|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-393 |
2.67e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 84 VQKGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQ------Q 153
Cdd:TIGR02168 655 VRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQisalrkD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 154 AEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQ---ELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCR 227
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 228 MQNELEDMERIRGDYEMEIASLRAEMEmkssEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERW 307
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLE----DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 308 LQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC--------CELEELQHHRQVSEEEQRRL 379
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysLTLEEAEALENKIEDDEEEA 970
|
330
....*....|....
gi 319655558 380 QRELKCAQNEVLRF 393
Cdd:TIGR02168 971 RRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-347 |
6.76e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 101 LSLTETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELRSLREEISlleh 180
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLE---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEmEIASLRAEMEMKSSEP 260
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 261 SEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQ 340
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
....*..
gi 319655558 341 LRDAEEQ 347
Cdd:COG1196 479 LAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-402 |
3.24e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftkQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 181 EKE---SELKEIEQELHLAQAEIQSLRQA---AEDSATEHESDIASLQEDLCRMQNELEdmerirgdyemEIASLRAEME 254
Cdd:TIGR02168 303 QKQilrERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELE-----------ELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 255 MKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSmtsaesqtsemdflepDPEM 334
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE----------------EAEL 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655558 335 QLLRQQLRDAEEqmhgmknkcqelccELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQS 402
Cdd:TIGR02168 436 KELQAELEELEE--------------ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
107-395 |
3.59e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftKQIQQLQGELRSLREEISLLE---HEKE 183
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE---RQKEAIERQLASLEEELEKLTeeiSELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 184 SELKEIEQELHLAQAEIQSL-----RQAAEDSAtEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkss 258
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE---- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 259 EPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLEsERTQRATERWLQSQT-LSMTSAESQTSEMDFLEPDPEMQLL 337
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD-KEFAETRDELKDYREkLEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 319655558 338 RQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQT 395
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-383 |
6.17e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 105 ETELEELRAQV------LQLVAELEETRELAGQHEDDSLELQ-GLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:COG1196 199 ERQLEPLERQAekaeryRELKEELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 178 L----------EHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIA 247
Cdd:COG1196 279 LeleleeaqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 248 SLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEmdf 327
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE--- 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 319655558 328 lepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQREL 383
Cdd:COG1196 436 -----EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-349 |
1.65e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 108 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELRSLREEISLLEhEKESE 185
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 186 LKEIEQELHLAQAEIQSLRQ---AAEDSATEHESDIASLQEDLCRMQNELEDME-------------------------R 237
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEdlarlelralleerfaaalgdaverE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 238 IRGDYEMEIASLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTs 317
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNENSI- 845
|
250 260 270
....*....|....*....|....*....|..
gi 319655558 318 aESQTsemDFLepdpemQLLRQQLRDAEEQMH 349
Cdd:COG4913 846 -EFVA---DLL------SKLRRAIREIKERID 867
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-402 |
3.92e-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: 58.93 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 161 IQQLQGELRSLREEISLLE---HEKESELKEIEQELHLAQAEIQSLRQAAEDSA---TEHESDIASLQEDLCRMQNELED 234
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 235 MERIRGDYEMEIASLRAEMEmkssepSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESErtqraterwLQSQTLS 314
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALN------DLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK---------LNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 315 MTSAESqtsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQ 394
Cdd:TIGR02169 828 KEYLEK------------EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
....*...
gi 319655558 395 TSHSVTQS 402
Cdd:TIGR02169 896 AQLRELER 903
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-264 |
6.41e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 98 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 178 LEH----------EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIA 247
Cdd:COG4913 364 LEAllaalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
170
....*....|....*..
gi 319655558 248 SLRAEMEMKSSEPSEEL 264
Cdd:COG4913 444 ALRDALAEALGLDEAEL 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-302 |
1.54e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIEELES 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 181 EKESELKE---IEQELHLAQAEIQSL----------RQAAEDSATEHESDIASLQEDLCRMQNELEDM-ERIRGDYEMEI 246
Cdd:TIGR02168 874 ELEALLNErasLEEALALLRSELEELseelreleskRSELRRELEELREKLAQLELRLEGLEVRIDNLqERLSEEYSLTL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 247 ASLRAEMEMKSSEPS------------------------EELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQR 302
Cdd:TIGR02168 954 EEAEALENKIEDDEEearrrlkrlenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
148-366 |
1.90e-08 |
|
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: 55.93 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 148 LASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKES---ELKEIEQELHLAQAEIQSLRQ---AAEDSATEHESDIASL 221
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQelaALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 222 QEDLCRMQNELEdmERIRGDYEMEIASlrAEMEMKSSEPSEELQELRERYHFLNEEYRALQEsnsSLTGQLADLESERTQ 301
Cdd:COG4942 96 RAELEAQKEELA--ELLRALYRLGRQP--PLALLLSPEDFLDAVRRLQYLKYLAPARREQAE---ELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 319655558 302 RATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ 366
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-290 |
4.85e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQqaevFTKQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 181 EKESELKEIEQ--------ELHLAQAEIQSLRQAAEDSATEHEsdiaSLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:TIGR02168 415 RRERLQQEIEEllkkleeaELKELQAELEELEEELEELQEELE----RLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 319655558 253 MEMkssepseeLQELRERYHFLNEEYRALQESNSSLTG 290
Cdd:TIGR02168 491 LDS--------LERLQENLEGFSEGVKALLKNQSGLSG 520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
96-301 |
6.55e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 96 NKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaevftkqIQQLQGELRSLREEI 175
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-------------IPEIQAELSKLEEEV 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 176 SLLE---HEKESELKEIEQELHLAQAEIQSL---RQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL 249
Cdd:TIGR02169 808 SRIEarlREIEQKLNRLTLEKEYLEKEIQELqeqRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 319655558 250 RAEMEmkssEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQ 301
Cdd:TIGR02169 888 KKERD----ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-394 |
1.31e-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: 53.91 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 153 QAEVFTKQIQQLQGELRSLREEISllehEKESELKEIEQELHLAQAEIQSLRqaaeDSATEHESDIASLQEDLCRMQNEL 232
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELK----EAEEELEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 233 EDMERIRGDYEMEIASLRAEMEMKSsepsEELQELRERYHFLNEEYRALQESNSSLTGQLADLESErtqraterwlqsqt 312
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELE----AQLEELESKLDELAEELAELEEKLEELKEELESLEAE-------------- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 313 LSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLR 392
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
..
