|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-355 |
5.44e-14 |
|
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: 77.02 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 34 VQKGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQ------Q 103
Cdd:TIGR02168 655 VRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQisalrkD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 104 AEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQ---ELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCR 177
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 178 MQNELEDMERIRGDYEMEIASLRAEMEMkssepsgslglsdysgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADL 257
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLED----------------LEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 258 ESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC--------CELEELQH 329
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysLTLEEAEA 958
|
330 340
....*....|....*....|....*.
gi 2462615707 330 HRQVSEEEQRRLQRELKCAQNEVLRF 355
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-309 |
1.84e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 51 LSLTETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELRSLREEISlleh 130
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLE---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 131 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEp 210
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 211 sgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwLQSQTLSMTSAESQTSEMDfl 290
Cdd:COG1196 399 -----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEEEEALLELLAELLE-- 470
|
250
....*....|....*....
gi 2462615707 291 epdpEMQLLRQQLRDAEEQ 309
Cdd:COG1196 471 ----EAALLEAALAELLEE 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-406 |
5.33e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 58 LEELRAQVlqlvAELEETRELAGQH-----EDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELRSLREEISLLEHEK 132
Cdd:COG1196 195 LGELERQL----EPLERQAEKAERYrelkeELKELEAELLLLKLRELEAELEEL-EAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 133 E---SELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEdlcRMQNELEDMERIrgdyEMEIASLRAEMEmksse 209
Cdd:COG1196 270 EelrLELEELELELEEAQAEEYELLAELA----RLEQDIARLEE---RRRELEERLEEL----EEELAELEEELE----- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 210 psgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLsmtsaesqtsemdf 289
Cdd:COG1196 334 -----------ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL-------------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 290 LEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQtshsvTQNEELKS 369
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-----EEEEALLE 463
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462615707 370 RLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMK 406
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
57-387 |
1.03e-11 |
|
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: 69.71 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftKQIQQLQGELRSLREEISLLE---HEKE 133
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE---RQKEAIERQLASLEEELEKLTeeiSELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 134 SELKEIEQELHLAQAEIQSL-----RQAAEDSAtEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkss 208
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE---- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 209 epsgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLEsERTQRATERWLQSQT-LSMTSAESQTSEM 287
Cdd:TIGR02169 340 ------------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD-KEFAETRDELKDYREkLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 288 DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE-- 365
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEls 486
|
330 340
....*....|....*....|..
gi 2462615707 366 ELKSRLCTLQKKYDTSQDEQNE 387
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRG 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-652 |
2.11e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQqaevFTKQIQQLQGELRSLREEISLLEH 130
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 131 EKESELKEIEQ--------ELHLAQAEIQSLRQAAEDSATEHEsdiaSLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 202
Cdd:TIGR02168 415 RRERLQQEIEEllkkleeaELKELQAELEELEEELEELQEELE----RLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 203 MEMkssepsgslglsdysglqeeLQELRERYHFLNEEYRALQESNSSLTG---QLADLES--ERTQRATERWLQS--QTL 275
Cdd:TIGR02168 491 LDS--------------------LERLQENLEGFSEGVKALLKNQSGLSGilgVLSELISvdEGYEAAIEAALGGrlQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 276 SMTSAESQTSEMDFLEPD--------PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEE------------LQHHRQVSE 335
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsylLGGVLVVDD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 336 EEQ-RRLQRELKCAQNEVL---------------RFQTSHSVTQN----EELKSRLCTLQKKYDTSQDEQNELLKMQLQL 395
Cdd:TIGR02168 631 LDNaLELAKKLRPGYRIVTldgdlvrpggvitggSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 396 QTELRQLKVM------------KSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAELQHLRDT 463
Cdd:TIGR02168 711 EEELEQLRKEleelsrqisalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 464 VASFKESNEKDTETHAQLQEMkqlYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKCANK-------- 535
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAE---LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeieeleel 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 536 CDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKS--QELLTKLEDLCE 613
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGleVRIDNLQERLSE 947
|
650 660 670
....*....|....*....|....*....|....*....
gi 2462615707 614 lqlLYQGMQEEqkkLIQNQDCVLKEQLEIHEELRRFKES 652
Cdd:TIGR02168 948 ---EYSLTLEE---AEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-417 |
1.36e-10 |
|
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: 65.85 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 103 QAEVFTKQIQQLQGELRSLREEISllehEKESELKEIEQELHLAQAEIQSLRqaaeDSATEHESDIASLQEDLCRMQNEL 182
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELK----EAEEELEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 183 EDMERirgdyemEIASLRAEMEMKSSEpsgslglsdYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESErt 262
Cdd:TIGR02168 298 SRLEQ-------QKQILRERLANLERQ---------LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 263 qraterwlqsqtLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQ 342
Cdd:TIGR02168 360 ------------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615707 343 RELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 417
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
58-311 |
1.68e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 58 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELRSLREEISLLEhEKESE 135
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 136 LKEIEQELHLAQAEIQSLRQ---AAEDSATEHESDIASLQEDLCRMQNELEDMERI-RGDYEMEIASLRAEMEMKSSEPS 211
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLaRLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 212 GSLGLSD-YSGLQEELQELRE-----------RYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTs 279
Cdd:COG4913 767 LRENLEErIDALRARLNRAEEeleramrafnrEWPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNENSI- 845
|
250 260 270
....*....|....*....|....*....|..
gi 2462615707 280 aESQTsemDFLepdpemQLLRQQLRDAEEQMH 311
Cdd:COG4913 846 -EFVA---DLL------SKLRRAIREIKERID 867
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-204 |
3.35e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 48 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 127
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 128 LEH----------EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIA 197
Cdd:COG4913 364 LEAllaalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
....*..
gi 2462615707 198 SLRAEME 204
Cdd:COG4913 444 ALRDALA 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-733 |
4.14e-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: 61.23 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 58 LEELRAQV--LQLVAEL-EETRELAGQHEDDSLELQGL----LEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 129
Cdd:TIGR02168 195 LNELERQLksLERQAEKaERYKELKAELRELELALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRl 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 130 --HEKESELKEIEQELHLAQAEIQSL---RQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 204
Cdd:TIGR02168 275 evSELEEEIEELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 205 MKSSEpsgslgLSDYSGLQEEL----QELRERYHFLNEEYRALQESNSSLTGQLADLES--ERTQRATERWLQSQTlsmt 278
Cdd:TIGR02168 355 SLEAE------LEELEAELEELesrlEELEEQLETLRSKVAQLELQIASLNNEIERLEArlERLEDRRERLQQEIE---- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 279 SAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTS 358
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 359 HS-----VTQNEELKSRLCTLQKKYDTSQDEQNELLK-----MQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQ 428
Cdd:TIGR02168 505 SEgvkalLKNQSGLSGILGVLSELISVDEGYEAAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 429 H-QNVTCEKEKLLERQQQLQEELQCHEAELQHLRDT-------VASFKESNEKDTETHAQL------------------- 481
Cdd:TIGR02168 585 EiQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgg 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 482 ---QEMKQLYQASK-DELERQKhmyDQLEQDLLLCQLELKELKASHPIPEDKGkcankcDTLLSRLTELQEKYKASQKEM 557
Cdd:TIGR02168 665 sakTNSSILERRREiEELEEKI---EELEEKIAELEKALAELRKELEELEEEL------EQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 558 GQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQElltklEDLCELQLLYQGMQEEQKKLIQNqdcvLK 637
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-----AEIEELEAQIEQLKEELKALREA----LD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 638 EQLEIHEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQ 717
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
730
....*....|....*.
gi 2462615707 718 ADLQLCLEEMQLLQVQ 733
Cdd:TIGR02168 887 EALALLRSELEELSEE 902
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
113-440 |
4.27e-09 |
|
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: 60.85 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 113 QLQGELRSLREEISLLEHEKES---ELKEIEQELHlaqaEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 189
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSlqsELRRIENRLD----ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 190 GDYEMEIASLRAEMEMKSSEpsgslgLSDY----SGLQEELQEL-----RERYHFLNEEYRALQESNSSLTGQLADLESE 260
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEAR------IEELeedlHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 261 RTQRATERWLQSQtlSMTSAESQTSEMDFLEPD--PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQ 338
Cdd:TIGR02169 821 LNRLTLEKEYLEK--EIQELQEQRIDLKEQIKSieKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 339 RRLQRELK--CAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELL---KMQLQLQTELRQLKVMKS-TLVEN 412
Cdd:TIGR02169 899 RELERKIEelEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsleDVQAELQRVEEEIRALEPvNMLAI 978
|
330 340
....*....|....*....|....*...
