|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-597 |
6.89e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELtDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQL 177
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 178 QDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQhIIRLESLQAEQVL 257
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 258 EIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 338 LQSSAATSTSLLSE--IEQSMEAEELEQEREQLRLQLWEAYcqVRYLCSHLRGNDSADSAVSTDSSMDESSETSSAKDVP 415
Cdd:COG1196 495 LLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAA--YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 416 AGSLR--TALNELKRLIQSIVDGMEPTGSRRLDDDSLEEQIRQTSEDSRALRELMEGERgkLRQSLEELQRLHSQVTLLS 493
Cdd:COG1196 573 RATFLplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR--LEAALRRAVTLAGRLREVT 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 494 VEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQD 573
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
490 500
....*....|....*....|....
gi 578824461 574 DMHRVIDRQLMDTHLKERSQPAAA 597
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALE 754
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-338 |
1.16e-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: 68.16 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQL 177
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEAEAEIEEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 178 QDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSM------QVHALREDFREKNSSTNQHIIRLESL 251
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrleDLEEQIEELSEDIESLAAEIEELEEL 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 252 QAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQvkvEE 331
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ---ER 944
|
....*..
gi 578824461 332 LTEERSL 338
Cdd:TIGR02168 945 LSEEYSL 951
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-337 |
3.89e-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: 60.08 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 118 KALLERNQDMSRQYEQMHKELT---DKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELERQQIHLREADRE 194
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSslqSELRRIENRLDELSQELS----DASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 195 KSRAVQELSEQNQRLLDQLSRASEVERQLsmqvHALREDFREKNSSTNQHIIR-LESLQAEQVLEIKMLSDRKRELEHRL 273
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEARLSHSRIPeIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824461 274 SATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-530 |
4.95e-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: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 120 LLERNQDMSRQYEQMhKELTDKLEHLEQEKHELRRRFEnregewegrvsELESDVKQLQDELERQQIHLREADREKSRAV 199
Cdd:TIGR02168 672 ILERRREIEELEEKI-EELEEKIAELEKALAELRKELE-----------ELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 200 QElSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEE 279
Cdd:TIGR02168 740 AE-VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 280 NDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERslqssaatsTSLLSEIEQSMEAE 359
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL---------EALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 360 ELEQEREQlrlqlweaycqvrylcshlrgndsadsavSTDSSMDESSETSSAKDVPAGSLRTALNELKRLIQSIvdgmep 439
Cdd:TIGR02168 890 ALLRSELE-----------------------------ELSEELRELESKRSELRRELEELREKLAQLELRLEGL------ 934
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 440 tgsrRLDDDSLEEQIRQ----TSEDSRALRELMEGERGKLRQSLEELQRLHSQ---VTLLSV-EMTALKEERDRLRVTSE 511
Cdd:TIGR02168 935 ----EVRIDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpVNLAAIeEYEELKERYDFLTAQKE 1010
|
410 420
....*....|....*....|
gi 578824461 512 D-KEPKEQLQKAIRDRDEAI 530
Cdd:TIGR02168 1011 DlTEAKETLEEAIEEIDREA 1030
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-577 |
1.23e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 98 ELLSVIRQKEKDLVLAARLGKALLERNQdmsrQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQL 177
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 178 QDE----LERQQ------IHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDfREKNSSTNQHIIR 247
Cdd:COG1196 368 LEAeaelAEAEEeleelaEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-EEEEEEEEEALEE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 248 LESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQgHDKDLQLHQSQLELQEVRLSCRQLQV 327
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-EADYEGFLEGVKAALLLAGLRGLAGA 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 328 KVEELTEERSLQssAATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAYCQVRYLCSHLRGNDSADSAVSTDSSMDESSE 407
Cdd:COG1196 526 VAVLIGVEAAYE--AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 408 TSSAKDVPAGSLRTALNELkrLIQSIVDGMEPTGSRRLDDDSLEEQIRQTSEDSRALRELMEGERGKLRQSLEELQRLHS 487
Cdd:COG1196 604 VASDLREADARYYVLGDTL--LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 488 QVTLLSVEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQ 567
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
490
....*....|
gi 578824461 568 LEAWQDDMHR 577
Cdd:COG1196 762 LEELERELER 771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-583 |
1.86e-08 |
|
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: 57.76 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 258 EIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERs 337
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI- 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 338 lqssaatsTSLLSEIEQSMEAEELEQEREQLRLQLWEAYcqvrylcshlrgndsadsavstdssMDESSETSSAKDvpag 417
Cdd:TIGR02168 764 --------EELEERLEEAEEELAEAEAEIEELEAQIEQL-------------------------KEELKALREALD---- 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 418 SLRTALNELKRLIQSIVDGMEPTGSRRLDDDSLEEQIRQTSEDSRALRELMEGERGKLRQSLEElqrLHSQVTLLSVEMT 497
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE---LESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 498 ALKEERDRLR-----VTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQ 572
Cdd:TIGR02168 884 SLEEALALLRseleeLSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
330
....*....|.
