|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
166-479 |
9.67e-122 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 361.55 E-value: 9.67e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 166 QEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRtSSLEPVFEEFISQLQRQVDVLTTEQLRQNTEIRN 245
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEP-SRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 246 MQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKYLFDTELSQIQTHVSDTNVILS 325
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 326 MDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQ 405
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51092293 406 VEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESR 479
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
132-163 |
3.43e-17 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 78.93 E-value: 3.43e-17
10 20 30
....*....|....*....|....*....|..
gi 51092293 132 PSYPPGGIHEVTINQSLLEPLHLEVDPEIQRV 163
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
338-484 |
3.64e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 338 IDAVRAQYEIIAQKSKDEAEAL--YQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISD 415
Cdd:COG1196 262 LAELEAELEELRLELEELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51092293 416 AEERGERA---LQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESRMSGAL 484
Cdd:COG1196 342 LEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
219-474 |
6.19e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 219 EEFISQLQRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDvdaafmgKSDLQSKVDTLYGE 298
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE-------KLNIQKNIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 299 INFLKYLFDTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDavraqyeiiAQKSKDEAEALYQTKYQELQITAGKHGD-- 376
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEK---------KQQEINEKTTEISNTQTQLNQLKDEQNKik 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 377 --------DLKNSKMEISELNRNIQRLRAEIANIKKQ-VEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAK 447
Cdd:TIGR04523 267 kqlsekqkELEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
250 260
....*....|....*....|....*..
gi 51092293 448 LLRDYQAMLGAKLSLDVEIATYRQLLE 474
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIE 373
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
237-474 |
2.14e-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: 44.28 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 237 LRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVdaafmgkSDLQSKVDTLYGEINFLKYLFDTELSQIQTh 316
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL-------EQLRKELEELSRQISALRKDLARLEAEVEQ- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 317 vsdtnviLSMDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKyQELQITAGKHGDDLKNSKMEISELNRNIQRLR 396
Cdd:TIGR02168 745 -------LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 397 AEIANIKKQVEGMHGLISDAEERGERALQNAKQKLQDMEEA---LQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLL 473
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
.
gi 51092293 474 E 474
Cdd:TIGR02168 897 E 897
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
307-447 |
3.36e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 307 DTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDAVRAQYEiIAQKSKDEAEALYQTKYQELQITAGKHGD---DLKNSKM 383
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS-AAEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51092293 384 EISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGeralQNAKQKLQDMEE----ALQQAKEDLAK 447
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRrlnvALAQRVQELNR 194
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
212-407 |
3.58e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 212 SSLEPVFEEF--ISQLQRQVDVLTTEQLRQnteirnmqdVVEDYKNKYEDEINKRTNAendfvvlkkdvdaafmgKSDLQ 289
Cdd:PRK05771 60 DKLRSYLPKLnpLREEKKKVSVKSLEELIK---------DVEEELEKIEKEIKELEEE-----------------ISELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 290 SKVDTLYGEINFLKYL--FDTELSQIQTHvSDTNVILSMDNNRSLDLDSIIDAVRAQYEI----------IAQKSKDEAE 357
Cdd:PRK05771 114 NEIKELEQEIERLEPWgnFDLDLSLLLGF-KYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvVVVLKELSDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 51092293 358 ALYQTK---YQELQITAGKHGDD-LKNSKMEISELNRNIQRLRAEIANIKKQVE 407
Cdd:PRK05771 193 VEEELKklgFERLELEEEGTPSElIREIKEELEEIEKERESLLEELKELAKKYL 246
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
170-405 |
6.45e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 170 QIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTS-SLEPVFEE---FISQLQRQVDVLTTEQLRQNTEIRN 245
Cdd:TIGR01612 580 EIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAiDLKKIIENnnaYIDELAKISPYQVPEHLKNKDKIYS 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 246 MqdVVEDYKNKYEDEINKRTNaENDFVVLKKDVDAA--FMGKSDLQSKVDTLYGEINflkylfDTELSQIQTHVSdtnvi 323
Cdd:TIGR01612 660 T--IKSELSKIYEDDIDALYN-ELSSIVKENAIDNTedKAKLDDLKSKIDKEYDKIQ------NMETATVELHLS----- 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 324 lSMDNNRSLDLDSIidaVRAQYEIIAQKSKDEAEALYQTKYQELQITA-----GKHGDDLKNSKMEISELnRNIQRLRAE 398
Cdd:TIGR01612 726 -NIENKKNELLDII---VEIKKHIHGEINKDLNKILEDFKNKEKELSNkindyAKEKDELNKYKSKISEI-KNHYNDQIN 800
|
....*..
