|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
93-406 |
1.84e-130 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 381.19 E-value: 1.84e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 93 NEKEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQR-HAEPSRVGELFQRELRELRAQLEEASSARAQALLERDGL 171
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 172 AEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQVHDEEVAELLATLQASSQAAAE 251
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 252 VDVAvaKPDLTSALREIRAQYESLAAKNLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRG 331
Cdd:pfam00038 161 DAAR--KLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1703221 332 ANESLERQILELEERHSAEVAGYQDSIGQLESDLRNTKSEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 406
Cdd:pfam00038 239 QKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-364 |
1.41e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 66 YRRLpaSDGLDLSQAAARTNEYKIIRtnekEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQR 145
Cdd:COG1196 215 YREL--KEELKELEAELLLLKLRELE----AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 146 ELRELRAQLEEASSARAQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELA 225
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 226 FVRQVHDEEVAELLATLQASSQaaaevdvavakpdLTSALREIRAQYESLAAKNLQSAEEwykskFANLNEQAARSTEAI 305
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLE-------------ALRAAAELAAQLEELEEAEEALLER-----LERLEEELEELEEAL 430
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1703221 306 RASREEIHEYRRQLQARTIEIEGLRGANESLERQILELEERHSAEVAGYQDSIGQLESD 364
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
10-92 |
4.64e-12 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 61.64 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 10 CSASSYRKVFGDGSRLSARLSGPGASGSFRSQSLSRSNVASTAACSSASSLGLGLAYRRLPASDGLDLSQAAARTNEYKI 89
Cdd:pfam04732 1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSSRSYSRSSSSSPSSSSRRSSRSSSRSSYPSLAADSLDFSLADALNQEFKA 80
|
...
gi 1703221 90 IRT 92
Cdd:pfam04732 81 TRT 83
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-406 |
5.69e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 110 EKVHQLETQNRALEAELAALRQRHAEpsRVGELFQRELRELRAQLEEASSARAQALLERDGLAEEVQRLRARCEEESRGR 189
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELE--AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 190 EGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQVHDEEVAELLATLQASSQAAAEVDvavakpDLTSALREIR 269
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE------EAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 270 AQYESLAAKNLQSAEEWykskfANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELEERHSA 349
Cdd:COG1196 365 EALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1703221 350 EvagyQDSIGQLESDLRNTKSEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 406
Cdd:COG1196 440 E----EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-409 |
3.23e-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: 59.69 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 144 QRELRELRAQLEEASSARAQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDE 223
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 224 LAFVrqvhDEEVAELLATLQASSQAAAEVDVAVAKPDLTSALREIRAQYESLAAKNLQSAEEWYKSKFANLNEQAARSTE 303
Cdd:TIGR02168 756 LTEL----EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 304 AIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELE---ERHSAEVAGYQDSIGQLESDLRNTKSEMARHLREYQ 380
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEselEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250 260
....*....|....*....|....*....
gi 1703221 381 DLLNVKMALDIEIAAYRKLLEGEETRFST 409
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
95-364 |
4.54e-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: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 95 KEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELF---------QRELRELRAQLE--EASSARAQ 163
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELErlDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 164 ALLER-DGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELA---FVRQVHDEEVAELL 239
Cdd:COG4913 689 ALEEQlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerFAAALGDAVERELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 240 ATLQASSQAAAEVDVAVAKpDLTSALREIRAQYESLAAK---NLQSAEEW--------------YKSKFAN-LNEQAARS 301
Cdd:COG4913 769 ENLEERIDALRARLNRAEE-ELERAMRAFNREWPAETADldaDLESLPEYlalldrleedglpeYEERFKElLNENSIEF 847
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1703221 302 TE----AIRASREEIHEYRRQLqartieieglrgaNESLERQI--------LELEERHSAEVAGYQDSIGQLESD 364
Cdd:COG4913 848 VAdllsKLRRAIREIKERIDPL-------------NDSLKRIPfgpgrylrLEARPRPDPEVREFRQELRAVTSG 909
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-278 |
5.31e-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: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 96 EQLQGLNDRFavfiEKVHQLETQNRALEAELAALRQRHAEpsRVGELFQRELRELRAQLEEASSARAQALLERDGLAEEV 175
Cdd:COG4913 252 ELLEPIRELA----ERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 176 QRLRARCEEESRGR-EGAERALKAQQRDVDGATLARLDLEKKVESL-----LDELAFVRQVhdEEVAELLATLQASSQAA 249
Cdd:COG4913 326 DELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALglplpASAEEFAALR--AEAAALLEALEEELEAL 403
|
170 180 190
....*....|....*....|....*....|.
