|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
142-453 |
6.05e-150 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 432.04 E-value: 6.05e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 142 EEKEQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEHKTTR-TNLEPMFEAYITNLRRQLECLGGERSRLETELKSM 220
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 221 QDVVEDFKNKYEEEIHRRTAAENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLRAFFEAELAQLQAQISETSVVLSM 300
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 301 DNNRSLNLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQRSAGQRGDDLRTTKMEISELNRAMQRLRSEIDNLKKQC 380
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109735018 381 ATLQASIADAEQRGELALKDAKNKLAELEDALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEECR 453
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
16-139 |
1.60e-18 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 82.78 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 16 NFSASSASLLPGCRPGFSSVSVSQSGKSFGGGIGGGFG---TRSLHSFGGNKRISIGGGYRSTRASFG------------ 80
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGgfgSRSLYNLGGSKSISISVAGGGSRPGSGfgfgggggggfg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109735018 81 -----------------GSACGLGVSGIGYRVGGAYGGYGYGGGMAPGAGGIHEVTVNQSLLTPLHLEIDPSLQRV 139
Cdd:pfam16208 81 ggfgggggggfgggggfGGGFGGGGYGGGGFGGGGFGGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-464 |
6.17e-12 |
|
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: 68.54 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 147 IKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEHKTTRTNLEPMFEAYITNLRRQLECLGGERSRLETELKSMQDVVED 226
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 227 FKNKYEEEIHRRTAAENEFVVLKKdvdaaymNKVELEAKVEALMDEINFLRaffeAELAQLQAQISETSVVLSMDNNRSL 306
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALR----EALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 307 NLDSIIAEVKAQYEDIANRSRAEAESwyQTKYEELQRSAGQRGDDLRTT----KMEISELNRAMQRLRSEIDNLKKQCAT 382
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSED--IESLAAEIEELEELIEELESElealLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 383 LQASIADAEQrgelALKDAKNKLAELEDALQKAKQDMARQLR----EYQELMNVKLALDIEIATYRKLLEGEECRLTGE- 457
Cdd:TIGR02168 906 LESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRLKRLENKi 981
|
....*...
gi 109735018 458 -GVGAVNI 464
Cdd:TIGR02168 982 kELGPVNL 989
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-441 |
4.28e-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: 59.30 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 165 EQQNKVLETKwsllQEHKTTRTNLEpMFEAYITNLRRQLECLGGERSRLETELKSMQDVVEDFKNKYEEEIHRRTAAENE 244
Cdd:TIGR02168 667 KTNSSILERR----REIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 245 FVVLKKDVDAAYMNKVELEAKVEALMDEINFLRAFF---EAELAQLQAQISEtsvvlsmDNNRSLNLDSIIAEVKAQYED 321
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELaeaEAEIEELEAQIEQ-------LKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 322 --IANRSRAEAESWYQTKYEELQRSAGQRGDDLRTTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGELALK 399
Cdd:TIGR02168 815 lnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 109735018 400 DAKNKLAELEDALQKAKQdmARQLREYQELMNVKLALDIEIA 441
Cdd:TIGR02168 895 ELEELSEELRELESKRSE--LRRELEELREKLAQLELRLEGL 934
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-448 |
3.22e-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: 53.52 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 209 ERSRLETELKSMQDVVEDFKNKYEEEIHRRTAAENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLraffEAELAQLQ 288
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL----EERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 289 AQISEtsvvlsmdnnrslnLDSIIAEVKAQYEDI-ANRSRAEAESwyqtkyEELQRSAGQRGDDLRTTKMEISELNRAMQ 367
Cdd:TIGR02168 754 KELTE--------------LEAEIEELEERLEEAeEELAEAEAEI------EELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 368 RLRSEIDNLKKQCATLQASIADAEQRGELA---LKDAKNKLAELEDALQKAKQDMARQLREYQELMNVKLALDIEIATYR 444
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
....
gi 109735018 445 KLLE 448
Cdd:TIGR02168 894 SELE 897
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
281-426 |
4.31e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 51.89 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 281 EAELAQLQAQISETSVVLSMDNNRSLNLDSIIAEVKAQYEDI-ANRSRAEAesWYQTKYEELQRSAGQRGD---DLRTTK 356
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQA--LLAELAGAGAAAEGRAGElaqELDSEK 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 357 MEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGelalKDAKNKLAELEDALQKAKQDMARQLREY 426
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRRLNVALAQRVQELNRY 195
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
277-456 |
5.32e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 277 RAFFEAELAQLQAQISEtsvvlsmdnnrslnLDSIIAEVKAQYEDIANRSRA----EAESWYQTKYEELQR---SAGQRG 349
Cdd:COG4913 612 LAALEAELAELEEELAE--------------AEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAEReiaELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 350 DDLRTTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRgelaLKDAKNKLAELEDALQKAKQDMARQLREYQEL 429
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170 180 190
....*....|....*....|....*....|....*...
