|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
163-476 |
3.69e-122 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 362.70 E-value: 3.69e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 163 QEREQIMVLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTsTGTNNLEPLLENYIGDLRRQVDLLSAEQMRQNAEVRS 242
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKG-AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 243 MQDVVEDYKSKYEDEINKRTGSENDFVVLKKDVDAAYVSKVDLESRVDTLTGEVNFLKYLFLTELSQVQTHISDTNVILS 322
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 323 MDNNRSLDLDSIIDAVRTQYELIAQRSKDEAEALYQTKYQELQITAGRHGDDLKNSKMEIAELNRTVQRLQAEISNVKKQ 402
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194018511 403 IEQMQSLISDAEERGEQALQDAWQKLQDLEEALQQSKEELARLLRDYQAMLGVKLSLDVEIATYRQLLEGEESR 476
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
56-160 |
1.03e-26 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 105.89 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 56 FGSRSLYNLGGSRSISINLMG---RSTSGFCQGGGVGGFGGGRGFGVGSTGAGGFGGGGFG--GAGFGTSNFGLGGFG-- 128
Cdd:pfam16208 40 FGSRSLYNLGGSKSISISVAGggsRPGSGFGFGGGGGGGFGGGFGGGGGGGFGGGGGFGGGfgGGGYGGGGFGGGGFGgr 119
|
90 100 110
....*....|....*....|....*....|....*..
gi 194018511 129 -----PYCPPGGIQEVTINQSLLEPLHLEVDPEIQRI 160
Cdd:pfam16208 120 ggfggPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
136-482 |
3.05e-08 |
|
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: 56.67 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 136 IQEVTINQSLLEPLHLEVDPEIQRIKTQEReQIMVLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTGTNNLEPLL 215
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKER-AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 216 ENYIGD-LRRQVDLLSAEQMRQNAEVRSMQdvVEdyKSKYEDEINKRTGSENDFVVLKKDVDAayvsKV-DLESRVDTLT 293
Cdd:pfam15921 560 KDKVIEiLRQQIENMTQLVGQHGRTAGAMQ--VE--KAQLEKEINDRRLELQEFKILKDKKDA----KIrELEARVSDLE 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 294 GEVNFLKYLFLTELSQVQTHISDTNVILSMDNNRSLDLDSIIDavrtQYELIAQRskdeaealYQTKYQELQITAGRHGD 373
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE----DYEVLKRN--------FRNKSEEMETTTNKLKM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 374 DLKNSKMEIAELNRTVQRLQAEISNVKKQIEQMQSLISdaEERGE-QALQdawQKLQDLEEALQQSKEElARLLRDYQAM 452
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQIT--AKRGQiDALQ---SKIQFLEEAMTNANKE-KHFLKEEKNK 773
|
330 340 350
....*....|....*....|....*....|
gi 194018511 453 LGVKLSldvEIATyrqllegEESRMSGELQ 482
Cdd:pfam15921 774 LSQELS---TVAT-------EKNKMAGELE 793
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
335-482 |
3.03e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 335 IDAVRTQYELIAQRSKDEAEALYQTKYQELQITAG--RHGDDLKNSKMEIAELNRTVQRLQAEISNVKKQIEQMQSLISD 412
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 413 AEERGEQALQDAWQKLQDLEEALQQSKEELARLLRDYQAmlgvKLSLDVEIATYRQLLEGEESRMSGELQ 482
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE----LLEALRAAAELAAQLEELEEAEEALLE 414
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
305-444 |
3.43e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 305 TELSQVQTHISDTNVILSMDNNRSLDLDSIIDAVRTQYElIAQRSKDEAEALYQTKYQELQITAGRHGD---DLKNSKME 381
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS-AAEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQV 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194018511 382 IAELNRTVQRLQAEISNVKKQIEQMQSLISDAEERGeqalQDAWQKLQDLEE----ALQQSKEELAR 444
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRrlnvALAQRVQELNR 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
374-455 |
3.89e-05 |
|
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: 46.30 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 374 DLKNSKMEIAELNRTVQRLQAEISNVKKQIEQMQSLISDAEER---GEQALQDAWQKLQDLEEALQQSKEELARLLRDYQ 450