gi 1703221 250 AEVD--VAVAKPDLTSALREIRAQYESLAAK 278
Cdd:COG4913 404 EEALaeAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-374 |
1.07e-06 |
|
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: 51.61 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 110 EKVHQLETQNRALEAELAALRQRHAE-PSRVGELFQrELRELRAQLEEASSARAQALLERDGLAEEVQRLRARCEEESRG 188
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRiENRLDELSQ-ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 189 REGAERALKAQQRDVDGATLARLDLEKKVESLLDELAfvrqvhDEEVAELLATLQassqaaaevdvavakpDLTSALREI 268
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLS------HSRIPEIQAELS----------------KLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 269 RAQYESLAAK--NLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELE-- 344
Cdd:TIGR02169 811 EARLREIEQKlnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKke 890
|
250 260 270
....*....|....*....|....*....|.
gi 1703221 345 -ERHSAEVAGYQDSIGQLESDLRNTKSEMAR 374
Cdd:TIGR02169 891 rDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
144-398 |
1.51e-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: 50.15 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 144 QRELRELRAQLEEASSARAQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDE 223
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 224 LafvrqvhdeevAELLATLQASSQAAAEVDVAVAKpDLTSALReiRAQYeslaaknlqsaeewykskFANLNEQAARSTE 303
Cdd:COG4942 106 L-----------AELLRALYRLGRQPPLALLLSPE-DFLDAVR--RLQY------------------LKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 304 AIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELEERHSAEVAgyqdsigQLESDLRNTKSEMARHLREYQDLL 383
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA-------RLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*
gi 1703221 384 NVKMALDIEIAAYRK 398
Cdd:COG4942 227 ALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-378 |
3.59e-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: 49.67 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 76 DLSQAAARTNEYKIIRTNEKEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRELRAQLE 155
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 156 EASSARAQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDElafvRQVHDEEV 235
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE----RASLEEAL 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 236 AELLATLQ-ASSQAAAEVDVAVAKPDLTSALREIRAQYESlaakNLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHE 314
Cdd:TIGR02168 890 ALLRSELEeLSEELRELESKRSELRRELEELREKLAQLEL----RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1703221 315 YRRQLQARTIEIEG----LRGANESLERQILELEERHSaEVAGYQDSIGQLESDLRNTKSEMARHLRE 378
Cdd:TIGR02168 966 DEEEARRRLKRLENkikeLGPVNLAAIEEYEELKERYD-FLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
76-343 |
6.59e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 76 DLSQAAARTNEYKIIRTNEKEQLQGLNDRFAVFIEKVHQLETQ----NRALEAE----------LAALRQ---------- 131
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladyQQALDVQqtraiqyqqaVQALEKaralcglpdl 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 132 -------RHAEPSRVGELFQRELRELRAQLEEASSARAQ-----ALLERdgLAEEVQRLRARCEEESRGREGAERALKAQ 199
Cdd:COG3096 435 tpenaedYLAAFRAKEQQATEEVLELEQKLSVADAARRQfekayELVCK--IAGEVERSQAWQTARELLRRYRSQQALAQ 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 200 QRDVDGATLA----RLDLEKKVESLLDELA--FVRQVHD-EEVAELLATLQA--SSQAAAEVDVAVAKPDLTSALREIRA 270
Cdd:COG3096 513 RLQQLRAQLAeleqRLRQQQNAERLLEEFCqrIGQQLDAaEELEELLAELEAqlEELEEQAAEAVEQRSELRQQLEQLRA 592
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1703221 271 QYESLAAKnlqsAEEWYK--SKFANLNEQaarsTEAIRASREEIHEYRRQLQAR----TIEIEGLRGANESLERQILEL 343
Cdd:COG3096 593 RIKELAAR----APAWLAaqDALERLREQ----SGEALADSQEVTAAMQQLLERereaTVERDELAARKQALESQIERL 663
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-379 |
