|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-434 |
1.49e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 195 AEEWKK-RDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRnLQELQDSIRRAKEdc 273
Cdd:COG1196 212 AERYRElKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE-LEELELELEEAQA-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 274 ihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPE--IRLQSEINLLTLEKVELERKLESATKS 351
Cdd:COG1196 289 --EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEelEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 352 KLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQD 431
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
...
gi 1034643727 432 STE 434
Cdd:COG1196 447 AAE 449
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-430 |
2.53e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 161 EYKAALELEMWKEMQEDIfenQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASV 240
Cdd:COG1196 224 ELEAELLLLKLRELEAEL---EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 241 ESELQREKKELQsERQRNLQELQDSIRRAKEDCIH---QVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKD 317
Cdd:COG1196 301 EQDIARLEERRR-ELEERLEELEEELAELEEELEEleeELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 318 QQN--NKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRLRY 395
Cdd:COG1196 380 ELEelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270
....*....|....*....|....*....|....*
gi 1034643727 396 LAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQ 430
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
229-436 |
2.20e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 229 DLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKIL 308
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 309 EKEFQQFKDQQNNKPE--IRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQE 386
Cdd:COG1196 301 EQDIARLEERRRELEErlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034643727 387 EL----EQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIA 436
Cdd:COG1196 381 LEelaeELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-466 |
3.81e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 157 RETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQ 236
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 237 LASVESELQREKKELQsERQRNLQELQDSIRRAKEDC---IHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQ 313
Cdd:TIGR02168 763 IEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 314 QFKDQ--QNNKPEIRLQSEINLLTLEKVELERKLESATKSKlhykqqwgRALKELARLKQREQESQMARLkkQQEELEQM 391
Cdd:TIGR02168 842 DLEEQieELSEDIESLAAEIEELEELIEELESELEALLNER--------ASLEEALALLRSELEELSEEL--RELESKRS 911
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034643727 392 RLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSvlEEGLDDYLTRLIEERDTL 466
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD--EEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
186-435 |
4.37e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 186 KELAHMQALAEEWKKRDRERESLVKKKvaeyTILEGKLQKTLIDLEKREQQLASVESELQR--EKKELQSERQRNLQELQ 263
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIEQleQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 264 DSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYkiLEKEFQQFKDQQNNKPEIRLQSEINLltlekVELER 343
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARL-----REIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 344 KLEsatksKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELeQMRLRYLAAEEKDTVKTERQ---ELLDIRNELNR 420
Cdd:TIGR02169 820 KLN-----RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL-NGKKEELEEELEELEAALRDlesRLGDLKKERDE 893
|
250
....*....|....*....
gi 1034643727 421 ----LRQQEQKQYQDSTEI 435
Cdd:TIGR02169 894 leaqLRELERKIEELEAQI 912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-427 |
4.77e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 181 NQLKQKELAhmqALAEEWKKRDRERESLvKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQSErqrnLQ 260
Cdd:TIGR02168 220 AELRELELA---LLVLRLEELREELEEL-QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 261 ELQDSIRRAKEDCIHQVElerlKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNnkpeiRLQSEINLLTLEKVE 340
Cdd:TIGR02168 292 ALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKLE-----ELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 341 LERKLESATKSKLHYKQQWGRALKELARLKQRE--QESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNEL 418
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
....*....
gi 1034643727 419 NRLRQQEQK 427
Cdd:TIGR02168 443 EELEEELEE 451
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-395 |
9.52e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 151 EIQTEPRETLEYKAALELEMwKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDL 230
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEV-SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 231 EKREQQLASVESELQREKKELQSERQRNLQELQDSiRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEK 310
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEEL-ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 311 EFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQ--ESQMARLKKQQEEL 388
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDaaERELAQLQARLDSL 494
|
....*..
