|
Name |
Accession |
Description |
Interval |
E-value |
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
173-347 |
6.46e-57 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 189.24 E-value: 6.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 173 NRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKE 252
Cdd:pfam14662 17 NQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLEEARRSLLAQNKQLEKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 253 QQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQE 332
Cdd:pfam14662 97 NQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKSTVEEYSSIEEE 176
|
170
....*....|....*
gi 2462563097 333 LRLEISRLEEQLSQT 347
Cdd:pfam14662 177 LRAEKSRLESQLPDM 191
|
|
| EF-hand_9 |
pfam14658 |
EF-hand domain; |
38-105 |
1.35e-26 |
|
EF-hand domain;
Pssm-ID: 405361 Cd Length: 66 Bit Score: 102.50 E-value: 1.35e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462563097 38 NSTFEACDPQRTGTVAVAQVLAYLEAVTGQGPQDARLQTLANSLDPNGEGPkaTVDLDTFLVVMRDWI 105
Cdd:pfam14658 1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDA--LVDLDTFLRVMRDWI 66
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-349 |
3.97e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKamdEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEM 260
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR---ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 261 ETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRL 340
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
....*....
gi 2462563097 341 EEQLSQTYE 349
Cdd:TIGR02168 942 QERLSEEYS 950
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
180-392 |
5.43e-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: 55.84 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 180 NAKLQRSMETAEEGSARLGEEILALRKQLHSTQ----QALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQH 255
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 256 LVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLfecehliCQRDTILSERTRDVESLAQTLEEYRVTTQELRL 335
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL-------KDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462563097 336 EISRLEEQLSQTYEGPDELPEGAQlrrvgwtellppSLGLEIEAIRQKQEVATADLS 392
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKE------------DKALEIKKQEWKLEQLAADLS 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-354 |
5.70e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 174 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA-----------MDEELEDLKTLARSLEEQNRSL 242
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarleqdiarLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 243 LAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQT 322
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180 190
....*....|....*....|....*....|..
gi 2462563097 323 LEEYRVTTQELRLEISRLEEQLSQTYEGPDEL 354
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEE 440
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-413 |
6.66e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 174 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA----MDEELEDLKTLARSLEEQNRSLLAQARQA 249
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 250 EKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVT 329
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 330 TQELRLEISRLEEQLSQTY--------EGPDELPEGAQLRRVGWTEL-LPPSLGLEIEAIRQKQEVATADLSNPLCGVWQ 400
Cdd:COG1196 451 EAELEEEEEALLELLAELLeeaalleaALAELLEELAEAAARLLLLLeAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
250
....*....|...
gi 2462563097 401 WEEVIHETSEETE 413
Cdd:COG1196 531 GVEAAYEAALEAA 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-393 |
5.90e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 174 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAmdeELEDLKTLARSLEEQNRSLLAQARQAEKEQ 253
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK---ELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 254 QHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLA-------QTLEEY 326
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvaqleLQIASL 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462563097 327 RVTTQELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGWTELLPPSLGLEIEAIRQKQEVATADLSN 393
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
181-346 |
6.31e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA----MDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHL 256
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEErleeLEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 257 VAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLE 336
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170
....*....|
gi 2462563097 337 ISRLEEQLSQ 346
Cdd:COG1196 437 EEEEEEALEE 446
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-346 |
1.22e-06 |
|
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: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 174 RRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQfakAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQ 253
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---ELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 254 QHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQEL 333
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170
....*....|...
gi 2462563097 334 RLEISRLEEQLSQ 346
Cdd:COG1196 392 LRAAAELAAQLEE 404
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
182-363 |
1.45e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 182 KLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAM--DEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAE 259
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 260 METLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEhlicqrdtilsertRDVESLAQTLEEYRVTTQELRLEISR 339
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE--------------EELEELEAALRDLESRLGDLKKERDE 893
|
170 180
....*....|....*....|....