1.63e-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: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 110 EKVHQLETQNRALEAELAALRqrhaepsrvgelfqreLRELRAQLEEASSARAQALLERDGLAEEVQRLRARCEEESRGR 189
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLR----------------LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 190 EGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQvHDEEVAELLATLQASSQAAAEVDVavakpDLTSALREIR 269
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-QLEELEAQLEELESKLDELAEELA-----ELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 270 AQYESLAAKNLQSAEEWykskfANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLR----GANESLERQILELEE 345
Cdd:TIGR02168 351 EELESLEAELEELEAEL-----EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarleRLEDRRERLQQEIEE 425
|
250 260 270
....*....|....*....|....*....|....*...
gi 1703221 346 R----HSAEVAGYQDSIGQLESDLRNTKSEMARHLREY 379
Cdd:TIGR02168 426 LlkklEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
95-379 |
4.28e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 95 KEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRELRA-------QLEEASSARAQALLE 167
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEELREE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 168 RDGLAEEVQRLRARCEEESRGREGAERALKAQQ-----RDVDGATLARL--DLEKKVESLLDELAFVRQVHdEEVAELLA 240
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSPHVETieEDRERVEELEAELEDLEEEV-EEVEERLE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 241 TLQASSQAAAEVDVAVAKPDLTSALREIR---AQYESLAAKNLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHEYRR 317
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1703221 318 QLQARTIEIEGLRGANESLerqileleerhsAEVAGYQDSIGQLEsDLRNTKSEMARHLREY 379
Cdd:PRK02224 580 KLAELKERIESLERIRTLL------------AAIADAEDEIERLR-EKREALAELNDERRER 628
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
135-376 |
4.79e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 135 EPSRVGELFQR------ELRELRAQLEEASsARAQALLERDGLAEEVQRLRARCEEESRGREGAEraLKAQQRDVDGATL 208
Cdd:COG4913 219 EEPDTFEAADAlvehfdDLERAHEALEDAR-EQIELLEPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 209 ARLDLEKKVESLLDELAFVRQVHDEEVAELLATLQASSQAAAEvdvavakpDLTSALREIRAQYESLAAKnlqsaeewyK 288
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--------RLEQLEREIERLERELEER---------E 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 289 SKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRGANE----SLERQILELEERH---SAEVAGYQDSIGQL 361
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELrelEAEIASLERRKSNI 438
|
250
....*....|....*
gi 1703221 362 ESDLRNTKSEMARHL 376
Cdd:COG4913 439 PARLLALRDALAEAL 453
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
76-349 |
7.94e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 76 DLSQAAARTNEYKIIRTNEKEQLQGLNDRFAVFIEKVHQLETqnraLEAELAALRQRHAEPSRVGELFQRELRELRAQLE 155
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 156 EASSARAQAL-------LERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLldelafvr 228
Cdd:PRK02224 290 ELEEERDDLLaeaglddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL-------- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 229 qvhDEEVAELLATLQASSQAAAEVDVAVAkpDLTSALREIRAQYESLAAK--NLQSAEEWYKSKFANLNEQAARSTEAIR 306
Cdd:PRK02224 362 ---REEAAELESELEEAREAVEDRREEIE--ELEEEIEELRERFGDAPVDlgNAEDFLEELREERDELREREAELEATLR 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1703221 307 ASREEIHEYRRQLQA--------------RTIEIEGLRGANESLERQILELEERHSA 349
Cdd:PRK02224 437 TARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEE 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-267 |
9.96e-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: 45.05 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 110 EKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRELRAQLEEASSARAQALLERDGLAEEVQRLRARCE--EESR 187