gi 2462615707 413 QSEKELLCRLQKLHLQHQNVTCEKEKLL 440
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-264 |
5.29e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELRSLREEISlleh 130
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIE---- 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 131 EKESELKEIEQELHLAQAEIQSLRQAAEDSAT---EHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL------RA 201
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEelrELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseEY 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 202 EMEMKSSEPSGSLGLSDYSGLQ---------------------EELQELRERYHFLNEEYRALQESNSSLTGQLADLESE 260
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARrrlkrlenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
....
gi 2462615707 261 RTQR 264
Cdd:TIGR02168 1030 ARER 1033
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-328 |
7.14e-09 |
|
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: 59.01 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 98 LASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKES---ELKEIEQELHLAQAEIQSLrqaaEDSATEHESDIASLQED 174
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRAL----EQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 175 LCRMQNELEDMERirgdyemEIASLRAEMEMKSSEPSGSLGLSdysglQEELQELRERYHFLNEEYRALQESNSSLTGQL 254
Cdd:COG4942 92 IAELRAELEAQKE-------ELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462615707 255 ADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ 328
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-357 |
9.83e-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: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 55 ETELEELRAQVLQLVAELEETRelAGQHEDDslelqgllederlasaqqaevftKQIQQLQGELRSLREEISLLEHEKEs 134
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELR--LEVSELE-----------------------EEIEELQKELYALANEISRLEQQKQ- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 135 elkEIEQELHLAQAEIQSLrqaaEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSepsgsl 214
Cdd:TIGR02168 306 ---ILRERLANLERQLEEL----EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES------ 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 215 glsdysgLQEELQELRERyhfLNEEYRALQESNSSLTGQLADLES--ERTQRATERWLQSQtlsmTSAESQTSEMDFLEP 292
Cdd:TIGR02168 373 -------RLEELEEQLET---LRSKVAQLELQIASLNNEIERLEArlERLEDRRERLQQEI----EELLKKLEEAELKEL 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615707 293 DPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQT 357
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-497 |
4.62e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEhEKESEL 136
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-EALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 137 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGL 216
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 217 SDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEM 296
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 297 QLLRQQLRDAEEqmhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRlctLQK 376
Cdd:COG1196 594 RGAIGAAVDLVA---------SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA---GGS 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 377 KYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAE 456
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2462615707 457 LQHLRDTVASFKESNEKDTETHAQLQEMKQLyqasKDELER 497
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERL----EREIEA 778
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
55-260 |
5.50e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 55 ETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEISLLEHEKES 134
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLSELES------QLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 135 ELKEIEQELhlAQAEIQSLRQAAEDSatehESDIASLQEdlcRMQNELEDMERIRGdyemEIASLRAEMEMKSSEPSGSL 214
Cdd:COG3206 252 GPDALPELL--QSPVIQQLRAQLAEL----EAELAELSA---RYTPNHPDVIALRA----QIAALRAQLQQEAQRILASL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462615707 215 GlSDYSGLQEELQELRERYhflnEEYRALQESNSSLTGQLADLESE 260
Cdd:COG3206 319 E-AELEALQAREASLQAQL----AQLEARLAELPELEAELRRLERE 359
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-283 |
5.81e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 57 ELEELRAQVLQLVAELEETRELAGQhEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEisllEHEKESEL 136
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEE-ELAELEEELEELEEELEELEE------ELEEAEEELEEAEAE----LAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 137 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEpsgslgL 216
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE------E 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615707 217 SDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQ 283
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
60-438 |
5.85e-08 |
|
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: 57.39 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 60 ELRAQVLQLVAELEE-TRELAG-QHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISllehEKESEL 136
Cdd:TIGR02169 671 SEPAELQRLRERLEGlKRELSSlQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 137 KEIEQELHLAQAEIQSLrqaaedsatehESDIASLQEDLCRMQNELEDMERirgdyemeiaslraememkssepsgslgl 216
Cdd:TIGR02169 747 SSLEQEIENVKSELKEL-----------EARIEELEEDLHKLEEALNDLEA----------------------------- 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 217 sdysglqeelQELRERYHFLNEEYRALQESNSSLTGQLADLESErtqraterwLQSQTLSMTSAESqtsemdflepdpEM 296
Cdd:TIGR02169 787 ----------RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK---------LNRLTLEKEYLEK------------EI 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 297 QLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQtshsvTQNEELKSRLCTLQK 376
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-----AQLRELERKIEELEA 910
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462615707 377 KYDTSQDEQNELlkmQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEK 438
Cdd:TIGR02169 911 QIEKKRKRLSEL---KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
104-350 |
2.25e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 104 AEVFTKQ-IQQLQGELRSLREEIsllehekESELKEIEQELHLAQAEIQSLRQ-----AAEDSATEHESDIASLQEDLCR 177
Cdd:COG3206 158 AEAYLEQnLELRREEARKALEFL-------EEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 178 MQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQEsnssltgQLADL 257
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA-------QIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 258 ESERTQRATERWLQSQTlSMTSAESQTSEmdflepdpemqlLRQQLRDAEEQMHGMKNKcqelcceleelqhhrqvsEEE 337
Cdd:COG3206 304 RAQLQQEAQRILASLEA-ELEALQAREAS------------LQAQLAQLEARLAELPEL------------------EAE 352
|
250
....*....|...
gi 2462615707 338 QRRLQRELKCAQN 350
Cdd:COG3206 353 LRRLEREVEVARE 365
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
55-196 |
5.10e-07 |
|
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: 52.23 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 55 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELRSLREEISLLEheke 133
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462615707 134 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 196
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-263 |
5.79e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 136
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 137 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERI---------RGDYEMEIASLRAEMEmks 207
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAleelpeppdLEELERELERLEREIE--- 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 208 sepsgSLG----LSDysglqEELQELRERYHFLNEeyralqesnssltgQLADLESERTQ 263
Cdd:COG1196 778 -----ALGpvnlLAI-----EEYEELEERYDFLSE--------------QREDLEEARET 813
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
36-509 |
6.07e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 36 KGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETRelagqheddslelqglledERLASAQQaevftkQIQQLQ 115
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE-------------------EELEELEA------ELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 116 GELRSLREEISLLEHEKesELKEIEQELHLAQAEIQSLRQAAEDSAtEHESDIASLQEDLCRMQNELEDmerirgdyEME 195
Cdd:COG4717 116 EELEKLEKLLQLLPLYQ--ELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEE--------LLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 196 IASLRAEMEMKSSepsgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTL 275
Cdd:COG4717 185 QLSLATEEELQDL-------AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 276 SMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMhgMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKcaqneVLRF 355
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL--LAREKASLGKEAEELQALPALEELEEEELEELLA-----ALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 356 QTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLkmQLQLQTELRQLkvMKSTLVEN-----------QSEKELLCRLQK 424
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAAL--LAEAGVEDeeelraaleqaEEYQELKEELEE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 425 LHLQhqnvtCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQL-QEMKQLyqASKDELERQKHMYD 503
Cdd:COG4717 407 LEEQ-----LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeAELEQL--EEDGELAELLQELE 479
|
....*.