gi 109735018 430 M-----------NVKLALDIEIATYRKLLEGEECRLTG 456
Cdd:COG4913 754 RfaaalgdaverELRENLEERIDALRARLNRAEEELER 791
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
262-467 |
8.52e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 262 LEAKVEALMDEINFLRAFFEAELAQLQAQISET----------SVVLSMDNNRSLNLDSIiAEVKAQYEDiANRSRAEAE 331
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAeaaleefrqkNGLVDLSEEAKLLLQQL-SELESQLAE-ARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 332 SWYQTKYEELQRSAGQRGD------------DLRTTKMEISELNR-------AMQRLRSEIDNLKKQcatLQASIADAEQ 392
Cdd:COG3206 240 ARLAALRAQLGSGPDALPEllqspviqqlraQLAELEAELAELSArytpnhpDVIALRAQIAALRAQ---LQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109735018 393 RGELALKDAKNKLAELEDALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEG-EECRLTgEGVGAVNISVV 467
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRlEEARLA-EALTVGNVRVI 391
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
135-430 |
8.63e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 135 SLQRVRKEEKEQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEHKTTRTNLEPMFEAYITNLRRQLECLGGERSRLE 214
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 215 TELKSMQDVVEDFKN-KYEEEIHRRT------AAENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLRAFF------E 281
Cdd:pfam07888 150 TELERMKERAKKAGAqRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 282 AELAQLQAQISETSVVLSMDNNRSLNLDSIIAEVKAQyedianRSRAEAEsWYQTKYEELQ-----------------RS 344
Cdd:pfam07888 230 AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQ------RDRTQAE-LHQARLQAAQltlqladaslalregraRW 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 345 AGQRGDDLRTTKME---ISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGELALKDAKNKLAELEDALQKAKQDMAR 421
Cdd:pfam07888 303 AQERETLQQSAEADkdrIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQ 382
|
....*....
gi 109735018 422 QLREYQELM 430
Cdd:pfam07888 383 LQAEKQELL 391
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-449 |
1.07e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 146 QIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEHKTTRtnlepmfEAYITNLRRQLECLGGERSRLETELKSMQDVVE 225
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-------RLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 226 DFKNKYEEEIHRRTAAENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLraffEAELAQLQAQISEtsvvlsmdnnRS 305
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA----EAELAEAEEALLE----------AE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 306 LNLDSIIAEVKAQYEDIANRSRAEAEswYQTKYEELQRSAGQRGDDLRTTKMEISELNRAMQRLRSEIDNLKKQcatlQA 385
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAE--LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA----LE 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109735018 386 SIADAEQRGELALKDAKNKLAELEDALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEG 449
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
241-445 |
1.58e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 241 AENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLraffEAELAQLQAQISETSVvlSMDNNRSlNLDSIIAEVKAQYE 320
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQA--EIDKLQA-EIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 321 DIANRSRAEAESWYQTKYEELQRSAGQRGDDLRTTKMeISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGELALKD 400
Cdd:COG3883 87 ELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 109735018 401 AKNKLAELEDALQKAKQDMARQLREYQELMNVKLALDIEIATYRK 445
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
131-451 |
1.75e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 131 EIDPS-LQRVRKEEKEQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEHKTTRTNLEPMFEAYITNLRRQLeclGGE 209
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHY---NEK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 210 RSRLETELKSMQDVVEDFKNKYEEEIHRRTAAENEfvvlKKDVDAAYMNKVE-LEAKVEALMDEINFLrAFFEAELAQLQ 288
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE----EINKSINEYNKIEsARADLEDIKIKINEL-KDKHDKYEEIK 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 289 AQISETSV-VLSMDNNRSLNLDSIIA------------EVKAQYEDIANRSRaEAESWYQTKYEELQRSAGQRGDD---L 352
Cdd:PRK01156 553 NRYKSLKLeDLDSKRTSWLNALAVISlidietnrsrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannL 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 353 RTTKMEISELNRAMQRLRSEIDNLKKQCATLQaSIADAEQRGELALKDAKNKLAELEDALQKAKQDMARQLREYQELMNV 432
Cdd:PRK01156 632 NNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTR 710
|
330
....*....|....*....
