|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
196-529 |
8.57e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 196 AREAERQLV-LRLKERCEQQTRQLGVAQGELKRAicgfdaLAVATQHFFRKN-ESALVKEKELSIELANIRDEVAFHTAK 273
Cdd:TIGR02168 195 LNELERQLKsLERQAEKAERYKELKAELRELELA------LLVLRLEELREElEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 274 CEKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQLQfEAEMARLQ---EEHGDQLLSIRCQHQEQVEDLTAShDAA 350
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELY-ALANEISRLEQQKQIL-RERLANLErqlEELEAQLEELESKLDELAEELAEL-EEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 351 LLEMENNHTVaitiLQDDHD--HKVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE 428
Cdd:TIGR02168 346 LEELKEELES----LEAELEelEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 429 EQLEIALAPYQH-LEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDqntvVTRQL 507
Cdd:TIGR02168 422 EIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD----SLERL 497
|
330 340
....*....|....*....|..
gi 1370463760 508 SEENANLQEYVEKETQEKKRLS 529
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-535 |
6.97e-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: 62.00 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 252 KEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLS 331
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 332 IRCQHQEQVEDLTASHDAALLEMENNHTV---AITILQDDHD------HKVQELMSTHELEKKELEENFEKLRLSLQDQV 402
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTllneeaANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 403 DTLTFQSQSLRDrarrfEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELE----KLAEKNII 478
Cdd:TIGR02168 852 EDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRreleELREKLAQ 926
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463760 479 LEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEK-KRLSRTNEEL 535
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-499 |
4.53e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 195 QAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKC 274
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 275 EKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEM 354
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALD-ELRAELTLLNEEAA-NLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 355 ENnHTVAITILQDDHDHKVQELMSThelekkeleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIA 434
Cdd:TIGR02168 862 EE-LEELIEELESELEALLNERASL------------EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370463760 435 LApyqhleedmkslKQVLEMKNQQIHEQ--EKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQ 499
Cdd:TIGR02168 929 LR------------LEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
269-534 |
1.37e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.83 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 269 FHTAKCEKLQKEKEELERRFE--------DEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLSiRCQHQEQV 340
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVErrrkleeaEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE-RIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 341 EDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRlslQDQVDTLTFQSQSLRD-RARRF 419
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR---AEQEEARQREVRRLEEeRAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 420 EEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQ-IHEQEKKILELEKLAEKNIILEE--KIQVLQQQNEDLKA- 495
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKrAEEQRRKILEKELEERKQAMIEEerKRKLLEKEMEERQKa 528
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370463760 496 -------RIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEE 534
Cdd:pfam17380 529 iyeeerrREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-536 |
2.56e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 276 KLQKEKEELERR---FEDEVKRlgwQQQAELQELEERLQLQFEAEMARLQEEHGdQLLSIRCQHQEQVEDLTAshdaaLL 352
Cdd:COG1196 217 ELKEELKELEAElllLKLRELE---AELEELEAELEELEAELEELEAELAELEA-ELEELRLELEELELELEE-----AQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 353 EMENNHTVAITILQDDHDHKVQELmsthelekKELEENFEKlrlsLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLE 432
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERR--------RELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 433 IAlapyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNtvvTRQLSEENA 512
Cdd:COG1196 356 AE----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL---EEELEELEE 428
|
250 260
....*....|....*....|....