gi 1034643727 389 EQMRLRY 395
Cdd:TIGR02168 495 ERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-434 |
4.05e-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: 56.22 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 220 EGKLQKTLIDLEKREQQLASVESELqrEKKELQSERQRNLQELQDSIRRAkedcihQVELERLKIKQLEEDKHRLQQQLN 299
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQL--KSLERQAEKAERYKELKAELREL------ELALLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 300 DAENKYKILEKEFQQfkdqqnnkpeirLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQ--ESQ 377
Cdd:TIGR02168 250 EAEEELEELTAELQE------------LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlERQ 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034643727 378 MARLKKQQEELEQMRLRYLA-----AEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTE 434
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEelaelEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-430 |
6.15e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 177 DIFENQLKQKElAHMQALAEEWKKRDRERESLVKKKVAEYTILEgkLQKTLIDLEKREQQLASVESELQR------EKKE 250
Cdd:COG4913 613 AALEAELAELE-EELAEAEERLEALEAELDALQERREALQRLAE--YSWDEIDVASAEREIAELEAELERldassdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 251 LQSERQRnLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKI-----LEKEFQQFKDQQNNKpEI 325
Cdd:COG4913 690 LEEQLEE-LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAALGDAVER-EL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 326 R--LQSEINLLTLEKVELERKLESATKSklhYKQQW--------------GRALKELARLKQR---EQESQMARLKKQQE 386
Cdd:COG4913 768 RenLEERIDALRARLNRAEEELERAMRA---FNREWpaetadldadleslPEYLALLDRLEEDglpEYEERFKELLNENS 844
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034643727 387 ELEQMRLRYLAAEEKDTVkteRQELLDIRNELNRLRQQEQKQYQ 430
Cdd:COG4913 845 IEFVADLLSKLRRAIREI---KERIDPLNDSLKRIPFGPGRYLR 885
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
247-485 |
2.53e-07 |
|
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: 53.20 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 247 EKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKdQQNNKPEIR 326
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIR-QEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 327 LQSEINLLTLEKVE----LERKLESATKSKLhykqqwgraLKELARLKQREQESQMARLKKQQEELEQMRLRYLAAEEKD 402
Cdd:pfam17380 376 RMRELERLQMERQQknerVRQELEAARKVKI---------LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 403 TVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGS-----VLEEGLDDYLTRLIEERDTL---------MR 468
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEeqrrkILEKELEERKQAMIEEERKRkllekemeeRQ 526
|
250
....*....|....*..
gi 1034643727 469 TGVYNHEDRIISELDRQ 485
Cdd:pfam17380 527 KAIYEEERRREAEEERR 543
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-497 |
1.46e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 181 NQLKQKELAHMQA----LAEEWKKRDRERESLVKKKVAEYTILEGKlqktlidleKREQQLASVESELQREKKELQSERQ 256
Cdd:PTZ00121 1500 DEAKKAAEAKKKAdeakKAEEAKKADEAKKAEEAKKADEAKKAEEK---------KKADELKKAEELKKAEEKKKAEEAK 1570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 257 RNLQELQDSIRRAKEdcIHQVELERLK--IKQLEEDKHRLQQQLNDAENKyKILEKEFQQFKDQQNNKPEIRLQSEINLL 334
Cdd:PTZ00121 1571 KAEEDKNMALRKAEE--AKKAEEARIEevMKLYEEEKKMKAEEAKKAEEA-KIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 335 TLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQM-RLRYLAAEEK---DTVKTERQE 410
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeELKKKEAEEKkkaEELKKAEEE 1727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 411 LLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSVLEEGLDDYLTRlieERDTLMRTGVYNHEDRIISELDRQIREIl 490
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK---EKEAVIEEELDEEDEKRRMEVDKKIKDI- 1803
|
....*..
gi 1034643727 491 aKSNASN 497
Cdd:PTZ00121 1804 -FDNFAN 1809
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-428 |
1.65e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 168 LEMWKEMQEDIFENQLKQKELA-HMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQR 246
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 247 EKKELQ------SERQRNLQELQDSIRRAKEDCIHQV--ELERLK--IKQLEEDKHRLQQQLNDAENKYKILEKEFQQFK 316
Cdd:TIGR02169 256 LTEEISelekrlEEIEQLLEELNKKIKDLGEEEQLRVkeKIGELEaeIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 317 DQ---------QNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKqREQESQMARLKKQQEE 387
Cdd:TIGR02169 336 AEieelereieEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK-REINELKRELDRLQEE 414
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034643727 388 LEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQ 428
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
250-497 |
2.46e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 250 ELQSERQRNLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQ--QNNKPEIRL 327
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEK----ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 328 QSEINLLtleKVELERKLESATKSKLHYK-------QQWGRALKELARLKQ--REQESQMARLKKQQEELEQmrLRYLAA 398
Cdd:COG4942 96 RAELEAQ---KEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAA--LRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 399 EEKDTVKTERQELLDIRNELNRLRQQEQKQyqdsteIASGKKDgphgsvlEEGLDDYLTRLIEERDTLmrtgvynheDRI 478
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKL------LARLEKE-------LAELAAELAELQQEAEEL---------EAL 228
|
250
....*....|....*....