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 194018511 451 AMLGV 455
Cdd:COG4942 108 ELLRA 112
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
185-452 |
3.99e-05 |
|
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: 46.65 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 185 LEQQNQVLQTKWELLQQVNTSTGTnnleplLENYIGDLRRQVDLLSAEQMRQNAEVRSMQDVVEDYKSKyedeinkrtgs 264
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQ------LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK----------- 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 265 endfvvlKKDVDAAYVSKVDLESRVDTLTGEVNFLKylflTE---LSQVQTHISDTNVILSmdnnrslDLDSIIDAVRTQ 341
Cdd:pfam15921 509 -------ERAIEATNAEITKLRSRVDLKLQELQHLK----NEgdhLRNVQTECEALKLQMA-------EKDKVIEILRQQ 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 342 YE----LIAQRSKDEAEALYQTKYQELQITAGRHgdDLKNSKMEIAELNRTVQRLQAEISNVkkQIEQMQsLISDAEERg 417
Cdd:pfam15921 571 IEnmtqLVGQHGRTAGAMQVEKAQLEKEINDRRL--ELQEFKILKDKKDAKIRELEARVSDL--ELEKVK-LVNAGSER- 644
|
250 260 270
....*....|....*....|....*....|....*
gi 194018511 418 EQALQDAWQKLQDLEEALQQSKEELARLLRDYQAM 452
Cdd:pfam15921 645 LRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVL 679
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
337-478 |
7.51e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.79 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 337 AVRTQYELIAQRSKdEAEALyQTKYQELQITAGRHGDDLKNSKMEIAELNRTVQRLQAEISNVKKQI---EQMQSLISDA 413
Cdd:pfam05667 322 KVETEEELQQQREE-ELEEL-QEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYkvkKKTLDLLPDA 399
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194018511 414 EERGEqalqdawqKLQDLEEALQQSKEELARLLRDYQAMLgvklsldveIATYRQLLEGEESRMS 478
Cdd:pfam05667 400 EENIA--------KLQALVDASAQRLVELAGQWEKHRVPL---------IEEYRALKEAKSNKED 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-483 |
8.13e-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: 45.82 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 162 TQEREQ-IMVLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVntstgtnnlepllenyIGDLR-------RQVDLLSAEQ 233
Cdd:TIGR02168 672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEE----------------LEQLRkeleelsRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 234 MRQNAEVRSMQDVVEDYKSKYEDEINKRTGSENDFVVLKKDVDAAYVSKVDLESRVDTLTGEVNFLKylflTELSQVQTH 313
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----EALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 314 ISDTNVILSMDNNRSLDLDSIIDAVRTQYELIAQRSKDEAEALYQTKYQ--ELQITAGRHGDDLKNSKMEIAELNRTVQR 391
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALAL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 392 LQAEISNVKKQIEQMQSLISDAeergEQALQDAWQKLQDLEEALQQSKEELARLLR----DYQAMLGVKLSLDVEIATYR 467
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSEL----RRELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDE 967
|
330
....*....|....*.
gi 194018511 468 QLLEGEESRMSGELQS 483
Cdd:TIGR02168 968 EEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
335-483 |
9.23e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 335 IDAVRTQYELIAQRsKDEAEALYQTKYQELQITAGRhgddLKNSKMEIAELNRTVQRLQAEISNVKKQIEQMQSLISDAE 414
Cdd:COG1196 234 LRELEAELEELEAE-LEELEAELEELEAELAELEAE----LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194018511 415 ERGEQALQDAWQ---KLQDLEEALQQSKEELARLLRDYQAMLGVKLSLDVEIATYRQLLEGEESRMSGELQS 483
Cdd:COG1196 309 ERRRELEERLEEleeELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-452 |
1.04e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 346 AQRSKDEAEALYQTKYQELQITAGRHGDDlknsKMEIAELNRTVQRLQAEISNVKKQI----EQMQSLISDAEERGEQaL 421
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSEL----EEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQ-L 325
|
90 100 110
....*....|....*....|....*....|.