gi 2462615707 504 QLEQDL 509
Cdd:COG4717 480 ELKAEL 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
135-345 |
8.20e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 135 ELKEIEQELHLAQAEIQSLRQAAEDsATEHESDIASLQE-DLCRMQNELEDMERIRGDYEMEIASLRAEMEmkssepsgs 213
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIREL-AERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELA--------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 214 lglsdysGLQEELQELRERYHFLNEEYRALQE---SNS-----SLTGQLADLESERTQRATERWLQSQTLSMTSAESQTS 285
Cdd:COG4913 306 -------RLEAELERLEARLDALREELDELEAqirGNGgdrleQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462615707 286 EMDFLE-----------PDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQREL 345
Cdd:COG4913 379 AEEFAAlraeaaalleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
51-417 |
8.23e-07 |
|
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: 53.64 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 129
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQa 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 130 --HEKESELKEIEQELHLAQAEI---QSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 204
Cdd:pfam01576 230 qiAELRAQLAKKEEELQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 205 mkssepsgslGLSDYSGLQEELQELRERYhfLNEEYRALQESNSSLTGQLADLESERTQ---RATERWLQSQTLSMTSAE 281
Cdd:pfam01576 310 ----------DTLDTTAAQQELRSKREQE--VTELKKALEEETRSHEAQLQEMRQKHTQaleELTEQLEQAKRNKANLEK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 282 S-QTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVlrfqtSHS 360
Cdd:pfam01576 378 AkQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL-----NEA 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615707 361 VTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 417
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEE 509
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
57-365 |
1.47e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.99 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASaqqaevftkqiQQLQGELRSLREEISLLEhekeSEL 136
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLRRELAGLTRRLSAAE----GEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 137 KEIEQELHLAQAEIQSLRQAAEDSATEhESDIASLQEDLcrmQNELEDMERIRGDYEMEIASLRAEMEMKSSepsgslgl 216
Cdd:pfam19220 86 EELVARLAKLEAALREAEAAKEELRIE-LRDKTAQAEAL---ERQLAAETEQNRALEEENKALREEAQAAEK-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 217 sDYSGLQEELQELRERYHFLNEEYRALQ----ESN---SSLTGQLADLESER-TQRATERWLQSQtLSMTSAESQTSEMD 288
Cdd:pfam19220 154 -ALQRAEGELATARERLALLEQENRRLQalseEQAaelAELTRRLAELETQLdATRARLRALEGQ-LAAEQAERERAEAQ 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615707 289 FLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELcceLEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE 365
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQL---LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEAD 305
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
51-378 |
1.53e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISlleh 130
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 131 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL---------RA 201
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllaRE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 202 EMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFL----NEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSM 277
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPpdlsPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 278 TSAESQTSEM--DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCC---------ELEELQHHRQVSEEEQRRLQRELK 346
Cdd:COG4717 377 AEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELA 456
|
330 340 350
....*....|....*....|....*....|....*.
gi 2462615707 347 CAQNEVLRFQTSHSVTQN----EELKSRLCTLQKKY 378
Cdd:COG4717 457 ELEAELEQLEEDGELAELlqelEELKAELRELAEEW 492
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
49-205 |
2.38e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 49 RGLSLtETELEELRAQVLqlvAELEETRELAGQHEDDSLELqgllEDERlasaqqaevftkqIQQLQGELRSLREEISLL 128
Cdd:COG2433 374 RGLSI-EEALEELIEKEL---PEEEPEAEREKEHEERELTE----EEEE-------------IRRLEEQVERLEAEVEEL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 129 E---HEKESELKEIEQELHLAQAEiqslrqaaEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEM 205
Cdd:COG2433 433 EaelEEKDERIERLERELSEARSE--------ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKL 504
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
60-415 |
2.53e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.98 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 60 ELRAQvlqLVAELEETRELAGQHEDDSLElQGLLEderlASAQQAEVfTKQIQQLQGELRSLREEISLL---EHEKESEL 136
Cdd:PRK10929 83 ELRQQ---LNNERDEPRSVPPNMSTDALE-QEILQ----VSSQLLEK-SRQAQQEQDRAREISDSLSQLpqqQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 137 KEIEQELHLAQAEIQSLRQAAedsatehesdIASLQEDLCRMQ---NELEdMERIRGDYEMEIASLRAEMEMKSSEPsgs 213
Cdd:PRK10929 154 NEIERRLQTLGTPNTPLAQAQ----------LTALQAESAALKalvDELE-LAQLSANNRQELARLRSELAKKRSQQ--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 214 lglsdysgLQEELQELRERYHFL--NEEYRALqESNSSLTGQLADL-ESERTQRATERWLqSQTLSmtsaeSQTSEMDFL 290
Cdd:PRK10929 220 --------LDAYLQALRNQLNSQrqREAERAL-ESTELLAEQSGDLpKSIVAQFKINREL-SQALN-----QQAQRMDLI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 291 -----EPDPEMQLLRQQLRDAEEQMH--GMKN-----------------KCQELCCELEELQHHRQVSEEEQRRLQRELK 346
Cdd:PRK10929 285 asqqrQAASQTLQVRQALNTLREQSQwlGVSNalgealraqvarlpempKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQ 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462615707 347 CAQNEvlrfqtSHSVTQNEelksrlctlQKKYDTSQDEQNELLKMQLQ----LQTELRQLKVMKSTLVENQSE 415
Cdd:PRK10929 365 IRQAD------GQPLTAEQ---------NRILDAQLRTQRELLNSLLSggdtLILELTKLKVANSQLEDALKE 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-345 |
3.13e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 108 TKQIQQLQGELRSLREEISLLehekESELKEIEQELHLAQAEIQSLRQAAEDSatEHESDIASLQEDLCRMQNELEDMER 187
Cdd:COG4913 609 RAKLAALEAELAELEEELAEA----EERLEALEAELDALQERREALQRLAEYS--WDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 188 irgdyemeiaslraememkssepsgslGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQrate 267
Cdd:COG4913 683 ---------------------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE---- 731
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462615707 268 rwLQSQTLSMTSAESQTSEMDFLEpdpemQLLRQQLRDAEEQMHgmknkcqelccelEELQHHRQVSEEEQRRLQREL 345
Cdd:COG4913 732 --LQDRLEAAEDLARLELRALLEE-----RFAAALGDAVERELR-------------ENLEERIDALRARLNRAEEEL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
49-213 |
6.89e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 49 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 118
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 119 RSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIAS 198
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170
....*....|....*
gi 2462615707 199 LRAEMEMKSSEPSGS 213
Cdd:COG4942 232 LEAEAAAAAERTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-971 |
7.02e-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: 50.44 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 296 MQLLRQQLRDAEeqmhgmknKCQELCCELEELQHHRQVSEEEQrrLQRELKCAQNEVLRFQTSHsvtqnEELKSRLCTLQ 375
Cdd:TIGR02168 202 LKSLERQAEKAE--------RYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEEL-----EELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 376 KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLveNQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEA 455
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 456 ELQHLRDTVASFKESNEkdtETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKAShpIPEDKGKCANK 535
Cdd:TIGR02168 345 KLEELKEELESLEAELE---ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR--LERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 536 CDTLLSRLTELQE-KYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKsgLLLKSQELLTKLEDLCEL 614
Cdd:TIGR02168 420 QQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA--AERELAQLQARLDSLERL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 615 QLLYQGMQEEQKKLIQNQDC------VLKEQLEIHEELRRFKE----SHFQEVL-ENPDDSKLA----KSSKCNRNKQSK 679
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGlsgilgVLSELISVDEGYEAAIEaalgGRLQAVVvENLNAAKKAiaflKQNELGRVTFLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 680 LLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEemQLLQVQSPSIKMSLESY--------------- 744
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLG--GVLVVDDLDNALELAKKlrpgyrivtldgdlv 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 745 ---GKSYGSMVPSN----------ENCRKTYDTTVDDNES-------YYKSYTSTQTSSKSFLKSYDSSTSASEAYGKSY 804
Cdd:TIGR02168 656 rpgGVITGGSAKTNssilerrreiEELEEKIEELEEKIAElekalaeLRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 805 CTTSNSSITYKKSYGSTSSSDT-------CQKSFVSSCTDEEPAEPEDMERFEEMVVKVLIKLQAVQAMYQISQEEHSQL 877
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTeleaeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 878 QEQMEKLLAKQKDLKEELDACEREFKECMECLEKPMAPQNDKN-EIKELQTKLRELQLQYQASMDEQGRLLVVQEQLEGQ 956
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
730
....*....|....*
gi 2462615707 957 LQCCQEELRQLREKR 971
Cdd:TIGR02168 896 LEELSEELRELESKR 910
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
51-187 |
7.23e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSlELQGLLEDERLASAQQAEV---FTK---QIQQLQGELRSLREE 124
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELsarYTPnhpDVIALRAQIAALRAQ 306
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462615707 125 IsllEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDlcrmQNELEDMER 187
Cdd:COG3206 307 L---QQEAQRILASLEAELEALQAREASLQAQLA----QLEARLAELPEL----EAELRRLER 358
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
90-403 |
1.10e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 90 QGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEiqSLRQAAEDSA----TEHE 165
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 166 SDIASLQEDLCRMQNE--LEDMERIRG-DYEMEIASLRA------EMEMKSSEPSGSL-GLSDYSGLQEELQELRERYHF 235
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIRQeEIAMEISRMRElerlqmERQQKNERVRQELeAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 236 LNEEYRALQESNSSLTGQLADLESERT-----QRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQL--------LRQQ 302
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREmervrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkiLEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 303 LRDAEEQMHGMKNKCQELCCELEELQhhRQVSEEEQRRLQRELKCAQNEV-LRFQTSHSVTQNEELKSRLCTLQKKYD-T 380
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMeERRRIQEQMRKATEERSRLEAMEREREmM 578
|
330 340
....*....|....*....|...