gi 109735018 433 KLALDIEIATYRKLLEGEE 451
Cdd:PRK01156 711 INELSDRINDINETLESMK 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
221-445 |
2.31e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 221 QDVVEDFKNKyeEEIHRRTAAENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLRAFF-EAELAQLQAQISEtsvvls 299
Cdd:COG4913 228 DALVEHFDDL--ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFaQRRLELLEAELEE------ 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 300 mdnnrslnLDSIIAEVKAQYEDIANRsRAEAEswyqTKYEELQRS-AGQRGDDLRTTKMEISELNRAMQRLRSEIDNLKK 378
Cdd:COG4913 300 --------LRAELARLEAELERLEAR-LDALR----EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109735018 379 QCATLQASIADAEQRGELALKDAKNKLAELEDALQKAKQDMARQLREYQELMNVKLALDIEIATYRK 445
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
209-445 |
3.85e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 209 ERSRLETELKSMQDVVEDFKNKYEEEIHRRTAAENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLRAffeaELAQLQ 288
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA----ELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 289 AQISETSVVLSMDNNRSlnldsiIAEVKAQYEDIANRSRAeaeswyQTKYEELQRSAGQRGDDLRTTKMEIselnramQR 368
Cdd:COG4942 104 EELAELLRALYRLGRQP------PLALLLSPEDFLDAVRR------LQYLKYLAPARREQAEELRADLAEL-------AA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109735018 369 LRSEIDNLKKQCATLQASIADAEQRGELALKDAKNKLAELEDALQKAKQDMARQLREYQELMNVKLALDIEIATYRK 445
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
144-429 |
5.98e-06 |
|
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: 49.25 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 144 KEQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEHKTTRTNLEPMFEAYITNLRRQLECLGGERSRLETELKSMQDV 223
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 224 VEDFKnKYEEEIhrrTAAENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLRAFFEAELAQLQAQISEtsvvLSMDNN 303
Cdd:TIGR04523 210 IQKNK-SLESQI---SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 304 RSLNLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQRSAGQRGDDLRTTKMEISELNRAMQRLRSEIDNLKKQCATL 383
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 109735018 384 QASIADAEQRGELALKDAKNKLAELEDaLQKAKQDMARQLREYQEL 429
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKN-LESQINDLESKIQNQEKL 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
196-429 |
6.16e-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: 49.28 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 196 ITNLRRQLECLGGERSRLETELKSMQDVVEDFKNKYEEEIHRRTAAENEFVVLKKDVDAAYMNKVELEAKVEalmdeinf 275
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ-------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 276 lraFFEAELAQLQAQISETSVVLSMDNNRSLNLDSIIAEVKAQYEDIANR--SRAEAESWYQTKYEELQRSAGQRGDDLR 353
Cdd:TIGR02168 306 ---ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEleSLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 354 TTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRG--------ELALKDAKNKLAELEDALQKAKQDMARQLRE 425
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkkleEAELKELQAELEELEEELEELQEELERLEEA 462
|
....
gi 109735018 426 YQEL 429
Cdd:TIGR02168 463 LEEL 466
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
281-445 |
1.84e-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: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 281 EAELAQ----LQAQISETSVVLSMDNNRSLN-----LDSIIAEVKAQYEDIANRSRAEAESWYQTKYE--ELQRSAGQRG 349
Cdd:TIGR02168 208 QAEKAErykeLKAELRELELALLVLRLEELReeleeLQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 350 DDLRTTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGELA---LKDAKNKLAELEDALQKAKQDMARQLREY 426
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAEL 367
|
170
....*....|....*....