gi 1370463760 513 NLQEYVEKETQEKKRLSRTNEELL 536
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
255-535 |
3.91e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 255 ELSIELANIRDEVAFHTAKCEKLQKEKEELERrfedevkrlgwqqqaELQELEERL-QLQFEAEMARLQEEHGDQLLSIR 333
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRK---------------ELEELEEELeQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 334 CQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQElmsthelekkeleenfEKLRLSLQDQVDTLTFQSQSLR 413
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA----------------EAEIEELEAQIEQLKEELKALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 414 DRARRFEEALRkNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDL 493
Cdd:TIGR02168 803 EALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1370463760 494 KARIDQNTVVTRQLSEENANLQEYVEKETQEKKR-LSRTNEEL 535
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRReLEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-519 |
4.25e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 195 QAREAERQLVLRLKERcEQQTRQLGVAQGELKRAIcgfdalavatqhffRKNESALVKEKELSIELANIRDEVafhtakc 274
Cdd:COG1196 219 KEELKELEAELLLLKL-RELEAELEELEAELEELE--------------AELEELEAELAELEAELEELRLEL------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 275 EKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEM 354
Cdd:COG1196 277 EELELELEEAQAEEYELLAELA-RLEQDIARLEERRR-ELEERLEELEEELAELEEELE-ELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 355 EnnhtvaitILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIA 434
Cdd:COG1196 354 E--------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 435 LApyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANL 514
Cdd:COG1196 426 LE--EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
....*
gi 1370463760 515 QEYVE 519
Cdd:COG1196 504 EGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-499 |
1.04e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 197 REAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKElsiELANIRDEVAFHTAKCEK 276
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS---ELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 277 LQKEKEELERRFEDEvkrlGWQQ-QAELQELEE---RLQLQFEAEMARLQEEHGD-QLLSIRCQH-QEQVEDLTASHDAA 350
Cdd:TIGR02169 777 LEEALNDLEARLSHS----RIPEiQAELSKLEEevsRIEARLREIEQKLNRLTLEkEYLEKEIQElQEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 351 LLEMENNHTVAITILQ--DDHDHKVQELMSTHELEKKELEENFEKLRlSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE 428
Cdd:TIGR02169 853 EKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLR-ELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 429 EQLEIALAPYQHLEE-----DMKSLKQVLEMKNQQIHEQE----KKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQ 499
Cdd:TIGR02169 932 ELSEIEDPKGEDEEIpeeelSLEDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
275-552 |
7.03e-06 |
|
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: 49.35 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 275 EKLQKEKEELERRFE-DEVKRLGWQQQAELQELEERLQlQFEAEMARLQEEHGDQLLSIRcqhqeqveDLTASHDAALLE 353
Cdd:pfam15921 591 EKAQLEKEINDRRLElQEFKILKDKKDAKIRELEARVS-DLELEKVKLVNAGSERLRAVK--------DIKQERDQLLNE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 354 ME------NNHTVAITILQDDHDHKVQELMSTHelekkeleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNT 427
Cdd:pfam15921 662 VKtsrnelNSLSEDYEVLKRNFRNKSEEMETTT-----------NKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAM 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 428 EEQLEIALAPYQ--HLEEDMKSLKQVLEMKNQQIH----EQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNT 501
Cdd:pfam15921 731 GMQKQITAKRGQidALQSKIQFLEEAMTNANKEKHflkeEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1370463760 502 VVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTSPIKLSP 552
Cdd:pfam15921 811 VALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKP 861
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-499 |
1.26e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 248 SALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFE--DEVKRLGWQQ------QAELQELEERLQL------- 312
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEidvasaEREIAELEAELERldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 313 ---------QFEAEMARLQEEHGDQLLSIRcQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMsthele 383
Cdd:COG4913 687 laaleeqleELEAELEELEEELDELKGEIG-RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL------ 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 384 kkeLEENFEKLRLSLQDQVDTltfqsqsLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEM----KNQQI 459
Cdd:COG4913 760 ---GDAVERELRENLEERIDA-------LRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALldrlEEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1370463760 460 HEQEKKILELEKLAEKNIIlEEKIQVLQQQNEDLKARIDQ 499
Cdd:COG4913 830 PEYEERFKELLNENSIEFV-ADLLSKLRRAIREIKERIDP 868
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
410-540 |
1.62e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 410 QSLRDRARRFEEALRKNtEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQ 489
Cdd:COG1196 235 RELEAELEELEAELEEL-EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEER 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1370463760 490 NEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 540
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
298-541 |
4.55e-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: 46.60 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 298 QQQAELQELEERLQlQFEAEMARLQEE--HGDQLLSircQHQEQVEDLTASHDAALLEMEnnhtvaitILQDDHDHKVQE 375
Cdd:TIGR02169 671 SEPAELQRLRERLE-GLKRELSSLQSElrRIENRLD---ELSQELSDASRKIGEIEKEIE--------QLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 376 LmsthelekkeleenfEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIAlAPYQHL-EEDMKSLKQVLEM 454
Cdd:TIGR02169 739 L---------------EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN-DLEARLsHSRIPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 455 KNQQIHEQEKKILELE----KLAEKNIILEEKIQVLQQQNEDLKARIDQN---------------------TVVTRQLSE 509
Cdd:TIGR02169 803 LEEEVSRIEARLREIEqklnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeienlngkkeeleeeleelEAALRDLES 882
|
250 260 270
....*....|....*....|....*....|..
