSRAkaLSEKKSKAEKLKAEINKKFKEVMDRPEIKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 320 QCEEQQRQLEQLEFALQAQLLEETQLRQSNALKLEQVENLTIsLASLQLDKEGLKENLGE--AQKTLKNLQQKVDILQKQ 397
Cdd:PLN03229 579 KMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGV-LKSMGLEVIGVTKKNKDtaEQTPPPNLQEKIESLNEE 657
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24668309 398 YAEMCSLCQKT---KQQLELEKIEIAKMKQNGSLKESELMEKLKdyaaqcDELRKALAEAESRIDVQIKKTE 466
Cdd:PLN03229 658 INKKIERVIRSsdlKSKIELLKLEVAKASKTPDVTEKEKIEALE------QQIKQKIAEALNSSELKEKFEE 723
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
490-637 |
3.98e-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: 40.82 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 490 RIETLEQQLADVRSQKLHTVSLLQILLQQQEAKIKSTNEMEADWQQLLDALQATQSLEQEMRSELQHKTVELEHLNELFA 569
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24668309 570 GQNDELQKLQ-KLSQAQDEENRLELQLLKKTFQENLKINSAASINMQRLQGQVKSL------LDEKEEIAREERK 637
Cdd:TIGR02169 762 ELEARIEELEeDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIeqklnrLTLEKEYLEKEIQ 836
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
204-416 |
4.15e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 204 KQLLDLKSQM---EHQLE--LRSTTLRSVTAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQyyQQKLKRESSMEI 278
Cdd:COG3206 182 EQLPELRKELeeaEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA--QLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 279 MHSysmkfheeinrktSEIASLKNSLNELQAELM-LMSHMKEQCEEQQRQLEQLEfALQAQLLEETQLRQSNALKleQVE 357
Cdd:COG3206 260 LQS-------------PVIQQLRAQLAELEAELAeLSARYTPNHPDVIALRAQIA-ALRAQLQQEAQRILASLEA--ELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24668309 358 NLTISLASLQLDKEGLKE---NLGEAQKTLKNLQQKVDILQKQYAEMcslcQKTKQQLELEK 416
Cdd:COG3206 324 ALQAREASLQAQLAQLEArlaELPELEAELRRLEREVEVARELYESL----LQRLEEARLAE 381
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-594 |
4.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 156 LIDVLRRQKKMLLDDIQRISLEHDEKLSQLQQTVVGMELESKHVTGKCKQLLDLKSQMEhQLELRSTTLRSVTAERDQLR 235
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 236 QVIAELNETLQTQEHLLALKEQ--EFLDLKQYYQQKLKRESSME------------IMHSYSMKFHEEINRKTSEIASLK 301
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEaelaelqeeleeLLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 302 NSLNELQAELmlmSHMKEQCEEQQRQLEQLEFALQAQLLEETQLRQSNALKleqVENLTISLASLQLDKEGLKENLGEAQ 381
Cdd:COG4717 206 QRLAELEEEL---EEAQEELEELEEELEQLENELEAAALEERLKEARLLLL---IAAALLALLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 382 KTLKNLQQKVDIL----QKQYAEMCSLCQKTKQQLELEKIEIAKMKQNGSLKESELMEKLKDYAAQCDELRKALAEAESR 457
Cdd:COG4717 280 FLVLGLLALLFLLlareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 458 IDvqikktegwQVQLKHNQATQTDLEDPILVQRIETLEQQLADVRS----QKLHTVSLLQILLQQQEAKIKSTNEMEADW 533
Cdd:COG4717 360 EE---------ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEyqelKEELEELEEQLEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24668309 534 QQLLDALQATQSLEQEMRSELQHKTVELEHLNELFAGQNDELQKLQKLSQAQDEENRLELQ 594
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
57-585 |
4.50e-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: 40.72 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 57 VQRLLKSEQWYKQELKSQKHSRLQtlerlYAQERKYLMENQKLQQESIRLHTQC-------ATLEKQQEQGSpFSPGSSP 129
Cdd:TIGR00618 221 KQVLEKELKHLREALQQTQQSHAY-----LTQKREAQEEQLKKQQLLKQLRARIeelraqeAVLEETQERIN-RARKAAP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 130 FKADSES-HDSSFEAKQQEARLRDQRQLIDVLRRQKKMLLDDIQRIslehdEKLSQLQQTVVGMELESKHVTGKCKQLLD 208
Cdd:TIGR00618 295 LAAHIKAvTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSI-----EEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 209 LKSQmEHQLELRSTTLRSVTAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKqyyQQKLKRESSMEIMHSYSMKFHE 288