gi 194018511 422 QDAWQKLQDLEEALQQSKEELARLLRDYQAM 452
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESL 356
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
259-484 |
1.74e-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: 44.66 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 259 NKRTGSENDFVVLKKDVDAAYVSKVDLESRVDTLTGEVNFLKYLFLTELSQVQTHISDTNVILSMDNNRSLDLDSIiDAV 338
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL-EAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 339 RTQYELIAQRSKDEAEALYQTKyQELQITAGRHGDDLKNSKMEIAELNRTVQRLQAEISNVKKQIEQMQSLISDAEERGE 418
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194018511 419 QaLQDAWQKLQDLEEALQQSKEELARLLRDYQAMLGVKLSLDVEIATYRQLLEGEESRMSGELQSH 484
Cdd:TIGR02168 842 D-LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-430 |
2.93e-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: 43.89 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 137 QEVTINQSLLEPLHLEVDPEIQRIKTQErEQIMVLNNKFASFIDkvRFLEQQNQVLQTKWELLQQVNTSTGTNNLEPLLE 216
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 217 NYIGDLRRQVDLLSAEQMRQNAEVRSMQDVVEDYKSKYEDEINKRTGSENDFVVLKKDVDAAYVSKVDLESRVDTLTGEV 296
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 297 NFLKylflTELSQVQTHISDTNVilsmdnnrslDLDSIIDAVRTQYELIAqrskDEAEALYQTKYQELQiTAGRHGDDLK 376
Cdd:TIGR02168 918 EELR----EKLAQLELRLEGLEV----------RIDNLQERLSEEYSLTL----EEAEALENKIEDDEE-EARRRLKRLE 978
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194018511 377 NSKMEIAELNRTV--------QR---LQAEISNVKKQIEQMQSLISDAEERGEQALQDAWQKLQD 430
Cdd:TIGR02168 979 NKIKELGPVNLAAieeyeelkERydfLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNE 1043
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
302-483 |
4.58e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 302 LFLTELSQVQTHISDTNVILSMDNNRsldLDSIIDAVRTQYELIAQRSKDEAEALYQTKYQELQitagrhgddlknskME 381
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEAR---LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE--------------AE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 382 IAELNRT-------VQRLQAEISNVKKQIEQMQSLISDAEERGEQALQDAWQKLQDLEEALQQSKEELARLLRDYQAmlg 454
Cdd:COG3206 279 LAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR--- 355
|
170 180 190
....*....|....*....|....*....|..
gi 194018511 455 vkLSLDVEIA--TYRQLLEG-EESRMSGELQS 483
Cdd:COG3206 356 --LEREVEVAreLYESLLQRlEEARLAEALTV 385
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
152-474 |
4.91e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 152 EVDPE-IQRIKTQEREQIMVLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVN------TSTGTNNLEPLLENYIGDLRR 224
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHYNEKKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 225 ---QVDLLSAEQMRQNAEVRSMQDVVEDYKSKyedEINKRTGSENDFVVLKKDVDAAYVSKVDLESRVDTLTGEVNFLKY 301
Cdd:PRK01156 481 leeKIREIEIEVKDIDEKIVDLKKRKEYLESE---EINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 302 LFLTELSQVQTHISDTNVILSmdnnrSLDldsiIDAVRTQYELIAQRSKDEAEALYQ--------TKYQELQItaGRHGD 373
Cdd:PRK01156 558 LKLEDLDSKRTSWLNALAVIS-----LID----IETNRSRSNEIKKQLNDLESRLQEieigfpddKSYIDKSI--REIEN 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 374 D---LKNSKMEIAELNRTVQRLQAEISNVKKQIEQMQSLISDAEERGEQALQDAwQKLQDLEEALQQSKEELARLLRDYQ 450
Cdd:PRK01156 627 EannLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIE-DNLKKSRKALDDAKANRARLESTIE 705
|
330 340
....*....|....*....|....