gi 578824461 573 DDMHRVIDRQL 583
Cdd:TIGR02168 964 EDDEEEARRRL 974
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
135-375 |
7.73e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 135 HKELTDKLEHLEQEKHELRRR-FENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQL 213
Cdd:COG1196 215 YRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 214 SRASEVERQLSMQvhalredfREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDR 293
Cdd:COG1196 295 AELARLEQDIARL--------EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 294 VLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELteERSLQSSAATSTSLLSEIEQsMEAEELEQEREQLRLQLW 373
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEE-LEEALAELEEEEEEEEEA 443
|
..
gi 578824461 374 EA 375
Cdd:COG1196 444 LE 445
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-348 |
9.97e-08 |
|
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: 55.45 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 121 LERNQDMSRQYEQMHKELTD-------KLEHLEQEKHELRRRFENREGEWE---GRVSELESDVKQLQ------------ 178
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAelqeleeKLEELRLEVSELEEEIEELQKELYalaNEISRLEQQKQILRerlanlerqlee 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 179 -----DELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQA 253
Cdd:TIGR02168 321 leaqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 254 eqvlEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDK---DLQLHQSQLELQEVRLSCRQLQVKVE 330
Cdd:TIGR02168 401 ----EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeleELQEELERLEEALEELREELEEAEQA 476
|
250
....*....|....*...
gi 578824461 331 ELTEERSLQSSAATSTSL 348
Cdd:TIGR02168 477 LDAAERELAQLQARLDSL 494
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
129-332 |
2.94e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 129 RQYEQMHKELTDKLEHLEQEKHELRRRFENRE-GEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQ 207
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 208 RLLDQLSRaseverqlsmQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTV 287
Cdd:COG4913 338 DRLEQLER----------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578824461 288 EELQDRVLILERQGHD-----KDLQLHQSQL--ELQEVRLS-CRQLQVKVEEL 332
Cdd:COG4913 408 AEAEAALRDLRRELREleaeiASLERRKSNIpaRLLALRDAlAEALGLDEAEL 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-297 |
2.14e-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: 51.21 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEgrvsELESDVKQLQDELERQQIHLREADREKSR 197
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----TLRSKVAQLELQIASLNNEIERLEARLER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 198 AVQELSEQNQRLLDQLSRASEVERQ-LSMQVHALREDFREKNSSTNQHIIRLESLQaEQVLEIKMLSDRKRELEHRLSAT 276
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELR-EELEEAEQALDAAERELAQLQAR 490
|
170 180
....*....|....*....|.