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErlEDRR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 188 GR-----EGAERALKAQQRDVDGATLARLDLEKkvESLLDELAFVRQVHDEEVAELLATLQASSQAAAEVDVAVAKPDLT 262
Cdd:TIGR02168 417 ERlqqeiEELLKKLEEAELKELQAELEELEEEL--EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
....*
gi 1703221 263 SALRE 267
Cdd:TIGR02168 495 ERLQE 499
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
93-346 |
1.41e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 93 NEKEQLQGLnDRFA---VFIEKVHQLETQNRALEAELAALRQRHAEpsrvgelFQRELRELRAQLEEASSARAQAlLERD 169
Cdd:COG0497 139 DPDAQRELL-DAFAgleELLEEYREAYRAWRALKKELEELRADEAE-------RARELDLLRFQLEELEAAALQP-GEEE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 170 GLAEEVQRLrARCEEEsrgREGAERALKAqqrdVDGATLARLDLEKKVESLLDELAfvrqVHDEEVAELLATLQASSQAa 249
Cdd:COG0497 210 ELEEERRRL-SNAEKL---REALQEALEA----LSGGEGGALDLLGQALRALERLA----EYDPSLAELAERLESALIE- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 250 aevdvavakpdLTSALREIRAQYESLAAknlqSAEEwykskfanLNEQAARSTEAIRASR------EEIHEYRRQLQART 323
Cdd:COG0497 277 -----------LEEAASELRRYLDSLEF----DPER--------LEEVEERLALLRRLARkygvtvEELLAYAEELRAEL 333
|
250 260
....*....|....*....|...
gi 1703221 324 IEIEGLRGANESLERQILELEER 346
Cdd:COG0497 334 AELENSDERLEELEAELAEAEAE 356
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
91-308 |
3.49e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 91 RTNEKEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRELRAQLEEASSARAQALLERDG 170
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 171 LAEEV-QRLRARCEEESRGR-------EGAERALKAQQRdVDGATLARLDLEKKVESLLDELAFVRQVHDEEVAELLATL 242
Cdd:COG4942 102 QKEELaELLRALYRLGRQPPlalllspEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1703221 243 QAssQAAAEVDVAVAKPDLTSALREIRAQYESLAA--KNLQSAEEWYKSKFANLNEQAARSTEAIRAS 308
Cdd:COG4942 181 AE--LEEERAALEALKAERQKLLARLEKELAELAAelAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
76-294 |
3.87e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 76 DLSQAAARTNEYKIIRTNEKEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRELRAQLE 155
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 156 EASSARAQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQVHDEEV 235
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1703221 236 AELLATLQASSQAAAEVDVAVAKpdLTSALREIRAQYESLAAKNLQSAEEWYKSKFANL 294
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAE--LQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
143-324 |
6.95e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 143 FQRELRELRAQLEEASSARAQALLERDGLAEEVQR---LRARCEEESRGREGAERALKAQQRDVDgatLARLDLEkKVES 219
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESElaiSRQDYDGATAQLRAAQAAVKAAQAQLA---QAQIDLA-RRRV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 220 LLDELAFVRQVHDEEVAeLLATLQASsqaaaevdvavakpdltsaLREIRAQYESLAAKNLQSAEEWYKSkfanLNEQAA 299
Cdd:pfam00529 132 LAPIGGISRESLVTAGA-LVAQAQAN-------------------LLATVAQLDQIYVQITQSAAENQAE----VRSELS 187
|
170 180
....*....|....*....|....*
gi 1703221 300 RSTEAIRASREEIHEYRRQLQARTI 324
Cdd:pfam00529 188 GAQLQIAEAEAELKLAKLDLERTEI 212
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
110-367 |
8.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 110 EKVHQLETQNRALEAELAALRQRHAEPSRVGELfQRELRELRAQLEEASSARAQALLERDGLAEEVQRLRARCEE-ESRG 188
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAElEAEA 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 189 REGAERALKAQQRdVDGATLARLDLEKKVESLLDELAFVRQVHD--EEVAELLATLQA-SSQAAAEVDVAVAKPDLTSAL 265
Cdd:PRK02224 554 EEKREAAAEAEEE-AEEAREEVAELNSKLAELKERIESLERIRTllAAIADAEDEIERlREKREALAELNDERRERLAEK 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 266 REIRAQyesLAAKNLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLrganESLERQILELEE 345
Cdd:PRK02224 633 RERKRE---LEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRERREALEN 705
|
250 260
....*....|....*....|....*...