gi 319655558 393 FQ 394
Cdd:TIGR02168 440 AE 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-383 |
3.42e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 101 LSLTETELEELRAQVLQLvaelEETRELAGQHEDDSLELQGLledERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:COG4913 237 LERAHEALEDAREQIELL----EPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 181 EKEselkEIEQELHLAQAEIQSLRQAAEDSATEhesDIASLQEDLCRMQNELEDMERIRGDYEMEIASLraemEMKSSEP 260
Cdd:COG4913 310 ELE----RLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAAL----GLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 261 SEELQELRERyhflneeyralqesnssLTGQLADLESERTQraterwlqsqtlsmtsaesqtsemdflepdpemqlLRQQ 340
Cdd:COG4913 379 AEEFAALRAE-----------------AAALLEALEEELEA-----------------------------------LEEA 406
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 319655558 341 LRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQREL 383
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
105-246 |
4.27e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELRSLREEISLLEheke 183
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 319655558 184 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 246
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-304 |
5.72e-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: 51.99 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 99 RGLSLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGL------LEDERLASAQQAEVFTKQIQQLQGEL 168
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLaeieELEREIEEERKRRDKLteeyaeLKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 169 RSLREEISLLEHEKES------ELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDY 242
Cdd:TIGR02169 388 KDYREKLEKLKREINElkreldRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655558 243 EMEIASLRAEMEMKSSEPSEELQEL------------RERYHFLNEEyrALQESNSSLTGQLADLESERTQRAT 304
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELaeaeaqaraseeRVRGGRAVEE--VLKASIQGVHGTVAQLGSVGERYAT 539
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-283 |
7.57e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLED---ERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHE 181
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEElaeELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 182 KESELKEIEQELHLAQAEIQSLRQAAEDSAtEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMksseps 261
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL------ 495
|
170 180
....*....|....*....|..
gi 319655558 262 eeLQELRERYHFLNEEYRALQE 283
Cdd:COG1196 496 --LLEAEADYEGFLEGVKAALL 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
158-383 |
8.50e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 158 TKQIQQLQGELRSLREEISLLehekESELKEIEQELHLAQAEIQSLRQAAEDSatEHESDIASLQEDLCRMQNELEDMEr 237
Cdd:COG4913 609 RAKLAALEAELAELEEELAEA----EERLEALEAELDALQERREALQRLAEYS--WDEIDVASAEREIAELEAELERLD- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 238 irgdyemeiaslraememkssEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlqsQTLSMTS 317
Cdd:COG4913 682 ---------------------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL----DELQDRL 736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319655558 318 AESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHgmknkcqelccelEELQHHRQVSEEEQRRLQREL 383
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELR-------------ENLEERIDALRARLNRAEEEL 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
138-389 |
1.27e-06 |
|
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: 50.79 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 138 ELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEIS-------------------LLEHEKESE-----LKEIEQEL 193
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISntqtqlnqlkdeqnkikkqLSEKQKELEqnnkkIKELEKQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 194 HLAQAEIQSLR-QAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSEELQELRER-- 270
Cdd:TIGR04523 291 NQLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKqn 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 271 -YHFLNEEYRALQESNSSLTGQLADLESE-RTQRATERWLQSQTlsmtsaesQTSEMDFLEPDPEMQLLRQQLRDAEEQM 348
Cdd:TIGR04523 371 eIEKLKKENQSYKQEIKNLESQINDLESKiQNQEKLNQQKDEQI--------KKLQQEKELLEKEIERLKETIIKNNSEI 442
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 319655558 349 HGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 389
Cdd:TIGR04523 443 KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-302 |
3.16e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 98 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 178 LEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEheSDIASLQEDLCRMQNELEDMERIrgdyemeiaSLRAEmemks 257
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEP--PDLEELERELERLEREIEALGPV---------NLLAI----- 787
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 319655558 258 sepsEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQR 302
Cdd:COG1196 788 ----EEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-314 |
3.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 138 ELQGLLEDERLASAQQAEVF--TKQIQQLQGELRSLREEISLLEHEKES-----ELKEIEQELHLAQAEIQSLRQAAEdS 210
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAelQEELEELEEELEELEAELEELREELEKlekllQLLPLYQELEALEAELAELPERLE-E 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 211 ATEHESDIASLQEDLCRMQNELEDMERIRgdyEMEIASLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTG 290
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180
....*....|....*....|....