gi 2462615707 381 SQDEQNELLKMQLQLQTELRQLK 403
Cdd:pfam17380 579 RQIVESEKARAEYEATTPITTIK 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
54-268 |
1.23e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 54 TETELEELRAQVLQLVAELEETRELAGQHEDdslelqglLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKE 133
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEE--------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 134 --SELKEIEQELHLAQAEIQSLRQAAEDSATEH-ESDIASLQEDLCRMQNELED-MERIRGDYEMEIASLRAEMEmksse 209
Cdd:COG4913 738 aaEDLARLELRALLEERFAAALGDAVERELRENlEERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLE----- 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462615707 210 psgslGLSDYsglQEELQELRER--YHFLNEEYRALQE-SNSSLTGQLADLESERtQRATER 268
Cdd:COG4913 813 -----SLPEY---LALLDRLEEDglPEYEERFKELLNEnSIEFVADLLSKLRRAI-REIKER 865
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-419 |
1.30e-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: 49.63 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 55 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQaevfTKQIQQLQGELRSLREEISLLEHEKE- 133
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN----NKKIKELEKQLNQLKSEISDLNNQKEq 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 134 -------SELKEIEQELHLAQAEIQSLRQAA----------EDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 196
Cdd:TIGR04523 307 dwnkelkSELKNQEKKLEEIQNQISQNNKIIsqlneqisqlKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 197 ASLRA-----EMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 271
Cdd:TIGR04523 387 KNLESqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 272 SQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 351
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462615707 352 VLrfqTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELL 419
Cdd:TIGR04523 547 LN---KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-490 |
1.31e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 123 EEISLLEHEKESELKEIEQelhlaQAEIQSLRQAAEDSATEHESDIASLQEDlcRMQNELEDMERIRGDYEMEIASLRAE 202
Cdd:COG1196 189 ERLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 203 MEmkssepsgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERtQRATERWLQSQTlsmtsaes 282
Cdd:COG1196 262 LA----------------ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRELEE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 283 qtsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVT 362
Cdd:COG1196 317 ------------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 363 QNEELksrlcTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLcrLQKLHLQHQNVTCEKEKLLER 442
Cdd:COG1196 385 AEELL-----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462615707 443 QQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQA 490
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
56-201 |
2.05e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 56 TELEELRAQVLQLVAELEETRELAGQHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEIS-------- 126
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEaELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrle 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 127 LLEHE---KESELKEIEQE----------LHLA----QAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 189
Cdd:COG4913 342 QLEREierLERELEERERRrarleallaaLGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170
....*....|..
gi 2462615707 190 GDYEMEIASLRA 201
Cdd:COG4913 422 RELEAEIASLER 433
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
57-543 |
4.03e-05 |
|
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: 47.91 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLElQGLLEDERLASAQ-QAEVFTKQIQQLQGELRSLREEISLLEHEKESE 135
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIE-TAAADQEQLPSWQsELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 136 LKEIEQELHLAQAEIqslRQAAEDSATEHESDIASLQEDLcRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLg 215
Cdd:pfam12128 388 NNRDIAGIKDKLAKI---REARDRQLAVAEDDLQALESEL-REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPEL- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 216 LSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGqLADLESERTQRATERWLQSQtlsmtSAESQTSEMDFLEPDPE 295
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELRQARK-RRDQASEALRQASRRLEERQ-----SALDELELQLFPQAGTL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 296 MQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQrrlqreLKCAQNEVLRFQTSHSVTQNEELKSRLCTLQ 375
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELN------LYGVKLDLKRIDVPEWAASEEELRERLDKAE 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 376 KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELlcRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCH-E 454
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL--DLRRLFDEKQSEKDKKNKALAERKDSANERLNSlE 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 455 AELQHLRDTVASFKESNEKDTETH--AQLQEMKQLYQASKDELERQKH----MYDQLEQDLLLCQLELK-ELKASHPIPE 527
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQKREArtEKQAYWQVVEGALDAQLALLKAaiaaRRSGAKAELKALETWYKrDLASLGVDPD 768
|
490
....*....|....*.
gi 2462615707 528 DKGKCANKCDTLLSRL 543
Cdd:pfam12128 769 VIAKLKREIRTLERKI 784
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
57-217 |
5.48e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 46.67 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 136
Cdd:pfam09787 62 EIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 137 KEIEQELHLAQAEIQSlRQAAEDSATEHESDIASLQEDLCRMQNELEDM--ERIRGDYEMEiaslRAEMEMKSSEPSGSL 214
Cdd:pfam09787 142 KDREAEIEKLRNQLTS-KSQSSSSQSELENRLHQLTETLIQKQTMLEALstEKNSLVLQLE----RMEQQIKELQGEGSN 216
|
...
gi 2462615707 215 GLS 217
Cdd:pfam09787 217 GTS 219
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
51-202 |
5.70e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 51 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELRSLR 122
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 123 EEISLLEhEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 202
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
88-733 |
5.83e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 88 ELQGLLEDERLASAqqAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESD 167
Cdd:pfam02463 161 EAAGSRLKRKKKEA--LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 168 IASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYSGLQEELQE-----LRERYHFLNEEYRA 242
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKsellkLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 243 LQESNSSLTGQLADLESERTQRATERWLQS-QTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC 321
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 322 CELEELQHHRQVSEEEQRRL----------------QRELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQ 385
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEdllkeekkeeleileeEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 386 NELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCE-KEKLLERQQQLQEELQCHEAELQHLRDTV 464
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 465 ASFKESNEKDTETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHpipEDKGKCANKCDTLLSRLT 544
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE---DDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 545 ELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELhrltlplpksgLLLKSQELLTKLEDLCELQLLYQGMQEE 624
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL-----------EIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 625 QKKLIQNQDCVLKEQLEIHEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQSKLLMEQMQALQVMYDAGQAKQELLQQ 704
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
650 660
....*....|....*....|....*....
gi 2462615707 705 EQGRLLEERKRLQADLQLCLEEMQLLQVQ 733
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEE 813
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
51-246 |
8.22e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGL-------------LEDERLASAQQAEVFTKQIQQLQGE 117
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeiedlretiaeTEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 118 LRSLREE----------ISLLEHEKESELKEIEQELHLAQAEIQSLRQAAE---DSATEHESDIASLQEDLCRMQNELED 184
Cdd:PRK02224 295 RDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462615707 185 MERIRGDYEMEIASLRAEMEMKSSE----PSGSLGLSDYSG-LQEELQELRERYHFLNEEYRALQES 246
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERfgdaPVDLGNAEDFLEeLREERDELREREAELEATLRTARER 441
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
55-566 |
1.04e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 55 ETELEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 130
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 131 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCRMQNEL---------------------EDME 186
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 187 RIRGDYEMEIASLRAEMEMKSSEPSGSL--GLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLE-SERTQ 263
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMerQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEsSERTV 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 264 RATERWLQSQTLSMtsaESQTSEMDFLEPDPEMQLLR-QQLRDAEEQMHGMKNKCQELCCELEEL--------------- 327
Cdd:pfam15921 499 SDLTASLQEKERAI---EATNAEITKLRSRVDLKLQElQHLKNEGDHLRNVQTECEALKLQMAEKdkvieilrqqienmt 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 328 ----QHHRQVS--EEEQRRLQRELKCAQNEVLRFQT--SHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTE- 398
Cdd:pfam15921 576 qlvgQHGRTAGamQVEKAQLEKEINDRRLELQEFKIlkDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQEr 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 399 ---LRQLKVMKSTLVENQSEKELLCRlqklhlqhqNVTCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDT 475
Cdd:pfam15921 656 dqlLNEVKTSRNELNSLSEDYEVLKR---------NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAM 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 476 ETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKAS-----HPIPEDKGKCANKCDTLLSRLTELQEKY 550
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKlsqelSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
570
....*....|....*...