gi 109735018 427 QELMNVKLALDIEIATYRK 445
Cdd:TIGR02168 368 EELESRLEELEEQLETLRS 386
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
134-435 |
3.69e-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: 46.59 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 134 PSLQRVRKEEKEQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEHKTTRTNLEPMFEAYITNLRRQLECLGGERSRL 213
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 214 ETELKSMQDVVEDFKNKYEEEIHRRTAAENEFVVLKKDVDAAYMNKVELEAKVEALmdeinflraffEAELAQLQAQISE 293
Cdd:TIGR02168 802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL-----------AAEIEELEELIEE 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 294 tsvvlsmdnnrslnldsIIAEVKAQYEDIA--NRSRAEAESWYQTKYEELQRSAGQRG---DDLRTTKMEISELNRAMQR 368
Cdd:TIGR02168 871 -----------------LESELEALLNERAslEEALALLRSELEELSEELRELESKRSelrRELEELREKLAQLELRLEG 933
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109735018 369 LRSEIDNLKKQCAtlqasiadaeQRGELALKDAKNKLAELEDALQKAKQDMARQLREYQELMNVKLA 435
Cdd:TIGR02168 934 LEVRIDNLQERLS----------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
178-437 |
7.01e-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: 45.83 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 178 LQEHKTTRTNLEpMFEAYITNLRRQLECLGGERSRLEtELKSMQDVVEDFKnkYEEEIHRRTAAENEFVVLKKDVDAAYM 257
Cdd:TIGR02169 176 LEELEEVEENIE-RLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 258 NKVELEAKVEALMDEINFLraffEAELAQLQAQISEtsvvlsMDNNRSLNLDSIIAEVKAQyedIANRSRAEAEswyqtK 337
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEI----EQLLEELNKKIKD------LGEEEQLRVKEKIGELEAE---IASLERSIAE-----K 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 338 YEELQRSAGQRgddlrttkmeiselnramQRLRSEIDNLKKQCATLQASIADAEQRGELALKDAKNKLAELEDALQKAKQ 417
Cdd:TIGR02169 314 ERELEDAEERL------------------AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
250 260
....*....|....*....|
gi 109735018 418 DMARQLREYQELMNVKLALD 437
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLE 395
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
176-415 |
9.44e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 176 SLLQEHKTTRTNLEP---MFEAYITNLRRQLECLGGERSRLETELKSMQDVVEDFKNKYEEEIHRRTAAENEFVVLKKDV 252
Cdd:pfam01576 475 ELLQEETRQKLNLSTrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 253 DAAymnKVELEAKVEAlMDEINFLRAFFEAELAQLQAQISETSVVLSMDNNRSLNLDSIIAEVK---AQYEDiaNRSRAE 329
Cdd:pfam01576 555 EAL---TQQLEEKAAA-YDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKaisARYAE--ERDRAE 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 330 AESW-YQTKYEELQRSAgqrgDDLRTTKMEISELNRA----MQRLRSEIDNLKKQCATLQASIADAEQrgelALKDAKNK 404
Cdd:pfam01576 629 AEAReKETRALSLARAL----EEALEAKEELERTNKQlraeMEDLVSSKDDVGKNVHELERSKRALEQ----QVEEMKTQ 700
|
250
....*....|.
gi 109735018 405 LAELEDALQKA 415
Cdd:pfam01576 701 LEELEDELQAT 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-448 |
1.31e-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: 45.05 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 304 RSLNLDSIIAEVKAQYEDIANRSRAEAEswYQTKYEELQRSAGQRGDDLRTTKMEISELNRAMQRLRSEIDNLKKQCATL 383
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109735018 384 QASIADAEQRGELALKDAKNKLAELEDALQK---AKQDMARQLREYQELMNVKLALDIEIATYRKLLE 448
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
144-433 |
1.83e-04 |
|
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: 44.33 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 144 KEQIKTLNNKFASFIDKVRFLEQQnkvLETKWSLLQEHKTTRTNLEPMFEayitnlrrQLECLGGERSRLETELKSMQDV 223
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITME---LQKKSSELEEMTKFKNNKEVELE--------ELKKILAEDEKLLDEKKQFEKI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 224 VEDFKNKYEEEIHRRTAAENEFVVLKKDVDAAYMNKVELEAKVEALMDEInflraffEAELAQlQAQISETSVVLSMDNN 303
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL-------EKEKLK-NIELTAHCDKLLLENK 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 304 RSLNLDS-IIAEVKAQYEDIANRSRAE------------AESWYQTKYEELQRSAGQRGDDL-----------RTTKMEI 359
Cdd:pfam05483 503 ELTQEASdMTLELKKHQEDIINCKKQEermlkqienleeKEMNLRDELESVREEFIQKGDEVkckldkseenaRSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 360 SELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGElALKDAKN-----------KLAELEDALQKAKQDMARQLREYQE 428
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENK-ALKKKGSaenkqlnayeiKVNKLELELASAKQKFEEIIDNYQK 661
|
....*
gi 109735018 429 LMNVK 433
Cdd:pfam05483 662 EIEDK 666
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
280-421 |
1.87e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.88 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 280 FEAELAQLQAQISETSVVLSmDNNRSLNLDSIIAEVKAQYEdIANRSRAEAESWYQtKYEELQRSAGqrgddlrTTKMEI 359
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLA-RLEAELGAEAEIAAAEAQLA-AAQAQLDLAQRELE-RYQALYKKGA-------VSQQEL 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109735018 360 SELNRAMQRLRSEIDNLKKQCATLQASIADAEQrgelaLKDAKNKLAELEDALQKAKQDMAR 421
Cdd:COG1566 151 DEARAALDAAQAQLEAAQAQLAQAQAGLREEEE-----LAAAQAQVAQAEAALAQAELNLAR 207