gi 319655558 291 QLADLESERTQRATERWLQSQTLS 314
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLL 251
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
99-283 |
4.83e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 99 RGLSLtETELEELRAQVLqlvAELEETRELAGQHEDDSLELqgllEDERlasaqqaevftkqIQQLQGELRSLREEISLL 178
Cdd:COG2433 374 RGLSI-EEALEELIEKEL---PEEEPEAEREKEHEERELTE----EEEE-------------IRRLEEQVERLEAEVEEL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 179 E---HEKESELKEIEQELHLAQAEiqslrqaaEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRaemEM 255
Cdd:COG2433 433 EaelEEKDERIERLERELSEARSE--------ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLK---EL 501
|
170 180
....*....|....*....|....*...
gi 319655558 256 KSSEPSEELQELRERYHFLNEEYRALQE 283
Cdd:COG2433 502 WKLEHSGELVPVKVVEKFTKEAIRRLEE 529
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
99-261 |
1.03e-05 |
|
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: 47.45 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 99 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 168
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 169 RSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIAS 248
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170
....*....|...
gi 319655558 249 LRAEMEMKSSEPS 261
Cdd:COG4942 232 LEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-305 |
1.41e-05 |
|
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: 47.07 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 104 TETELEELRAQVLQLVAELEETRElagqheddslelqglledERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHE-- 181
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKK------------------EEKALLKQLAALERRIAALARRIRALEQELAALEAEla 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 182 -KESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERI---RGDYEMEIASLRAEMEMKS 257
Cdd:COG4942 87 eLEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLapaRREQAEELRADLAELAALR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 319655558 258 SEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATE 305
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
140-384 |
1.48e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 140 QGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEiqSLRQAAEDSA----TEHE 215
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 216 SDIASLQEDLCRMQNE--LEDMERIRgdyEMEIAslraeMEMKSSEPSEELQELRERYhflNEEYRalQESNSSLTGQLa 293
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIR---QEEIA-----MEISRMRELERLQMERQQK---NERVR--QELEAARKVKI- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 294 dLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPD--PEMQLLRQQLRDAEEQMHGMKNKCQEL---CCELEELQHH 368
Cdd:pfam17380 407 -LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEEraREMERVRLEEQERQQQVERLRQQEEERkrkKLELEKEKRD 485
|
250
....*....|....*..
gi 319655558 369 RQVSEEEQRR-LQRELK 384
Cdd:pfam17380 486 RKRAEEQRRKiLEKELE 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
96-305 |
2.02e-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: 46.94 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 96 NKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaQQAEVFTKQIQQLQGELRSLREEI 175
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQ----NEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 176 SLLE----------HEKESELKEIEQELHLAQAEIQSLRQAAEDSATEhesdIASLQEDLCRMQNELEDMERIR------ 239
Cdd:TIGR04523 394 NDLEskiqnqeklnQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE----IKDLTNQDSVKELIIKNLDNTResletq 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 240 -GDYEMEIASLRAEMEMKSSEPSE---ELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATE 305
Cdd:TIGR04523 470 lKVLSRSINKIKQNLEQKQKELKSkekELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
119-380 |
2.37e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 119 VAELEETRELAGQHEDDSLELQGLLE--DERLASAQQAEVFTKQIQQLQ------GELRSLREEISLLEHEKESELKEIE 190
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEevEERLERAEDLVEAEDRIERLEerredlEELIAERRETIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 191 QELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRgdyemEIASLRAEMEmkssepsEELQELRER 270
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-----TLLAAIADAE-------DEIERLREK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 271 YHFLNEEYRALQESNSSLTGQLADLESErtqraterwLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHG 350
Cdd:PRK02224 615 REALAELNDERRERLAEKRERKRELEAE---------FDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGA 685
|
250 260 270
....*....|....*....|....*....|
gi 319655558 351 MKNKCQelccELEELQHHRQVSEEEQRRLQ 380
Cdd:PRK02224 686 VENELE----ELEELRERREALENRVEALE 711
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
110-347 |
5.74e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 110 ELRAQvlqLVAELEETRELAGQHEDDSLElQGLLEderlASAQQAEVfTKQIQQLQGELRSLREEISLL---EHEKESEL 186
Cdd:PRK10929 83 ELRQQ---LNNERDEPRSVPPNMSTDALE-QEILQ----VSSQLLEK-SRQAQQEQDRAREISDSLSQLpqqQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 187 KEIEQELHLAQAEIQSLRQAAedsatehesdIASLQEDLCRMQ---NELEdMERIRGDYEMEIASLRAEMEMKSSEPSE- 262
Cdd:PRK10929 154 NEIERRLQTLGTPNTPLAQAQ----------LTALQAESAALKalvDELE-LAQLSANNRQELARLRSELAKKRSQQLDa 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 263 ELQELRERYHFL--NEEYRALqESNSSLTGQLADL-ESERTQRATERWLqSQTLSmtsaeSQTSEMDFL-----EPDPEM 334
Cdd:PRK10929 223 YLQALRNQLNSQrqREAERAL-ESTELLAEQSGDLpKSIVAQFKINREL-SQALN-----QQAQRMDLIasqqrQAASQT 295
|
250
....*....|...