gi 2462615707 551 KASQKEM--GQLQMEQCE 566
Cdd:pfam15921 807 ANMEVALdkASLQFAECQ 824
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
32-742 |
1.29e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 32 EQVQKggsvgslsvNKHRGLSLTETELEELRAQVLQLVaeleetrelaGQHEDDSLELQGLLEDERLASAQQAEVfTKQI 111
Cdd:pfam02463 278 EKEKK---------LQEEELKLLAKEEEELKSELLKLE----------RRKVDDEEKLKESEKEKKKAEKELKKE-KEEI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 112 QQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEhESDIASLQEDLCRMQNELEDMERIRGD 191
Cdd:pfam02463 338 EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA-AKLKEEELELKSEEEKEAQLLLELARQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 192 YEMEiasLRAEMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 271
Cdd:pfam02463 417 LEDL---LKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 272 SQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEeqmhgmKNKCQELCCELEELQHHRQVSEEEQrRLQRELKCAQNE 351
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG------RLGDLGVAVENYKVAISTAVIVEVS-ATADEVEERQKL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 352 VLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVmkstLVENQSEKELLCRLQKLHLQHQN 431
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDD----KRAKVVEGILKDTELTKLKESAK 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 432 VTCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEK---DTETHAQLQEMKQLYQASKDELERQKHMYDQLEQD 508
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKaesELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 509 LLLCQLELKELKASHPIPEDKGKCANKCDTLLSRL-----------TELQEKYKASQKEMGQLQMEQCELLEDQRRMqEE 577
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLkkeekeeekseLSLKEKELAEEREKTEKLKVEEEKEEKLKAQ-EE 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 578 QGQLQEELHRLTLPLPKSGLLLKSQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEELRRFKESHFQEV 657
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 658 LENPDD--SKLAKSSKCNRNKQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEEMQLLQVQSP 735
Cdd:pfam02463 882 QKLKDEleSKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
....*..
gi 2462615707 736 SIKMSLE 742
Cdd:pfam02463 962 NKRLLLA 968
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
51-648 |
1.39e-04 |
|
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: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 51 LSLTETELEELRAQVLQLvaelEETRELAGQHEDDSLELQGLledERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 130
Cdd:COG4913 237 LERAHEALEDAREQIELL----EPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 131 EKEselkEIEQELHLAQAEIQSLRQAAEDSATEhesDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkssep 210
Cdd:COG4913 310 ELE----RLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAALGLPLP------ 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 211 sgsLGLSDYSGLQEELQELRERyhfLNEEYRALQESNSSLTGQLADLESERTQRATE-RWLQSQTLSMtsaesqtsemdf 289
Cdd:COG4913 377 ---ASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEiASLERRKSNI------------ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 290 lepDPEMQLLRQQLRDAeeqmhgMKNKCQELC--CELEEL--------------------------QHHRQVSEE-EQRR 340
Cdd:COG4913 439 ---PARLLALRDALAEA------LGLDEAELPfvGELIEVrpeeerwrgaiervlggfaltllvppEHYAAALRWvNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 341 LQRELkcaqnEVLRFQTSHSVTQNEELKSRlcTLQKKYDTSQDEQNELLKMQLQlqtelRQLKVMKstlVENQSE----- 415
Cdd:COG4913 510 LRGRL-----VYERVRTGLPDPERPRLDPD--SLAGKLDFKPHPFRAWLEAELG-----RRFDYVC---VDSPEElrrhp 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 416 ---------KELLCRLQK---LHLQHQNVTCE--KEKLLERqqqlqeelqchEAELQHLRDTVASFKESNEKDTETHAQL 481
Cdd:COG4913 575 raitragqvKGNGTRHEKddrRRIRSRYVLGFdnRAKLAAL-----------EAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 482 QEMKQLYQASKDELERQKHMyDQLEQDLLLCQLELKELKASHPipedkgkcankcdtllsRLTELQEKYKASQKEMGQLQ 561
Cdd:COG4913 644 QERREALQRLAEYSWDEIDV-ASAEREIAELEAELERLDASSD-----------------DLAALEEQLEELEAELEELE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 562 MEQCELLEDQRRMQEEQGQLQEELHRLTLPLpKSGLLLKSQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLE 641
Cdd:COG4913 706 EELDELKGEIGRLEKELEQAEEELDELQDRL-EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNR 784
|
....*..
gi 2462615707 642 IHEELRR 648
Cdd:COG4913 785 AEEELER 791
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
55-573 |
1.58e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 55 ETELEELRAQVLQLVAELEETRELAGQHED--DSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEK 132
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 133 ESE------LKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQE----------DLCRMQNELEDMERI---RGDYE 193
Cdd:TIGR00618 417 SAFrdlqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslkereqQLQTKEQIHLQETRKkavVLARL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 194 MEIASLRAEMEMKSSEPSGSLGLSDYSG-LQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESE--RTQRATERWL 270
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqEIQQSFSILT 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 271 QSQTLSMTSAESQTSEMDFLEPDPEMQllrqqlrDAEEQMHGMKNKCQELccELEELQHHRQVSEEEQRRLQRElkcAQN 350
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNITVRLQDLTEKL-------SEAEDMLACEQHALLR--KLQPEQDLQDVRLHLQQCSQEL---ALK 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 351 EVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQlqlqTELRQLKVMKSTLVENQSE-KELLCRLQKLHLQH 429
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ----SEKEQLTYWKEMLAQCQTLlRELETHIEEYDREF 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 430 QNVTCEKEKLLERQQQLQEELQCHEAELQHLRDTV--ASFKESNEKDTETHAQLQEMKQLYQASKDELERQKhmydQLEQ 507
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR----LREE 796
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462615707 508 DlllcQLELKELKASHP--IPEDKGKCANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRR 573
Cdd:TIGR00618 797 D----THLLKTLEAEIGqeIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-556 |
2.11e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 54 TETELEELRAQVLQLVAELEETRELAGQHEddslELQGLLEDERlasaqqaevftKQIQQLQGELRSLREEISLLEhEKE 133
Cdd:PRK03918 205 VLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELE-----------KELESLEGSKRKLEEKIRELE-ERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 134 SELKEIEQELHLAQAEIQSLRQAAEDSATehesdiasLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGS 213
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIK--------LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 214 LGLSD-YSGLQEELQELRERyHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlqsqtLSMTSAESQTSEMDFLEP 292
Cdd:PRK03918 341 EELKKkLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE------LEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 293 DPEMQLLRQQLRDAEEQMHGMKNKC----------------QELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVL--- 353
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKAKGKCpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkes 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 354 RFQTSHSVT-QNEELKSRLCTLQ--------KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSE-KELLCRLQ 423
Cdd:PRK03918 494 ELIKLKELAeQLKELEEKLKKYNleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKlDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 424 KLH--LQHQNVTCEKE------------KLLERQQQLQEELQCHEAELQHLRDTV-ASFKESNEKDT---ETHAQLQEMK 485
Cdd:PRK03918 574 ELLkeLEELGFESVEEleerlkelepfyNEYLELKDAEKELEREEKELKKLEEELdKAFEELAETEKrleELRKELEELE 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 486 QLYqaSKDELERQKHMYDQLEQDL--LLCQLE------------LKELKASHPIPEDKGKCANKCDTLLSRLTELQEK-- 549
Cdd:PRK03918 654 KKY--SEEEYEELREEYLELSRELagLRAELEelekrreeikktLEKLKEELEEREKAKKELEKLEKALERVEELREKvk 731
|
....*...