gi 1034643727 479 ISELDRQIREILAKSNASN 497
Cdd:COG4942 229 IARLEAEAAAAAERTPAAG 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
155-465 |
4.61e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 155 EPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKRE 234
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 235 QQLASVESELQREKKELQSERQRNLQELQDSIRRAKEdcihqVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQ 314
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE-----EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 315 FKDQQNNKPEIRLQSEinlltlekvELERKLESATKSKLHYKqqwgRALKELArlKQREQESQMARLKKQQEELEQMRLR 394
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAE---------EDEKKAAEALKKEAEEA----KKAEELK--KKEAEEKKKAEELKKAEEENKIKAE 1733
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034643727 395 YLAAEEKDTvKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKdgphgSVLEEGLD--DYLTRLIEERDT 465
Cdd:PTZ00121 1734 EAKKEAEED-KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE-----AVIEEELDeeDEKRRMEVDKKI 1800
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-489 |
4.71e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 201 RDRERESLV-----KKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQ-----SERQRNLQELQDSIRRAK 270
Cdd:COG4913 595 RRRIRSRYVlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeySWDEIDVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 271 EdcihqvELERLK--IKQLEEdkhrLQQQLNDAENKYKILEKEFQQFKDQQnnkpeIRLQSEINLLTLEKVELERKLESA 348
Cdd:COG4913 675 A------ELERLDasSDDLAA----LEEQLEELEAELEELEEELDELKGEI-----GRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 349 TKSKLHYKQQwgRALKELARLKQREQESQMAR-LKKQQEELEQMRLRylaaeekdtvkterqelldIRNELNRLRQQEQK 427
Cdd:COG4913 740 EDLARLELRA--LLEERFAAALGDAVERELREnLEERIDALRARLNR-------------------AEEELERAMRAFNR 798
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034643727 428 QYQDST-EIASGKKDGP-----HGSVLEEGLDDYLTRLIEERDTLMRTGVynheDRIISELDRQIREI 489
Cdd:COG4913 799 EWPAETaDLDADLESLPeylalLDRLEEDGLPEYEERFKELLNENSIEFV----ADLLSKLRRAIREI 862
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
241-428 |
5.56e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 241 ESELQREKKELQSERQRNLQELQDSIRRAKEDcIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQN 320
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEE-LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 321 NKPEI----RLQSEINLLTLEKVELERKLE---SATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEELEQMRL 393
Cdd:COG4717 127 LLPLYqeleALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*
gi 1034643727 394 RYLAAEEKdtVKTERQELLDIRNELNRLRQQEQKQ 428
Cdd:COG4717 207 RLAELEEE--LEEAQEELEELEEELEQLENELEAA 239
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
229-391 |
1.18e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 47.71 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 229 DLEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDcIHQVELER----LKIKQLEEDKHRLQQQLNDAENK 304
Cdd:pfam05667 307 QFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESS-IQELEKEIkkleSSIKQVEEELEELKEQNEELEKQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 305 YKILEKEFQQFKDQQNNkpeirlqseinlltleKVELERKLESATKSKLHYKQQWG----------RALKELARLKQREQ 374
Cdd:pfam05667 386 YKVKKKTLDLLPDAEEN----------------IAKLQALVDASAQRLVELAGQWEkhrvplieeyRALKEAKSNKEDES 449
|
170
....*....|....*..
gi 1034643727 375 ESQMARLKKQQEELEQM 391
Cdd:pfam05667 450 QRKLEEIKELREKIKEV 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
235-437 |
1.98e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 235 QQLASVESELQREKKelQSERQRNLQELQDSIRRAKEDCIHQVELE--------RLKIKQLEEDKHRLQQQLNDAENKYK 306
Cdd:COG4913 235 DDLERAHEALEDARE--QIELLEPIRELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 307 ILEKEFQQFKDQqnnkpEIRLQSEINLLTLEKVE-LERKLESATKSKLHYKQQWGRALKELARLKQREQESQmarlkkqq 385
Cdd:COG4913 313 RLEARLDALREE-----LDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPASA-------- 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034643727 386 EELEQMRLRylAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQD-STEIAS 437
Cdd:COG4913 380 EEFAALRAE--AAALLEALEEELEALEEALAEAEAALRDLRRELRElEAEIAS 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-424 |
2.18e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 171 WKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKR----------------- 233
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaelskle 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 234 ------EQQLASVESELQRE--KKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKY 305
Cdd:TIGR02169 805 eevsriEARLREIEQKLNRLtlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 306 KILEKEFQQFKDQQNNkpeirLQSEINLLTLEkVELERKLESATKSKLHYKQQwgrALKELARLKQREQES--------- 376
Cdd:TIGR02169 885 GDLKKERDELEAQLRE-----LERKIEELEAQ-IEKKRKRLSELKAKLEALEE---ELSEIEDPKGEDEEIpeeelsled 955
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034643727 377 -QMARLKKQQ-------------EELEQMRLRYLAAEEK-DTVKTERQELLDIRNELNRLRQQ 424
Cdd:TIGR02169 956 vQAELQRVEEeiralepvnmlaiQEYEEVLKRLDELKEKrAKLEEERKAILERIEEYEKKKRE 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
171-423 |
3.58e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 171 WKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERE---SLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQRE 247
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEkelEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 248 KKELQSERQrNLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAEnKYKILEKEFQQFKDQQNN--KPEI 325
Cdd:PRK03918 244 EKELESLEG-SKRKLEEKIRELEE----RIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREieKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 326 RLQSEINLLTLEKVELERKLESATKSKLHYKQqwgrALKELARLKQREQESQMARLKKqqEELEQMRLRyLAAEEKDTVK 405
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKK--EELERLKKR-LTGLTPEKLE 390
|
250 260
....*....|....*....|..