gi 319655558 335 QLLRQQLRDAEEQ 347
Cdd:PRK10929 296 LQVRQALNTLREQ 308
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
101-383 |
8.44e-05 |
|
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: 45.17 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 179
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQa 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 180 --HEKESELKEIEQELHLAQAEI---QSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 254
Cdd:pfam01576 230 qiAELRAQLAKKEEELQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 255 --MKSSEPSEELQELRERYhfLNEEYRALQESNSSLTGQLADLESERTQ---RATERWLQSQTLSMTSAES-QTSEMDFL 328
Cdd:pfam01576 310 dtLDTTAAQQELRSKREQE--VTELKKALEEETRSHEAQLQEMRQKHTQaleELTEQLEQAKRNKANLEKAkQALESENA 387
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 319655558 329 EPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQREL 383
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
139-388 |
9.83e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 139 LQGLLEDERLASAQQAEVFTKQIQQLQGELRslreeisllehEKESELKEIEQELHLAQAEIQSlrQAAEDSATEHESDI 218
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELE-----------EAEAALEEFRQKNGLVDLSEEA--KLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 219 ASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKS-----SEPSEELQELRERYHFLNEEYRALQEsnssltgQLA 293
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlraqlAELEAELAELSARYTPNHPDVIALRA-------QIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 294 DLESERTQRATERWLQSQTlsmtsaesqtsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELcceleelqhhrQVSE 373
Cdd:COG3206 302 ALRAQLQQEAQRILASLEA--------------------ELEALQAREASLQAQLAQLEARLAEL-----------PELE 350
|
250
....*....|....*
gi 319655558 374 EEQRRLQRELKCAQN 388
Cdd:COG3206 351 AELRRLEREVEVARE 365
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
107-401 |
1.32e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.90 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASaqqaevftkqiQQLQGELRSLREEISLLEhekeSEL 186
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLRRELAGLTRRLSAAE----GEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 187 KEIEQELHLAQAEIQSLRQAAEDSATEhESDIASLQEDLcrmQNELEDMERIRGDYEMEIASLRAEM---EMKSSEPSEE 263
Cdd:pfam19220 86 EELVARLAKLEAALREAEAAKEELRIE-LRDKTAQAEAL---ERQLAAETEQNRALEEENKALREEAqaaEKALQRAEGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 264 LQELRERYHFLNEEYRALQESN-------SSLTGQLADLESER-TQRATERWLQSQtLSMTSAESQTSEMDFLEPDPEMQ 335
Cdd:pfam19220 162 LATARERLALLEQENRRLQALSeeqaaelAELTRRLAELETQLdATRARLRALEGQ-LAAEQAERERAEAQLEEAVEAHR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319655558 336 LLRQQLRDAEEQMHGMKNKCQELcceLEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQ 401
Cdd:pfam19220 241 AERASLRMKLEALTARAAATEQL---LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLE 303
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
101-306 |
1.42e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGL-------------LEDERLASAQQAEVFTKQIQQLQGE 167
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeiedlretiaeTEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 168 LRSLREE----------ISLLEHEKESELKEIEQELHLAQAEIQSLRQAAE---DSATEHESDIASLQEDLCRMQNELED 234
Cdd:PRK02224 295 RDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655558 235 MERIRGDYEMEIASLRAEMEmkssepseelqELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATER 306
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIE-----------ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL 435
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
102-237 |
1.68e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 102 SLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGEL--------- 168
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEarlaALRAQLGSGPDALPELLQSPVIQQLRA------QLAELEAELaelsarytp 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655558 169 -----RSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDlcrmQNELEDMER 237
Cdd:COG3206 289 nhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLER 358
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
107-233 |
1.95e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.21 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:pfam09787 62 EIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 319655558 187 KEIEQELHLAQAEIQSlRQAAEDSATEHESDIASLQEDLCRMQNELE 233
Cdd:pfam09787 142 KDREAEIEKLRNQLTS-KSQSSSSQSELENRLHQLTETLIQKQTMLE 187
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
96-380 |
2.36e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 96 NKHRGLSLTETELEELRAQVlqlvAELEETRELAGQHEDDSLELQGllEDERLASAQQAEvfTKQIQQLQGELRSLREEI 175
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQM----AEKDKVIEILRQQIENMTQLVG--QHGRTAGAMQVE--KAQLEKEINDRRLELQEF 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 176 SLLEHEKESELKEIE--------QELHLAQAEIQSLRqAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDY----- 242
Cdd:pfam15921 610 KILKDKKDAKIRELEarvsdlelEKVKLVNAGSERLR-AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFrnkse 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 243 EMEIASLRAEMEMKSSEpsEELQELRERYHFL--------------NEEYRALQESNSSLTGQLADLESERTQRATERWL 308
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQ--SELEQTRNTLKSMegsdghamkvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHF 766
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655558 309 QSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQ 380
Cdd:pfam15921 767 LKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
101-252 |
2.57e-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: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 101 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELRSLR 172
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 173 EEISLLEhEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
105-300 |
2.64e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 105 ETELEELRaqvlqlvaeleetrelagqheddslelqgllederlasaQQAEVFTKQIQQLQGELRSLREEISLLEHEKES 184
Cdd:pfam09787 46 TLELEELR---------------------------------------QERDLLREEIQKLRGQIQQLRTELQELEAQQQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 185 ELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELED-----MERIRgDYEMEIASLRAEMeMKSSE 259
Cdd:pfam09787 87 EAESSREQLQELEEQLATERSARR----EAEAELERLQEELRYLEEELRRskatlQSRIK-DREAEIEKLRNQL-TSKSQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 319655558 260 PSEELQELRERYHFLNE-------EYRALQESNSSLTGQLADLESERT 300
Cdd:pfam09787 161 SSSSQSELENRLHQLTEtliqkqtMLEALSTEKNSLVLQLERMEQQIK 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
159-306 |
2.72e-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: 42.22 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 159 KQIQQLQGELRSLREEISLLEHEK---ESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASL-----QEDLCRMQN 230
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELaalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319655558 231 ELEDMERIRGDYEMEIASLRAEMEMKssepSEELQELRERYHFLNEEYRALQEsnsSLTGQLADLESERTQRATER 306
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEEL----EEELAELEAELAELEAELEEKKA---ELDEELAELEAELEELEAER 165
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
105-270 |
3.23e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 105 ETELEELRAQVLQLVAELEETrelagqheDDSLelqGLLEDERLASAQQAEVFTK----------------QIQQLQGEL 168
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDP--------SAAL---NKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 169 RSLREEISLLEH------EKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELEDMERIRGDY 242
Cdd:PHA02562 302 TKIKDKLKELQHslekldTAIDELEEIMDEFNEQSKKLLELKNKIS----TNKQSLITLVDKAKKVKAAIEELQAEFVDN 377
|
170 180
....*....|....*....|....*...