gi 578824461 277 LEENDLLQGTVEELQDRVLIL 297
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKAL 511
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
105-319 |
4.71e-06 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 48.87 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 105 QKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRR---------------FENREGEWEGRVSE 169
Cdd:pfam04849 77 EKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKddllqiysndaeeseTESSCSTPLRRNES 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 170 LESDVKQLQDELERQQIHLREADREKSRA--------VQELSEQNQRLL----DQLSRASEverqlsmQVHALREDFREK 237
Cdd:pfam04849 157 FSSLHGCVQLDALQEKLRGLEEENLKLRSeashlkteTDTYEEKEQQLMsdcvEQLSEANQ-------QMAELSEELARK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 238 NSSTNQHIIRLESLQAEQV---LEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqghdkdlQLHQSQLE 314
Cdd:pfam04849 230 MEENLRQQEEITSLLAQIVdlqHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLG-------MLHEAQEE 302
|
....*
gi 578824461 315 LQEVR 319
Cdd:pfam04849 303 LKELR 307
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
168-352 |
5.46e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.69 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 168 SELESDVKQLQDELERQQIHLREADREksraVQELSEQNQRLLdqlSRASEVERQLSmqvhalrEDFREKNSSTNQHIIR 247
Cdd:COG5022 867 ETIYLQSAQRVELAERQLQELKIDVKS----ISSLKLVNLELE---SEIIELKKSLS-------SDLIENLEFKTELIAR 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 248 LESLQAEqvLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVL---ILERQGHDKDLQLHQSQLELQEVRLSCRQ 324
Cdd:COG5022 933 LKKLLNN--IDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKkstILVREGNKANSELKNFKKELAELSKQYGA 1010
|
170 180
....*....|....*....|....*...
gi 578824461 325 LQVKVEELTEERSLQSSAATSTSLLSEI 352
Cdd:COG5022 1011 LQESTKQLKELPVEVAELQSASKIISSE 1038
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
95-355 |
2.97e-05 |
|
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: 47.02 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 95 QDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKEL-TDKLEHLEQEKHELRRRFENREgewegrvseLESD 173
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELeKEKLKNIELTAHCDKLLLENKE---------LTQE 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 174 VKQLQDELERQQihlreadreksRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQA 253
Cdd:pfam05483 508 ASDMTLELKKHQ-----------EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 254 EQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELT 333
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
|
250 260
....*....|....*....|....
gi 578824461 334 E--ERSLQSSAATSTSLLSEIEQS 355
Cdd:pfam05483 657 DnyQKEIEDKKISEEKLLEEVEKA 680
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
139-337 |
5.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 139 TDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELER-QQIHLREADREKSRAVQELSEQNQRLLDQLSRAS 217
Cdd:COG4913 609 RAKLAALEAELAELEEELA----EAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 218 EVERQLSMQVHALREDFREknsstnqhiirleslqAEQvlEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLIL 297
Cdd:COG4913 685 DDLAALEEQLEELEAELEE----------------LEE--ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578824461 298 ERQGHDKDLQLHQSQLELQEVRlscRQLQVKVEELTEERS 337
Cdd:COG4913 747 LRALLEERFAAALGDAVERELR---ENLEERIDALRARLN 783
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
131-534 |
9.19e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 131 YEQMHKELTDKLEHLEQEKHELRRRFENRE---GEWEGR---VSELESDVKQLQD---ELERQQIHLREADREKSRAVQE 201
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADevlEEHEERreeLETLEAEIEDLREtiaETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 202 LSEQNQRLLDQL-------SRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLqAEQVLEIKMLSDRKRE----LE 270
Cdd:PRK02224 291 LEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL-REDADDLEERAEELREeaaeLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 271 HRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE-RSLQSSAATSTSLL 349
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATlRTARERVEEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 350 S-----EIEQSMEAEELEQEREqlrlqlwEAYCQVRYLCSHLrgndsadsavstdSSMDESSETSSAKDVPAGSLRTALN 424
Cdd:PRK02224 450 EagkcpECGQPVEGSPHVETIE-------EDRERVEELEAEL-------------EDLEEEVEEVEERLERAEDLVEAED 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 425 ELKRLIQSIVDGMEPTGSRRLDDDSLEEQIRQTSEDSRALRELMEGERGKLRQSLEELQRLHSQVTLLSVEMTALKEERD 504
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
410 420 430
....*....|....*....|....*....|...