gi 2462563097 340 LEEQLSQTYEGPDELPEGAQLRRV 363
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRK 917
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
181-368 |
2.19e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQfakAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEM 260
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELE---QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 261 ETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQ-----ELRL 335
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQ 183
|
170 180 190
....*....|....*....|....*....|...
gi 2462563097 336 EISRLEEQLSQTYEGPDELPEGAQLRRVGWTEL 368
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
181-365 |
2.38e-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: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELE-DLKTLARSLEEQNRSLLAQARQAEKEQQH---- 255
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkEIAELRAELEAQKEELAELLRALYRLGRQppla 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 256 ------------------------LVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSE 311
Cdd:COG4942 124 lllspedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462563097 312 RTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGW 365
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
196-366 |
7.81e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 196 RLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSL--LAQARQAEKEQQHLVAEMETLQEENGKLLAE 273
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 274 RDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTI----LSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQTYE 349
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170
....*....|....*..
gi 2462563097 350 GPDELPEGAQLRRVGWT 366
Cdd:COG4717 235 ELEAAALEERLKEARLL 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
175-349 |
9.93e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 175 RLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFakamDEELEDLKTLAR---SLEEQNRSLLA---QARQ 248
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY----SWDEIDVASAEReiaELEAELERLDAssdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 249 AEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRv 328
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR- 768
|
170 180
....*....|....*....|.
gi 2462563097 329 ttQELRLEISRLEEQLSQTYE 349
Cdd:COG4913 769 --ENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-362 |
3.02e-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: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 199 EEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEE------QNRSLLAQAR--QAEKEQQHLVAEMETLQEENGKL 270
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAarerlaELEYLRAALRlwFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 271 LAERDGVKKRSQELAMEKDTLKRQLF--------ECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEE 342
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180
....*....|....*....|
gi 2462563097 343 QLSQTYEGPDELPEGAQLRR 362
Cdd:COG4913 388 EAAALLEALEEELEALEEAL 407
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-362 |
3.21e-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: 46.98 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 176 LVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALqfaKAMDEELEDL-KTLARSLEEQNRSLLAQARQAEKEQQ 254
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL---EELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 255 HLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELR 334
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180
....*....|....*....|....*...
gi 2462563097 335 LEISRLEEQLSQTYEGPDELPEGAQLRR 362
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLS 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
197-393 |
3.76e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 197 LGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLqEENGKLLAERDG 276
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVKELKELKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 277 VKKRSQELAMEKDTLKRQLFECEHLIC---QRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLsQTYEGPDE 353
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSrleEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKA 369
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462563097 354 LPEGAQLRRVGWTELLPPSLGLEIEAIRQKQEVATADLSN 393
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-350 |
8.30e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 195 ARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLaQARQAEKEQQHLVAEMETLQEENGKLLA-- 272
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAEREIAELEAELERLDASSDDLAAle 691
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462563097 273 -ERDGVKKRSQELAMEKDTLKRQLFECEHlicQRDTILSERTRdVESLAQTLEEYRVTTQELRLEiSRLEEQLSQTYEG 350
Cdd:COG4913 692 eQLEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDE-LQDRLEAAEDLARLELRALLE-ERFAAALGDAVER 765
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
205-405 |
3.13e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 205 RKQLHSTQQALqfakamdEELEDLktlARSLEEQNRSLLAQARQAEK------------------EQQHLVAEMETLQEE 266
Cdd:TIGR02168 178 ERKLERTRENL-------DRLEDI---LNELERQLKSLERQAEKAERykelkaelrelelallvlRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 267 NGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQ 346
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462563097 347 TYEGPDELPEGAQLRRVGWTELLPpslglEIEAIRQKQEVATADLSNPLCGVWQWEEVI 405
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKE-----ELESLEAELEELEAELEELESRLEELEEQL 381
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
188-367 |
3.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 188 ETAEEGSAR----LGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVA---EM 260
Cdd:PRK03918 161 ENAYKNLGEvikeIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 261 ETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLIcQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRL 340
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180
....*....|....*....|....*..