gi 319655558 243 EMEIASLRAEMEMKSSEPSEELQELRER 270
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
101-401 |
3.56e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 179
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQe 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 180 --HEKESELKEIEQELHLAQAE------------------IQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 239
Cdd:COG4717 221 elEELEEELEQLENELEAAALEerlkearlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 240 GDYEMEIASLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAE 319
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 320 SQTSEM--DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCC---------ELEELQHHRQVSEEEQRRLQRELKCAQN 388
Cdd:COG4717 381 VEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAELEA 460
|
330
....*....|...
gi 319655558 389 EVLRFQTSHSVTQ 401
Cdd:COG4717 461 ELEQLEEDGELAE 473
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
96-388 |
4.14e-04 |
|
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: 42.79 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 96 NKHRGLSLTETELEELRAQVLQLVAELEETRELAGQheddsLELQGLLEDERLA-SAQQAEVFTKQIQQLQGELRSLREE 174
Cdd:pfam05483 237 DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQ-----LEEKTKLQDENLKeLIEKKDHLTKELEDIKMSLQRSMST 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 175 ISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSA---TEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRA 251
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 252 EMEMKSSEPSEELQELRERYHFLNEEYRALQESNS--SLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLE 329
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLK 471
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 319655558 330 PDPEM--QLLRQQLRDAEEQMHG----MKNK--CQELCCELEELQHHRQVSEEEQRRLQRELKCAQN 388
Cdd:pfam05483 472 EVEDLktELEKEKLKNIELTAHCdkllLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
101-317 |
4.54e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFT------KQIQQLQGELRSLREE 174
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLelldriEELQELLREAEELEEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 175 ISLLEHEKE-----------------------SELKEIEQELHLAQAEIQSLRQAAEDSATEHesDIASLQEDLCRMQNE 231
Cdd:COG4717 363 LQLEELEQEiaallaeagvedeeelraaleqaEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 232 LEDMERIRGDYEMEIASLRAEMEMKssEPSEELQELRERYHFLNEEYRALQESNSSLtgQLADLESERTQRATERWLQSQ 311
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAAL--KLALELLEEAREEYREERLPP 516
|
....*.
gi 319655558 312 TLSMTS 317
Cdd:COG4717 517 VLERAS 522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
96-393 |
4.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 96 NKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGlLEDERLASAQQAEVFTKQIQQLQGELRSLREEI 175
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 176 SLLEhEKESELKEIEqELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMErirgdyemeiaslraEMEM 255
Cdd:PRK03918 276 EELE-EKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE---------------EKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 256 KSSEPSEELQELRERYHFLNEEYRALQESNsSLTGQLADLESERTQRATERWLQS-QTLSMTSAESQTSEMDFLEPDPEM 334
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 319655558 335 QLLRQQLRDAEEQMHGMKNKCQELCCELEElqHHRqvsEEEQRRLQRELKCAQNEVLRF 393
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCPVCGRELTE--EHR---KELLEEYTAELKRIEKELKEI 471
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
182-358 |
6.30e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 42.15 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 182 KESELKEIEQELHLAQAEIQSLRQaaedsaTEHE--SDIASLQEDLCRMQNELEdmeRIRGDYEMEIASLRAEMEMKSSE 259
Cdd:pfam09726 393 KPDALVRLEQDIKKLKAELQASRQ------TEQElrSQISSLTSLERSLKSELG---QLRQENDLLQTKLHNAVSAKQKD 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 260 pSEELQELRERyhfLNEEyralQESNSSLTGQLAD------LESERTQRATErwlQSQTLSMTSAESQTSEMDFLEPdpE 333
Cdd:pfam09726 464 -KQTVQQLEKR---LKAE----QEARASAEKQLAEekkrkkEEEATAARAVA---LAAASRGECTESLKQRKRELES--E 530
|
170 180
....*....|....*....|....*
gi 319655558 334 MQLLRQQLRDAEEQMHGMKNKCQEL 358
Cdd:pfam09726 531 IKKLTHDIKLKEEQIRELEIKVQEL 555
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
107-389 |
7.20e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 107 ELEELRAQVLQLVAELEETRELAGQHeDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLrEEISLLEHEKESEL 186
Cdd:pfam05557 22 ELEHKRARIELEKKASALKRQLDRES-DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL-EALNKKLNEKESQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 187 KEIEQELHLAQAEIQSLRQAAEDSA---TEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRA--------EMEM 255
Cdd:pfam05557 100 ADAREVISCLKNELSELRRQIQRAElelQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrikelEFEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 256 KSSEPSE--------------ELQELRERYHFLNEEYRALQESNSSLTGQLADLES-------------------ERTQR 302
Cdd:pfam05557 180 QSQEQDSeivknskselaripELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekyreeaatlelekEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 303 ATERWL---QSQTLSMTSAESQTSEMDFLEPD-----PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEE 374
Cdd:pfam05557 260 ELQSWVklaQDTGLNLRSPEDLSRRIEQLQQReivlkEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA 339
|
330
....*....|....*
gi 319655558 375 EQRRLQRELKCAQNE 389
Cdd:pfam05557 340 LVRRLQRRVLLLTKE 354
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
98-298 |
7.42e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 40.66 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 98 HRGLSLTETELEELRAQVLQLVAELEETRelagqHEDDSLELQGLLEDERLASAQQAE-VFTKQIQQLQGELRSLREEIS 176
Cdd:pfam15619 3 QRVLSARLHKIKELQNELAELQSKLEELR-----KENRLLKRLQKRQEKALGKYEGTEsELPQLIARHNEEVRVLRERLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 177 LL---EHEKESELKEIEQELHLAQAEIQSLRQAAEDSateHESDIASLQEDLCRMQNELEDMERirgdyemEIASLRAEM 253
Cdd:pfam15619 78 RLqekERDLERKLKEKEAELLRLRDQLKRLEKLSEDK---NLAEREELQKKLEQLEAKLEDKDE-------KIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 319655558 254 EMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESE 298
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