Cdd:TIGR00618 370 ISCQ-QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQ---GQLAHAKKQQELQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 289 EINRKTSEIASLKNSLNELQ---AELMLMSHMKEQCEEQQRQLEQLEFALQAQLLEETQLRQSNALKLEQVENLTISLAS 365
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAqslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGP 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 366 LQLDKEGLKENLGEAQKTLKNLQQKVDILQKQYAEMCSLCQKTKQQLELEKIEIAKMKQNGSlKESELMEKLKDYAAQCD 445
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP-NLQNITVRLQDLTEKLS 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 446 ELRKALAEAESRIDVQIKKTEGWQVQLKHNQATQTD--LEDPILVQRIETLEQQ-----LADVRSQKLHTVSLLQILLQQ 518
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQElaLKLTALHALQLTLTQErvrehALSIRVLPKELLASRQLALQK 684
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24668309 519 QEAKIKSTNEMEADWQQLLDALQATQSLEQEMRSELQHKTVELEHLNELFAGQNDELQKLQKLSQAQ 585
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
48-656 |
4.56e-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: 40.81 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 48 QELLRTRSEVQRLLKSEQWYKQELKSQKHSRLQTLERLYAQERKYLMENQKLQQESIRLHTQCATLEKQQEqgspfspgs 127
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 128 spfkadseshdssfEAKQQEARLRDQRQLIDVLRRQKKMLLDDIQRISLEHDEKLSQLQQTVVGMELESKHVTGKCKQLL 207
Cdd:TIGR02168 306 --------------ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 208 DLKSQMEHQLELRSTTLRSVTAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQYYQQKLKRESSMEIMHSYSMKF- 286
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEe 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 287 ---------------HEEINRKTSEIASLKNSLNELQAELMLMSHMKEQCEEQQRQL----------------------- 328
Cdd:TIGR02168 452 lqeelerleealeelREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkallknqsglsgilgvlselisv 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 329 -EQLEFALQAQLLEETQ----------------LRQSNALKLEQVENLTISLASLQLDKEGLKENLGEAQKTLKNLQQKV 391
Cdd:TIGR02168 532 dEGYEAAIEAALGGRLQavvvenlnaakkaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFD 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 392 DILQKQYAEM---CSLCQKTKQQLELEKIEIAKM---------------------KQNGSLKE-----SELMEKLKDYAA 442
Cdd:TIGR02168 612 PKLRKALSYLlggVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitggsaKTNSSILErrreiEELEEKIEELEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 443 QCDELRKALAEAESRIdvQIKKTEGWQVQLKHNQATQTDLEDPILVQRIETLEQQLADVRSQKLHTVSLLQILLQQQEAK 522
Cdd:TIGR02168 692 KIAELEKALAELRKEL--EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 523 IKSTN----EMEADWQQLLDALQATQSLEQEMRSELQHKTVELEHLNELFAGQNDELQKLQKLSQAQDEENRlELQLLKK 598
Cdd:TIGR02168 770 LEEAEeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIE 848
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24668309 599 TFQENLKINSAA----SINMQRLQGQVKSLLDEKEEIAREERKAVECLRSLGHVL-EMETGRR 656
Cdd:TIGR02168 849 ELSEDIESLAAEieelEELIEELESELEALLNERASLEEALALLRSELEELSEELrELESKRS 911
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
131-640 |
5.52e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 131 KADSESHDSSFEAKQQEARLRDQRQLIDVLRRQKKMLLDDIQRISLEHDEKL----------SQLQQTVVGMELE----S 196
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERReeletleaeiEDLRETIAETEREreelA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 197 KHVTGKCKQLLDLKSQMEHQL---ELRSTTLRSVTAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKqyyqqklkre 273
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLaeaGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR---------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 274 ssmeimhsysmkfhEEINRKTSEIASLKNSLNELQAELmlmSHMKEQCEEQQRQLEQLEFALQAqlleetqLRQSNALKL 353