gi 578824461 505 RLRVTSEDKEPKEQLQKAI---RDRDEAIAKKN 534
Cdd:PRK02224 590 SLERIRTLLAAIADAEDEIerlREKREALAELN 622
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-545 |
2.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 136 KELTDKLEHLEQEKHELRRRFENREgEWEGRVSELESDVKQLQDELER--QQIHLREADREKSRAVQELSEQNQRLlDQL 213
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERL-EEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 214 SRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQV----LEIKMLSDRKRELEHRLSATLEENDLLQGTVEE 289
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELqdlaEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 290 LQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAATSTSLL------SEIEQSMEAEELEQ 363
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLllarekASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 364 EREQLRLQLWEAYCQVRylcsHLRGNDSADSAVSTDSSMDESSETSSAKDVPAGSLRTA--LNELKRLIQSIVDGMEPTG 441
Cdd:COG4717 312 ALEELEEEELEELLAAL----GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 442 SRRLDDDSLEEQIRQTSEDSRALRELMEGERGKLRQSL------EELQRLHSQVTLLSVEMTALKEERDRLRVTSEDKEP 515
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeleEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420 430
....*....|....*....|....*....|
gi 578824461 516 KEQLQKAIRDRDEAIAKKNAVELELAKCRM 545
Cdd:COG4717 468 DGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
125-335 |
2.69e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 125 QDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAvqelsE 204
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI-----E 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 205 QNQRLLDQLSRASEVERQLSMQV---HALREDFREKNSSTNQHIIRLESLQAEqvLEIKMLSDRKRELEHRLSATLEEND 281
Cdd:TIGR00606 769 EQETLLGTIMPEEESAKVCLTDVtimERFQMELKDVERKIAQQAAKLQGSDLD--RTVQQVNQEKQEKQHELDTVVSKIE 846
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578824461 282 LLQGTVEELQDRVLILErqghDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE 335
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLK----SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
136-335 |
4.36e-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: 43.52 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 136 KELTDKLEHLEQEKH------ELRRRFENREG-EWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQR 208
Cdd:TIGR02169 194 DEKRQQLERLRREREkaeryqALLKEKREYEGyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 209 LldqlsraseveRQLSMQVHALRED----FREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQ 284
Cdd:TIGR02169 274 L-----------EELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578824461 285 GTVEELQdrvlilerqghdkdLQLHQSQLELQEVRLSCRQLQVKVEELTEE 335
Cdd:TIGR02169 343 REIEEER--------------KRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
121-300 |
5.04e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRR---FENREGEWEGRVSELESDVKQLQDELERQQIHLRE------- 190
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 191 ---ADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKR 267
Cdd:COG4942 116 lgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578824461 268 E-------LEHRLSATLEENDLLQGTVEELQDRVLILERQ 300
Cdd:COG4942 196 ErqkllarLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-291 |
8.36e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQL 177
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 178 QDELERQQIHLREADReKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVL 257
Cdd:COG4942 121 PLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
170 180 190
....*....|....*....|....*....|....