109-306 |
8.14e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 109 EELRAQV--LQLVAELEETRELAGQHEDDSLELQGLLEDERlasaQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:PRK11281 39 ADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 187 KEIEQELHLAQ-----AEIQSLRQAAEDSATEHESDIASLQEDLCRMQNEL-EDMERIrgdyeMEIASLRAEMEMKSSEP 260
Cdd:PRK11281 115 RETLSTLSLRQlesrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALyANSQRL-----QQIRNLLKGGKVGGKAL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 319655558 261 SEELQELreryhfLNEEYRALQESNS----SLTG--QLADLESERTQRATER 306
Cdd:PRK11281 190 RPSQRVL------LQAEQALLNAQNDlqrkSLEGntQLQDLLQKQRDYLTAR 235
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-394 |
1.06e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 105 ETELEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCRMQNEL---------------------EDME 236
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 237 RIRGDYEMEIASLRAEMEMKSSEPSEELQELRERYHFLNEEYralqESNSSLTGQLADLE-------SERTQRATERWLQ 309
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKemlrkvvEELTAKKMTLESS 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 310 SQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNkcqelccELEELQHHRqvSEEEQRRLQRELKCAQNE 389
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKN-------EGDHLRNVQ--TECEALKLQMAEKDKVIE 565
|
....*
gi 319655558 390 VLRFQ 394
Cdd:pfam15921 566 ILRQQ 570
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-392 |
1.18e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 161 IQQLQGELRSLREEISLLE--HEKESELKEIEQELHLAQ-AEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMER 237
Cdd:COG1196 195 LGELERQLEPLERQAEKAEryRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 238 IRGDYEMEIASLRAEMEMKSSEPSEELQELReryhFLNEEYRALQESNSSLTGQLADLESERTQRATERwlqsqtlsmts 317
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLEELEEELAELEEELEELEEEL----------- 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 319655558 318 AESQTsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLR 392
Cdd:COG1196 340 EELEE----------ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
138-388 |
1.47e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 138 ELQGLleDERLASaqqaevFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQelhLAQAEIQSLRQAAEDSATEH--- 214
Cdd:pfam00038 5 QLQEL--NDRLAS------YIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYS---LYEKEIEDLRRQLDTLTVERarl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 215 ESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME---MKSSEPSEELQELRERYHFL----NEEYRALQESNSS 287
Cdd:pfam00038 74 QLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDeatLARVDLEAKIESLKEELAFLkknhEEEVRELQAQVSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 288 --------------LTGQLADLE------SERTQRATERWLQSQTLSMTSAESQTSEMdflepdpemqllrqqLRDAEEQ 347
Cdd:pfam00038 154 tqvnvemdaarkldLTSALAEIRaqyeeiAAKNREEAEEWYQSKLEELQQAAARNGDA---------------LRSAKEE 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 319655558 348 MHGMKNKCQELCCELEELQH-----HRQVSEEEQrRLQRELKCAQN 388
Cdd:pfam00038 219 ITELRRTIQSLEIELQSLKKqkaslERQLAETEE-RYELQLADYQE 263
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-302 |
1.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 104 TETELEELRAQVLQLVAELEETREL------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELiklkelAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 178 LE-------------HEKESELKEIEQELHLA--------QAEIQSLRQAAED--SATEHESDIASLQEDLCRMQNELED 234
Cdd:PRK03918 551 LEelkkklaelekklDELEEELAELLKELEELgfesveelEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDK 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319655558 235 MERIRGDYEMEIASLRAEMEMKSSEPSEE--------LQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQR 302
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEeyeelreeYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
99-268 |
1.68e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 99 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELRSLREEISLL 178
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 179 EHEKESELKEIEQELHLAQAEIQSLRQaaedsatehesDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSS 258
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA 186
|
170
....*....|
gi 319655558 259 EPSEELQELR 268
Cdd:PRK09039 187 QRVQELNRYR 196
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
106-224 |
2.26e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 106 TELEELRAQVLQLVAELEEtrelagqheddslelqgLLEDERLASAQQAEVFTKQIQQLQGELRSLREEislLEHEKE-- 183
Cdd:COG0542 411 EELDELERRLEQLEIEKEA-----------------LKKEQDEASFERLAELRDELAELEEELEALKAR---WEAEKEli 470
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 319655558 184 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQED 224
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
90-306 |
2.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 90 VGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHE---DDSLELQGLLEDERLASAQQAEVFTKqIQQLQG 166
Cdd:PRK02224 521 LEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEeeaEEAREEVAELNSKLAELKERIESLER-IRTLLA 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 167 ELRSLREEISLLEhEKESELKEIEQElhlAQAEIQSLRQAAEDSATEHESD-IASLQEDLCRMQNELEDMERIRGDYEME 245
Cdd:PRK02224 600 AIADAEDEIERLR-EKREALAELNDE---RRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREE 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655558 246 IASLRAEMEMKSSEpSEELQELRERYHFLNEEYRALQ---ESNSSLTGQLADLESERTQRATER 306
Cdd:PRK02224 676 RDDLQAEIGAVENE-LEELEELRERREALENRVEALEalyDEAEELESMYGDLRAELRQRNVET 738
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
105-285 |
2.42e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 105 ETELEELRAQVLQLVA-----ELEETRELAGQHEDDSLELQGLLEDERLA---SAQQAEVFTKQIQQLQGELRSLREEIS 176
Cdd:PRK04778 255 EKEIQDLKEQIDENLAlleelDLDEAEEKNEEIQERIDQLYDILEREVKArkyVEKNSDTLPDFLEHAKEQNKELKEEID 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 177 ------LLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHesdiASLQEDLCRMQNELEDMERIRGDYEMEIASLR 250
Cdd:PRK04778 335 rvkqsyTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAY----SELQEELEEILKQLEEIEKEQEKLSEMLQGLR 410
|
170 180 190
....*....|....*....|....*....|....*.