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
193-417 |
1.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 193 EAYITNLRRQLECLGGERSRLETELKSMQDVVEDFKNKYEEEIHRRTAAENEFVVLKKDVDaaymnkvELEAKVEALMDE 272
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 273 I-NFLRAFFEAelaqlQAQISETSVVLSMDN-----NRSLNLDSIIAEVKAQYEDIaNRSRAEAESwYQTKYEELQRSAG 346
Cdd:COG3883 88 LgERARALYRS-----GGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEEL-KADKAELEA-KKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109735018 347 QRGDDLRTTKmeiSELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGELALKDAKNKLAELEDALQKAKQ 417
Cdd:COG3883 161 ALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
212-425 |
2.36e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 212 RLETELKSMQDVVEDFKNKYEEEIHRRTAAE----------NEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLRAffe 281
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADevleeheerrEELETLEAEIEDLRETIAETEREREELAEEVRDLRE--- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 282 aELAQLQAQISETSVVLSMDNNRSLNLDSIIAEVKAQYEDI----------ANRSRAEAESW------YQTKYEELQRSA 345
Cdd:PRK02224 287 -RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELrdrleecrvaAQAHNEEAESLredaddLEERAEELREEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 346 GQRGDDLRTTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGELALK---DAKNKLAELEDALQKAKQDM--A 420
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTARERVeeA 445
|
....*
gi 109735018 421 RQLRE 425
Cdd:PRK02224 446 EALLE 450
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
164-431 |
2.40e-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: 43.95 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 164 LEQQNKVLETKWSLLQEHKTTRTNLEPMFEAyitnLRRQLECLGGERSRLETELKSMQDVVEDFKNKyEEEIHrrtAAEN 243
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEM----LRKVVEELTAKKMTLESSERTVSDLTASLQEK-ERAIE---ATNA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 244 EFVVLKKDVDaaymnkVELEaKVEALMDEINFLRAFfEAELAQLQAQISETSVVLSMDNNRSLNLDSIIAE--------- 314
Cdd:pfam15921 518 EITKLRSRVD------LKLQ-ELQHLKNEGDHLRNV-QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagamq 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 315 -VKAQYEDIANRSRAEAESW--YQTKYEELQRSAGQRGDDLRTTKMEI----SELNRAMQRLRSEIDNLKKQCATLQASI 387
Cdd:pfam15921 590 vEKAQLEKEINDRRLELQEFkiLKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 109735018 388 ADAEQRGELALKDAKNKLAELEDALQKAKQDMARQLREYQELMN 431
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
210-422 |
3.47e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 210 RSRLETELKSMQDVVEDFKNKYEEEIHRRTAAENEFVVLKKDV----------DAA----YMNKVELEAKVEALMDEINF 275
Cdd:pfam01576 63 RARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIqdleeqldeeEAArqklQLEKVTTEAKIKKLEEDILL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 276 L---RAFFEAELAQLQAQISETSVVLSMDNNRSLNLDSIIAEVKAQYEDIANRSRAEAESWyqtkyEELQRSAgqrgddl 352
Cdd:pfam01576 143 LedqNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGR-----QELEKAK------- 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109735018 353 RTTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGE---LALKDAKNKLAELEDALQKAKQDMARQ 422
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEeetAQKNNALKKIRELEAQISELQEDLESE 283
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
253-428 |
3.69e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 253 DAAYMNKVELEAKVEALMDEINFLRAffEAELAQLQAQISEtsvVLSMDNNRSLNLDSIIAEVKAQYEDIANRsRAEAES 332
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAA---LLAEAGVEDEEELRAALEQAEEYQELKEE-LEELEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 333 WYQTKYEELQRSAGQRgdDLRTTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGELA-----LKDAKNKLAE 407
Cdd:COG4717 410 QLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAellqeLEELKAELRE 487
|
170 180
....*....|....*....|....
gi 109735018 408 LED---ALQKAKQDMARQLREYQE 428
Cdd:COG4717 488 LAEewaALKLALELLEEAREEYRE 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-459 |
4.86e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 136 LQRVRKEEKEQIKTLNNKFASFIDKVRFLEQQNKVletkWSLLQEHKTTRTNLEPMFEAYiTNLRRQLEclggERSRLET 215
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQL----LPLYQELEALEAELAELPERL-EELEERLE----ELRELEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 216 ELKSMQDVVEDFKNKYEEEIHRRT-AAENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLRA-----FFEAELAQLQA 289
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqlENELEAAALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 290 QISETS---------VVLSMDNNRSLNLDSIIAEV--------------KAQYEDIANRSRAEAESWYQTK---YEELQR 343
Cdd:COG4717 244 RLKEARlllliaaalLALLGLGGSLLSLILTIAGVlflvlgllallfllLAREKASLGKEAEELQALPALEeleEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 344 SAGQRGDDLRTTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGELALKDAKNklaelEDALQKAkqdmARQL 423
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED-----EEELRAA----LEQA 394
|
330 340 350
....*....|....*....|....*....|....*.