gi 51092293 399 IANIKKQ 405
Cdd:TIGR01612 801 IDNIKDE 807
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
329-471 |
1.10e-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: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 329 NRSLDLDSIIDAVRAQYEIiAQKSKDEAEALYQTKYQELQiTAGkhGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEG 408
Cdd:COG4913 295 AELEELRAELARLEAELER-LEARLDALREELDELEAQIR-GNG--GDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51092293 409 MHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQ 471
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
156-481 |
1.14e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.76 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 156 VDPEiQRVKTQEREQIKTLNNKFASFIDKVRfleqqNQVLQTKwellqqvNTSTRTSslEPVFEEFISQLQRQVD----- 230
Cdd:PLN03229 413 VDPE-RKVNMKKREAVKTPVRELEGEVEKLK-----EQILKAK-------ESSSKPS--ELALNEMIEKLKKEIDleyte 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 231 ------------VLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFM-----GKSDLQSKVD 293
Cdd:PLN03229 478 aviamglqerleNLREEFSKANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEfsrakALSEKKSKAE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 294 TLYGEIN-FLKYLFD-----------------TELSQIQTHVSDT-NVILSMDNNRSLDLDSIIDAVRAQYEIIAQKSKD 354
Cdd:PLN03229 558 KLKAEINkKFKEVMDrpeikekmealkaevasSGASSGDELDDDLkEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKD 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 355 EAEAL----YQTKYQELQITAGKHGDDLKNSkmeiSELNRNIQRLRAEIAnikkqvegmhglisdaeERGERALQNAKQK 430
Cdd:PLN03229 638 TAEQTpppnLQEKIESLNEEINKKIERVIRS----SDLKSKIELLKLEVA-----------------KASKTPDVTEKEK 696
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 51092293 431 LQDMEealQQAKEDLAKLLrDYQAMLGAKLSLDVEIATYRQLLEGEESRMS 481
Cdd:PLN03229 697 IEALE---QQIKQKIAEAL-NSSELKEKFEELEAELAAARETAAESNGSLK 743
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
309-478 |
1.23e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 309 ELSQIQTHVSDTNVILSMDNNRSLDLDSIIDAVRAQYEII--AQKSKDEAEALYQTKYQELQItagkhgddlknskmEIS 386
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELrlEVSELEEEIEELQKELYALAN--------------EIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 387 ELNRNIQRLRAEIANIKKQVEgmhgLISDAEERGERALQNAKQKLQDMEEALQQAKED-------LAKLLRDYQAMLGAK 459
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLE----ELEAQLEELESKLDELAEELAELEEKLEELKEElesleaeLEELEAELEELESRL 374
|
170 180
....*....|....*....|...
gi 51092293 460 LSLDVEIATYR----QLLEGEES 478
Cdd:TIGR02168 375 EELEEQLETLRskvaQLELQIAS 397
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
296-451 |
1.39e-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: 41.25 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 296 YGEINFLKYL-FDTEL-SQIQTHVSDTNVILSMDNNRSLDldSIIDAVRAQYEIIAQKskdeaEALYQTKYQELQITAGK 373
Cdd:TIGR04320 207 DDKINAGAYLgVSISNdGGVTIHFVNFNDSYIADGNKFDK--TPIPNPPNSLAALQAK-----LATAQADLAAAQTALNT 279
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51092293 374 HGDDLKNSKMEISELNRNIQRLRAEIANIKKQvegmhglisdAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRD 451
Cdd:TIGR04320 280 AQAALTSAQTAYAAAQAALATAQKELANAQAQ----------ALQTAQNNLATAQAALANAEARLAKAKEALANLNAD 347
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
349-455 |
1.66e-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: 40.90 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 349 AQKSKDEAEALyQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERgeraLQNAK 428
Cdd:COG4942 15 AAAQADAAAEA-EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELE 89
|
90 100
....*....|....*....|....*..