gi 319655558 251 -AEMEMKssepsEELQELRERYHflnEEYRALQESN 285
Cdd:PRK04778 411 kDELEAR-----EKLERYRNKLH---EIKRYLEKSN 438
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
162-259 |
2.56e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 162 QQLQGELRSLREEISLLEHEKESELKEIEQElhlaqaeiQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGD 241
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQ--------QQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ 216
|
90
....*....|....*...
gi 319655558 242 YEMEIASlRAEMEMKSSE 259
Cdd:PRK11448 217 KRKEITD-QAAKRLELSE 233
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
96-381 |
3.13e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 96 NKHRGLSLTETELE-ELRAQVLQLVAE---LEETRELAGQHEDDSLELQGLLE--DERLASAQQAEVFTKQIQQLQGELR 169
Cdd:PRK04863 279 NERRVHLEEALELRrELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQaaSDHLNLVQTALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 170 SLR---EEISLLEHEKESELKEIEQELHLAQAEIQSL---------------------RQA------------------- 206
Cdd:PRK04863 359 ELEerlEEQNEVVEEADEQQEENEARAEAAEEEVDELksqladyqqaldvqqtraiqyQQAvqalerakqlcglpdltad 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 207 -AEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEM-EMKSSEPSEELQELRERYhflnEEYRALQES 284
Cdd:PRK04863 439 nAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAgEVSRSEAWDVARELLRRL----REQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 285 NSSLTGQLADLESE-RTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQL--LRQQLRDAEEQMHGMKNKCQELCCE 361
Cdd:PRK04863 515 LQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLesLSESVSEARERRMALRQQLEQLQAR 594
|
330 340
....*....|....*....|
gi 319655558 362 LEELQHHRQVSEEEQRRLQR 381
Cdd:PRK04863 595 IQRLAARAPAWLAAQDALAR 614
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
104-209 |
3.44e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 104 TETELEELRAQVLQLvaeleETRELAGQHEDDSLELQGLLEDERLASAQQaevFTKQIQQLQGELRSLREEISLLEHEKE 183
Cdd:PRK04863 584 LRQQLEQLQARIQRL-----AARAPAWLAAQDALARLREQSGEEFEDSQD---VTEYMQQLLERERELTVERDELAARKQ 655
|
90 100
....*....|....*....|....*.
gi 319655558 184 SELKEIEQELHLAQAEIQSLRQAAED 209
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
104-206 |
3.48e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.93 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 104 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLlederlasAQQAEvftKQIQQLQGELRSLREEISLLEHEKE 183
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGL--------AAELE---EKQQELEAQLEQLQEKAAETSQERK 215
|
90 100 110
....*....|....*....|....*....|..
gi 319655558 184 SELKEIEQE----LHLAQAEI-----QSLRQA 206
Cdd:PRK11448 216 QKRKEITDQaakrLELSEEETrilidQQLRKA 247
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
94-342 |
3.60e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 94 SVNKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLED-------------ERLASAQQAEVFTKQ 160
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkseklqigtnlqRRQQFEEQLVELSTE 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 161 IQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEiqslRQAAEDSATEHESDIASLQEDLCRMQNELED-MERIR 239
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS----NKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYL 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 240 GDYEMEIASLRAEMemkssepsEELQELRERYhflNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAE 319
Cdd:TIGR00606 973 KQKETELNTVNAQL--------EECEKHQEKI---NEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHL 1041
|
250 260
....*....|....*....|...
