|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-436 |
9.62e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 9.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 175 ENDSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRE 254
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 255 LDAKLAEIRQLQMKLNG--GEQHAFGISRENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLfpkstEDLSRHL 332
Cdd:COG1196 318 LEELEEELAELEEELEEleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-----EELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 333 SSLDEEKAGTFpGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQ 412
Cdd:COG1196 393 RAAAELAAQLE-ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260
....*....|....*....|....
gi 30690248 413 ILGLEKALRQTMANQEEIKSSSDL 436
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLL 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
177-520 |
2.73e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 177 DSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELD 256
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 257 AKLAEIRQLQMKLNGGEQhafgiSRENLKEVNKALEKENNELKLKRSELEAALEASQkstsrklfpkstEDLSRHLSSLD 336
Cdd:COG1196 306 RLEERRRELEERLEELEE-----ELAELEEELEELEEELEELEEELEEAEEELEEAE------------AELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 337 EEkagtfpgkedmEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQtneyQRSQILGL 416
Cdd:COG1196 369 EA-----------EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE----LEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 417 EKALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKEHFERELAVAKED 496
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340
....*....|....*....|....
gi 30690248 497 AMKLSARLKDVDEQLESSKKEKEE 520
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYE 537
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
182-539 |
2.20e-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: 61.24 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 182 KKEKEFAEmLEERTRSMASAQARE---------LEKEREKSANLQILLQEERKQnetfkeELQSLRLDKEKTLMESNKVR 252
Cdd:TIGR02169 171 KKEKALEE-LEEVEENIERLDLIIdekrqqlerLRREREKAERYQALLKEKREY------EGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 253 RELDAKLAEIRQLQMKLNGGEQHAFGISREnLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLfpkstEDLSRHL 332
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQL-LEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI-----AEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 333 SSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQtneyqrsq 412
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD-------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 413 ilgLEKALRQTMANQEEIKSSSDL---EIRKSKGIIEDLNQKLAnclrtidSKNVELLNLQTALGQYYAEIEAKehfERE 489
Cdd:TIGR02169 390 ---YREKLEKLKREINELKRELDRlqeELQRLSEELADLNAAIA-------GIEAKINELEEEKEDKALEIKKQ---EWK 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 30690248 490 LAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSKVLHAENIAAEWKNRV 539
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-521 |
2.24e-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: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 184 EKEFAEMLEERTR-----SMASAQARELEKE-REKSANLQILLQEErkqnETFKEELQSLRLDKEKTLMESNKVRRELDA 257
Cdd:TIGR02169 687 KRELSSLQSELRRienrlDELSQELSDASRKiGEIEKEIEQLEQEE----EKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 258 KLAEIRQLQMKLNGGEQHAFGISRENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLFPkstedlsrhlsslde 337
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE--------------- 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 338 ekagtfpgKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTneyqRSQILGLE 417
Cdd:TIGR02169 828 --------KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL----KKERDELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 418 KALRQTMANQEEIKSssdlEIRKSKGIIEDLNQKLANC---LRTIDSKNVELLNLQTA---LGQYYAEIEAKEHFERELA 491
Cdd:TIGR02169 896 AQLRELERKIEELEA----QIEKKRKRLSELKAKLEALeeeLSEIEDPKGEDEEIPEEelsLEDVQAELQRVEEEIRALE 971
|
330 340 350
....*....|....*....|....*....|....
gi 30690248 492 ----VAKEDAMKLSARLKDVDEQLESSKKEKEEI 521
Cdd:TIGR02169 972 pvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
199-422 |
2.27e-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: 59.78 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 199 ASAQARELEKEREKsanlqilLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNggeqhafg 278
Cdd:COG4942 15 AAAQADAAAEAEAE-------LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 279 ISRENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRK-----LFPKSTEDLSRHLSSLDEekagTFPGKEDMEKSL 353
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPplallLSPEDFLDAVRRLQYLKY----LAPARREQAEEL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30690248 354 QRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQ 422
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
204-559 |
8.40e-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: 59.31 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 204 RELEKEREKSANLQILLQEERKQNETFKEE----LQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNGGEQHafgi 279
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRErekaERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE---- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 280 sRENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKlFPKSTEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKE 359
Cdd:TIGR02169 253 -LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 360 LEEARREKDKARQELKRLKqhlLEKETEESEkmdedsrlIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSsdleir 439
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEER---KRRDKLTEE--------YAELKEELEDLRAELEEVDKEFAETRDELKDYREK------ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 440 kskgiIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKEHFERELAVAKEDAmklSARLKDVDEQLESSKKEKE 519
Cdd:TIGR02169 394 -----LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK---ALEIKKQEWKLEQLAADLS 465
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 30690248 520 EITSKVLHAENIAAEWKNRVSKVEDDNAKVRRVLEQSMTR 559
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
178-446 |
2.51e-08 |
|
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: 57.44 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 178 SESHKKEKeFAEMLEERTRSMASAQARELEKEREksanlqilLQEERKQNETFKEELQSLRLDKEKTLMESNkvrRELDA 257
Cdd:pfam17380 285 SERQQQEK-FEKMEQERLRQEKEEKAREVERRRK--------LEEAEKARQAEMDRQAAIYAEQERMAMERE---RELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 258 KLAEIRQLQMKLNGGEQHAFGISRenLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLFPKSTEDLSRHLSSLDE 337
Cdd:pfam17380 353 IRQEERKRELERIRQEEIAMEISR--MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 338 EKAgtfpgKEDMEKSLQRLEKELEEARREKDKARQELKRLKQH---------LLEKETEESEKMDEDSRLI-----DELR 403
Cdd:pfam17380 431 EAR-----QREVRRLEEERAREMERVRLEEQERQQQVERLRQQeeerkrkklELEKEKRDRKRAEEQRRKIlekelEERK 505
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 30690248 404 QT--NEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKSKGIIE 446
Cdd:pfam17380 506 QAmiEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
68-411 |
6.86e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 68 ERYKAEINKLQKSESEIKALSVNYA-ALLKEKEDQISRLNQENGSLKQNLTSTNAALKESRLDLSRASNNNAIKGngdhs 146
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELeAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ----- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 147 pnrsqrsptnwknrnqmnngiaskpnGTENDSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQ 226
Cdd:COG1196 288 --------------------------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 227 NETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNggeqhafgisRENLKEVNKALEKENNELKLKRSELE 306
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA----------EELLEALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 307 AALEASQKSTSRklfpkstEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKET 386
Cdd:COG1196 412 LLERLERLEEEL-------EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340
....*....|....*....|....*
gi 30690248 387 EESEKMDEDSRLIDELRQTNEYQRS 411
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-554 |
9.99e-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: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 204 RELEKEREKSANLQILLQEERKQnetfkeeLQSLRLDKEKTLmESNKVRRELDAKLAEIRQLQMKLNGGEQhafgisrEN 283
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQ-------LEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAEL-------EE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 284 LKEVNKALEKENNELKLKRSELEAALEASQKSTSRKlfpksTEDLSRHLSSLDEEkagtfpgkedmEKSLQRLEKELEEA 363
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEEL-----ELELEEAQAEEYEL-----------LAELARLEQDIARL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 364 RREkdkaRQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKSKG 443
Cdd:COG1196 308 EER----RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 444 IIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKEHFERELAVAKEDAMKLSARLKDVDEQLESSKKEKEEITS 523
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350
....*....|....*....|....*....|.
gi 30690248 524 KVLHAENIAAEWKNRVSKVEDDNAKVRRVLE 554
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
170-555 |
1.15e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 170 KPNGTENDSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQslrldkEKTLMESN 249
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE------EKKKADEA 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 250 KVRRELDAKLAEirqlQMKLNGGEQHAFGISRENLKEVNKAlekenNELKLKRSELEAALEASQKSTSRklfpKSTEDLS 329
Cdd:PTZ00121 1397 KKKAEEDKKKAD----ELKKAAAAKKKADEAKKKAEEKKKA-----DEAKKKAEEAKKADEAKKKAEEA----KKAEEAK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 330 RhlSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEdSRLIDELRQTNEYQ 409
Cdd:PTZ00121 1464 K--KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE-AKKAEEAKKADEAK 1540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 410 RSQilglEKALRQTMANQEEIKSSSDL-EIRKSKGIIEDLNQKL--ANCLRTIDSKNV-ELLNLQTALGQYYAEIEAKEH 485
Cdd:PTZ00121 1541 KAE----EKKKADELKKAEELKKAEEKkKAEEAKKAEEDKNMALrkAEEAKKAEEARIeEVMKLYEEEKKMKAEEAKKAE 1616
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30690248 486 FER----ELAVAKEDAMKLSARLKDVDEQL---ESSKKEKEEITSKVLHAENIAAEWKNRVSKVEDDNAKVRRVLEQ 555
Cdd:PTZ00121 1617 EAKikaeELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-532 |
1.32e-07 |
|
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: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 178 SESHKKEKEFAEMLEERTRSMASAQARELEKEREKsanlqilLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDA 257
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEELREELEE-------LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 258 KLAEIRQlqmklnggeqhafgisreNLKEVNKALEKENNELKLKRSELEaALEASQKSTSrklfpkstEDLSRHLSSLDE 337
Cdd:TIGR02168 282 EIEELQK------------------ELYALANEISRLEQQKQILRERLA-NLERQLEELE--------AQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 338 EKAgtfpGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKEteesEKMDEDSRLIDELRQTNEYQRSQILGLE 417
Cdd:TIGR02168 335 LAE----ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE----EQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 418 KALRQTMANQEEIKSS-SDLEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKehfERELAVAKED 496
Cdd:TIGR02168 407 ARLERLEDRRERLQQEiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA---EQALDAAERE 483
|
330 340 350
....*....|....*....|....*....|....*.