gi 1703221 346 RHSA------EVAGYQDSIGQLESDLRN 367
Cdd:PRK02224 706 RVEAlealydEAEELESMYGDLRAELRQ 733
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
119-384 |
2.33e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 119 NRALEAELAALRQRHAEPSRVGELFQRELRELRAQLEEASSARAQALLERDGLAEEVQRLRARCEEESRGRegaERALKA 198
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK---NKALAE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 199 QQRDvdgATLARLDLEKKVESLLDELafvrQVHDEEVAELLATLQASSQAAAEVDVAVAKPDLTSALREIRAQYESLAAK 278
Cdd:pfam12128 676 RKDS---ANERLNSLEAQLKQLDKKH----QAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAE 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 279 nLQSAEEWYKSKFANLN-------------EQAARSTEAIRASREEIHEYRRQLQAR-TIEIEGLRGANESLERQILELe 344
Cdd:pfam12128 749 -LKALETWYKRDLASLGvdpdviaklkreiRTLERKIERIAVRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISEL- 826
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1703221 345 erhsaevagyQDSIGQLESD--LRNTKSEMARH-LREYQDLLN 384
Cdd:pfam12128 827 ----------QQQLARLIADtkLRRAKLEMERKaSEKQQVRLS 859
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
114-374 |
3.11e-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: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 114 QLETQNRALEAELAALRQ-----RHAEPSRVGELFQRELRELRAQLEEASSARAQALLERDGL--AEEVQRLRARCEEES 186
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGveaayEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpLDKIRARAALAAALA 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 187 RGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQVHDEEVAELLATLQASSQAAAEVdvavakPDLTSALR 266
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG------GSLTGGSR 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 267 EIRAQYESLAAKNLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELEER 346
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
250 260 270
....*....|....*....|....*....|.
gi 1703221 347 HSAEVAGYQD---SIGQLESDLRNTKSEMAR 374
Cdd:COG1196 748 LEEEALEELPeppDLEELERELERLEREIEA 778
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
95-380 |
3.61e-03 |
|
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: 40.16 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 95 KEQLQGLNDRFAVFIEKVHQLETQNRALEA----ELAALRQRHAEPSRvgeLFQRELRELRAQLEEASSARAQALLERDG 170
Cdd:pfam01576 698 KTQLEELEDELQATEDAKLRLEVNMQALKAqferDLQARDEQGEEKRR---QLVKQVRELEAELEDERKQRAQAVAAKKK 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 171 LAEEVQRLRARCEEESRGREGAERALK---AQ----QRDVDGATLARLDL-------EKKVESLLDELAfvrQVHDEEVA 236
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKklqAQmkdlQRELEEARASRDEIlaqskesEKKLKNLEAELL---QLQEDLAA 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 237 ELLATLQASSQAAAEVDVAVAKPDLTSALREIRAQYESLAAKNLQSAEEwYKSKFANLNEQAARSTEAIRASREEIHEYR 316
Cdd:pfam01576 852 SERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEE-EQSNTELLNDRLRKSTLQVEQLTTELAAER 930
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1703221 317 RQLQARtieieglRGANESLERQILEL----EERHSAEVAGYQDSIGQLESDLRNTKSEMARHLREYQ 380
Cdd:pfam01576 931 STSQKS-------ESARQQLERQNKELkaklQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQ 991
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-353 |
4.25e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 88 KIIRTNEKEQLQgLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRELRAQLEEASSARAQALLE 167
Cdd:TIGR02169 280 KIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 168 RDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELafvrQVHDEEVAELLATLQASSQ 247
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL----QRLSEELADLNAAIAGIEA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 248 aaAEVDVAVAKPDLTSALREIRAQYESLAAKnlqsaEEWYKSKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIE 327
Cdd:TIGR02169 435 --KINELEEEKEDKALEIKKQEWKLEQLAAD-----LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
250 260 270
....*....|....*....|....*....|....*...