gi 1034643727 406 TERQEL----LDIRNELNRLRQ 423
Cdd:PRK03918 391 KELEELekakEEIEEEISKITA 412
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
181-306 |
5.90e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 181 NQLKQKELAHMQalaEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELqSERQRNLQ 260
Cdd:PRK12704 52 EAIKKEALLEAK---EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKEL-EQKQQELE 127
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1034643727 261 ELQDSIRRAKEDciHQVELERLKIKQLEEDKHRLqqqLNDAENKYK 306
Cdd:PRK12704 128 KKEEELEELIEE--QLQELERISGLTAEEAKEIL---LEKVEEEAR 168
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
224-405 |
6.89e-05 |
|
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: 44.15 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 224 QKTLIDLEKREQQLASVESELQREKKELQsERQRNLQELQDSIRRAKEDcIHQVELER----LKIKQLEEDKHRLQQQLN 299
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELA-ELEDELAALEARLEAAKTE-LEDLEKEIkrleLEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 300 DAENkykilEKEFQQfkdqqnnkpeirLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARL------KQRE 373
Cdd:COG1579 84 NVRN-----NKEYEA------------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELeaeleeKKAE 146
|
170 180 190
....*....|....*....|....*....|..
gi 1034643727 374 QESQMARLKKQQEELEQMRLRYLAAEEKDTVK 405
Cdd:COG1579 147 LDEELAELEAELEELEAEREELAAKIPPELLA 178
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
150-425 |
7.16e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 150 SEIQTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEwkKRDRERESLVKKKVAEYTILEGKLQKTLID 229
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE--REKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 230 LEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHqVELERLKIKQLEEDKHRLQQQLNDAENKYKILE 309
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEE-LERLEEEITKEELLQELLLKEEELEEQKLKDEL 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 310 KEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQW-----GRALKELARLKQREQESQMARLKKQ 384
Cdd:pfam02463 889 ESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEellleEADEKEKEENNKEEEEERNKRLLLA 968
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034643727 385 QEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQE 425
Cdd:pfam02463 969 KEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
169-428 |
7.82e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 169 EMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKvAEYTILEGKLQKTLIDLEKREQQLASVESELqREK 248
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIKELEEKEERL-EEL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 249 KELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQ 328
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 329 SEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQmARLKKQQEELEQMRLRYLAAEEKDTVKTER 408
Cdd:PRK03918 424 LKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIE-EKERKLRKELRELEKVLKKESELIKLKELA 502
|
250 260
....*....|....*....|
gi 1034643727 409 QELLDIRNELNRLRQQEQKQ 428
Cdd:PRK03918 503 EQLKELEEKLKKYNLEELEK 522
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
192-434 |
9.06e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 192 QALAEEWKKRDRER-----ESLVKKKVAEYTILEGKL----QKTLIDLEKRE--QQLASVESELQREKKELQSERQRNLQ 260
Cdd:pfam02029 62 EAFLDRTAKREERRqkrlqEALERQKEFDPTIADEKEsvaeRKENNEEEENSswEKEEKRDSRLGRYKEEETEIREKEYQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 261 E--LQDSIRRAKEDCIHQvELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIRLQSEINLLTLEK 338
Cdd:pfam02029 142 EnkWSTEVRQAEEEGEEE-EDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 339 VELERKleSATKSKLHYKQQWGRALKELarlKQREQESQMARLKKQQEELEQMRLRYLAAE-EKDTVKTERQELLDIRNE 417
Cdd:pfam02029 221 VTTKRR--QGGLSQSQEREEEAEVFLEA---EQKLEELRRRRQEKESEEFEKLRQKQQEAElELEELKKKREERRKLLEE 295
|
250
....*....|....*..