gi 30690248 497 AMKLSARLKDVDEQLESSKKEKEEITSKVLHAENIA 532
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-454 |
1.39e-07 |
|
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: 55.06 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 175 ENDSESHKKEKEFAEMLE-----ERTRSMASAQARELEKEREKsanLQILLQEERKQNETFKEELQSLRLDKEKTLMESN 249
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEkiaelEKALAELRKELEELEEELEQ---LRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 250 KVRRELDAKLAEIRQLQMKLNGGEQHAFGIS--RENLKEVNKALEKENNELKLKRSELEAAL-----EASQKSTSRKLFP 322
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEaeIEELEAQIEQLKEELKALREALDELRAELtllneEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 323 KSTEDLSRHLSSLDEEKagtfpgkEDMEKSLQRLEKELEEARREKDKARQELKrlkqHLLEKETEESEKMDEDSRLIDEL 402
Cdd:TIGR02168 831 RRIAATERRLEDLEEQI-------EELSEDIESLAAEIEELEELIEELESELE----ALLNERASLEEALALLRSELEEL 899
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 30690248 403 RQTNEYQRSQIlgleKALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKLAN 454
Cdd:TIGR02168 900 SEELRELESKR----SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
282-565 |
2.11e-07 |
|
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: 54.69 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 282 ENLKEVNKALEKENNELKLKRSELEAalEASQKSTSRKLFPKSTEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELE 361
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIEN--RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 362 EARREKDKARQEL--KRLKQHLLEKETEESEKMDEDSRL------IDELRQTNEYQRSQILGLEKAL----------RQT 423
Cdd:TIGR02169 755 NVKSELKELEARIeeLEEDLHKLEEALNDLEARLSHSRIpeiqaeLSKLEEEVSRIEARLREIEQKLnrltlekeylEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 424 MANQEEIKSSSDLEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIE----AKEHFERELAVAKEDAMK 499
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDeleaQLRELERKIEELEAQIEK 914
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30690248 500 LSARLKDVDEQLESSKKEKEEITSKVLHAENIAAEwknrvSKVEDDNAKVRRVLEQSMTRLNRMSM 565
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-----ELSLEDVQAELQRVEEEIRALEPVNM 975
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
178-453 |
2.88e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 178 SESHKKEKEFAEMLEErtrsmASAQARELEKEREKSANLqILLQEERKQNETFKEELQSLRLDK-EKTLMESNKVRRELD 256
Cdd:PRK03918 462 KRIEKELKEIEEKERK-----LRKELRELEKVLKKESEL-IKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 257 AKLAEIRQLQMKLNggeqhafgiSRENLKEVNKALEKENNELKLKRSELEAALEasqkstsrKLFPKSTEDLSRHLSSLD 336
Cdd:PRK03918 536 KLKGEIKSLKKELE---------KLEELKKKLAELEKKLDELEEELAELLKELE--------ELGFESVEELEERLKELE 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 337 E------EKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEES-EKMDEDSRLIDELRQTNEYQ 409
Cdd:PRK03918 599 PfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeEEYEELREEYLELSRELAGL 678
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 30690248 410 RSQILGLEKALRQTMANQEEIKSSSDlEIRKSKGIIEDLNQKLA 453
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALE 721
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
183-551 |
3.11e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 183 KEKEFAEMLEE------------RTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLrldkEKTLMESNK 250
Cdd:PRK03918 198 KEKELEEVLREineisselpelrEELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL----EERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 251 VRRELDAKLAEIRQLQMKLNggEQHAFGISRENLKEVNKALEKENNELKLKRSELEAAL-EASQKSTSRKLFPKSTEDLS 329
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAE--EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkELEEKEERLEELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 330 RHLSSLdEEKAGTF----PGKEDMEK--------SLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSR 397
Cdd:PRK03918 352 KRLEEL-EERHELYeeakAKKEELERlkkrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 398 LIDEL-------RQTNEYQRSQILgleKALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKLANCLRTIDSKNV--ELLN 468
Cdd:PRK03918 431 LKKAKgkcpvcgRELTEEHRKELL---EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 469 LQTALGQYyaEIEAKEHFERELAVAKEDAMKLSARLKDVDEQLESS---KKEKEEITSKVLHAENIAAEWKNRVSK---- 541
Cdd:PRK03918 508 LEEKLKKY--NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEElgfe 585
|
410
....*....|.
gi 30690248 542 -VEDDNAKVRR 551
Cdd:PRK03918 586 sVEELEERLKE 596
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
179-513 |
5.99e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 179 ESHKKEKEFAEMLEERTRSMASAQArELEKEREksaNLQILLQEERKQNETFKEELQSLRLDKEKTLMESNKV---RREL 255
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIA-ETERERE---ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVearREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 256 DAKLAEIRQLQMKLNGGEQhAFGISRENLKEVNKALEKENNELKLKRSELEAALEASQKSTsrklfpkstEDLSRHLSSL 335
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV---------EDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 336 DEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLK-------------QHLLE-----------KETEESEK 391
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlrtarerveeaEALLEagkcpecgqpvEGSPHVET 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 392 MDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKskgiiEDLNQKLANCLRTIDSKNVELLNLQT 471
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERR-----EDLEELIAERRETIEEKRERAEELRE 544
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 30690248 472 ALGQYYAEIEAKEHFERELAVAKEDAM----KLSARLKDVDEQLES 513
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAReevaELNSKLAELKERIES 590
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-555 |
6.88e-07 |
|
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: 52.76 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 338 EKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLE 417
Cdd:TIGR02169 650 EKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 418 KALRQTMANQEEIKSssdlEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEI--EAKEHFERELAVAKE 495
Cdd:TIGR02169 730 QEEEKLKERLEELEE----DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshSRIPEIQAELSKLEE 805
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690248 496 DAMKLSARLKDVDEQLESSKKEKEEITSKVLHAENIAAEWKNRVS----KVEDDNAKVRRVLEQ 555
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKsiekEIENLNGKKEELEEE 869
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
347-563 |
7.97e-07 |
|
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: 52.75 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 347 EDMEKSLQRLEKELEEARREKDKARQELKRLKQhLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMAN 426
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRK-DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 427 QEEIKSSSDLEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKehfERELAVAKEDAMKLSARLKD 506
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT---ERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30690248 507 VDEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVEDDNAKVRRVLEQSMTRLNRM 563
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-394 |
9.13e-07 |
|
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: 52.37 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 66 EIERYKAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQENGSLKQNLTSTNAALKESRLDLSRASNNNAIKgngdh 145
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL----- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 146 spnrSQRsptnwknrnqmnngiaskpngtENDSESHKKEKEFAEMLEERTRSMASAQARELEkerEKSANLQILLQEERK 225
Cdd:TIGR02168 308 ----RER----------------------LANLERQLEELEAQLEELESKLDELAEELAELE---EKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 226 QNETFKEELQSLrldkEKTLMESNKVRRELDAKLAEIRQlQMKLNGGEQhafgisrENLKEVNKALEKENNELKLKRSEL 305
Cdd:TIGR02168 359 ELEELEAELEEL----ESRLEELEEQLETLRSKVAQLEL-QIASLNNEI-------ERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 306 EAALEASQKstsrklfpkstEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKE 385
Cdd:TIGR02168 427 LKKLEEAEL-----------KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
....*....