gi 578824461 258 EIKMLSDRKRELEHRLSATLEENDLLQGTVEELQ 291
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-537 |
8.86e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 155 RFENREGEWEGRVSELESDVKQLQD---ELERQQIHLrEADREKSRAVQELSEQnqrlldqlsrasevERQLSMQVHALR 231
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDilnELERQLKSL-ERQAEKAERYKELKAE--------------LRELELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 232 -EDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQ 310
Cdd:TIGR02168 234 lEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 311 SQLELQEVRLSCRQLQVKVEELTEErsLQSSAATSTSLLSEIEqSMEAEELEQEREQLrlqlweaycqvrylcshlrgnd 390
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEE--LAELEEKLEELKEELE-SLEAELEELEAELE---------------------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 391 sadsavstdssmdESSETSSAKDVPAGSLRTALNELKRLIQSI---VDGMEPTGSRrldddSLEEQIRQTSEDSRALREL 467
Cdd:TIGR02168 369 -------------ELESRLEELEEQLETLRSKVAQLELQIASLnneIERLEARLER-----LEDRRERLQQEIEELLKKL 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578824461 468 MEGERGKLRQSLEELQR-LHSQVTLLSVEMTALKEERDRLRvtsedkEPKEQLQKAIRDRDEAIAKKNAVE 537
Cdd:TIGR02168 431 EEAELKELQAELEELEEeLEELQEELERLEEALEELREELE------EAEQALDAAERELAQLQARLDSLE 495
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
127-254 |
1.06e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 127 MSRQYEQMHKELTDKLEHLeQEKHELRRRFENREGEWEGRVSELEsdvkqlqdeleRQQIHLREADREKSRAVQELSEQN 206
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLEL-QEFKILKDKKDAKIRELEARVSDLE-----------LEKVKLVNAGSERLRAVKDIKQER 655
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 578824461 207 QRLLDQLSRASEVERQLSMQVHALREDFREKN----SSTNQHIIRLESLQAE 254
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSeemeTTTNKLKMQLKSAQSE 707
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
136-278 |
1.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 136 KELTDKLEHLEQEKHELRRRFENR----EGEWEGRVSELES------DVKQLQDELERQQIHLREADREKSRAVQELSEQ 205
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824461 206 NQRLLDQLSRASEVERQLSMQVHA-LREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLE 278
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-304 |
1.50e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 104 RQKEKDLVLAARLGKALLERNQDMSRQYEQmHKELTDKLEHLEQEKHELRRRFENREGEwegrVSELESDVKQLQDELER 183
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESE-LEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEE 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 184 QQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLS 263
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578824461 264 DRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDK 304
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQ 1040
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
168-358 |
1.88e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 168 SELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQ----------LSMQVHALREDFREK 237
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaaleaelaeLEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 238 NSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLsatleenDLLQGTVEELQDRVLILERQghDKDLQLHQSQLELQE 317
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL-------QYLKYLAPARREQAEELRAD--LAELAALRAELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578824461 318 VRLScrqlQVKVEELTEERSLQSSAATSTSLLSEIEQSMEA 358
Cdd:COG4942 174 AELE----ALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
98-300 |
2.30e-03 |
|
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: 40.88 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQ----------EKHELRRRFENREGEwegrV 167
Cdd:pfam05557 52 ELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADarevisclknELSELRRQIQRAELE----L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 168 SELESDVKQLQDELERQQIHLREAdrekSRAVQELSEQNQRLLDQLSRASEVERQLSMQvhalrEDFREKNSSTNQHIIR 247
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEA----EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQ-----EQDSEIVKNSKSELAR 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578824461 248 LESLQAEQvleikmlsDRKRELEHRLSATLEENDLLQGTVEELQDRvliLERQ 300
Cdd:pfam05557 199 IPELEKEL--------ERLREHNKHLNENIENKLLLKEEVEDLKRK---LERE 240
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
129-289 |
2.46e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 129 RQYEQMHKELTDKLEHLEQEKHELR-RRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQ 207
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLRaERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 208 RLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLE-SLQAEQVLEIKMLSDRKRELEHRLSatlEENDLLQGT 286
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQrKKQQEEAERAEAEKQRQKELEMQLA---EEQKRLMEM 471
|
...
gi 578824461 287 VEE 289
Cdd:pfam15709 472 AEE 474
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-224 |
2.53e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 112 LAARLGKALLERN--QDMSRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEGRVSELESDVKQLQDELERQQI 186
Cdd:TIGR02169 817 IEQKLNRLTLEKEylEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
90 100 110
....*....|....*....|....*....|....*...