gi 1034643727 418 LNRLRQQEQKQYQDSTE 434
Cdd:pfam02029 296 EEQRRKQEEAERKLREE 312
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
157-369 |
9.30e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 157 RETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQ 236
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 237 LASVESELQREKKELQS---------ERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKI 307
Cdd:COG1196 388 LLEALRAAAELAAQLEEleeaeeallERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034643727 308 LEKEFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARL 369
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
234-431 |
9.79e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 234 EQQLASVESELQREKKELQSERQRN-LQELQDsirrakedcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEkef 312
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNgLVDLSE-----------EAKLLLQQLSELESQLAEARAELAEAEARLAALR--- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 313 QQFKDQQNNKPEIRLQSEINLLTLEKVELERKL--ESATKSKLHYK-QQWGRALKELARLKQREQESQMARLKKQQEELE 389
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAELEAELaeLSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034643727 390 QmRLRYLAAEEkDTVKTERQELLDIRNELNRLRQQ---EQKQYQD 431
Cdd:COG3206 327 A-REASLQAQL-AQLEARLAELPELEAELRRLEREvevARELYES 369
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
167-411 |
1.06e-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: 45.11 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 167 ELEMWKEMQEDIFENQLKQKELAHMQaLAEEWKKRDREREslvkkkvaEYTILEGKLQKTLIDLEKREQQLaSVESELQR 246
Cdd:pfam15921 332 ELREAKRMYEDKIEELEKQLVLANSE-LTEARTERDQFSQ--------ESGNLDDQLQKLLADLHKREKEL-SLEKEQNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 247 E---------------KKELqSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKE 311
Cdd:pfam15921 402 RlwdrdtgnsitidhlRREL-DDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 312 FQQFKDQQnnkpeIRLQSE---INLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQEsqmarLKKQQEEL 388
Cdd:pfam15921 481 VEELTAKK-----MTLESSertVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDH-----LRNVQTEC 550
|
250 260
....*....|....*....|...
gi 1034643727 389 EQMRLRylAAEEKDTVKTERQEL 411
Cdd:pfam15921 551 EALKLQ--MAEKDKVIEILRQQI 571
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-424 |
1.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 222 KLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQElqdsirrakedcihqvelerlKIKQLEEDKHRLQQQLNDA 301
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA---------------------ELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 302 ENKYKILEKEFQQFKDQQnnkpEIRLQSEINLLTLEKVELERKLESAtksklhykQQWGRALKELARLKQREQESQMARL 381
Cdd:COG4913 322 REELDELEAQIRGNGGDR----LEQLEREIERLERELEERERRRARL--------EALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034643727 382 KKQQEELEQMR--LRYLAAEEKDTVKTERQELLDIRNELNRLRQQ 424
Cdd:COG4913 390 AALLEALEEELeaLEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
184-351 |
4.14e-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: 41.83 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 184 KQKELAHMQALAEEWKKRDRERESLvKKKVAEytiLEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQR--NLQE 261
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKEL-PAELAE---LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 262 LQDSIRRAKE--DCIHQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKpEIRLQSEINLLTLEKV 339
Cdd:COG1579 81 QLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK-KAELDEELAELEAELE 159
|
170
....*....|..
gi 1034643727 340 ELERKLESATKS 351
Cdd:COG1579 160 ELEAEREELAAK 171
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
213-390 |
4.57e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 213 VAEYTILEGKLQKTLIDLEKREQQLasveseLQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEdkh 292
Cdd:PRK12704 19 VIGYFVRKKIAEAKIKEAEEEAKRI------LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEK--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 293 RLQQqlndaenKYKILEKefqqfKDQQNNKPEIRLQSEINLLTLEKVELERKLESAtkSKLHYKQQwgRALKELARLKQR 372
Cdd:PRK12704 90 RLLQ-------KEENLDR-----KLELLEKREEELEKKEKELEQKQQELEKKEEEL--EELIEEQL--QELERISGLTAE 153
|
170
....*....|....*...