gi 109735018 424 REYQELMNVKLALDIEIATYRKLLEGEECRLTGEGV 459
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
193-434 |
6.39e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 193 EAYITNLRRQLECLGGERSRLETELKSMQDVVEDFK------------NKYEEEIHRRTAAENEfvvlkkdvdaayMNKV 260
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgQPVEGSPHVETIEEDR------------ERVE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 261 ELEAKVEALMDEINFLraffEAELAQLQAQISETSVVLSMDNNRSlNLDSIIAEVKAQYE---DIANRSRAEAESwYQTK 337
Cdd:PRK02224 479 ELEAELEDLEEEVEEV----EERLERAEDLVEAEDRIERLEERRE-DLEELIAERRETIEekrERAEELRERAAE-LEAE 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 338 YEELQRSAGQRGDDLRTTKMEISELNRAMQRLRSEIDNLKKqCATLQASIADA--------EQRGELA---------LKD 400
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAedeierlrEKREALAelnderrerLAE 631
|
250 260 270
....*....|....*....|....*....|....*...
gi 109735018 401 AKNKLAELEDALQKAKQDMARQLR----EYQELMNVKL 434
Cdd:PRK02224 632 KRERKRELEAEFDEARIEEAREDKeraeEYLEQVEEKL 669
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
140-447 |
7.93e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 140 RKEE-KEQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEHKTTrtnLEPMFEAyITNLRRQLECLGGERSRLETELK 218
Cdd:PRK03918 187 RTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE---LEELKEE-IEELEKELESLEGSKRKLEEKIR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 219 SMQDVVEDFKNKyEEEIHRRTAAENEfvvLKKDVDAaYMNKVELEAKVEALMDEINFLRAFFEAELAQLQAQISEtsvvL 298
Cdd:PRK03918 263 ELEERIEELKKE-IEELEEKVKELKE---LKEKAEE-YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----L 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 299 SMDNNRSLNLDSIIAEVKAQYEDIANRSRAEAESwyQTKYEELQR-SAGQRGDDLRTTKMEISELNRAMQRLRSEIDNLK 377
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHELYEEA--KAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 378 KQCATLQASIADAEQRGElALKDAKNK----------------LAELEDALQKAKQDMARQLREYQELMNVKLALDIEIA 441
Cdd:PRK03918 412 ARIGELKKEIKELKKAIE-ELKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
....*.
gi 109735018 442 TYRKLL 447
Cdd:PRK03918 491 KESELI 496
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
131-463 |
1.15e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 131 EIDPSLQRVRKEEKEQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEHKTTRTNL------EPMFEAYITNLRRQLE 204
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIgtnlqrRQQFEEQLVELSTEVQ 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 205 CLGGERSRLETELKSMQDVVEDFKNKYEEEIHRRTA----AENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLRaff 280
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETsnkkAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK--- 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 281 EAELAQLQAQISETSvvlsmDNNRSLNLDsiiaeVKAQYEDIanRSRAEAESWYQ---------TKYEELQRSAGQRgdD 351
Cdd:TIGR00606 976 ETELNTVNAQLEECE-----KHQEKINED-----MRLMRQDI--DTQKIQERWLQdnltlrkreNELKEVEEELKQH--L 1041
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 352 LRTTKMEISELNRAMQRLRSEIDNLKKQcatlQASIADAEQRGELALKDAKNKLAEledalqKAKQDMARQLREYQELMN 431
Cdd:TIGR00606 1042 KEMGQMQVLQMKQEHQKLEENIDLIKRN----HVLALGRQKGYEKEIKHFKKELRE------PQFRDAEEKYREMMIVMR 1111
|
330 340 350
....*....|....*....|....*....|..