gi 578824461 187 HLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLS 224
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
134-293 |
2.86e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 134 MHKELtDKLEHLeQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRL---- 209
Cdd:COG1579 2 MPEDL-RALLDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkkye 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 210 --LDQLSRASEVErQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTV 287
Cdd:COG1579 80 eqLGNVRNNKEYE-ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
....*.
gi 578824461 288 EELQDR 293
Cdd:COG1579 159 EELEAE 164
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
124-335 |
2.91e-03 |
|
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: 40.77 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 124 NQDMSRQYEQMHKEL----------TDKLEHLEQEKHELRRRFENREGEWEgrvsELESDVKQLQDELErqqihlreadr 193
Cdd:TIGR04523 358 NSEKQRELEEKQNEIeklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQ----QKDEQIKKLQQEKE----------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 194 EKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHAL---REDFREKNSSTNQHI----IRLESLQAE---QVLEIKMLS 263
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntRESLETQLKVLSRSInkikQNLEQKQKElksKEKELKKLN 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824461 264 DRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRL--SCRQLQVKVEELTEE 335
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLekEIDEKNKEIEELKQT 576
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
108-345 |
3.52e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 108 KDLVLAARLGKALLERNqdmsrqyeqmhkELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELER---Q 184
Cdd:pfam07888 28 RAELLQNRLEECLQERA------------ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQsreK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 185 QIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNqhiiRLESLQAEQVLEIKMLSD 264
Cdd:pfam07888 96 HEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE----RMKERAKKAGAQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 265 RKRELEHRLSATLEENDLLQGTVEELQDrvliLERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE-RSLQSSAA 343
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRN----SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElRSLQERLN 247
|
..
gi 578824461 344 TS 345
Cdd:pfam07888 248 AS 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
118-337 |
3.93e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 118 KALLERNQDMSRQYEQMHKELTDKLEH---LEQEKHELRRRFENREGEWEgRVSELESDVKQLQDELERQQIHLR---EA 191
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREineISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRkleEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 192 DREKSRAVQELSEQNQRLLDQLSRASEVER--QLSMQVHALREDFREKNSSTNQHIIRLESLQA---EQVLEIKMLSDRK 266
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEkaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgieERIKELEEKEERL 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578824461 267 RELEHRLSATLEENDLLQGTVEELQD-RVLILERQGHDK---DLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEaKAKKEELERLKKrltGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
142-574 |
4.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 142 LEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERqqihLREADREKSRAVQELSEQNQRLLDQLSRASEVER 221
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 222 QLsmQVHALREDFREKNSSTNQHIIRLESLQaEQVLEIKMLSDRKRELEHRLSATLEENDllqgtvEELQDRVLILERQG 301
Cdd:COG4717 124 LL--QLLPLYQELEALEAELAELPERLEELE-ERLEELRELEEELEELEAELAELQEELE------ELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 302 HDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAYCQVRY 381
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 382 LCSHLRGNDSADSAVSTDSSMDESSETSSAKDVPAGSLRTALNELKRLIQSIVDGMEPTGSRRLDDDsLEEQIRQTSEDS 461
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE-LLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 462 RALRELMEgeRGKLRQSLEELQRLHSQVTLLSVEM--TALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVEL- 538
Cdd:COG4717 354 REAEELEE--ELQLEELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELe 431
|
410 420 430
....*....|....*....|....*....|....*..