gi 2462563097 341 EEQLSQTYEGPDELPEgaQLRRVGWTE 367
Cdd:PRK03918 320 EEEINGIEERIKELEE--KEERLEELK 344
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-387 |
4.04e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 184 QRSMETAEEGSARLGEEILALRKQLHSTQ----QALQFaKAMDEELEDLK--TLARSLEEQNRSLLAQARQAEKEQQhlv 257
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSLErqaeKAERY-KELKAELRELElaLLVLRLEELREELEELQEELKEAEE--- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 258 aEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLIC---QRDTILSERTRDVESLAQTLEEYRVTTQ--- 331
Cdd:TIGR02168 254 -ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEAQLEELEskl 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462563097 332 -ELRLEISRLEEQLSQTYEGPDELPEGAQLRRVGWTELLPPSLGLEIEAIRQKQEVA 387
Cdd:TIGR02168 333 dELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-345 |
4.88e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 175 RLVGENAKLQRSMETAEEGSARLGE------EILALRKQLHSTQQALQFAKAMDEELEDLKTlarslEEQNRSLlaqaRQ 248
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEElkkklkELEKRLEELEERHELYEEAKAKKEELERLKK-----RLTGLTP----EK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 249 AEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEhlICQRD-------TILSERTRDVESLAQ 321
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP--VCGRElteehrkELLEEYTAELKRIEK 466
|
170 180
....*....|....*....|....
gi 2462563097 322 TLEEYRVTTQELRLEISRLEEQLS 345
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLK 490
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-358 |
7.38e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 181 AKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKA-MDEELEDLKTLARSLEEQNRS---------------LLA 244
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeIEERREELGERARALYRSGGSvsyldvllgsesfsdFLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 245 QARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLE 324
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
170 180 190
....*....|....*....|....*....|....
gi 2462563097 325 EYRVTTQELRLEISRLEEQLSQTYEGPDELPEGA 358
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
219-344 |
9.60e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 219 KAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQhLVAEMETLQEEngKLLAERDGVKKRSQELAMEKDTLKRQLFEC 298
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAERYRE-LKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEEL 258
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462563097 299 EHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQL 344
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
183-362 |
1.45e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 183 LQRSMETAEEGSARLGEEILALRKQLHSTQQALQ-FAK-----AMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHL 256
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEeFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 257 VAEMETLQEENGKLLAER--DGVKKRSQELAMEKDTLKRQLFEcEH-----LICQRDT----ILSERTRDVESLAQTLEE 325
Cdd:COG3206 246 RAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTP-NHpdviaLRAQIAAlraqLQQEAQRILASLEAELEA 324
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462563097 326 YRVTTQELRLEISRLEEQLSQTyegPDELPEGAQLRR 362
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAEL---PELEAELRRLER 358
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
191-295 |
1.91e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 191 EEGSARLGEEILALRKQLHSTQQalqfakamdeELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLQEENGKL 270
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAR----------EKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAET 210
|
90 100 110
....*....|....*....|....*....|.
gi 2462563097 271 LAE-RDGVKKRSQELAM-----EKDTlkRQL 295
Cdd:PRK11448 211 SQErKQKRKEITDQAAKrlelsEEET--RIL 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-346 |
2.87e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 204 LRKQLHS----TQQALQFaKAMDEELEDLKTLARSLEEqnRSLLAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKK 279
Cdd:COG1196 198 LERQLEPlerqAEKAERY-RELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462563097 280 RSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQ 346
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
179-390 |
2.90e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 179 ENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVA 258
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 259 EMETLQEEnGKL---------------LAERDGvkkRSQELAMEKDTLKRQLFECEHLIcQRDTILSERTRDVESLAQTL 323
Cdd:PRK02224 444 EAEALLEA-GKCpecgqpvegsphvetIEEDRE---RVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEERR 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462563097 324 E--EYRVTTQELRLEisRLEEQLSQTYEGPDELPEGAQLRRVGWTEllppslgLEIEAIRQKQEVATAD 390
Cdd:PRK02224 519 EdlEELIAERRETIE--EKRERAEELRERAAELEAEAEEKREAAAE-------AEEEAEEAREEVAELN 578
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
204-354 |
3.28e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 204 LRKQLHSTQQALQFAK----AMDEELEDLKTLARSLE-------EQNRSLLAQARQAEKEQQHLVAEMETLQEENGKL-- 270
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKkenqSYKQEIKNLESQINDLEskiqnqeKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNns 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 271 ----LAERDGVKKRS-QELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLS 345
Cdd:TIGR04523 441 eikdLTNQDSVKELIiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
....*....