gi 30690248 386 TEESEKMDE 394
Cdd:TIGR02168 496 RLQENLEGF 504
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
178-529 |
1.26e-06 |
|
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: 51.89 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 178 SESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDA 257
Cdd:TIGR00618 509 SCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 258 KLAEIRQLQMKLNGGEQHafgisRENLKEVNKALEKENNElklKRSELEAALEASQKSTSRKLFPKSTEDLSRHLSSlDE 337
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEA-----EDMLACEQHALLRKLQP---EQDLQDVRLHLQQCSQELALKLTALHALQLTLTQ-ER 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 338 EKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLkQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLE 417
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML-AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 418 KALRQTMANQEE-----IKSSSDLEIRKSKGIIEDL--NQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAK-EHFERE 489
Cdd:TIGR00618 739 DALNQSLKELMHqartvLKARTEAHFNNNEEVTAALqtGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEiPSDEDI 818
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 30690248 490 LAVAKEdamKLSARLKDVDEQLESSKKEKEEITSKVLHAE 529
Cdd:TIGR00618 819 LNLQCE---TLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-379 |
1.28e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 201 AQARELEKEREKSANLQIL-----LQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQL--QMKLNGGE 273
Cdd:COG4913 259 ELAERYAAARERLAELEYLraalrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaQIRGNGGD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 274 QhafgisRENLKEVNKALEKENNELKLKRSELEAALEASQKSTsrklfPKSTEDLSRHLSSLDEEKAGTFPGKEDMEKSL 353
Cdd:COG4913 339 R------LEQLEREIERLERELEERERRRARLEALLAALGLPL-----PASAEEFAALRAEAAALLEALEEELEALEEAL 407
|
170 180
....*....|....*....|....*.
gi 30690248 354 QRLEKELEEARREKDKARQELKRLKQ 379
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
336-563 |
1.31e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 336 DEEKAGTFPGKEDMEKSLQRLE-------KELEEARREKDKAR--QELKRLKQ------HLLEKETEESEKMDEDSRlID 400
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAEryQALLKEKReyegyeLLKEKEALERQKEAIERQ-LA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 401 ELRQTNEYQRSQILGLEK---ALRQTMAN-QEEIKSSSDLEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQY 476
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKrleEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 477 YAEIEA----KEHFERELAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSKvlhaeniAAEWKNRVSKVEDDNAKVRRV 552
Cdd:TIGR02169 328 EAEIDKllaeIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE-------FAETRDELKDYREKLEKLKRE 400
|
250
....*....|.
gi 30690248 553 LEQSMTRLNRM 563
Cdd:TIGR02169 401 INELKRELDRL 411
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
281-566 |
1.64e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 281 RENLKEVNKALEKENNELKLKRSELEAALEasQKSTSRKLFPKSTEDLSRHLSSLDEEKagtfpgkEDMEKSLQRLEKEL 360
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAER--YQALLKEKREYEGYELLKEKEALERQK-------EAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 361 EEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRK 440
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 441 SKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKehfERELAVAKEDAMKLSARLKDVDEQLESSKKE--- 517
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV---DKEFAETRDELKDYREKLEKLKREINELKREldr 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 30690248 518 ----KEEITSKVLHAENIAAEWKNRVSKVEDDNAKVRRVLEQSMTRLNRMSMD 566
Cdd:TIGR02169 411 lqeeLQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-530 |
1.90e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 182 KKEKEFAEMLEErTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEKTlmesnkvRRELDAKLAE 261
Cdd:PRK02224 321 DRDEELRDRLEE-CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR-------REEIEELEEE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 262 IRQLQMKLNGGEqhafgISRENLKEVNKALEKENNELKLKRSELEAALEASQKST--SRKLF-----PKSTEDL--SRHL 332
Cdd:PRK02224 393 IEELRERFGDAP-----VDLGNAEDFLEELREERDELREREAELEATLRTARERVeeAEALLeagkcPECGQPVegSPHV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 333 SSLDEEkagtfpgkedmEKSLQRLEKELEEARREKDKARQELKRLKQHL-LEKETEES-EKMDEDSRLIDELRQTNEYQR 410
Cdd:PRK02224 468 ETIEED-----------RERVEELEAELEDLEEEVEEVEERLERAEDLVeAEDRIERLeERREDLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 411 SQILGLEKA---LRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKLANCLRTIDSKNvELLNLQTALGQYYAEIE------ 481
Cdd:PRK02224 537 ERAEELRERaaeLEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIErlrekr 615
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30690248 482 ------------------------AKEHFERELAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSKVLHAEN 530
Cdd:PRK02224 616 ealaelnderrerlaekrerkrelEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
71-530 |
2.36e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 71 KAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQENGSLKQNLTSTNAALKESrlDLSRASNNNAIKGNGDHSPNRS 150
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA--DEAKKKAEEKKKADEAKKKAEE 1442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 151 QRSPTNWKNRNQMnngiASKPNGTENDSESHKKEKEFAEMLEERTRsmASAQARELEKEREKSANLQILLQEERKQNETF 230
Cdd:PTZ00121 1443 AKKADEAKKKAEE----AKKAEEAKKKAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 231 KEELQSlrldKEKTLMESNKVRRELDAKLAEIRQLQMKLNGGEQhaFGISRENLKEVNKALEKENNELKLKRSELEAALE 310
Cdd:PTZ00121 1517 KAEEAK----KADEAKKAEEAKKADEAKKAEEKKKADELKKAEE--LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 311 ASQKSTSRKLFPKSTEDLSRHLSSLDEE--KAGTFPGKEDMEKSLQRLEKELEEarrEKDKArQELKRLKQHLLEKETEE 388
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAkiKAEELKKAEEEKKKVEQLKKKEAE---EKKKA-EELKKAEEENKIKAAEE 1666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 389 SEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTmANQEEIKSSSDLEIRKSKGIiedlnqklanclrtidsKNVELLN 468
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEEL-----------------KKAEEEN 1728
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30690248 469 LQTALGQYYAEIEAKEHFErELAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSKVLHAEN 530
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAE-EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
178-544 |
3.15e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 178 SESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKE-ELQSLRLDKEKTLMESNKVRRELD 256
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKaEEDKKKADELKKAAAAKKKADEAK 1424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 257 AKLAEIRQL-QMKLNGGEQHAFGISRENLKEVNKALE--------KENNELKLKRSELEAALEASQKSTSRKLFPKSTED 327
Cdd:PTZ00121 1425 KKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKAEEakkkaeeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 328 LSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKR---LKQHLLEKETEESEKMDEDS----RLID 400
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKaeeLKKAEEKKKAEEAKKAEEDKnmalRKAE 1584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 401 ELRQTNEYQRSQILGL---EKALRQTMANQEEIKSSSDLEIRKS---KGIIEDLNQKLANCLRTIDSKNVELLNLQTALG 474
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLyeeEKKMKAEEAKKAEEAKIKAEELKKAeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 475 QYYAEIEAKEHFERELAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVED 544
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
347-525 |
3.76e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.21 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 347 EDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDedsRLIDELRQtnEYQrsqilgleKALRQTMAN 426
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED---KLLEEAEK--EAQ--------QAIKEAKKE 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 427 QEEIksSSDLEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKEHF----------------EREL 490
Cdd:PRK00409 586 ADEI--IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVkylslgqkgevlsipdDKEA 663
|
170 180 190
....*....|....*....|....*....|....*
gi 30690248 491 AVaKEDAMKLSARLKDvdeqLESSKKEKEEITSKV 525
Cdd:PRK00409 664 IV-QAGIMKMKVPLSD----LEKIQKPKKKKKKKP 693
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
242-381 |
4.74e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 242 EKTLMESNKVRRELDAKLAEIRQLQMKLnggeqhafgisrENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLf 321
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQV------------ERLEAEVEELEAELEEKDERIERLERELSEARSEERREI- 461
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 322 pksteDLSRHLSSLDEEkagtfpgkedmeksLQRLEKELEEARREKDKARQELKRLKQHL 381
Cdd:COG2433 462 -----RKDREISRLDRE--------------IERLERELEEERERIEELKRKLERLKELW 502
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
192-544 |
5.96e-06 |
|
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: 49.97 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 192 EERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNG 271
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 272 GEQHAFGISRENLKEVNKALEKENNELKLKRSELEaaleasqKSTSRKLFPKSTEDLSRHLSSLDEEKagtfpgKEDMEK 351
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK-------LLAKEEEELKSELLKLERRKVDDEEK------LKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 352 SLQRLEKELEEARREKDKARQELKRL---KQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQE 428
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELeikREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 429 EIKSSSDLEIRKSKgIIEDLNQKLANCLRTIDSKNVELLNLQTAlgqYYAEIEAKEHFERELAVAKEDAMKLSARLKDVD 508
Cdd:pfam02463 402 EEEKEAQLLLELAR-QLEDLLKEEKKEELEILEEEEESIELKQG---KLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350
....*....|....*....|....*....|....*.