gi 2462615707 550 -YKASQKE 556
Cdd:PRK03918 732 kYKALLKE 739
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
54-569 |
2.63e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 54 TETELEELRAQVLQLvaeleETRELAGQHEDDSLELQGLLEDERLASAQQaevFTKQIQQLQGELRSLREEISLLEHEKE 133
Cdd:PRK04863 584 LRQQLEQLQARIQRL-----AARAPAWLAAQDALARLREQSGEEFEDSQD---VTEYMQQLLERERELTVERDELAARKQ 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 134 SELKEIEQELHLAQAEIQSLRQAAED----SATEHESDIaSLQE------------------DLCRMQNELEDMERIRGD 191
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAERfggvLLSEIYDDV-SLEDapyfsalygparhaivvpDLSDAAEQLAGLEDCPED 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 192 Y---EMEIASLR-AEMEMKSSEPSGSLGLSD----YSG------------------LQEELQELRERYHFLNEEYRALQE 245
Cdd:PRK04863 735 LyliEGDPDSFDdSVFSVEELEKAVVVKIADrqwrYSRfpevplfgraarekrieqLRAEREELAERYATLSFDVQKLQR 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 246 SNSSLTGQLA-------DLESERTQRATERWLQSQTLSMTSAESQTsemdflepdpemQLLRQQLRDAEEQMHGMkNKCQ 318
Cdd:PRK04863 815 LHQAFSRFIGshlavafEADPEAELRQLNRRRVELERALADHESQE------------QQQRSQLEQAKEGLSAL-NRLL 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 319 ---------ELCCELEELQHHRQVSEEEQRRLQRElkcaQNEVLRFQTSHSVTQNEElkSRLCTLQKKYDTSQDEQnELL 389
Cdd:PRK04863 882 prlnlladeTLADRVEEIREQLDEAEEAKRFVQQH----GNALAQLEPIVSVLQSDP--EQFEQLKQDYQQAQQTQ-RDA 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 390 KMQLQLQTELRQLKVMKS------TLVENQSEKELLcrLQKLHLQHQNVTCEKEKLLErqqqlqeelqcHEAELQHLRDT 463
Cdd:PRK04863 955 KQQAFALTEVVQRRAHFSyedaaeMLAKNSDLNEKL--RQRLEQAEQERTRAREQLRQ-----------AQAQLAQYNQV 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 464 VASFKESNEKDTETHAQL-QEMKQL-YQASKDELERQKHMYDQLEQDLLLCQLELKELKAshpipeDKGKCANKCDTLLS 541
Cdd:PRK04863 1022 LASLKSSYDAKRQMLQELkQELQDLgVPADSGAEERARARRDELHARLSANRSRRNQLEK------QLTFCEAEMDNLTK 1095
|
570 580
....*....|....*....|....*...
gi 2462615707 542 RLTELQEKYKASQKEMGQLQMEQCELLE 569
Cdd:PRK04863 1096 KLRKLERDYHEMREQVVNAKAGWCAVLR 1123
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-742 |
3.29e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 54 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLED-----ERLASAQQAEVfTKQIQQLQGELRSLREEISLL 128
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkiKDLGEEEQLRV-KEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 129 EHEKE---SELKEIEQELHLAQAEIQSLRQAAEDSATEHES---DIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 202
Cdd:TIGR02169 314 ERELEdaeERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 203 MEMKSSEPSGSLGLSDYsgLQEELQELRERYHFLNEEYRALQEsnssltgQLADLESERTQRATERWLQSQTLSMTSAEs 282
Cdd:TIGR02169 394 LEKLKREINELKRELDR--LQEELQRLSEELADLNAAIAGIEA-------KINELEEEKEDKALEIKKQEWKLEQLAAD- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 283 qtsemdflepdpeMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQR--RLQRELKCAQNEVL------- 353
Cdd:TIGR02169 464 -------------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggRAVEEVLKASIQGVhgtvaql 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 354 -----RFQTS----------HSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQlQLQTELRQLK--------------- 403
Cdd:TIGR02169 531 gsvgeRYATAievaagnrlnNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMR-DERRDLSILSedgvigfavdlvefd 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 404 ---------VMKSTLVEN--------------------------------QSEKELLCRLQKLHLQHQNVTCEKEKLLER 442
Cdd:TIGR02169 610 pkyepafkyVFGDTLVVEdieaarrlmgkyrmvtlegelfeksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRE 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 443 QQQLQEELQCHEAELQHLRDTVasfKESNEKDTETHAQLQEMKQLYQASKDELErqkhmydQLEQDLLLCQLELKELKAs 522
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQEL---SDASRKIGEIEKEIEQLEQEEEKLKERLE-------ELEEDLSSLEQEIENVKS- 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 523 hpipedkgkcanKCDTLLSRLTELQEKYKASQKEMGQLqmEQCELLEDQRRMQEEQGQLQEELHRLTLPLpksglllksQ 602
Cdd:TIGR02169 759 ------------ELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARL---------R 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 603 ELLTKLEDL-CELQLLYQGMQEEQKKLIQNQDCVLKEQLEIhEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQSKLL 681
Cdd:TIGR02169 816 EIEQKLNRLtLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462615707 682 MEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQlCLEEMQLLQVQSPSIKMSLE 742
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-EIEDPKGEDEEIPEEELSLE 954
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
141-267 |
3.37e-04 |
|
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: 43.37 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 141 QELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYS 220
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462615707 221 GLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATE 267
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
55-159 |
4.30e-04 |
|
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: 43.37 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 55 ETELEELRAQVLQLVAELEETREL------------------AGQHEDDSLEL-QGLLEDERLASAQQAEVFTKQIQQLQ 115
Cdd:COG1579 51 KTELEDLEKEIKRLELEIEEVEARikkyeeqlgnvrnnkeyeALQKEIESLKRrISDLEDEILELMERIEELEEELAELE 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462615707 116 GELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAED 159
Cdd:COG1579 131 AELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
57-351 |
5.11e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 57 ELEELRAQVLQLVAELEETRELAGQHeDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLrEEISLLEHEKESEL 136
Cdd:pfam05557 22 ELEHKRARIELEKKASALKRQLDRES-DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL-EALNKKLNEKESQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 137 KEIEQELHLAQAEIQSLRQAAEDSA---TEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLR-AEMEMKSSEPSG 212
Cdd:pfam05557 100 ADAREVISCLKNELSELRRQIQRAElelQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAeAEQRIKELEFEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 213 SLGLSDYSGLQE---------ELQELRERYHFLNEEYRALQESNSSLTGQLADLES-------------------ERTQR 264
Cdd:pfam05557 180 QSQEQDSEIVKNskselaripELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekyreeaatlelekEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 265 ATERWL---QSQTLSMTSAESQTSEMDFLEPD-----PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEE 336
Cdd:pfam05557 260 ELQSWVklaQDTGLNLRSPEDLSRRIEQLQQReivlkEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA 339
|
330
....*....|....*
gi 2462615707 337 EQRRLQRELKCAQNE 351
Cdd:pfam05557 340 LVRRLQRRVLLLTKE 354
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
194-410 |
5.18e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 194 MEIASLRAEMEM--KSSEPSGSLGLSDYSGLQEELQELRERyhflNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 271
Cdd:COG4717 46 MLLERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 272 SQTLsmtsaesqtsemDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 351
Cdd:COG4717 122 EKLL------------QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462615707 352 VLRfQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNEL------LKMQLQLQTELRQLKVMKSTLV 410
Cdd:COG4717 190 TEE-ELQDLAEELEELQQRLAELEEELEEAQEELEELeeeleqLENELEAAALEERLKEARLLLL 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
859-970 |
9.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 859 KLQAVQAMYQISQEEHSQLQEQMEKLLAKQKDLKEELDACEREFKECMECLEKPMAPQ-------------NDKNEIKEL 925
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiaeleaelerldASSDDLAAL 690
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462615707 926 QTKLRELQLQYQASMDEQGRLLVVQEQLEGQLQCCQEELRQLREK 970
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
459-742 |
1.04e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 459 HLRDTVASFKESNEKDTEthaQLQEMKQLYQASKDELERQKHMYDQLEQD-LLLCQLELKELKASHPIPEDKGKCANKCD 537
Cdd:PLN02939 97 HNRASMQRDEAIAAIDNE---QQTNSKDGEQLSDFQLEDLVGMIQNAEKNiLLLNQARLQALEDLEKILTEKEALQGKIN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 538 TLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPksglLLKSQELLTKLEdlcelqll 617
Cdd:PLN02939 174 ILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELD----VLKEENMLLKDD-------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 618 yqgMQEEQKKLIQNQDCvlKEQLEIHEELRRFKESHFQEVlenpdDSKLAkSSKCNRNKQSKL----LMEQMQALQVMYD 693
Cdd:PLN02939 242 ---IQFLKAELIEVAET--EERVFKLEKERSLLDASLREL-----ESKFI-VAQEDVSKLSPLqydcWWEKVENLQDLLD 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462615707 694 --AGQAKQELLQQEQGRLLEER-KRLQADL------QLCLEEMQLLQVQSPSIKMSLE 742
Cdd:PLN02939 311 raTNQVEKAALVLDQNQDLRDKvDKLEASLkeanvsKFSSYKVELLQQKLKLLEERLQ 368
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
21-717 |
1.15e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 21 EEEEEEV----EEEEEQVQKGGSVGSLSVNKHRGLSLTETELEEL------------------------RAQVLQLVAEL 72
Cdd:pfam02463 282 KLQEEELkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAekelkkekeeieelekelkeleikREAEEEEEEEL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 73 EETRELAGQHEDDSLELQGLLEDERLASAQQAE------VFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLA 146
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEeelelkSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 147 QAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYSGLQEEL 226
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 227 ------QELRERYHFLNEEYRALQESN----SSLTGQLADLESERTQRATERWLQSQTLS--MTSAESQTSEMDFLEPDP 294
Cdd:pfam02463 522 griisaHGRLGDLGVAVENYKVAISTAviveVSATADEVEERQKLVRALTELPLGARKLRllIPKLKLPLKSIAVLEIDP 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 295 EMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRqvsEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRLCTL 374
Cdd:pfam02463 602 ILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK---ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 375 QKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHE 454
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 455 A--ELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKC 532
Cdd:pfam02463 759 KeeKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 533 ANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEdqrrmqeeqgqlqeeLHRLTLPLPKSGLLLKSQELLTKLEDLC 612
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK---------------EEELEEQKLKDELESKEEKEKEEKKELE 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 613 ELQLLYQgMQEEQKKLIQNQDCVLKEQLEI-HEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQSKLLMEQ--MQALQ 689
Cdd:pfam02463 904 EESQKLN-LLEEKENEIEERIKEEAEILLKyEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVnlMAIEE 982
|
730 740
....*....|....*....|....*...