Cdd:PRK02224 349 --------------EDADDLEERAEELREEAAELESEL---EEAREAVEDRREEIEELEEEIEE-------LRERFGDAP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 354 EQVENLTISLASLQLDKEGLKENLGEAQKTLKNLQQKVDILQKQYAE-MCSLCQKtkqqlELEKIEIAKMKQNGSLKESE 432
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgKCPECGQ-----PVEGSPHVETIEEDRERVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 433 LMEKLKDYAAQCDELR------KALAEAESRIDVQIKKTEGWQVQLKHNQATQTDLEDpilvqRIETLEQQLADVRSQKL 506
Cdd:PRK02224 480 LEAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE-----RAEELRERAAELEAEAE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 507 HTVSLLQILLQQQEAKIKSTNEMEADWQQLLDALQATQSLEqEMRSELQHKTVELEHLNEL---FAGQNDE-LQKLQKLS 582
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-TLLAAIADAEDEIERLREKreaLAELNDErRERLAEKR 633
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24668309 583 QAQDE------ENRLE-LQLLKKTFQ-------ENLKINSAASINMQRLQGQVKSLLDEKEEIaREERKAVE 640
Cdd:PRK02224 634 ERKREleaefdEARIEeAREDKERAEeyleqveEKLDELREERDDLQAEIGAVENELEELEEL-RERREALE 704
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
228-456 |
6.10e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 228 TAERDQLRQVIAELNETLQTQEHLLALKEQEFLDLKQyyqqKLKRESSMEIMHSYSMKFHEEINRKTSEIASLKNSLNEL 307
Cdd:pfam10174 177 GEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLRE----ELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 308 QAELMLMSHMKE-QCEEQQRQLEQLEFALQ---------AQLLEETQLRQSNALKLE-QVENLTISLASLQLDKEGLKEN 376
Cdd:pfam10174 253 EDEVQMLKTNGLlHTEDREEEIKQMEVYKShskfmknkiDQLKQELSKKESELLALQtKLETLTNQNSDCKQHIEVLKES 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 377 LGEAQKTLKNLQQKVDILQKQYAEMCS-LCQKTKQQLELEK------IEIAKMKQNGSLKESE----------LMEKLKD 439
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEEKESfLNKKTKQLQDLTEekstlaGEIRDLKDMLDVKERKinvlqkkienLQEQLRD 412
|
250
....*....|....*..
gi 24668309 440 YAAQCDELRKALAEAES 456
Cdd:pfam10174 413 KDKQLAGLKERVKSLQT 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-423 |
6.29e-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: 40.44 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 160 LRRQKKMLLDDIQRISLEHD---EKLSQLQQTVVGMELESKHVTGKCKQLLDlksqmEHQLELRsTTLRSVTAERDQLRQ 236
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEkltEEISELEKRLEEIEQLLEELNKKIKDLGE-----EEQLRVK-EKIGELEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 237 VIAELNETLQTQEHLLALKEQEFLDLK--------QYYQQKLKRESSMEIMHSysmkFHEEINRKTSEIASLKNSLNELQ 308
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLaeieelerEIEEERKRRDKLTEEYAE----LKEELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 309 AELMlmsHMKEQCEEQQRQLEQLEFALQAQLLEETQLRQSNALKLEQVENLTISLASLQLDKEGLKENLGEAQKTLKNLQ 388
Cdd:TIGR02169 385 DELK---DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
250 260 270
....*....|....*....|....*....|....*
gi 24668309 389 QKVDILQKQYAEMCSLCQKTKQQLELEKIEIAKMK 423
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
314-581 |
6.75e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 314 MSHMKEQCEEQQRQLEQLEFALQAQLLEETQLRQSNalkleqvenltisLASLQLDKEGLKENLGE---AQKTLKNLQQ- 389
Cdd:PRK10929 139 LSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQ-------------LTALQAESAALKALVDElelAQLSANNRQEl 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 390 ---KVDILQKQYAEMCSLCQKTKQQLE----------LEKIEIAKmKQNGSLKESeLMEKLKdyaaQCDELRKALAEAES 456
Cdd:PRK10929 206 arlRSELAKKRSQQLDAYLQALRNQLNsqrqreaeraLESTELLA-EQSGDLPKS-IVAQFK----INRELSQALNQQAQ 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24668309 457 RIDV---QIKKTEGWQVQLKhnQATQTDLE-------DPIL-------VQRI------ETLEQQLADVRSQKLHTVSLLQ 513
Cdd:PRK10929 280 RMDLiasQQRQAASQTLQVR--QALNTLREqsqwlgvSNALgealraqVARLpempkpQQLDTEMAQLRVQRLRYEDLLN 357
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24668309 514 ILLQQQEAKIKSTNEMEADWQQLLDALQATQSleqemrselqhktvelEHLNELFAGQNDELQKLQKL 581
Cdd:PRK10929 358 KQPQLRQIRQADGQPLTAEQNRILDAQLRTQR----------------ELLNSLLSGGDTLILELTKL 409
|
|
| |