gi 30690248 509 EQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVED 544
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLL 513
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
68-451 |
7.06e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 68 ERYKAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQEngsLKQNLTSTNAALKESRLDLSRASNNNAIKGNGDHSP 147
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE---KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 148 NRSQRSPTNWKNRNQMnngiASKPNGTENDSESHKKEKEfaemlEERTRSMASAQARELEKEREKSANLQILLQEERKQN 227
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEE----AKKADEAKKKAEEAKKKAD-----EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 228 ETFK---EELQSLRLDKEKTLMESNKVRRELDAKLAEIRQlQMKLNGGEQhAFGISRENLKEVNKALEKENnelKLKRSE 304
Cdd:PTZ00121 1537 DEAKkaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK-NMALRKAEE-AKKAEEARIEEVMKLYEEEK---KMKAEE 1611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 305 LEAALEASQKSTSRKLFPKSTEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKArQELKRLKQHLLEK 384
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA-EEAKKAEEDEKKA 1690
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30690248 385 EtEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQK 451
Cdd:PTZ00121 1691 A-EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-442 |
8.15e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 176 NDSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEKtlMESNKvrREL 255
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR--LEQQK--QIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 256 DAKLAEIRQLQMKLNGGEQHAF---GISRENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKlfpkstEDLSRHL 332
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELEsklDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL------EELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 333 SSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEE-SEKMDEDSRLIDELRQTNEYQRS 411
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLEE 461
|
250 260 270
....*....|....*....|....*....|.
gi 30690248 412 QILGLEKALRQtmANQEEIKSSSDLEIRKSK 442
Cdd:TIGR02168 462 ALEELREELEE--AEQALDAAERELAQLQAR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
179-432 |
1.03e-05 |
|
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: 49.30 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 179 ESHKKEKEFAEMLEERTRSMAsaqaRELEKEREKSANLQILLQEERKQNETFKEELQSLRLD--------KEKTLMESNK 250
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLE----QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeIQAELSKLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 251 VRRELDAKLAEIRQlqmKLNGGEQhafgiSRENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLfpKSTEDLSR 330
Cdd:TIGR02169 806 EVSRIEARLREIEQ---KLNRLTL-----EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE--EELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 331 HLSSLDEEkagtfpgKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQr 410
Cdd:TIGR02169 876 ALRDLESR-------LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP- 947
|
250 260
....*....|....*....|..
gi 30690248 411 SQILGLEKALRQTMANQEEIKS 432
Cdd:TIGR02169 948 EEELSLEDVQAELQRVEEEIRA 969
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
361-573 |
4.00e-05 |
|
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: 47.37 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 361 EEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQ----------ILGLEKALRQTMANQEEI 430
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLkekreyegyeLLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 431 KSSSDLEIRKSKGIIEDLNQKLANCLRTIDSKNV--------ELLNLQTALGQYYAEIeakEHFERELAVAKEDAMKLSA 502
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKIGELEAEI---ASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30690248 503 RLKDVDEQLESSKKEKEEITSKVlhaeniaAEWKNRVSKVEDDNAKVRRVLEQSMTRLNRMSMDSDFLVDR 573
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREI-------EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
252-458 |
5.20e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 252 RRELDAKLAEIRQLQMKLNggeqhafgisrenlkevnkALEKENNELKLKRSELEAALEASQKSTSRKLFPKSTEDLSRH 331
Cdd:COG4913 609 RAKLAALEAELAELEEELA-------------------EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 332 LSSLDEEKagtfpgkEDMEKS---LQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEY 408
Cdd:COG4913 670 IAELEAEL-------ERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 30690248 409 QRS-QILGLEKALRQTM--ANQEEIKSSSDLEIRKSKGIIEDLNQKLANCLRT 458
Cdd:COG4913 743 ARLeLRALLEERFAAALgdAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
194-389 |
6.42e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 194 RTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDAK--LAEIRQLQMKLNG 271
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 272 GEQHAFGIsRENLKEVnKALEKENNELKLKRSELEAALEASQKSTSrklfpkstEDLSRHLSSLDEEkagtfpgKEDMEK 351
Cdd:COG4717 144 LPERLEEL-EERLEEL-RELEEELEELEAELAELQEELEELLEQLS--------LATEEELQDLAEE-------LEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*...
gi 30690248 352 SLQRLEKELEEARREKDKARQELKRLKQHLLEKETEES 389
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
64-548 |
7.47e-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: 46.17 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 64 NPEIERYKAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQENGSLKQNLTSTNAALKESRLDLSRASNNNAikgNG 143
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID---KI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 144 DHSPNRSQRSPTNWKNRNQMNNGIASKPNGTENDSESHKKE-KEFAEMLEERTRSMASAQAR------ELEKEREKSANL 216
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNiEKKQQEINEKTTEISNTQTQlnqlkdEQNKIKKQLSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 217 QILLQEERKQNETFKEELQSLR-----LDKEKTLMESNKVRRELDAKLAEIRQLQMKLNGGEQHafgISRenLKEVNKAL 291
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKseisdLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI---ISQ--LNEQISQL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 292 EKENNELKLKRSELEAALEasQKSTSRKLFPKSTEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKAR 371
Cdd:TIGR04523 348 KKELTNSESENSEKQRELE--EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 372 QELKRLKQHLLEKETEESEKMDEDSRL---IDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDL----------EI 438
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKeliIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSkekelkklneEK 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 439 RKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKE-------------HFERELAVAKEDAMKLSARLK 505
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelkkenlekeidEKNKEIEELKQTQKSLKKKQE 585
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 30690248 506 DVDEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVEDDNAK 548
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-551 |
8.48e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 66 EIERYKAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQENGSLKQNLtstnAALKESRLDLSRASNNNAIKGNGDH 145
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV----KELKELKEKAEEYIKLSEFYEEYLD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 146 SPNRSQRSPTNWknRNQMNNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAqaRELEKEREKSANLQILLQEERK 225
Cdd:PRK03918 308 ELREIEKRLSRL--EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH--ELYEEAKAKKEELERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 226 QN-ETFKEELQSLRLDKEKTLMESNKV---RRELDAKLAEIRQLQMKLNGG------------EQHAFGISRENLKEVN- 288
Cdd:PRK03918 384 LTpEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAkgkcpvcgreltEEHRKELLEEYTAELKr 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 289 -----KALEKENNELKLKRSELEAALEASQKSTSRKLFPKSTEDLSRHLSSLDEEKAgtfpgkEDMEKSLQRLEKELEEA 363
Cdd:PRK03918 464 iekelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEEL------EKKAEEYEKLKEKLIKL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 364 RREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIksssdLEIRKSKG 443
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEY-----LELKDAEK 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 444 IIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKEH----------------FERELAVAKEDAMKLSARLKDV 507
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeeyeelreeyleLSRELAGLRAELEELEKRREEI 692
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 30690248 508 DEQLESSKKEKEEITSKVLHAENIaaewKNRVSKVEDDNAKVRR 551
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEKL----EKALERVEELREKVKK 732
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-429 |
9.36e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 198 MASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEktlmESNKVRRELDAKLAEIRQLQMKLNGGEQHaf 277
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD----LSPEELLELLDRIEELQELLREAEELEEE-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 278 gISRENLKEVNKALEKENNELKLKrsELEAALEASQKSTS-RKLFPKSTEDLSRHLSSLDEEKAGTfpGKEDMEKSLQRL 356
Cdd:COG4717 363 -LQLEELEQEIAALLAEAGVEDEE--ELRAALEQAEEYQElKEELEELEEQLEELLGELEELLEAL--DEEELEEELEEL 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30690248 357 EKELEEARREKDKARQELKRLKQHL--LEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEkALRQTMANQEE 429
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEWAALKLALE-LLEEAREEYRE 511
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
68-552 |
1.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 68 ERYKAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQENGslKQNLTSTNAALKESRLDLSRASNNNAIKGNGDHSP 147
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA--ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 148 NRSQRSPTNWKNRNQMNNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAQARELEK---EREKSANLQILLQEER 224
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaeEAKKAEEAKKKAEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 225 KQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNGGEQHAFGISRENLKEVNKALEKENNELKLKRSE 304
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 305 LEAALEASQKSTSRKLFPKSTEDLSRHLSSLDEEKAgtfpgkedmekslqrleKELEEARREKD-KARQELKRLKQHLLE 383
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA-----------------KKAEEARIEEVmKLYEEEKKMKAEEAK 1613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 384 KETEESEKMdEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKskgiiEDLNQKLANCLRTIDSKn 463
Cdd:PTZ00121 1614 KAEEAKIKA-EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-----AEEDKKKAEEAKKAEED- 1686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 464 vellnlqtalgqyyaEIEAKEHFERElAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVE 543
Cdd:PTZ00121 1687 ---------------EKKAAEALKKE-AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
....*....
gi 30690248 544 DDNAKVRRV 552
Cdd:PTZ00121 1751 KDEEEKKKI 1759
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
220-562 |
1.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 220 LQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNGGEQHAFGISRE--NLKEVNKALEKENNE 297
Cdd:PRK02224 218 LDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEvrDLRERLEELEEERDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 298 LkLKRSELEAAleasqkstsrklfpkSTEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRL 377
Cdd:PRK02224 298 L-LAEAGLDDA---------------DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 378 KqhllEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDlEIRKSKgiiEDLNQKLANC-- 455
Cdd:PRK02224 362 R----EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE-ELREER---DELREREAELea 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 456 -LRTIDSKNVELLNLQTA-----LGQyyaEIEAKEHFEReLAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSkvlhae 529
Cdd:PRK02224 434 tLRTARERVEEAEALLEAgkcpeCGQ---PVEGSPHVET-IEEDRERVEELEAELEDLEEEVEEVEERLERAED------ 503
|
330 340 350
....*....|....*....|....*....|...