gi 1370463760 510 ENANLQEYVEKETQEKKRLSRTNEELLWKLQT 541
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
252-535 |
1.17e-04 |
|
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: 45.01 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 252 KEKElsIELANIRDEVAFHTAKCEKLQKEKEELERRFEdevkrlgwQQQAELQELEERLQlQFEAEMARLQEEHgDQLLS 331
Cdd:TIGR04523 366 EEKQ--NEIEKLKKENQSYKQEIKNLESQINDLESKIQ--------NQEKLNQQKDEQIK-KLQQEKELLEKEI-ERLKE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 332 IRCQHQEQVEDLTaSHDAALLEMENNH--------------TVAITILQDDHDHKVQELMSTHELEKKELEENFEklrls 397
Cdd:TIGR04523 434 TIIKNNSEIKDLT-NQDSVKELIIKNLdntresletqlkvlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE----- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 398 LQDQVDTLTFQSQSLRDRARRFE-EALRKNTEeqleialapYQHLEEDMKSLKQVLEMKN--QQIHEQEKKILEL----E 470
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLEsEKKEKESK---------ISDLEDELNKDDFELKKENleKEIDEKNKEIEELkqtqK 578
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463760 471 KLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 535
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
254-533 |
1.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 254 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAE-LQELEERLqlqfeaemarlqEEHGDQLLSI 332
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqLKELEEKL------------KKYNLEELEK 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 333 RCQHQEQVEDLtashdaaLLEMENNhtvaITILQDDHDhKVQELMStHELEKKELEENFEKLRLSLQDQVDTLTFQS-QS 411
Cdd:PRK03918 523 KAEEYEKLKEK-------LIKLKGE----IKSLKKELE-KLEELKK-KLAELEKKLDELEEELAELLKELEELGFESvEE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 412 LRDRARRFEEALR-----KNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILEL---------EKLAEKNI 477
Cdd:PRK03918 590 LEERLKELEPFYNeylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseeeyEELREEYL 669
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463760 478 ILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNE 533
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| PHA03381 |
PHA03381 |
tegument protein VP22; Provisional |
37-182 |
1.71e-04 |
|
tegument protein VP22; Provisional
Pssm-ID: 177618 [Multi-domain] Cd Length: 290 Bit Score: 43.85 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 37 PQSPAPSPGTVHSQSRAG--QPPEFHLNGTMQYVVSFVWHLSLMLLrlICLVAGSTFGNEEQPVLKASLPSKDTP----K 110
Cdd:PHA03381 25 FISPDASPARVSFEEPADraRRGAGQARGRSQAERRFHHYDEARAD--YPYYTGSSSEDERPADPRPSRRPHAQPeasgP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 111 GAGRVAPPASSSVTAPRRSLLPAPKSTSTPAG-----TKKDAQKDQDT--NKPAVSSPKRV---AASTTKLHSPGYPKQR 180
Cdd:PHA03381 103 GPARGARGPAGSRGRGRRAESPSPRDPPNPKGasaprGRKSACADSAAllDAPAPAAPKRQktpAGLARKLHFSTAPTSP 182
|
..