gi 194018511 451 AMLGVKLSLDVEIATYRQLLEGEE 474
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMK 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-471 |
8.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 330 DLDSIIDAVRTqyeliAQRSKD---EAEALYQtKYQELQITAGRHgDDLKNS-------------KMEIAELNRTVQRLQ 393
Cdd:COG4913 236 DLERAHEALED-----AREQIEllePIRELAE-RYAAARERLAEL-EYLRAAlrlwfaqrrlellEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 394 AEISNVKKQIEQMQSLISDAEergEQALQDAWQKLQDLE---EALQQSKEELARLLRDYQAML-GVKLSLDVEIATYRQL 469
Cdd:COG4913 309 AELERLEARLDALREELDELE---AQIRGNGGDRLEQLEreiERLERELEERERRRARLEALLaALGLPLPASAEEFAAL 385
|
..
gi 194018511 470 LE 471
Cdd:COG4913 386 RA 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-483 |
1.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 330 DLDSIIDAVRTQYELIAQRSKDEAE---ALYQTKYQELQITAGRHGDDLKNSKMEIAELNRTVQRLQAEISNVK-KQIEQ 405
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQrrlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 406 MQSLISDAE---ERGEQALQDAWQKLQDLEEALQQSKEELARLLRDYQAMLGVKLSLDVEIATYRQLLEGEESRMSGELQ 482
Cdd:COG4913 343 LEREIERLErelEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
.
gi 194018511 483 S 483
Cdd:COG4913 423 E 423
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
330-448 |
1.34e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 330 DLDSIIDAVRTQYELI------AQRSKDEAEALYQT------KYQElQITAGRHGDDLKNSKMEIAELNRTVQRLQAEIS 397
Cdd:COG1579 35 ELEDELAALEARLEAAkteledLEKEIKRLELEIEEvearikKYEE-QLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 194018511 398 NVKKQIEQMQSLISDAEERGEQALQDAWQKLQDLEEALQQSKEELARLLRD 448
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-484 |
1.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 330 DLDSIIDAVRTQ---YELIAQRSKDEAEALY-QTKYQELQitagRHGDDLKNSKMEIAELNRTVQRLQAEISNVKKQIEQ 405
Cdd:COG4913 635 ALEAELDALQERreaLQRLAEYSWDEIDVASaEREIAELE----AELERLDASSDDLAALEEQLEELEAELEELEEELDE 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 406 MQSLISDAEERGEQAlQDAWQKLQDLEEALQQSK--------EELARLLRDYQAMLGVKLSLDVEIATYRQLLEGEESRM 477
Cdd:COG4913 711 LKGEIGRLEKELEQA-EEELDELQDRLEAAEDLArlelrallEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
....*..
gi 194018511 478 SGELQSH 484
Cdd:COG4913 790 ERAMRAF 796
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
373-484 |
2.57e-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: 40.80 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 373 DDLKNSKMEIAELNRTVQRLQAEISNVKKQIEQMQSLISDAEERGEQALQDAWQKLQDLEEALQQSKEELARLLRDYQAM 452
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRE 327
|
90 100 110
....*....|....*....|....*....|..
gi 194018511 453 LGVKLSLDVEIATYRQLLEGEESRMSGELQSH 484
Cdd:TIGR00606 328 LEKLNKERRLLNQEKTELLVEQGRLQLQADRH 359
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
330-481 |
2.86e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 330 DLDSIIDAVRTQY-ELIAQRSKDEAE-ALYQTKYQELQITAGRHGDDLKNSKMEIAELNRTVQRLQAEISNVK------- 400
Cdd:COG1579 14 ELDSELDRLEHRLkELPAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 401 --KQIEQMQSLISDAEER---GEQALQDAWQKLQDLEEALQQSKEELARLLRDYQAMLGvklSLDVEIATYRQLLEGEES 475
Cdd:COG1579 94 lqKEIESLKRRISDLEDEileLMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAEREELAA 170
|
....*.