gi 2462615707 690 VMYDAGQAKQELLQQEqgRLLEERKRLQ 717
Cdd:pfam02463 983 FEEKEERYNKDELEKE--RLEEEKKKLI 1008
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
49-199 |
1.52e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 49 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELRSLREEISLL 128
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462615707 129 EHEKESELKEIEQELHLAQAEIQSLRQaaedsatehesDIASLQEDLCRMQNELEDMERIRGDYEMEIASL 199
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
109-267 |
1.53e-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: 41.45 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 109 KQIQQLQGELRSLREEISLLEHEK---ESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASL-----QEDLCRMQN 180
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELaalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 181 ELEDMERIRGDYEMEIASLRAEMEMKSSEpsgslglsdYSGLQEELQELRERyhfLNEEYRALQESNSSLTGQLADLESE 260
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEE---------LAELEAELAELEAE---LEEKKAELDEELAELEAELEELEAE 164
|
....*..
gi 2462615707 261 RTQRATE 267
Cdd:COG1579 165 REELAAK 171
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
59-245 |
1.60e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 59 EELRAQV--LQLVAELEETRELAGQHEDDSLELQGLLEDERlasaQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 136
Cdd:PRK11281 39 ADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 137 KEIEQELHLAQ-----AEIQSLRQAAEDSATEHESDIASLQEDLCRMQNEL-EDMERI---------------------R 189
Cdd:PRK11281 115 RETLSTLSLRQlesrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALyANSQRLqqirnllkggkvggkalrpsqR 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615707 190 GDYEMEIASLRAEMEMKSSEPSGSLGLSDYsgLQEELQELRERYHFLNEEYRALQE 245
Cdd:PRK11281 195 VLLQAEQALLNAQNDLQRKSLEGNTQLQDL--LQKQRDYLTARIQRLEHQLQLLQE 248
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
136-401 |
1.64e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 136 LKEIEQELHLAQAEIQSLRQAAE--DSATEHESDIASLQEDLCRMQNELEDMERirgdyemEIASLRAEMEMKSSEPSGS 213
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQTLAllDKIDRQKEETEQLKQQLAQAPAKLRQAQA-------ELEALKDDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 214 LGLSDysgLQEELQELRERyhfLNEEYRALQESNSSLTGQlaDLESERTQRA-TERWLQSQTLSMTSAESQTSEMDfLEP 292
Cdd:PRK11281 121 LSLRQ---LESRLAQTLDQ---LQNAQNDLAEYNSQLVSL--QTQPERAQAAlYANSQRLQQIRNLLKGGKVGGKA-LRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 293 DpemqllRQQLRDAEEQMHGMKNKCQELccELEE-------LQHHRQVSEEEQRRLQRELKCAQ---NEVLRFQTSHSVT 362
Cdd:PRK11281 192 S------QRVLLQAEQALLNAQNDLQRK--SLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQeaiNSKRLTLSEKTVQ 263
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462615707 363 QNEELKsrlctlqkkyDTSQDEQNELLKMQLQLQTELRQ 401
Cdd:PRK11281 264 EAQSQD----------EAARIQANPLVAQELEINLQLSQ 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
159-409 |
1.69e-03 |
|
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: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 159 DSATEHESDIASLQEDLCRMQNELEDMERIRGDYEmEIASLRAEMEMKSSEpsgsLGLSDYSGLQEELQELRERYHFLNE 238
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYL----RAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 239 EYRALQESNSSLTGQLADLESERtQRATERWLQSQTlsmtsaesqtsemdflepdPEMQLLRQQLRDAEEQMHGMKNKCQ 318
Cdd:COG4913 303 ELARLEAELERLEARLDALREEL-DELEAQIRGNGG-------------------DRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 319 ELCCELEELQHHRQVSEEEQRRLQRELKCAQnevlrfqtshsvtqnEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTE 398
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALL---------------EALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
250
....*....|.
gi 2462615707 399 LRQLKVMKSTL 409
Cdd:COG4913 428 IASLERRKSNI 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
94-265 |
2.14e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 94 EDERLASAQQAEVFTKQIQQLQGELRSLREEISllehEKESELKEIEQELHLAQAEIQSLrqaaedsatehESDIASLQE 173
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELE----ELNEEYNELQAELEALQAEIDKL-----------QAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 174 DLCRMQNELEdmERIRGDYEMEIASLRAEMEMKSSEPSGSLG---------------LSDYSGLQEELQELRERyhfLNE 238
Cdd:COG3883 80 EIEERREELG--ERARALYRSGGSVSYLDVLLGSESFSDFLDrlsalskiadadadlLEELKADKAELEAKKAE---LEA 154
|
170 180
....*....|....*....|....*..
gi 2462615707 239 EYRALQESNSSLTGQLADLESERTQRA 265
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQE 181
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
415-738 |
2.54e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 415 EKELLCRLQKLHLQHQNVtcEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQASKDE 494
Cdd:COG1196 222 LKELEAELLLLKLRELEA--ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 495 LERQKHMYDQLEQDLLLCQLELKELKASHpipedkgkcANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRM 574
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAEL---------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 575 QEEQGQLQEELHRLTlplpksglllksQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEELrrfkeshf 654
Cdd:COG1196 371 EAELAEAEEELEELA------------EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL-------- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 655 QEVLENPDDSKLAKSSkcnRNKQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEEMQLLQVQS 734
Cdd:COG1196 431 AELEEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
....