gi 30690248 530 niAAEWKNRVSKVEDDNAKVRRVLEQSMTRLNR 562
Cdd:PRK02224 504 --LVEAEDRIERLEERREDLEELIAERRETIEE 534
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
187-414 |
1.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 187 FAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRlDKEKTLMESNKVRRELDAKLAEIRQLQ 266
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 267 mklnggEQHAFGISRENLKEVNKALEKENNELKLKRSELEAALEASQkstsrklfpKSTEDLSRHLSSLDEEKAGTfpgK 346
Cdd:COG4717 126 ------QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE---------ELEAELAELQEELEELLEQL---S 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30690248 347 EDMEKSLQRLEKELEEARREKDKARQELKRLKQHlLEKETEESEKMDEDSRLIDELRQTNEYQRSQIL 414
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEE-LEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
66-271 |
1.90e-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: 44.37 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 66 EIERYKAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQENGSLKQNLTSTNAALKESRLDLSRASNNNAIKGNgdh 145
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 146 spNRSQRSPTNWKNRNQMNNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAQArELEKEREKSANLQILLQEERK 225
Cdd:COG4942 105 --ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-ELAALRAELEAERAELEALLA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 30690248 226 QNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNG 271
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
233-404 |
2.01e-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: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 233 ELQslRLDKEktLMESNKVRRELDAKLAEIRQLQMKLnggeqhafgisRENLKEVNKALEKENNELKLKRSELEAALEAS 312
Cdd:COG1579 11 DLQ--ELDSE--LDRLEHRLKELPAELAELEDELAAL-----------EARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 313 QKSTSRKLFPKSTEDLSRHLSSLDEEKAGtfpgKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKM 392
Cdd:COG1579 76 KKYEEQLGNVRNNKEYEALQKEIESLKRR----ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|..
gi 30690248 393 DEDSRLIDELRQ 404
Cdd:COG1579 152 AELEAELEELEA 163
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
347-564 |
2.09e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 347 EDMEKSLQRLEKELEEARREKD------KARQELKRLKQHLLEKE--------TEESEKMDEDSRLIDELRQTNEYQRSQ 412
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKslerqaEKAERYKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 413 ILGLEKALRQTMANQEEIKSssdlEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIeakEHFERELAV 492
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL---EELESKLDE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30690248 493 AKEDAMKLSARLKDVDEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVEDDNAKVRRVLEQSMTRLNRMS 564
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-426 |
2.93e-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: 44.29 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 66 EIERYKAE---INKLQKSESEIKALSVNYAALLKEKED---QISRLNQENGSLKQNLTSTNAALKESRLDLSRAsnNNAI 139
Cdd:TIGR02169 204 RREREKAEryqALLKEKREYEGYELLKEKEALERQKEAierQLASLEEELEKLTEEISELEKRLEEIEQLLEEL--NKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 140 KGNGDHSPNRSQRSPTNWK-NRNQMNNGIAskpngtENDSESHKKEKEFAEMLEE--RTRSMASAQARELEKEREKSANL 216
Cdd:TIGR02169 282 KDLGEEEQLRVKEKIGELEaEIASLERSIA------EKERELEDAEERLAKLEAEidKLLAEIEELEREIEEERKRRDKL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 217 QILLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLN--GGEQHAFGISRENLKEVNKALEKE 294
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDrlQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 295 NNELKLKRSELEAALEASQkstsRKLfpkstEDLSRHLSSLDEEkagtfpgKEDMEKSLQRLEKELEEARREKDKARQEL 374
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQE----WKL-----EQLAADLSKYEQE-------LYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 30690248 375 KRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMAN 426
Cdd:TIGR02169 500 RASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNN 551
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-543 |
3.16e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 66 EIERYKAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQENGSLKQNLTSTNAALKESRLDLSRASNNNAIKGNGDH 145
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 146 SPNRSQRSptnwknrnqmnngIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERK 225
Cdd:COG1196 390 EALRAAAE-------------LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 226 QNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNGGEQHAFGISRENLKEVNKALEKENNELKLKRSEL 305
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 306 EAALEASQKSTSRKLFPKSTEDLSRHLSSLDEEKAG--TFpgkEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLE 383
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGraTF---LPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 384 KETEESEKMDEDSrLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKLANCLRTIDSKN 463
Cdd:COG1196 614 RYYVLGDTLLGRT-LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 464 VELLNLQTAL-GQYYAEIEAKEHFERELAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKV 542
Cdd:COG1196 693 LELEEALLAEeEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
.
gi 30690248 543 E 543
Cdd:COG1196 773 E 773
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
344-556 |
3.63e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 344 PGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKEteesEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQT 423
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ----AELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 424 M-ANQEEIKSSSDLEIRKSKGIIEDLNQKLANcLRTIDSKNVELLNlqtalgQYYAEIEAKEHFERELAVAKEDAMKLSA 502
Cdd:COG3883 92 ArALYRSGGSVSYLDVLLGSESFSDFLDRLSA-LSKIADADADLLE------ELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 30690248 503 RLKDVDEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVEDDNAKVRRVLEQS 556
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
338-534 |
3.96e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 43.98 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 338 EKAGTFPGKEDMEksLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDE-DSRLIDELRQTNEYQRSQILGL 416
Cdd:COG1193 503 ERARELLGEESID--VEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEElEEEKEEILEKAREEAEEILREA 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 417 EKALRQTMANQEEIKSSSDlEIRKSKGIIEDLNQKLANCL---RTIDSKNVELLNLQ-------TALGQyYAEIEAKEHF 486
Cdd:COG1193 581 RKEAEELIRELREAQAEEE-ELKEARKKLEELKQELEEKLekpKKKAKPAKPPEELKvgdrvrvLSLGQ-KGEVLEIPKG 658
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 30690248 487 ERelAVAKEDAMKLSARLKDvdeqLESSKKEKEEITSKVLHAENIAAE 534
Cdd:COG1193 659 GE--AEVQVGILKMTVKLSD----LEKVEKKKPKKPKKRPAGVSVSVS 700
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
93-381 |
4.43e-04 |
|
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: 43.67 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 93 ALLKEKEDQISRLNQENGSLKQNLTSTNAALKESRLDLSRASN---------NNAIKgngDHSPNRSQRSPTNWKNRNQM 163
Cdd:pfam12128 618 EKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDekqsekdkkNKALA---ERKDSANERLNSLEAQLKQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 164 NNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAQ-ARELEKEREKSANLQILLQEERKQnetfkeELQSLRLDkE 242
Cdd:pfam12128 695 DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALlKAAIAARRSGAKAELKALETWYKR------DLASLGVD-P 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 243 KTLMESNKVRRELDAKLAEIRQLQMKLNGGE---QHAFGISRENLKEVNKALEKENNELK--LKRSELEAALEASQKSTS 317
Cdd:pfam12128 768 DVIAKLKREIRTLERKIERIAVRRQEVLRYFdwyQETWLQRRPRLATQLSNIERAISELQqqLARLIADTKLRRAKLEME 847
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30690248 318 RKLFPKSTEDLSRHLSSLDEEKAGTFPGKED-----MEKSLQRLEKELEEARREKDKARQELKRLKQHL 381
Cdd:pfam12128 848 RKASEKQQVRLSENLRGLRCEMSKLATLKEDanseqAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHF 916
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
216-560 |
4.73e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 216 LQILLQE-ERKQNETFKEELQSLRLDKEKtLMESNKVRRELDAKLAEIRQLQMKLNGGEQhafgiSRENLKEVNKALEKE 294
Cdd:COG4717 44 RAMLLERlEKEADELFKPQGRKPELNLKE-LKELEEELKEAEEKEEEYAELQEELEELEE-----ELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 295 NNELKLKRSELEAALEASQKSTSRKLFPKSTEDLSRHLSSLdeekagtfpgkEDMEKSLQRLEKELEEARREKDKARQEL 374
Cdd:COG4717 118 LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-----------RELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 375 KRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQilgLEKALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKLAN 454
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE---LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 455 CLRTIDSKNVELLNLQTALGQ---YYAEIEAKEHFERELAVAKEDAMKLSARLKD--VDEQLESSKKEKEEITSKVLHAE 529
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGllaLLFLLLAREKASLGKEAEELQALPALEELEEeeLEELLAALGLPPDLSPEELLELL 343
|
330 340 350
....*....|....*....|....*....|..
gi 30690248 530 NIAAEWKNRVSKVEDDNAKVRR-VLEQSMTRL 560
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLeELEQEIAAL 375
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
347-438 |
5.02e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 347 EDMEKSLQRLEKELEEARREKDKARQE-LKRLKQHLLEKETE--------ESEKmdEDSRLIDELRQTNEYQRSQILGLE 417
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEElealkarwEAEK--ELIEEIQELKEELEQRYGKIPELE 491
|
90 100
....*....|....*....|.