gi 2462563097 346 QTYEGPDEL 354
Cdd:TIGR04523 521 SLKEKIEKL 529
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
210-342 |
3.78e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 210 STQQALqfAKAMDEELEDLKTLARSLEEQNRsllAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQELAMEKD 289
Cdd:COG2433 377 SIEEAL--EELIEKELPEEEPEAEREKEHEE---RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELS 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462563097 290 TLKRQlfecEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEE 342
Cdd:COG2433 452 EARSE----ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-460 |
3.78e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 179 ENAKLQRSMETAEEgsARLGEEIlalrKQLHSTQQALQFAKAmdEEL---EDLKTL--ARSLEEQNRSLLAQARQAEKEQ 253
Cdd:PTZ00121 1519 EEAKKADEAKKAEE--AKKADEA----KKAEEKKKADELKKA--EELkkaEEKKKAeeAKKAEEDKNMALRKAEEAKKAE 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 254 QHLVAEMETLQEENGKLLAERdgvKKRSQELAMEKDTLKRQLfECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQEL 333
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEE---AKKAEEAKIKAEELKKAE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 334 RL---EISRLEEQLSQTYEgpDELPEGAQLRRVGWTELLPPSL-GLEIEAIRQKQEVATADLSNPLcgvwQWEEVIHETS 409
Cdd:PTZ00121 1667 AKkaeEDKKKAEEAKKAEE--DEKKAAEALKKEAEEAKKAEELkKKEAEEKKKAEELKKAEEENKI----KAEEAKKEAE 1740
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462563097 410 EETEFPSEAPAG-GQRN-----FQGEPAHPEEGRKEPSMWLTRREEEEDAESQVTAD 460
Cdd:PTZ00121 1741 EDKKKAEEAKKDeEEKKkiahlKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
173-334 |
5.70e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 173 NRRLVGENAKLQRSMETAEEGSARLGEEILALRKQLHSTQQALQFAKAM----DEELEDLKTLARSL------------- 235
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlknaRLDLRRLFDEKQSEkdkknkalaerkd 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 236 --EEQNRSLLAQARQAEKEQQHLVAEM-ETLQEENGKLLAERDGVKKR--------SQELAMEKDTLKRQLFECEHlicQ 304
Cdd:pfam12128 679 saNERLNSLEAQLKQLDKKHQAWLEEQkEQKREARTEKQAYWQVVEGAldaqlallKAAIAARRSGAKAELKALET---W 755
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462563097 305 RDTIL----------SERTRDVESLAQTLEEYRVTTQELR 334
Cdd:pfam12128 756 YKRDLaslgvdpdviAKLKREIRTLERKIERIAVRRQEVL 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
200-346 |
6.74e-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: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 200 EILALRKQlhsTQQAL-----QFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLQEENG------ 268
Cdd:TIGR04523 296 EISDLNNQ---KEQDWnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEekqnei 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462563097 269 -KLLAERDGVKKRSQELAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYRVTTQELRLEISRLEEQLSQ 346
Cdd:TIGR04523 373 eKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
204-347 |
7.34e-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: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462563097 204 LRKQLHSTQQALQFAKAMDEELEDLKTLARSLEEQNRSLLAQARQAEKEQQHLVAEMETLQEENGKLLAERDGVKKRSQE 283
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462563097 284 LAMEKDTLKRQLFECEHLICQRDTILSERTRDVESLAQTLEEYR-----VTTQELRLEISRLEEQLSQT 347
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEI 326
|
|
| |