gi 51092293 429 QKLQDMEEALQQAKEDLAKLLRDYQAM 455
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRL 116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-479 |
3.25e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 346 EIIAQKSKDEAE-ALYQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERA- 423
Cdd:COG1196 257 ELEAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELe 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 51092293 424 --LQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESR 479
Cdd:COG1196 337 eeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-449 |
3.71e-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: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 149 LEPLHLEVDP--EIQRVKTQERE-QIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQvNTSTRTSSLEpVFEEFISQL 225
Cdd:TIGR02168 202 LKSLERQAEKaeRYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTA-ELQELEEKLE-ELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 226 QRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKYL 305
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 306 FDTELSQIQ---THVSDTNVILSMDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLKNSK 382
Cdd:TIGR02168 360 LEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51092293 383 MEISELNRNIQRLRAEIANIKKQVEGMHGLISDAE------ERGERALQNAKQKLQDMEEALQQAKEDLAKLL 449
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEqaldaaERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
305-484 |
4.18e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 305 LFDTELSQIQTHVSDTNVILSMDNNRsldLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQitagkhgddlknskME 384
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEAR---LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE--------------AE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 385 ISELNRN-------IQRLRAEIANIKKQVEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAmlg 457
Cdd:COG3206 279 LAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR--- 355
|
170 180 190
....*....|....*....|....*....|
gi 51092293 458 akLSLDVEIA--TYRQLLEG-EESRMSGAL 484
Cdd:COG3206 356 --LEREVEVAreLYESLLQRlEEARLAEAL 383
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
364-460 |
4.38e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 40.03 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 364 YQELQITAGKHGDdlKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERALQ---NAKQKlQDMEEALQQ 440
Cdd:pfam14817 60 YGGLQDKGKAESR--QSAAARRLELQKEIERLRAEISRLDKQLEARELELSREEAERERALDeisDSRHR-QLLLEAYDQ 136
|
90 100
....*....|....*....|
gi 51092293 441 AKEDLAKLLRDYQAMLGAKL 460
Cdd:pfam14817 137 QCEEARKILAEDHQRLQGQL 156
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
188-455 |
4.87e-03 |
|
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: 40.10 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 188 LEQQNQVLQTKWELLQQVntSTRTSSLEPVFEefisQLQRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKyeDEINKRTNA 267
Cdd:pfam15921 446 MERQMAAIQGKNESLEKV--SSLTAQLESTKE----MLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 268 EndfvvlkkdvdaafmgKSDLQSKVDTLYGEINFLKYLFDtELSQIQTHVSDTNVILSmdnnrslDLDSIIDAVRAQYEI 347
Cdd:pfam15921 518 E----------------ITKLRSRVDLKLQELQHLKNEGD-HLRNVQTECEALKLQMA-------EKDKVIEILRQQIEN 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 348 IAQKSKDEAEALYQTKYQELQITagkhgDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMH----GLISDAEERgERA 423
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQLE-----KEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvKLVNAGSER-LRA 647
|
250 260 270
....*....|....*....|....*....|..
gi 51092293 424 LQNAKQKLQDMEEALQQAKEDLAKLLRDYQAM 455
Cdd:pfam15921 648 VKDIKQERDQLLNEVKTSRNELNSLSEDYEVL 679
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
155-477 |
6.59e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 155 EVDPEIQRVKTQE-REQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVN------TSTRTSSLEPVFEEF---ISQ 224
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHYnekKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 225 LQRQVDVLTTEQLRQNTEIRNMQDVvEDYKNKyeDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKY 304
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKR-KEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 305 LFDTELSQIQTHVSDTNVILSmdnnrSLDldsiIDAVRAQYEIIAQKSKDEAEALYQTK--------YQELQITA-GKHG 375
Cdd:PRK01156 558 LKLEDLDSKRTSWLNALAVIS-----LID----IETNRSRSNEIKKQLNDLESRLQEIEigfpddksYIDKSIREiENEA 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 376 DDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERALQnAKQKLQDMEEALQQAKEDLAKLLRDYQAM 455
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIND-IEDNLKKSRKALDDAKANRARLESTIEIL 707
|
330 340
....*....|....*....|..
gi 51092293 456 LGAKLSLDVEIATYRQLLEGEE 477
Cdd:PRK01156 708 RTRINELSDRINDINETLESMK 729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
222-479 |
6.72e-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: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 222 ISQLQRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFvvlkkdvdaafmgkSDLQSKVDTLYGEINF 301
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--------------YELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 302 LKylfdTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLkns 381
Cdd:COG1196 307 LE----ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE--- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 382 kmEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLS 461
Cdd:COG1196 380 --ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250
....*....|....*...
gi 51092293 462 LDVEIATYRQLLEGEESR 479
Cdd:COG1196 458 EEALLELLAELLEEAALL 475
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
331-479 |
9.24e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.84 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 331 SLDLDSIIDAVRAQYEII--AQKSKDEAEALYQTKYQELQITAGKH-------GDDLKNSKMEISELNRNIQRLRAEIAN 401
Cdd:PHA02562 187 DMKIDHIQQQIKTYNKNIeeQRKKNGENIARKQNKYDELVEEAKTIkaeieelTDELLNLVMDIEDPSAALNKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 402 IKKQVEGMHGL----------------ISDAEERGERALQNAKQkLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVE 465
Cdd:PHA02562 267 IKSKIEQFQKVikmyekggvcptctqqISEGPDRITKIKDKLKE-LQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNK 345
|
170
....*....|....
gi 51092293 466 IATYRQLLEGEESR 479
Cdd:PHA02562 346 ISTNKQSLITLVDK 359
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
338-484 |
9.79e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 338 IDAVRAQYEIiAQKSKDEAEALYQTKYQELQITAGKhgddLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAE 417
Cdd:COG1196 234 LRELEAELEE-LEAELEELEAELEELEAELAELEAE----LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51092293 418 ERgeraLQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESRMSGAL 484
Cdd:COG1196 309 ER----RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
333-483 |
9.84e-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: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 333 DLDSIIDAVRAQ---YEIIAQKSKDEAEALY-QTKYQELQITAgkhgDDLKNSKMEISELNRNIQRLRAEIANIKKQVEG 408
Cdd:COG4913 635 ALEAELDALQERreaLQRLAEYSWDEIDVASaEREIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDE 710
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51092293 409 MHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESRMSGA 483
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
|
| |