gi 1703221 328 GLRGANESLE----------RQILELEERHSA--EVAG 353
Cdd:TIGR02169 508 GGRAVEEVLKasiqgvhgtvAQLGSVGERYATaiEVAA 545
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
120-321 |
4.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 120 RALEAELAALRQRHAepsRVGELFQRELRELRAQLEEASSAR---AQALLERDGLAEEVQRLRARCEEESRGREGAERAL 196
Cdd:COG4717 49 ERLEKEADELFKPQG---RKPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 197 KAQQrdvdgATLARLDLEKKVESLLDELAFVRQvHDEEVAELLATLQASSQaaaevdvavakpDLTSALREIRAQYESLA 276
Cdd:COG4717 126 QLLP-----LYQELEALEAELAELPERLEELEE-RLEELRELEEELEELEA------------ELAELQEELEELLEQLS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1703221 277 AKNLQSAEEWyKSKFANLNEQAARSTEAIRASREEIHEYRRQLQA 321
Cdd:COG4717 188 LATEEELQDL-AEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
73-239 |
4.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 73 DGLDLSQAAARTNEYKIIRTNEKEQLQGLNDRFAVFIEKVHQLETQNRA---------------LEAELAALRQRHAEPS 137
Cdd:COG4913 279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEleaqirgnggdrleqLEREIERLERELEERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 138 RVGELFQRELRELRAQLEEASSARAQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDgATLARL-----D 212
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIASLerrksN 437
|
170 180 190
....*....|....*....|....*....|
gi 1703221 213 LEKKVESLLDELAFVRQVHDEE---VAELL 239
Cdd:COG4913 438 IPARLLALRDALAEALGLDEAElpfVGELI 467
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
79-281 |
4.93e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 79 QAAARTNEY--KIIRTNEKEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRH--AEPSRVGELFQRELRELRAQL 154
Cdd:COG3206 149 LAAAVANALaeAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 155 EEASSARAQALLERDGLAEEVQRLRARCEE--ESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQVHD 232
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1703221 233 EEVAELLATLQASSQAAAEVDVavakpDLTSALREIRAQYESLAAKNLQ 281
Cdd:COG3206 309 QEAQRILASLEAELEALQAREA-----SLQAQLAQLEARLAELPELEAE 352
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
114-390 |
5.68e-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: 39.33 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 114 QLETQNRALEAELAALRQRHAEpsRVGELFQRELRELRAQLEEASSARAQAllerdglaeevQRLRARCEeesrgregae 193
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQHQD--RIEQLISEHEVEITGLTEKASSARSQA-----------NSIQSQLE---------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 194 rALKAQQRDVDGATLARL-DLEKKVESLLDELAFVRQVHDEEVAELLATLQASSQAAAEVDVAVAKPDLTSAlrEIRAQY 272
Cdd:pfam15921 303 -IIQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESG--NLDDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1703221 273 ESLAAKNLQSAEEWYKSKfanlnEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELEERHSAEVA 352
Cdd:pfam15921 380 QKLLADLHKREKELSLEK-----EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQ 454
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1703221 353 GYQDS---IGQLESDLRNTKsEMARHLREyqDLLNVKMALD 390
Cdd:pfam15921 455 GKNESlekVSSLTAQLESTK-EMLRKVVE--ELTAKKMTLE 492
|
|
| |