gi 2462615707 735 PSIK 738
Cdd:COG1196 508 EGVK 511
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
56-174 |
2.94e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 56 TELEELRAQVLQLVAELEEtrelagqheddslelqgLLEDERLASAQQAEVFTKQIQQLQGELRSLREEislLEHEKE-- 133
Cdd:COG0542 411 EELDELERRLEQLEIEKEA-----------------LKKEQDEASFERLAELRDELAELEEELEALKAR---WEAEKEli 470
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462615707 134 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQED 174
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
187-403 |
2.97e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 187 RIRGDYEMEIASLRaememkssEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQrat 266
Cdd:pfam09787 18 RILQSKEKLIASLK--------EGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQE--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 267 erwlqsqtlsmtsaesqtsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRR----LQ 342
Cdd:pfam09787 87 ----------------------------EAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRskatLQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462615707 343 RELKCAQNEV--LRFQ---TSHSVTQNEELKSRLCTL-------QKKYDTSQDEQNELlkmQLQLQTELRQLK 403
Cdd:pfam09787 139 SRIKDREAEIekLRNQltsKSQSSSSQSELENRLHQLtetliqkQTMLEALSTEKNSL---VLQLERMEQQIK 208
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
88-350 |
3.20e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 88 ELQGLleDERLASaqqaevFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQelhLAQAEIQSLRQAAEDSATEH--- 164
Cdd:pfam00038 5 QLQEL--NDRLAS------YIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYS---LYEKEIEDLRRQLDTLTVERarl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 165 ESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLR----------AEMEMKssepsgslglsdYSGLQEELQELRERYh 234
Cdd:pfam00038 74 QLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdldeatlarVDLEAK------------IESLKEELAFLKKNH- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 235 flNEEYRALQESNSS--------------LTGQLADLE------SERTQRATERWLQSQTLSMTSAESQTSEMdflepdp 294
Cdd:pfam00038 141 --EEEVRELQAQVSDtqvnvemdaarkldLTSALAEIRaqyeeiAAKNREEAEEWYQSKLEELQQAAARNGDA------- 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462615707 295 emqllrqqLRDAEEQMHGMKNKCQELCCELEELQH-----HRQVSEEEQrRLQRELKCAQN 350
Cdd:pfam00038 212 --------LRSAKEEITELRRTIQSLEIELQSLKKqkaslERQLAETEE-RYELQLADYQE 263
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
86-428 |
3.25e-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: 41.75 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 86 SLELQGLLEDERLASAQQAEVFTKQIQQLQGeLRSLREEISLLEHEKESeLKEIEQELHLAQAEIQslrqaaedsatEHE 165
Cdd:pfam12128 205 ILEDDGVVPPKSRLNRQQVEHWIRDIQAIAG-IMKIRPEFTKLQQEFNT-LESAELRLSHLHFGYK-----------SDE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 166 SDIASLQEDLCRMQNELEdmerirgdyeMEIASLRAEMEMKSSEPSGSLglsdySGLQEELQELRERYHFLNEEYRALQE 245
Cdd:pfam12128 272 TLIASRQEERQETSAELN----------QLLRTLDDQWKEKRDELNGEL-----SAADAAVAKDRSELEALEDQHGAFLD 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 246 SN-SSLTGQLADLESERTQ-RATERWLQSQTlsmTSAESQTSEMDFLEPDPEMQLLRQ----------QLRDAEEQMHGM 313
Cdd:pfam12128 337 ADiETAAADQEQLPSWQSElENLEERLKALT---GKHQDVTAKYNRRRSKIKEQNNRDiagikdklakIREARDRQLAVA 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 314 KNKCQELCCELEElQHHRQVSE--EEQRRLQRELkcaqnEVLRFQTShSVTQNEELKSRLCTLQKKYDTSQDEQNELLKM 391
Cdd:pfam12128 414 EDDLQALESELRE-QLEAGKLEfnEEEYRLKSRL-----GELKLRLN-QATATPELLLQLENFDERIERAREEQEAANAE 486
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2462615707 392 QLQLQTELRQLKvmksTLVENQSEK---------ELLCRLQKLHLQ 428
Cdd:pfam12128 487 VERLQSELRQAR----KRRDQASEAlrqasrrleERQSALDELELQ 528
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
46-402 |
3.70e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 46 NKHRGLSLTETELE-ELRAQVLQLVAE---LEETRELAGQHEDDSLELQGLLE--DERLASAQQAEVFTKQIQQLQGELR 119
Cdd:PRK04863 279 NERRVHLEEALELRrELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQaaSDHLNLVQTALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 120 SLREEislLEhekesELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDL-------CRMQNELEDMERIRG-- 190
Cdd:PRK04863 359 ELEER---LE-----EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALdvqqtraIQYQQAVQALERAKQlc 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 191 ---DYEME-----IASLRAEME------------MKSSEPSGS------------LGLSDYSGLQEELQELRERYhflnE 238
Cdd:PRK04863 431 glpDLTADnaedwLEEFQAKEQeateellsleqkLSVAQAAHSqfeqayqlvrkiAGEVSRSEAWDVARELLRRL----R 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 239 EYRALQESNSSLTGQLADLESE-RTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQL--LRQQLRDAEEQMHGMKN 315
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLesLSESVSEARERRMALRQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 316 KCQELCCELEELQHHRQVSEEEQRRLQRelkcaqnevLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQL 395
Cdd:PRK04863 587 QLEQLQARIQRLAARAPAWLAAQDALAR---------LREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQAL 657
|
....*..
gi 2462615707 396 QTELRQL 402
Cdd:PRK04863 658 DEEIERL 664
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
108-689 |
6.62e-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: 40.48 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 108 TKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMER 187
Cdd:pfam05483 73 SEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 188 IRgdyemEIASLRAEMEMKSSEPSgslglsdySGLQEELQELRERYHFLN----------EEYRaLQESNSSLT------ 251
Cdd:pfam05483 153 TR-----HLCNLLKETCARSAEKT--------KKYEYEREETRQVYMDLNnniekmilafEELR-VQAENARLEmhfklk 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 252 ---GQLADLESERTQRATERWLQSQTL--SMTSAESQTSEMDFL--EPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCEL 324
Cdd:pfam05483 219 edhEKIQHLEEEYKKEINDKEKQVSLLliQITEKENKMKDLTFLleESRDKANQLEEKTKLQDENLKELIEKKDHLTKEL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 325 EELQHHRQVSEEEQRRLQRELKCAQNEVLRF--------------QTSHSVTQNEeLKSRLCTLQKKYDTSQ------DE 384
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDLQIATKTICQLteekeaqmeelnkaKAAHSFVVTE-FEATTCSLEELLRTEQqrleknED 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 385 QNELLKMQLQLQT-ELRQL-KVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAELQHLRD 462
Cdd:pfam05483 378 QLKIITMELQKKSsELEEMtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 463 TVASFKESNEKdtethaQLQEMKQLyqasKDELERQKHMYDQLEQDLLLCQLELKEL--KASHPI------PEDKGKCAN 534
Cdd:pfam05483 458 QLTAIKTSEEH------YLKEVEDL----KTELEKEKLKNIELTAHCDKLLLENKELtqEASDMTlelkkhQEDIINCKK 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 535 KCDTLLSRLTELQEKYKASQKEMGQLQME--------QCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQELLT 606
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEfiqkgdevKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 607 K-LEDL-CELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEELRRFKE--SHFQEVLEnpdDSKLAKSSKCNRNKQSKLLM 682
Cdd:pfam05483 608 KnIEELhQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEiiDNYQKEIE---DKKISEEKLLEEVEKAKAIA 684
|
....*..
gi 2462615707 683 EQMQALQ 689
Cdd:pfam05483 685 DEAVKLQ 691
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
112-209 |
6.63e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 112 QQLQGELRSLREEISLLEHEKESELKEIEQElhlaqaeiQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGD 191
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQ--------QQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ 216
|
90
....*....|....*...
gi 2462615707 192 YEMEIASlRAEMEMKSSE 209
Cdd:PRK11448 217 KRKEITD-QAAKRLELSE 233
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
55-144 |
7.50e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 38.37 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 55 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaEVFTKQIQQLQGELRSLREEISLLEHEKES 134
Cdd:pfam09744 49 NVELEELREDNEQLETQYEREKALRKRAEEELEEIEDQWEQET-------KDLLSQVESLEEENRRLEADHVSRLEEKEA 121
|
90
....*....|
gi 2462615707 135 ELKEIEQELH 144
Cdd:pfam09744 122 ELKKEYSKLH 131
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
54-156 |
8.55e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 54 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLlederlasAQQAEvftKQIQQLQGELRSLREEISLLEHEKE 133
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGL--------AAELE---EKQQELEAQLEQLQEKAAETSQERK 215
|
90 100 110
....*....|....*....|....*....|..
gi 2462615707 134 SELKEIEQE----LHLAQAEI-----QSLRQA 156
Cdd:PRK11448 216 QKRKEITDQaakrLELSEEETrilidQQLRKA 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
295-722 |
8.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 295 EMQLLRQQLRDAEEQMHgmknkcqelccELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTshsVTQNEELKSRLCTL 374
Cdd:COG4717 72 ELKELEEELKEAEEKEE-----------EYAELQEELEELEEELEELEAELEELREELEKLEK---LLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 375 QKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLerqqqlqeelqcHE 454
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE------------LQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 455 AELQHLRDTVASFKESNEkdtETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKCAN 534
Cdd:COG4717 206 QRLAELEEELEEAQEELE---ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 535 KCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQELLTKLEDLCEl 614
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 615 QLLYQGMQEEQKKLIQNQDCVLKEQL-EIHEELRRFKE-----SHFQEVLENPDDSKLAKSSKCNRNKqsklLMEQMQAL 688
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELrAALEQAEEYQElkeelEELEEQLEELLGELEELLEALDEEE----LEEELEEL 437
|
410 420 430
....*....|....*....|....*....|....
gi 2462615707 689 QVMYDAGQAKQELLQQEQGRLLEERKRLQADLQL 722
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-978 |
9.25e-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: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615707 844 EDMERFEEMVVKVLIKLQAVQAMYQISQEEHSQLQEQMEKLLAKQKDLKEELDACEREFKEcmecLEKpmAPQNDKNEIK 923
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----LES--RLEELEEQLE 382
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462615707 924 ELQTKLRELQLQYQASMDEQGRLLVVQEQLEGQLQCCQEELRQLREKRPSVVKEA 978
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
|
| |