gi 30690248 418 KALRQTMANQEEIKSSSDLEI 438
Cdd:COG0542 492 KELAELEEELAELAPLLREEV 512
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
346-517 |
5.44e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 346 KEDMEKSLQRLEKELEEARREKDKARQELKRLKQ--HLLEKETEESEKMDEDSRLIDELRQTNEyQRSQILGLEKALRQT 423
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARA-ELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 424 MANQEEIKS--SSDLEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKEhfERELAVAKEDAMKLS 501
Cdd:COG3206 249 LGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA--QRILASLEAELEALQ 326
|
170
....*....|....*.
gi 30690248 502 ARLKDVDEQLESSKKE 517
Cdd:COG3206 327 AREASLQAQLAQLEAR 342
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
231-441 |
5.57e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 231 KEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNGgeqhafgiSRENLKEVNKALEKENNELKLKRSELEAALE 310
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA--------LQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 311 ASQKSTSRKLF------PKSTEDLSRHLSSLDEEKAGTfpgkEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEK 384
Cdd:COG3883 94 ALYRSGGSVSYldvllgSESFSDFLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30690248 385 ETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKS 441
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| c_cpa1 |
TIGR00844 |
na(+)/h(+) antiporter; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36) The ... |
96-362 |
7.91e-04 |
|
na(+)/h(+) antiporter; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36) The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals. Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in (1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles. This model is specific for the fungal members of this family. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273295 [Multi-domain] Cd Length: 810 Bit Score: 42.99 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 96 KEKEDQISRLNQENGSL---KQNLTSTNaalkesrlDLSRASNNNAIKGNGdHSPNRSQRSPTNWKNRNQMNNGIASKpN 172
Cdd:TIGR00844 520 KEMEDDIEMNDLGRERLqkeKEAHAATF--------DLSTTTTTQLGTENG-RGGGLEERSKTNIKERSENVNTIYGL-D 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 173 GTENDSESH-------------KKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQE------ERKQNETF--- 230
Cdd:TIGR00844 590 KLARDTENRdvtyvptsrydgiESEIDDVYTYENDSESIASSERRRIKKLREEEQQAYIAYTEdnqviiENRQGEILeyv 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 231 KEELQSLRlDKEKTLMESNKVRRELDAKLAEIRQLQMKLNGGEQHAFGISRENLkevnkaLEKENNELkLKRSELeaale 310
Cdd:TIGR00844 670 DIHDRGAR-DAEVGVHNGGRLKRALSPPLEKLHQITNEAKKSKYYAYKVGNDLI------IEDESGEV-FRRYRI----- 736
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 30690248 311 aSQKSTSRKLFPKSTEdlsrhLSSLDEEKAGTFPGK--EDMEKSLQRLEKELEE 362
Cdd:TIGR00844 737 -SPHGGKRKIKKRNDS-----VVSVDEEKAIEGPSRvpERGNHDLLHSEDEMAD 784
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
191-432 |
8.88e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 191 LEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEKTLMES-----NKVRRELDAKLAEIRQL 265
Cdd:PRK05771 33 IEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDveeelEKIEKEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 266 QMKLnggeqhafgisrenlkevnKALEKENNELK-LKRSELEAALEASQKSTSRKLFPKSTEDLSRhlSSLDEEKAGTFP 344
Cdd:PRK05771 113 ENEI-------------------KELEQEIERLEpWGNFDLDLSLLLGFKYVSVFVGTVPEDKLEE--LKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 345 GKEDMEKS------LQRLEKELEEARREKDKARQEL---KRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILG 415
Cdd:PRK05771 172 ISTDKGYVyvvvvvLKELSDEVEEELKKLGFERLELeeeGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLA 251
|
250
....*....|....*..
gi 30690248 416 LEKALRQtMANQEEIKS 432
Cdd:PRK05771 252 LYEYLEI-ELERAEALS 267
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
282-544 |
1.07e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 282 ENLKEVNKALEKENNELK--LKRSE-LEAALEASQKSTSRKLfpKSTEDLSRHLSSLDEEKAGTFPGKEDMEKslqrLEK 358
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEkfIKRTEnIEELIKEKEKELEEVL--REINEISSELPELREELEKLEKEVKELEE----LKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 359 ELEEARREKDKARQELKRLKQHL------LEKETEESEKMDEDSRLIDELRQTNEyQRSQILGLEKALRQTMANQEEIKS 432
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIreleerIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 433 SSDLEIRKSKGIIEDLNQKlanclrtiDSKNVELLNLQTALGQYYAEIEAKEHFERELAVAKEDAMKLSARLK-----DV 507
Cdd:PRK03918 318 RLEEEINGIEERIKELEEK--------EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgltpeKL 389
|
250 260 270
....*....|....*....|....*....|....*..
gi 30690248 508 DEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVED 544
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
346-569 |
1.25e-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: 41.67 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 346 KEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESE---KMDEDSRLIDELRQTNEYQRSQILGLEKALRQ 422
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 423 TMANQEEIKSSSDLEIRKSKgiiEDLNQKLANcLRTIDSKNVELLNLQTALGQYYAEIEAKEhfeRELAVAKEDAMKLSA 502
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSP---EDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALR---AELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30690248 503 RLKDVDEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVEDDNAKVRRVLEQSMTRLNRMSMDSDF 569
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
57-515 |
1.37e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 57 NGFESPVNPEIERYKAEI-NKLQKSESEIKALSVNYAALLKEKEDQISRLNQENgslkQNLTSTNAALKESRLDLSRASN 135
Cdd:COG5022 938 NNIDLEEGPSIEYVKLPElNKLHEVESKLKETSEEYEDLLKKSTILVREGNKAN----SELKNFKKELAELSKQYGALQE 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 136 NNaikgngdhspnrsqrsptnwKNRNQMNNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMA-----SAQARELEKER 210
Cdd:COG5022 1014 ST--------------------KQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLennqlQARYKALKLRR 1073
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 211 EKSANLQILLQEERKQNETFKEelqslrldKEKTLMESNKVRRELDAKLAEIRQLQMKLNGGEQHafgiSRENLKEVNKA 290
Cdd:COG5022 1074 ENSLLDDKQLYQLESTENLLKT--------INVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQE----ISKFLSQLVNT 1141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 291 LEKENNelKLKRSELEAALEASQKSTSRKLFPKSTEDLSRhlSSLDEEKAGTFPGKEDMEkSLQRLEKELEEARReKDKA 370
Cdd:COG5022 1142 LEPVFQ--KLSVLQLELDGLFWEANLEALPSPPPFAALSE--KRLYQSALYDEKSKLSSS-EVNDLKNELIALFS-KIFS 1215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 371 RQELKRLKQHLLEKE---TEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKSKGIIed 447
Cdd:COG5022 1216 GWPRGDKLKKLISEGwvpTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYI-- 1293
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30690248 448 lNQKLANCLRTIDSKnvellnlqtalgqyyaeIEAKEHFERELAVAKEDAMKLSARLKDVDEQLESSK 515
Cdd:COG5022 1294 -NVGLFNALRTKASS-----------------LRWKSATEVNYNSEELDDWCREFEISDVDEELEELI 1343
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
220-442 |
1.44e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.13 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 220 LQEERKQNETFKEELQslrlDKEKTLMESNKVRRELDAKLAEIRQLQMKLNGGEQHAFG----ISRENLKEVNKALEKEN 295
Cdd:NF012221 1547 VSKHAKQDDAAQNALA----DKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALEtngqAQRDAILEESRAVTKEL 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 296 NELKLKRSELEAALEASQKSTSRKLFPKSTEDLSRHLSSLDEEKAGTfpgKEDMEKSLQRLEKELEEARREKDKARQELK 375
Cdd:NF012221 1623 TTLAQGLDALDSQATYAGESGDQWRNPFAGGLLDRVQEQLDDAKKIS---GKQLADAKQRHVDNQQKVKDAVAKSEAGVA 1699
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30690248 376 RLKQHLLEKETE-ESEKMDEDSRLIDELRQTNEYQRSQilglEKAlrQTMANQEEIKSSSDLEIRKSK 442
Cdd:NF012221 1700 QGEQNQANAEQDiDDAKADAEKRKDDALAKQNEAQQAE----SDA--NAAANDAQSRGEQDASAAENK 1761
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
64-552 |
1.70e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 64 NPEIERYKAEINKLQKSES----EIKALSVNYAALLKEKEDQISRLNQENgSLKQNLTSTNAALKESRLDLSRASNNNAI 139
Cdd:PRK01156 196 NLELENIKKQIADDEKSHSitlkEIERLSIEYNNAMDDYNNLKSALNELS-SLEDMKNRYESEIKTAESDLSMELEKNNY 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 140 KGNGDHSPNRSQRSPTnWKNRNQMN------NGIASKPNGTEN-DSE------SHKK----EKEFAEMLEERTR-SMASA 201
Cdd:PRK01156 275 YKELEERHMKIINDPV-YKNRNYINdyfkykNDIENKKQILSNiDAEinkyhaIIKKlsvlQKDYNDYIKKKSRyDDLNN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 202 QARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLN---GGEQHAFG 278
Cdd:PRK01156 354 QILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISskvSSLNQRIR 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 279 ISRENLKEVNKAL-----------------EKENNELKLKRSELEAALEASQKSTSRKLfpKSTEDLSRHLSSLDEEKAG 341
Cdd:PRK01156 434 ALRENLDELSRNMemlngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEV--KDIDEKIVDLKKRKEYLES 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 342 TFPGK--------EDMEKSLQRLEKELEEARREKDKARQ---ELKRLKQHLLEKETEESEKMDE--DSRLIDELRQTNEY 408
Cdd:PRK01156 512 EEINKsineynkiESARADLEDIKIKINELKDKHDKYEEiknRYKSLKLEDLDSKRTSWLNALAviSLIDIETNRSRSNE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 409 QRSQILGLEKALRQTMANQEEIKSSSDLEIRKskgiIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKEHFER 488
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSYIDKSIRE----IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIP 667
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690248 489 ELAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVEDDNAKVRRV 552
Cdd:PRK01156 668 DLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-542 |