gi 1034643727 373 EQESQMarLKKQQEELEQ 390
Cdd:PRK12704 154 EAKEIL--LEKVEEEARH 169
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
234-434 |
8.82e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 234 EQQLASVESELQREKKELQSERQRnLQELQDSIrrakedcihqvelerLKIKQLEEDKHRlqqQLNDAENKYKILEKEFQ 313
Cdd:PRK10929 108 EQEILQVSSQLLEKSRQAQQEQDR-AREISDSL---------------SQLPQQQTEARR---QLNEIERRLQTLGTPNT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 314 QFKDQQNnkpeIRLQSEINLLTLEKVELERKLESAtksklHYKQqwgralkELARLkqreqesQMARLKKQQEELEQmrl 393
Cdd:PRK10929 169 PLAQAQL----TALQAESAALKALVDELELAQLSA-----NNRQ-------ELARL-------RSELAKKRSQQLDA--- 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034643727 394 rylaaeekdtvkterqELLDIRNELNRLRQQEQKQYQDSTE 434
Cdd:PRK10929 223 ----------------YLQALRNQLNSQRQREAERALESTE 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
151-319 |
9.52e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 151 EIQTEPRETLEYKAALElEMWKEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLvkkkvAEYTILEGKLQKTLIDL 230
Cdd:COG4717 85 EKEEEYAELQEELEELE-EELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL-----AELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 231 EKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEK 310
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE----ELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
....*....
gi 1034643727 311 EFQQFKDQQ 319
Cdd:COG4717 235 ELEAAALEE 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
175-401 |
1.06e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 175 QEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQSE 254
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 255 RQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEDKHRLQ--QQLNDAenkykiLEKEFQQFKDQQNnkpeiRLQSEIN 332
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPA------RREQAEELRADLA-----ELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034643727 333 LLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQR--EQESQMARLKKQQEELEQMRLRYLAAEEK 401
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKElaELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
174-412 |
1.07e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 174 MQEDIFENQLKQKELAHMQALAEEWKKRDRERESlvkkKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKELQS 253
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELES----RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 254 ERQRNLQ---ELQDSIRRAKEDCI-HQVELERLK---------IKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQN 320
Cdd:pfam07888 123 QRAAHEArirELEEDIKTLTQRVLeRETELERMKerakkagaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 321 NKPE--IRLQSEINLLTL-------EKVELERKLE--SATKSKLHYKQQ----WGRALKELARLKQREQ-ESQMARLKKQ 384
Cdd:pfam07888 203 QRDTqvLQLQDTITTLTQklttahrKEAENEALLEelRSLQERLNASERkvegLGEELSSMAAQRDRTQaELHQARLQAA 282
|
250 260
....*....|....*....|....*...
gi 1034643727 385 QEELEQMRLRYLAAEEKDTVKTERQELL 412
Cdd:pfam07888 283 QLTLQLADASLALREGRARWAQERETLQ 310
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-324 |
1.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 163 KAALELEMWKEMQE--DIFENQLKQKEL-AHMQALAEEWKKRDRERESLVKKKVAeytiLEGKLQKTLIDLEKRE-QQLA 238
Cdd:COG4913 266 AARERLAELEYLRAalRLWFAQRRLELLeAELEELRAELARLEAELERLEARLDA----LREELDELEAQIRGNGgDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 239 SVESELQREKKELQsERQRNLQELQDSIR--------------RAKEDCIHQVELERLKIKQLEEDKHRLQQQLNDAENK 304
Cdd:COG4913 342 QLEREIERLERELE-ERERRRARLEALLAalglplpasaeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
170 180
....*....|....*....|
gi 1034643727 305 YKILEKEFQQFKDQQNNKPE 324
Cdd:COG4913 421 LRELEAEIASLERRKSNIPA 440
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
294-436 |
2.02e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 294 LQQQLNDAENKYKILEKEFQQFKdQQNNkpEIRLQSEINLLTLEKVELERKLESAT------KSKLHY-KQQWGRALKEL 366
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFR-QKNG--LVDLSEEAKLLLQQLSELESQLAEARaelaeaEARLAAlRAQLGSGPDAL 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034643727 367 ARLKQREQESQM-ARLKKQQEELEQMRLRYLaaEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIA 436
Cdd:COG3206 257 PELLQSPVIQQLrAQLAELEAELAELSARYT--PNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEAL 325
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
230-420 |
2.41e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 230 LEKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEEdkhRLQQQLNDAENKYKile 309
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEE---RLVQKEEQLDARAE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 310 kefqqfkdqqnnkpeirlqsEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARLKQREQESQMARLKKQQEElE 389
Cdd:PRK12705 99 --------------------KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELE-E 157
|
170 180 190
....*....|....*....|....*....|.