gi 578824461 539 -ELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDD 574
Cdd:COG4717 432 eELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
122-349 |
4.14e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 122 ERNQDMSRQYEQMHKELTDKLEHLE----QEKHELRRRFENREgewegrVSELESDVKQLQDELERQQIHLREADrekSR 197
Cdd:PRK11281 80 EETEQLKQQLAQAPAKLRQAQAELEalkdDNDEETRETLSTLS------LRQLESRLAQTLDQLQNAQNDLAEYN---SQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 198 AV--QELSEQNQRLLDQ-LSRASEVERQLsmqvhalredfreKNSSTNQHIIRLES---LQAEQVLEIKMLSDRKRELEH 271
Cdd:PRK11281 151 LVslQTQPERAQAALYAnSQRLQQIRNLL-------------KGGKVGGKALRPSQrvlLQAEQALLNAQNDLQRKSLEG 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824461 272 rlSATLEenDLLQGTVEELQDRVLILERQghdkdLQLhqsqleLQEVrLSCRQLQVKVEELTEERSLQSSAATSTSLL 349
Cdd:PRK11281 218 --NTQLQ--DLLQKQRDYLTARIQRLEHQ-----LQL------LQEA-INSKRLTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
174-354 |
4.50e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 174 VKQLQDELERQQIHlrEADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQ--VHALREDFREKNSSTNQHIIRLESL 251
Cdd:COG3096 481 VCKIAGEVERSQAW--QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQqnAERLLEEFCQRIGQQLDAAEELEEL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 252 QAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLI-------LERQGHdkdlQLHQSQLELQEVrLSCRQ 324
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaaqdaLERLRE----QSGEALADSQEV-TAAMQ 633
|
170 180 190
....*....|....*....|....*....|.
gi 578824461 325 LQVKVE-ELTEERSLqsSAATSTSLLSEIEQ 354
Cdd:COG3096 634 QLLERErEATVERDE--LAARKQALESQIER 662
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
120-554 |
8.39e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.33 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 120 LLERNQDMSRQYEQMHK----ELTDKLEHLEQEKHELRRRFE-------NREGEWEGRVSELESDVKQLQDELerqqihl 188
Cdd:pfam15921 261 LLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEiiqeqarNQNSMYMRQLSDLESTVSQLRSEL------- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 189 READREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLeSLQAEQVleiKMLSDR--- 265
Cdd:pfam15921 334 REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-SLEKEQN---KRLWDRdtg 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 266 --------KRELEHRLSATLEENDLLQGTVEELQDRvliLERQG---HDKDLQLHQSQLELQEVRLSCRQLQVKVEELTE 334
Cdd:pfam15921 410 nsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQ---MERQMaaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 335 ER-SLQSSAATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAYCQVrylCSHLRgnDSADSAVSTDSSMDESSETSSAKD 413
Cdd:pfam15921 487 KKmTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE---LQHLK--NEGDHLRNVQTECEALKLQMAEKD 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 414 VPAGSLRtalNELKRLIQSIVDGMEPTGSRRLDDDSLEEQIRQTSEDSRALRELMEGERGKLRQsleelqrLHSQVTLLS 493
Cdd:pfam15921 562 KVIEILR---QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRE-------LEARVSDLE 631
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824461 494 VEMTAL-KEERDRLRVTSEDKEPKEQLQKAIRD---------RDEAIAKKN------AVELELAKCRMDMMSLNSQL 554
Cdd:pfam15921 632 LEKVKLvNAGSERLRAVKDIKQERDQLLNEVKTsrnelnslsEDYEVLKRNfrnkseEMETTTNKLKMQLKSAQSEL 708
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
98-236 |
9.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQ-----YEQMHKELTDKLEHLEQEKHELRRRFENREgEWEGRVSELES 172
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLlqllpLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEA 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824461 173 DVKQLQDELERQQIHLREADREksrAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFRE 236
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
448-583 |
9.76e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824461 448 DSLEEQIRQTSEDSRALRELMEGERGKLRQSLEELQRLHSQVTLLSVEMTALKEERDRLRVTSEDKEpkEQLQKAIRDRD 527
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE--EELAELEEELE 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 578824461 528 EAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQL 583
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
|
|