1.87e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 179 ESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEElqSLRLDKEKTLMESNKVRRELDAK 258
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE--EKKKADEAKKAEEKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 259 LAEIRQLQMKLNGGEQhafgiSRENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLFPKSTEDLSRHLSSLDEE 338
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEE-----AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 339 KAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEK 418
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 419 ALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKlANCLRTIDSKNVELLNLQTALGQYYAEiEAKEHFERELA------- 491
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKAdeakkae 1543
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 30690248 492 -VAKEDAMKLSARLKDVDE--QLESSKKEKEEITSKVLHAENIAAEWKNRVSKV 542
Cdd:PTZ00121 1544 eKKKADELKKAEELKKAEEkkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
175-315 |
2.00e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 175 ENDSESHKKEKEFA---EMLEERtrsmasaqaRELEKE-REKSANLQILLQEERKQNETFKEELQSLRLDK---EKTLME 247
Cdd:PRK12704 48 KKEAEAIKKEALLEakeEIHKLR---------NEFEKElRERRNELQKLEKRLLQKEENLDRKLELLEKREeelEKKEKE 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690248 248 SNKVRRELDAKLAEIRQLQMKLNGGEQHAFGISRENLKEVnkALEKENNELK------LKRSELEAALEASQKS 315
Cdd:PRK12704 119 LEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEI--LLEKVEEEARheaavlIKEIEEEAKEEADKKA 190
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
67-439 |
2.10e-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: 41.64 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 67 IERYKAEINKLQKSESEIKALSvnyaALLKEKEDQISRLNQENGSLKqnltstnaalkeSRLDLsRASNNNAIKGNGDHS 146
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLT----ASLQEKERAIEATNAEITKLR------------SRVDL-KLQELQHLKNEGDHL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 147 pnrsqrsptnwknRNQMNNGIASKPNGTENDSESHKKEKEFAEMLE-----ERTRSMASAQARELEKE----REKSANLQ 217
Cdd:pfam15921 544 -------------RNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhGRTAGAMQVEKAQLEKEindrRLELQEFK 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 218 ILLQEERKQNETFKEELQSLRLDKEK-------TLMESNKVRRELDAKLAEIRQLQMKLNGGEQHaFGISRENLKEVNKA 290
Cdd:pfam15921 611 ILKDKKDAKIRELEARVSDLELEKVKlvnagseRLRAVKDIKQERDQLLNEVKTSRNELNSLSED-YEVLKRNFRNKSEE 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 291 LEKENNELKLKRSELEAALEASQKSTsrklfpKSTEDLSRHLSSLDEEKAGTFPGK----EDMEKSLQRLEKELEEARRE 366
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQTRNTL------KSMEGSDGHAMKVAMGMQKQITAKrgqiDALQSKIQFLEEAMTNANKE 763
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30690248 367 KDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIR 439
Cdd:pfam15921 764 KHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-513 |
3.29e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 66 EIERYKAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQENGSLKQNLTSTNAALK--ESRLDLSRASNNNAIKGNG 143
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEeaEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 144 DHSPNRSQRSpTNWKNRNQMNNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEE 223
Cdd:COG1196 369 EAEAELAEAE-EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 224 RKQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLN-------GGEQHAFGISRENLKEVNKALEKENN 296
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLllleaeaDYEGFLEGVKAALLLAGLRGLAGAVA 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 297 ELKLKRSELEAALEASQKSTSRKLFPKSTEDLSRHLSSLDEEKAG--TFPGKEDMEKS---------------------- 352
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGraTFLPLDKIRARaalaaalargaigaavdlvasd 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 353 -------LQRLEKELEEARREKDKARQELKRLKQhLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMA 425
Cdd:COG1196 608 lreadarYYVLGDTLLGRTLVAARLEAALRRAVT-LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 426 NQEEIKSSSDLEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKEHFERELAVAKEDAM----KLS 501
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELE 766
|
490
....*....|..
gi 30690248 502 ARLKDVDEQLES 513
Cdd:COG1196 767 RELERLEREIEA 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
66-534 |
3.35e-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: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 66 EIERYKAEINKLQKSESEIKALSVNYaallKEKEDQISRLNQENGSLKQNLTSTNAALKESRLDLSRASNN-NAIKGNGD 144
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNLKKKIQKN----KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlNQLKDEQN 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 145 HSPNRSQRSPTNWKNRNQMNNGIASKPNGTENDSESHKKEKEfaemlEERTRSMASaqarELEKEREKSANLQILLQEER 224
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE-----QDWNKELKS----ELKNQEKKLEEIQNQISQNN 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 225 KQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQmklngGEQHAFGISRENLKEVNKALEKENNELKLKRSE 304
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK-----KENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 305 LEAALEASQKSTSR-----KLFPKSTEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQ 379
Cdd:TIGR04523 410 KDEQIKKLQQEKELlekeiERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 380 HLLEKETEESEKMDEDSRL----------IDELRQTNEYQRSQILGLEKALRQTmaNQEEIKSSSDLEIRKSKGIIEDLN 449
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELeekvkdltkkISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEIDEKN 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 450 QKLANCLRTIDSKNVELLNLQTALGQYYAEIEA-----------KEHFERELAVAKEDAMKLSARLKDVDEQLESSKKEK 518
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDlikeieekekkISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
490
....*....|....*.
gi 30690248 519 EEITSKVLHAENIAAE 534
Cdd:TIGR04523 648 KQIKETIKEIRNKWPE 663
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
326-452 |
3.66e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 326 EDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKarqeLKRLKQHLLEKETEESEKMDEDSRLIDELRQT 405
Cdd:PRK09039 56 DRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSR----LQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 30690248 406 NEYQRSQILGLEK---ALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKL 452
Cdd:PRK09039 132 SARALAQVELLNQqiaALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
55-411 |
3.85e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 55 MANGFESPVNPEIERYKAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQENGSLKQNLtstnaalkesrldlsras 134
Cdd:TIGR02169 727 QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL------------------ 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 135 nnnaikgngdhspnrsqrsptnwknrnqmnngiaskpngteNDSESHKKEKEFAEMLEERTRsmASAQARELEKEREKSA 214
Cdd:TIGR02169 789 -----------------------------------------SHSRIPEIQAELSKLEEEVSR--IEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 215 NLQILLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNGgeqhafgiSRENLKEVNKALEKE 294
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES--------RLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 295 NNELKLKRSELEAALEASQKSTSRKLFPKSTedLSRHLSSLDEEKA------GTFPGKEDMEKSLQRLEKELEEARREKD 368
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEA--LEEELSEIEDPKGedeeipEEELSLEDVQAELQRVEEEIRALEPVNM 975
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 30690248 369 KARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRS 411
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
160-519 |
4.02e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 160 RNQMNNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRL 239
Cdd:PTZ00121 1063 KAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKA 1142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 240 DKEKTLMESNKV---RRELDAKLAEIRQLQMKLNGGEQHAFGISRENLKEVNKALEKENNELKLKRSELEAALEASQKST 316
Cdd:PTZ00121 1143 EEARKAEDAKRVeiaRKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 317 SRKL--------FPKSTEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKR----LKQHLLEK 384
Cdd:PTZ00121 1223 AKKAeavkkaeeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkadeAKKAEEKK 1302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 385 ETEESEKMDEDSRLIDELRQTNEYQRSQILGL-----EKALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKLANCLRTI 459
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKADAAkkkaeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 460 DSKNVELLNLQTALGQYYAEIEAKEHFERELAVAKEDAMKLSARLKDVDEQLESSKKEKE 519
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-366 |
4.46e-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: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 66 EIERYKAEINKLQK----SESEIKALSVNYAALLKEKE---DQISRLNQENGSLKQNLTSTNAALKESRLDLSRASNNNA 138
Cdd:TIGR02168 706 ELEELEEELEQLRKeleeLSRQISALRKDLARLEAEVEqleERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 139 I------KGNGDHSPNRSQRSPTNwKNRNQMNNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAQAR---ELEKE 209
Cdd:TIGR02168 786 EleaqieQLKEELKALREALDELR-AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 210 REKSANLQI---LLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIR----QLQMKLNGGEQHAFGIsRE 282
Cdd:TIGR02168 865 EELIEELESeleALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELReklaQLELRLEGLEVRIDNL-QE 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 283 NLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKL---------FPKSTEDLSRHLSSLDEEKagtfpgkEDMEKSL 353
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnlaAIEEYEELKERYDFLTAQK-------EDLTEAK 1016
|
330
....*....|...