gi 194018511 476 RMSGEL 481
Cdd:COG1579 171 KIPPEL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
335-452 |
3.21e-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: 40.13 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 335 IDAVRTQYELIAQRSKDEAEALYQTKYQELQITagrhgDDLKNSKMEIAELNRTVQRLQAEISNVKKQIEQMQslisdae 414
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALL-----KQLAALERRIAALARRIRALEQELAALEAELAELE------- 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 194018511 415 ergeqalqdawQKLQDLEEALQQSKEELARLLRDYQAM 452
Cdd:COG4942 90 -----------KEIAELRAELEAQKEELAELLRALYRL 116
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
343-478 |
4.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 343 ELIAQRSKDEAEalyqtkYQELQITAGRhgddLKNSKMEIAELNRTVQRLQAEISNVKKQIEQMQSLISDAEErgeqalq 422
Cdd:PRK03918 218 ELREELEKLEKE------VKELEELKEE----IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE------- 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 194018511 423 dawqKLQDLEEaLQQSKEELARLLRDYQAMLGVKLSLDVEIATYRQLLEGEESRMS 478
Cdd:PRK03918 281 ----KVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
185-442 |
5.14e-03 |
|
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: 39.70 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 185 LEQQNQVLQTKWELLQQVNTSTGTnnLEPLLENYIGDLRR---QVDLLSAEQMRQNAEVRSMQDVVEDYKSKYEdEINKR 261
Cdd:pfam05483 337 MEELNKAKAAHSFVVTEFEATTCS--LEELLRTEQQRLEKnedQLKIITMELQKKSSELEEMTKFKNNKEVELE-ELKKI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 262 TGSENDFVVLKKDVdaayvskvdlESRVDTLTGEVNFLKYLFLTELSQVQthisdtnvilsmdnnrslDLDSIIDAVRTQ 341
Cdd:pfam05483 414 LAEDEKLLDEKKQF----------EKIAEELKGKEQELIFLLQAREKEIH------------------DLEIQLTAIKTS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 342 YELIAQRSKDEAEALYQTKYQELQITAGRHGDDLKNSKM--EIAELNRTVQRLQAEISNVKKQIEQMQSLISDAEERgEQ 419
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELtqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK-EM 544
|
250 260
....*....|....*....|...
gi 194018511 420 ALQDawqKLQDLEEALQQSKEEL 442
Cdd:pfam05483 545 NLRD---ELESVREEFIQKGDEV 564
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
180-466 |
5.49e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 180 DKVRFLEQQNQVLQTKWELL-QQVNTStgtnnlepllENYIGDLRRQvdllsaeqmrQNAEVRSMQDVVEDYKSKYED-- 256
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIqQQIKTY----------NKNIEEQRKK----------NGENIARKQNKYDELVEEAKTik 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 257 -EINKRTGSENDFVVLKKDVDAAY----VSKVDLESRVDTLTGEVNFLkylflTELSQVQTHISDtnviLSMDNNRSLDL 331
Cdd:PHA02562 234 aEIEELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMY-----EKGGVCPTCTQQ----ISEGPDRITKI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 332 DSIIDAVRTQYELIAQRSKDEAEALYQtkYQELQITAgrhgDDLKNskmEIAELNRTVQRLQAEISNVKKQIEQMQSLIS 411
Cdd:PHA02562 305 KDKLKELQHSLEKLDTAIDELEEIMDE--FNEQSKKL----LELKN---KISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194018511 412 DAEERGEQaLQDawqKLQDLEEALQQSKEE------LARLLRDYqamlGVKLSLdveIATY 466
Cdd:PHA02562 376 DNAEELAK-LQD---ELDKIVKTKSELVKEkyhrgiVTDLLKDS----GIKASI---IKKY 425
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
331-468 |
6.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 331 LDSIIDAVRTQYELIAQRsKDEAEALY---QTKYQELQIT-AGRHGDDLKNSKMEIAELNRTVQRLQAEISNVKKQIEQM 406
Cdd:COG4913 293 LEAELEELRAELARLEAE-LERLEARLdalREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194018511 407 QSLISDAEERGEQALQDAWQKLQDLEEALQQSKEELARLLRDYQAMLGVKLSLDVEIATYRQ 468
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-487 |
6.18e-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: 39.65 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 225 QVDLLSAEQMRQNAEVRSMQDVVEDYKSKYEDEINKRTGSENDFVVLKKDVDAAYVSKVDLESRVDTLTGEVNFL---KY 301
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 302 LFLTELSQVQTHISDTNVILSMDNNRSLDLDSIIDAVRTQYELIAQRSKDEAEALyqTKYQELQITAGRHGDDLKNskmE 381
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEAELEELESRLEELEE---Q 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 382 IAELNRTVQRLQAEISNVKKQIEQMQSLISDAEERGEQALQDAWQKLQDLEEA--------LQQSKEELARLLRDYQAML 453
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelqaeLEELEEELEELQEELERLE 460
|
250 260 270
....*....|....*....|....*....|....*..