gi 1034643727 390 QMRLRYLAAEEKDTVKTERQELLDIRNELNR 420
Cdd:PRK12705 158 EKAQRVKKIEEEADLEAERKAQNILAQAMQR 188
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-352 |
3.05e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 153 QTEPRETLEYKAALELEMWKEMQEDIFENQLKQKELAHMQAlaEEWKKRDRERESL--VKKKVAEYTILEGKLQKTLIDL 230
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEEEN 1659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 231 EKREQQLASVESELQREKKELQSERQRNLQELQDSIRRAKEdcihQVELERLKIKQLEEDKHRLQQQLNDAENKYKILEK 310
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE----AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034643727 311 EFQQFKDQQNNKPEIRLQSEINLLTLEKVELERKLESATKSK 352
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
155-450 |
3.05e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 155 EPRETLEYKAALELEMWKEMQEdifENQLKQKelAHMQALAEEWKKRDREreslvKKKVAEYTILEGKLQKTLIDLEKRE 234
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKK---ADEAKKK--AEEAKKADEAKKKAEE-----AKKKADAAKKKAEEAKKAAEAAKAE 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 235 QQLASVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELErlkiKQLEEDKHRLQQQLNDAENKYKilekefqq 314
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK----KKAEEDKKKADELKKAAAAKKK-------- 1419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 315 fKDQQNNKPEIRLQSEinlltlekvELERKLESATKS-KLHYKQQWGRALKELArlKQREQESQMARLKKQQEELEQMRL 393
Cdd:PTZ00121 1420 -ADEAKKKAEEKKKAD---------EAKKKAEEAKKAdEAKKKAEEAKKAEEAK--KKAEEAKKADEAKKKAEEAKKADE 1487
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034643727 394 RYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKKDGPHGSVLEE 450
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
222-431 |
3.11e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 222 KLQKTLIDLEKREQQLASVESELQREKKELQSERQRnLQELQDSIRRakedcihQVELERLKIKQLEEDKH--RLQQQLN 299
Cdd:COG3206 202 RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE-AEARLAALRA-------QLGSGPDALPELLQSPViqQLRAQLA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 300 DAENKYKILEKEFqqfkdqQNNKPEIR-LQSEINlltlekvELERKLESATksklhyKQQWGRALKELARLKQREQE--S 376
Cdd:COG3206 274 ELEAELAELSARY------TPNHPDVIaLRAQIA-------ALRAQLQQEA------QRILASLEAELEALQAREASlqA 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034643727 377 QMARLKKQQEELEQMRLRYLAAEEKdtVKTERQELLDIRNELNRLRQQEQKQYQD 431
Cdd:COG3206 335 QLAQLEARLAELPELEAELRRLERE--VEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
210-436 |
4.28e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 210 KKKVAEYTILEGKLQKTLIDLEKREQQLaSVESELQREKKELQSERQRNLQELQDSIRRAKEDCIHQVELERLKIKQLEE 289
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKL-QELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 290 DKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKPEIrlQSEINLLTLEKVELERKLESATKSKLHYKQQWGRALKELARL 369
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ--EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034643727 370 KQREQESQMARLKKQQEELEQMRLRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIA 436
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
219-321 |
4.73e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 219 LEGKLQKTLIDLEKREQQLASVESELQREKKELQSERQRNLQEL----QDSIRRAKE--DCIHQVELERLKIKQLEEDKH 292
Cdd:PRK00409 528 LERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaQQAIKEAKKeaDEIIKELRQLQKGGYASVKAH 607
|
90 100
....*....|....*....|....*....
gi 1034643727 293 RLQQQLNDAENKYKILEKEFQQFKDQQNN 321
Cdd:PRK00409 608 ELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
172-350 |
6.86e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.23 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 172 KEMQEDIFENQLKQKELAHMQALAEEWKKRDRERESLVKKKVAEYTILEGKLQKTLIDLEKREQQLASVESELQREKKEL 251
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 252 QSERQRNLQeLQDSIRRAKEDcIHQVElerLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFKDQQNNKpeirlQSEI 331
Cdd:TIGR04523 429 ERLKETIIK-NNSEIKDLTNQ-DSVKE---LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK-----EKEL 498
|
170
....*....|....*....
gi 1034643727 332 NLLTLEKVELERKLESATK 350
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTK 517
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
233-400 |
8.12e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 233 REQQLASVESELQrEKKELQSERQRNLQELQdsirRAKEDcihqveLERLKIKQL--------EEDKHRLQQQLNDAENK 304
Cdd:PRK04863 784 REKRIEQLRAERE-ELAERYATLSFDVQKLQ----RLHQA------FSRFIGSHLavafeadpEAELRQLNRRRVELERA 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 305 YKILEKEFQQFKDQ-QNNKPEI----RLQSEINLL---TLEK--VELERKLESATKSKLhYKQQWGRALKELarlkqreq 374
Cdd:PRK04863 853 LADHESQEQQQRSQlEQAKEGLsalnRLLPRLNLLadeTLADrvEEIREQLDEAEEAKR-FVQQHGNALAQL-------- 923
|
170 180
....*....|....*....|....*.