gi 30690248 354 QRLEKELEEARRE 366
Cdd:TIGR02168 1017 ETLEEAIEEIDRE 1029
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
170-396 |
5.18e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 170 KPNGTENDSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEE------LQSLRLDKEK 243
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakkAEELKKKEAE 1713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 244 TLMESNKVRRELDAKLAEIRQLQMKLNGGEQHA--FGISRENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLF 321
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30690248 322 PKSTEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDS 396
Cdd:PTZ00121 1794 MEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEA 1868
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
290-431 |
7.17e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 290 ALEKENNE-LKLKRSELEAALEASQKSTSRklfpkstedlsrhLSSLDEEKAGTfpgKEDMEKSLQRLEKELEEARREKD 368
Cdd:PRK09039 70 SLERQGNQdLQDSVANLRASLSAAEAERSR-------------LQALLAELAGA---GAAAEGRAGELAQELDSEKQVSA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 369 KARQELKRLKQHL---------LEKETEESEKMDEDSR-------------LIDELRQTNEYqRSQILGlekALRQTMAN 426
Cdd:PRK09039 134 RALAQVELLNQQIaalrrqlaaLEAALDASEKRDRESQakiadlgrrlnvaLAQRVQELNRY-RSEFFG---RLREILGD 209
|
....*
gi 30690248 427 QEEIK 431
Cdd:PRK09039 210 REGIR 214
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
193-407 |
7.47e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 193 ERTRSMASAQARELEKEREKSANLQILLQEERKQNET----FKEELQSLRLDKEktlMESNKVRR------ELDAKLAEI 262
Cdd:pfam01576 853 ERARRQAQQERDELADEIASGASGKSALQDEKRRLEAriaqLEEELEEEQSNTE---LLNDRLRKstlqveQLTTELAAE 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 263 RQLQMKLNGGEQHafgisrenlkevnkaLEKENNELKLKRSELEAALEASQKSTSRKLFPKsTEDLSRHLSSLDEEKAGT 342
Cdd:pfam01576 930 RSTSQKSESARQQ---------------LERQNKELKAKLQEMEGTVKSKFKSSIAALEAK-IAQLEEQLEQESRERQAA 993
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30690248 343 FPGKEDMEKSLQRLEKELEEARR-------EKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNE 407
Cdd:pfam01576 994 NKLVRRTEKKLKEVLLQVEDERRhadqykdQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATE 1065
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
177-525 |
8.05e-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: 39.72 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 177 DSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQslrlDKEKTLMESNKVRRE-- 254
Cdd:pfam15921 197 EEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQ----NKIELLLQQHQDRIEql 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 255 LDAKLAEIRQLQMKLNGGEQHAFGISREnLKEVNKALEKENNELKLKRSELEAALeasqkstsrklfpkstedlSRHLSS 334
Cdd:pfam15921 273 ISEHEVEITGLTEKASSARSQANSIQSQ-LEIIQEQARNQNSMYMRQLSDLESTV-------------------SQLRSE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 335 LDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQE-------LKRLKQHLLEKETEESEKMDEDSRL--------- 398
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnlddqLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsi 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 399 -IDELRQTNEYQRSQILGLEKALRQtmanqeeIKSSSDLEIRKSKGIIEDLNQKlancLRTIDSKNVELLNLQTALGQYY 477
Cdd:pfam15921 413 tIDHLRRELDDRNMEVQRLEALLKA-------MKSECQGQMERQMAAIQGKNES----LEKVSSLTAQLESTKEMLRKVV 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 30690248 478 AEIEAKehfERELAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSKV 525
Cdd:pfam15921 482 EELTAK---KMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV 526
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
160-430 |
8.45e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 39.47 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 160 RNQMNNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAQARELEKEREKS-ANLQILLQEERKQNETFKEELQSLR 238
Cdd:pfam02029 41 HNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIAdEKESVAERKENNEEEENSSWEKEEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 239 LDKEKTLMESN-KVRRELDAKLAEIRQLQMKLNGGEQHAFGISRENLKEVNKALEKENNELKLKRSELEAALEASQKSTS 317
Cdd:pfam02029 121 RDSRLGRYKEEeTEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 318 RKLFPKST-----EDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKE--LEEARREKD-KARQELKRLKQHLLEKETEES 389
Cdd:pfam02029 201 KRGHPEVKsqngeEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEqkLEELRRRRQeKESEEFEKLRQKQQEAELELE 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 30690248 390 E---KMDEDSRLIDELRQTNEYQRSQILGLEKALRQTManQEEI 430
Cdd:pfam02029 281 ElkkKREERRKLLEEEEQRRKQEEAERKLREEEEKRRM--KEEI 322
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
282-521 |
8.87e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.22 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 282 ENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLFPKSTEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELE 361
Cdd:pfam05262 216 QQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDE 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 362 EARREKDKARQELKRlkqhllekETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKs 441
Cdd:pfam05262 296 EALKAKDHKAFDLKQ--------ESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSNPVYGLK- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 442 kgIIEDlnQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKEHferELAVAKEDAMKLSARLKDVD-EQLESSKKEKEE 520
Cdd:pfam05262 367 --VVDP--ITNLSELVLIDLKTEVRLRESAQQTIRRRGLYEREK---DLVAIAITSGNAKLQLVDIDlKNLEVIKESNFE 439
|
.
gi 30690248 521 I 521
Cdd:pfam05262 440 I 440
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
184-530 |
9.64e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 184 EKEFAEMLEERTRSMASAQARELEKEREKsanLQILLQEERKQNETFKEELQSLRldkeKTLMESNKVRRELDAKLAEIR 263
Cdd:COG4717 108 EAELEELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 264 QLQMKLNGGEQHAFGISRENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLFPKSTEDLSRHLSSL-------- 335
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLliaaalla 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 336 -------DEEKAGTFPG---------------KEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMD 393
Cdd:COG4717 261 llglggsLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 394 EDSRLIDELRQtneyQRSQILGLEKALRQtmaNQEEIKSSSDLEIRKSKGiIEDLNQKLANcLRTIDSKNVELLNLQTAL 473
Cdd:COG4717 341 ELLDRIEELQE----LLREAEELEEELQL---EELEQEIAALLAEAGVED-EEELRAALEQ-AEEYQELKEELEELEEQL 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 30690248 474 GQYYAEIEAKEHFERELAVAKEDAmKLSARLKDVDEQLESSKKEKEEITSKVLHAEN 530
Cdd:COG4717 412 EELLGELEELLEALDEEELEEELE-ELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
76-534 |
9.68e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.32 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 76 KLQKSESEIKALSVNYAALLKEKEDQISRLNQENGSLKQNLTSTNAALKESRLDLSRASNNNAIKGNGDHSPNRSQRSPT 155
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 156 NWKN--RNQMNNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAQARE---LEKEREKSANLQILLQEERKQNETF 230
Cdd:pfam05483 296 KELEdiKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHsfvVTEFEATTCSLEELLRTEQQRLEKN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 231 KEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNggeqhafgiSRENLKEVNKALEKENNELKLKRSELEAALE 310
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILA---------EDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 311 ASQK------------STSRKLFPKSTEDLSrhlSSLDEEKAGTFpgkeDMEKSLQRLEKELEEARREKDKARQELKRLK 378
Cdd:pfam05483 447 AREKeihdleiqltaiKTSEEHYLKEVEDLK---TELEKEKLKNI----ELTAHCDKLLLENKELTQEASDMTLELKKHQ 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 379 QHLLEKETEESEKMDEDSRLID---ELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKLANC 455
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLEEkemNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690248 456 LRTID--SKNVELLNLQTALGQYYAEIEAKEHFERELAVAKEDAMKLSARLK------DVDEQLESSKKEKEEITSKVLH 527
Cdd:pfam05483 600 KKQIEnkNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKfeeiidNYQKEIEDKKISEEKLLEEVEK 679
|
....*..
gi 30690248 528 AENIAAE 534
Cdd:pfam05483 680 AKAIADE 686
|
|
| |