gi 319655558 320 SQTSEMDFLEPDPEMQLLRQQLR 342
Cdd:TIGR00606 1042 KEMGQMQVLQMKQEHQKLEENID 1064
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
184-394 |
3.92e-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: 39.36 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 184 SELKEIEQELHLAQAEIQSLRQAAEDSatehESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSEE 263
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 264 LQELRERYHFLNEEYRALQESNSSLTGQLAdLESERTQRATERWLQSQTLsmtsAESQTSEMDFLEPDpeMQLLRQQLRD 343
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALL-LSPEDFLDAVRRLQYLKYL----APARREQAEELRAD--LAELAALRAE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 319655558 344 AEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQ 394
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-394 |
4.27e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 196 AQAEIQslRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSEELQELRERYHFLN 275
Cdd:COG3883 12 AFADPQ--IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 276 EEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSmtsaESQTSEMDFLEPDpeMQLLRQQLRDAEEQMHGMKNKC 355
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIA----DADADLLEELKAD--KAELEAKKAELEAKLAELEALK 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 319655558 356 QELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQ 394
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
185-401 |
4.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 185 ELKEIEQELHLAQAEIQSLRQAAEDSAtEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKssEPSEEL 264
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELA--ELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 265 QELRERYhflnEEYRALQESNSSLTGQLADLESERTQraterwlqsqtlsmtsaesqtsemdflepdpemqLLRQQLRDA 344
Cdd:COG4717 149 EELEERL----EELRELEEELEELEAELAELQEELEE----------------------------------LLEQLSLAT 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655558 345 EEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQ 401
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
104-240 |
5.01e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 38.89 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 104 TETELEELRAQVLQLVAEL---------------EETRELAGQHEDDSLELQGLLE--DERLASAQQAEVFtKQIQQLQG 166
Cdd:cd22656 108 DDEELEEAKKTIKALLDDLlkeakkyqdkaakvvDKLTDFENQTEKDQTALETLEKalKDLLTDEGGAIAR-KEIKDLQK 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655558 167 ELRSLREEISLlehEKESELKEIEQELHLAQAEIQSLRQAAEDsATEHESDIASLQEDlcrMQNELEDMERIRG 240
Cdd:cd22656 187 ELEKLNEEYAA---KLKAKIDELKALIADDEAKLAAALRLIAD-LTAADTDLDNLLAL---IGPAIPALEKLQG 253
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
107-383 |
5.33e-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: 39.39 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDE-RLASAQQAEVFTKQIQQ---LQGELRSLREEISLLEHEK 182
Cdd:pfam01576 300 ELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQAleeLTEQLEQAKRNKANLEKAK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 183 ESelkeIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEdlcrMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSE 262
Cdd:pfam01576 380 QA----LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE----LQARLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 263 elqelreryhfLNEEYRALQESNSSLTGQLADLEsERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEM-QLLRQQL 341
Cdd:pfam01576 452 -----------AEGKNIKLSKDVSSLESQLQDTQ-ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAkRNVERQL 519
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 319655558 342 RDAEEQMHGMKNKCQELCCELEELqhhrqvsEEEQRRLQREL 383
Cdd:pfam01576 520 STLQAQLSDMKKKLEEDAGTLEAL-------EEGKKRLQREL 554
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
105-194 |
5.64e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 37.21 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaEVFTKQIQQLQGELRSLREEISLLEHEKES 184
Cdd:pfam09744 49 NVELEELREDNEQLETQYEREKALRKRAEEELEEIEDQWEQET-------KDLLSQVESLEEENRRLEADHVSRLEEKEA 121
|
90
....*....|
gi 319655558 185 ELKEIEQELH 194
Cdd:pfam09744 122 ELKKEYSKLH 131
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
100-305 |
5.72e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.27 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 100 GLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLE-LQGLLE--DERLASAQQAEVFTKQIQQLQGELRSLREEIS 176
Cdd:PRK10929 10 AWLLSWGAYAATAPDEKQITQELEQAKAAKTPAQAEIVEaLQSALNwlEERKGSLERAKQYQQVIDNFPKLSAELRQQLN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 177 LLEHE-----KESELKEIEQEL-----------HLAQAEIQSLRQAAeDSAteheSDIASLQEDLCRMQNELEDMERIRG 240
Cdd:PRK10929 90 NERDEprsvpPNMSTDALEQEIlqvssqlleksRQAQQEQDRAREIS-DSL----SQLPQQQTEARRQLNEIERRLQTLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 241 D------------YEMEIASLRA-----EMEMKSSEPSEELQELR-----ERYHFLNEEYRALQESNSSLTGQLADLESE 298
Cdd:PRK10929 165 TpntplaqaqltaLQAESAALKAlvdelELAQLSANNRQELARLRselakKRSQQLDAYLQALRNQLNSQRQREAERALE 244
|
....*..
gi 319655558 299 RTQRATE 305
Cdd:PRK10929 245 STELLAE 251
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
134-384 |
5.98e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.84 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 134 DDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDsate 213
Cdd:PHA02562 157 EDLLDISVLSEMDKLNKDKIREL-NQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKT---- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 214 HESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPS--EE-------LQELRERyhflNEEYRALQES 284
Cdd:PHA02562 232 IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKggvcptcTQQISEG----PDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 285 NSSLTGQLaDLESERTQRATERWLQSQTLSMTSAESQTsemDFLEPDPEMQLLRQQLRDAEEqmhgmknkcqelccELEE 364
Cdd:PHA02562 308 LKELQHSL-EKLDTAIDELEEIMDEFNEQSKKLLELKN---KISTNKQSLITLVDKAKKVKA--------------AIEE 369
|
250 260
....*....|....*....|
gi 319655558 365 LQHHRQVSEEEQRRLQRELK 384
Cdd:PHA02562 370 LQAEFVDNAEELAKLQDELD 389
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
158-289 |
7.82e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655558 158 TKQIQQLQGELRSLREEIsllEHEKESELKEIEQElhlAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMER 237
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEA---KKEAEAIKKEALLE---AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 319655558 238 IRGDYEMEIASLRAEMEMKssepSEELQELRERYHFLNEEYRALQESNSSLT 289
Cdd:PRK12704 104 LLEKREEELEKKEKELEQK----QQELEKKEEELEELIEEQLQELERISGLT 151
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