gi 194018511 454 GVKLSLDVEIATYRQLL---EGEESRMSGELQSHVSI 487
Cdd:TIGR02168 461 EALEELREELEEAEQALdaaERELAQLQARLDSLERL 497
|
|
| GrpE |
COG0576 |
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein ... |
381-471 |
6.36e-03 |
|
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440341 [Multi-domain] Cd Length: 147 Bit Score: 37.44 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 381 EIAELNRTVQRLQAEISNVKKQIEQmqslisDAEERGEQALQDAWQKLQ----DLEEALQQSKEElarllRDYQAML-GV 455
Cdd:COG0576 7 ELAELKDRLLRLQAEFENYRKRTER------EREEARKYALEKLAEDLLpvldNLERALAAAEED-----EDVKSLLeGV 75
|
90
....*....|....*.
gi 194018511 456 KLsldveiaTYRQLLE 471
Cdd:COG0576 76 EM-------TLKQLLD 84
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
306-482 |
6.50e-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: 39.67 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 306 ELSQVQTHISDTNVILSMDNNRSLDLDSIIDAVRTQyelIAQRSKDEAEALyQTKYQELQITAGRHGDDLKNSKMEIAEL 385
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK---IKDLGEEEQLRV-KEKIGELEAEIASLERSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 386 NRTVQRLQAEISNVKKQIEQMQSLIsdAEERGEQ-ALQDAWQKLQDLEEALQQSKEEL---ARLLRDYQAMLGVKLSldv 461
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREI--EEERKRRdKLTEEYAELKEELEDLRAELEEVdkeFAETRDELKDYREKLE--- 395
|
170 180
....*....|....*....|.
gi 194018511 462 EIATYRQLLEGEESRMSGELQ 482
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQ 416
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
380-448 |
6.64e-03 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 38.02 E-value: 6.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194018511 380 MEIAELNRTVQRLQAEISNVKKQIEQMQSLisdaeergeQALQDAWQKLQDLEEALQQSKEELARLLRD 448
Cdd:COG3166 45 GQIAQQQARNAALQQEIAKLDKQIAEIKEL---------KKQKAELLARLQVIEQLQQSRPPWVHLLDE 104
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-444 |
7.10e-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: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 229 LSAEQMRQNAEVRSMQDVVEDYKSKYEDEINKRTGSENDFVVLKKDVDAAYVSKVDLESRVDTLTGEVNFLKylflTELS 308
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----AELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018511 309 QVQTHISDTNVILSMDNNRS-----LDLDSIIDAVRTQ--YELIAQRSKDEAEALYQTKyQELQITAGRHGDDLKNSKME 381
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPplallLSPEDFLDAVRRLqyLKYLAPARREQAEELRADL-AELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194018511 382 IAELNRTVQRLQAEISNVKKQIEQMQSLISDAEERgEQALQDAWQKLQDLEEALQQSKEELAR 444
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAE-LAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
384-451 |
8.24e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 37.30 E-value: 8.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194018511 384 ELNRTVQRLQAEISNVKKQIEQMQSLISDAEER---GEQALQDAWQKLQDLEEALQQSKEELARLLRDYQA 451
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQ 126
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-448 |
8.86e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 8.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194018511 382 IAELNRTVQRLQAEISNVKKQIEQMQSLISDAEERGE-----QALQDAWQKLQDLEEALQQSKEELARLLRD 448
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlAEYSWDEIDVASAEREIAELEAELERLDAS 683
|
|
| |