gi 109735018 432 VKLALDIEIATYRKLLEGEECRLTGEGVGAVN 463
Cdd:TIGR00606 1112 TTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
160-430 |
1.27e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 160 KVRFLEQQNKVLETKWSLLQEHKTTRTNLEPMfeayitnlrrqleclgGERSRLETELKSMQDVVEDFKNKYEEEIHRRT 239
Cdd:PLN02939 151 RLQALEDLEKILTEKEALQGKINILEMRLSET----------------DARIKLAAQEKIHVEILEEQLEKLRNELLIRG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 240 AAENEFVV-LKKDVDAaymnkveLEAKVEALMDEINFLRAffeaELAQLQAqiSETSVVLsMDNNRSLnLDSIIAEVKAQ 318
Cdd:PLN02939 215 ATEGLCVHsLSKELDV-------LKEENMLLKDDIQFLKA----ELIEVAE--TEERVFK-LEKERSL-LDASLRELESK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 319 Y----EDIANRSRAEAESWYQtKYEELQrsagqrgDDLRTTKMEISELNRAMQR---LRSEIDNLKkqcATLQASIADAE 391
Cdd:PLN02939 280 FivaqEDVSKLSPLQYDCWWE-KVENLQ-------DLLDRATNQVEKAALVLDQnqdLRDKVDKLE---ASLKEANVSKF 348
|
250 260 270
....*....|....*....|....*....|....*....
gi 109735018 392 QRGELALKDAKNKLaeLEDALQKAKQDMARQLREYQELM 430
Cdd:PLN02939 349 SSYKVELLQQKLKL--LEERLQASDHEIHSYIQLYQESI 385
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
159-425 |
1.93e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 159 DKVRFLEQQNKVLETKWSLLQEHKTTRTNlepmfeaYITNLRRQleclGGERSrleTELKSMQDVVEDFKNKYEEEIHRR 238
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNK-------NIEEQRKK----NGENI---ARKQNKYDELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 239 TAAENEFVVLKKDVDAAyMNKVELE-AKVEALMDEINFLRAFFE--AELAQLQAQISETsvvlsmdNNRSLNLDSIIAEV 315
Cdd:PHA02562 240 TDELLNLVMDIEDPSAA-LNKLNTAaAKIKSKIEQFQKVIKMYEkgGVCPTCTQQISEG-------PDRITKIKDKLKEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 316 KAQYEDIanrsraeaeswyQTKYEELQrsagQRGDDLRTTKMEISELNramqrlrSEIDNLKKQCATLQASIADAE---Q 392
Cdd:PHA02562 312 QHSLEKL------------DTAIDELE----EIMDEFNEQSKKLLELK-------NKISTNKQSLITLVDKAKKVKaaiE 368
|
250 260 270
....*....|....*....|....*....|...
gi 109735018 393 RGELALKDAKNKLAELEDALQKAKQDMARQLRE 425
Cdd:PHA02562 369 ELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-451 |
2.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 186 TNLEPMFEAYiTNLRRQLECLGGERSRLETELKSMQDVVEDFKNKyeeeihrrtaaENEFVVLKKDVDAAYMNKVELEAK 265
Cdd:PRK03918 155 LGLDDYENAY-KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEK-----------EKELEEVLREINEISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 266 VEALMDEINFLRAFFEaELAQLQAQISETSVVLSMDNNRSLNLDSIIAEVKAQYEDI-ANRSRAEAESWYQTKYEELQRS 344
Cdd:PRK03918 223 LEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 345 agqrgddLRTTKMEISELNRAMQRLRSEIDNLKKQcatlqasIADAEQRGElALKDAKNKLAELEDALQKAKQDmarqLR 424
Cdd:PRK03918 302 -------YEEYLDELREIEKRLSRLEEEINGIEER-------IKELEEKEE-RLEELKKKLKELEKRLEELEER----HE 362
|
250 260
....*....|....*....|....*..