gi 1034643727 375 ESQMARLKKQQEELEQMRLRYLAAEE 400
Cdd:PRK04863 924 EPIVSVLQSDPEQFEQLKQDYQQAQQ 949
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
176-408 |
8.17e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.76 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 176 EDIFENQLK-QKELAHMQALAEEWKKRDRERESLVKKKVAEytiLEGKLQKTLIDLEKREQQLASVESELQREKKELQSE 254
Cdd:PRK05771 46 RKLRSLLTKlSEALDKLRSYLPKLNPLREEKKKVSVKSLEE---LIKDVEEELEKIEKEIKELEEEISELENEIKELEQE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 255 RQR---------NLQELQDS---------IRRAKEDCIHQVElERLKIKQLEEDKHRLQQQLNDAENKYKILEKEFQQFK 316
Cdd:PRK05771 123 IERlepwgnfdlDLSLLLGFkyvsvfvgtVPEDKLEELKLES-DVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 317 DQQNNKPEIRLQSE-INLLTLEKVELERKLESatksklhykqqwgrALKELARLKQREQESQMArlkkQQEELEQMRLRY 395
Cdd:PRK05771 202 FERLELEEEGTPSElIREIKEELEEIEKERES--------------LLEELKELAKKYLEELLA----LYEYLEIELERA 263
|
250
....*....|...
gi 1034643727 396 LAAEEkdTVKTER 408
Cdd:PRK05771 264 EALSK--FLKTDK 274
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
41-74 |
8.49e-03 |
|
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 35.89 E-value: 8.49e-03
10 20 30
....*....|....*....|....*....|....
gi 1034643727 41 LLVELWHKDKMSKDLLLGIARIQLSNILSSEKTR 74
Cdd:cd00030 63 LTVEVWDKDRFSKDDFLGEVEIPLSELLDSGKEG 96
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
238-369 |
8.50e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 38.69 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 238 ASVESELQREKKELQSERQRNLQELQDSIRRAKEDciHQVELERL--KIKQLEEDKHRLQQQLNDAENKYKILEKEFQQF 315
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTE--EEEEIRRLeeQVERLEAEVEELEAELEEKDERIERLERELSEA 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034643727 316 KDQQNNkpEIRLQSEINLLTLEKVELERKLESA--TKSKLHYKQQwgrALKELARL 369
Cdd:COG2433 454 RSEERR--EIRKDREISRLDREIERLERELEEEreRIEELKRKLE---RLKELWKL 504
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
222-440 |
8.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 222 KLQKTLIDLEKREQQLASVESELQREKKELQSErqrnLQELQDSIRRAKEdcihqvelerlKIKQLEEDKHRLQQQLNDA 301
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEE----YNELQAELEALQA-----------EIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 302 ENKYKilekefQQFKDQQNNKpeiRLQSEINLLT--------LEKVELERKLESATKSKLhyKQQwgRALKELARLKQRE 373
Cdd:COG3883 85 REELG------ERARALYRSG---GSVSYLDVLLgsesfsdfLDRLSALSKIADADADLL--EEL--KADKAELEAKKAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034643727 374 QESQMARLKKQQEELEQMR-----LRYLAAEEKDTVKTERQELLDIRNELNRLRQQEQKQYQDSTEIASGKK 440
Cdd:COG3883 152 LEAKLAELEALKAELEAAKaeleaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
268-428 |
8.72e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 38.78 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 268 RAKEDCIHQVELERlKIKQLEEDKHRLQQQLNDAENKYKILEKEfqqfkdQQNNKPEIRL----QSEINLLTLEKVELER 343
Cdd:pfam15709 339 RAERAEMRRLEVER-KRREQEEQRRLQQEQLERAEKMREELELE------QQRRFEEIRLrkqrLEEERQRQEEEERKQR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643727 344 KLESATKSKLHYKQQ-WGRALKELARLKQREQESQMARLKKQQEEL------EQMRLRYLAAEEKDTVKTERQELLD-IR 415
Cdd:pfam15709 412 LQLQAAQERARQQQEeFRRKLQELQRKKQQEEAERAEAEKQRQKELemqlaeEQKRLMEMAEEERLEYQRQKQEAEEkAR 491
|
170
....*....|...
gi 1034643727 416 NELNRLRQQEQKQ 428
Cdd:pfam15709 492 LEAEERRQKEEEA 504
|
|
| |