gi 109735018 425 EYQELMnvklALDIEIATYRKLLEGEE 451
Cdd:PRK03918 363 LYEEAK----AKKEELERLKKRLTGLT 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
261-462 |
3.15e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 261 ELEAKVEALMDEINFLRAFfEAELAQLQAQISETSVVLSMdnnrslnldsiIAEVKAQYEDIANRSRAEAE-SWYQTKYE 339
Cdd:COG4717 82 EAEEKEEEYAELQEELEEL-EEELEELEAELEELREELEK-----------LEKLLQLLPLYQELEALEAElAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 340 ELQRsagqrgddlrtTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRgelALKDAKNKLAELEDALQKAKQDM 419
Cdd:COG4717 150 ELEE-----------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 109735018 420 ARQLREYQELMNVKLALDIEIATYRKLLEGEECRLTGEGVGAV 462
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAL 258
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-365 |
3.47e-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: 40.43 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 136 LQRVRKEEKEQIKTLNNKFASFIDKVRFLEQQNKVLET-------KWSLLQEHKTTRTNLEPMFEAYITNLRRQLECLGG 208
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAqleelesKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 209 ERSRLETELKSMQDVVEDFKNKYEEEIHRRTAAENEFVVLKKDVDAaymnkveLEAKVEALMDEINFL-RAFFEAELAQL 287
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-------LEDRRERLQQEIEELlKKLEEAELKEL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109735018 288 QAQISETSVVLsmdnnrsLNLDSIIAEVKAQYEDIANRsRAEAESWYQTKYEELQRsAGQRGDDLRTTKMEISELNRA 365
Cdd:TIGR02168 439 QAELEELEEEL-------EELQEELERLEEALEELREE-LEEAEQALDAAERELAQ-LQARLDSLERLQENLEGFSEG 507
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
318-447 |
4.06e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 39.28 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 318 QYEDIANRSRAEAESWYQTKYEELQRSAGQRGDDLRTtkmEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRGELA 397
Cdd:cd22656 92 YYAEILELIDDLADATDDEELEEAKKTIKALLDDLLK---EAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDL 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 109735018 398 LKD-----AKNKLAELEDALQKAKQDMARQLREYQELMNVKLA-LDIEIATYRKLL 447
Cdd:cd22656 169 LTDeggaiARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIAdDEAKLAAALRLI 224
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
262-451 |
5.26e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 262 LEAKVEALMDEINflraffEAELAQLQAQISetsvVLSMDnnrslnLDSIIAEVKAQ--YEDIANRSRAEAESWYQTKYE 339
Cdd:PHA02562 160 LDISVLSEMDKLN------KDKIRELNQQIQ----TLDMK------IDHIQQQIKTYnkNIEEQRKKNGENIARKQNKYD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 340 ELQRSA-------GQRGDDLRTTKMEISELNRAMQRLR-------SEIDNLKKQ---------CATLQASIADAEQRgel 396
Cdd:PHA02562 224 ELVEEAktikaeiEELTDELLNLVMDIEDPSAALNKLNtaaakikSKIEQFQKVikmyekggvCPTCTQQISEGPDR--- 300
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 109735018 397 aLKDAKNKLAELE---DALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEE 451
Cdd:PHA02562 301 -ITKIKDKLKELQhslEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
281-451 |
5.68e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 281 EAELAQ----LQAQISETSVVLSMDNNRSLNLDsiIAEVKAQYEDIANRSRAEaeswyQTKYEELQRSAGQRGDDLRTTK 356
Cdd:COG1196 208 QAEKAEryreLKEELKELEAELLLLKLRELEAE--LEELEAELEELEAELEEL-----EAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 357 MEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRgelaLKDAKNKLAELEDALQKAKQDMARQLREYQELMNVKLAL 436
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170
....*....|....*
gi 109735018 437 DIEIATYRKLLEGEE 451
Cdd:COG1196 357 EAELAEAEEALLEAE 371
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
344-429 |
6.24e-03 |
|
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: 38.98 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 344 SAGQRGDDLRTTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADAEQRgelaLKDAKNKLAELEDALQKAKQDMARQL 423
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELE 89
|
....*.
gi 109735018 424 REYQEL 429
Cdd:COG4942 90 KEIAEL 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
135-405 |
7.63e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.27 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 135 SLQRVRKEEKEQIKTLNNKFASFIDKVRFL-EQQNKVLETKWSLLQEHKTTRTNLEpMFEAYITNLRRQLECLGGERSRL 213
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLnEEAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEIEEL 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 214 ETELKSMQDVVEDFKNKYEEEIHRRTAAENEFVVLKKDVDAAYMNKVELEAKVEALMDEINFLR---AFFEAELAQLQAQ 290
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrlEGLEVRIDNLQER 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 291 ISEtsvvlsmdnNRSLNLDSIIAEVKAQYEDIANrsraeaeswYQTKYEELQRSAGQRGDDLRTTKMEISELNRAMQRLR 370
Cdd:TIGR02168 945 LSE---------EYSLTLEEAEALENKIEDDEEE---------ARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
|
250 260 270
....*....|....*....|....*....|....*
gi 109735018 371 SEIDNLKKQCATLQASIADAEQRGELALKDAKNKL 405
Cdd:TIGR02168 1007 AQKEDLTEAKETLEEAIEEIDREARERFKDTFDQV 1041
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
332-417 |
8.84e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.55 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109735018 332 SWYQTKYEELQrsagqrgDDLRTTKMEISELNRAMQRLRSEIDNLKKQCATLQASIADA----EQRGELALKDAKNKLAE 407
Cdd:TIGR04320 257 AALQAKLATAQ-------ADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAqaqaLQTAQNNLATAQAALAN 329
|
90
....*....|
gi 109735018 408 LEDALQKAKQ 417
Cdd:TIGR04320 330 AEARLAKAKE 339
|
|
| |