gi 1370463760 181 TA 182
Cdd:PHA03381 183 TA 184
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-541 |
2.15e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 242 FFRKNESAL-------VKEKELSIELANIRDEVafhtakcEKLQKEKEELERrFEDEVKRL----GWQQQAELQELEERL 310
Cdd:TIGR02169 168 FDRKKEKALeeleeveENIERLDLIIDEKRQQL-------ERLRREREKAER-YQALLKEKreyeGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 311 QlQFEAEMARLQEEhgdqllsircqhqeqVEDLTASHDAALLEMEnnhtvAITILQDDHDHKVQELMSTHELEKKELEEN 390
Cdd:TIGR02169 240 E-AIERQLASLEEE---------------LEKLTEEISELEKRLE-----EIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 391 FEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTE--EQLEIALAPYQ----HLEEDMKSLKQVLEMKNQqiheqek 464
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAeiEELEREIEEERkrrdKLTEEYAELKEELEDLRA------- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 465 kilELEKLAEKNIILEEKIQVLQQQNEDLKARI-------DQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLW 537
Cdd:TIGR02169 372 ---ELEEVDKEFAETRDELKDYREKLEKLKREInelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
....
gi 1370463760 538 KLQT 541
Cdd:TIGR02169 449 EIKK 452
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
420-549 |
3.49e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 420 EEALRKNTEEQLEialapyQHLEEDMKSLKQV-----------LEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQ 488
Cdd:PHA02562 108 ESASSKDFQKYFE------QMLGMNYKSFKQIvvlgtagyvpfMQLSAPARRKLVEDLLDISVLSEMDKLNKDKIRELNQ 181
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370463760 489 QNEDLKARID--------QNTVVTRQLSEENANLQEY-------VEKETQEKKRLSRTNEELL-WKLQTGDPTSPIK 549
Cdd:PHA02562 182 QIQTLDMKIDhiqqqiktYNKNIEEQRKKNGENIARKqnkydelVEEAKTIKAEIEELTDELLnLVMDIEDPSAALN 258
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
207-535 |
3.80e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 207 LKERCEQQ---TRQLGVAQGELKRAICGFDALAVATQhFFRKNESALVKEKELSIELANIRDE------VAFHTAKC--- 274
Cdd:pfam05483 284 LKELIEKKdhlTKELEDIKMSLQRSMSTQKALEEDLQ-IATKTICQLTEEKEAQMEELNKAKAahsfvvTEFEATTCsle 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 275 EKLQKEKEELERRfEDEVKRLGWQQQAELQELEERLQLQF--EAEMARLQEEHGDQ--LLSIRCQHQEQVEDLTASHDAA 350
Cdd:pfam05483 363 ELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMTKFKNnkEVELEELKKILAEDekLLDEKKQFEKIAEELKGKEQEL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 351 LLEME------NNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEklrlsLQDQVDTLTFQSQSLRDRARRFEEALR 424
Cdd:pfam05483 442 IFLLQarekeiHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE-----LTAHCDKLLLENKELTQEASDMTLELK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 425 K------NTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKI-LELEKLAEKNIILEEKIQVLQQQNEDLKARI 497
Cdd:pfam05483 517 KhqediiNCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
330 340 350
....*....|....*....|....*....|....*...
gi 1370463760 498 DQntvVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 535
Cdd:pfam05483 597 NN---LKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
212-488 |
4.74e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 212 EQQTR--QLGVAQGELKRA--ICGFDAL----AVATQHFFRKNESA-----LVKEKELSIE-------------LANIRD 265
Cdd:COG3096 407 VQQTRaiQYQQAVQALEKAraLCGLPDLtpenAEDYLAAFRAKEQQateevLELEQKLSVAdaarrqfekayelVCKIAG 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 266 EV----AFHTAKceklqkekeELERRFEDEVKRLGWQQQ--AELQELEERLQLQFEAEmaRLQEEHGdQLLSIRCQHQEQ 339
Cdd:COG3096 487 EVersqAWQTAR---------ELLRRYRSQQALAQRLQQlrAQLAELEQRLRQQQNAE--RLLEEFC-QRIGQQLDAAEE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 340 VEDLTASHDAallemennhtvaitiLQDDHDHKVQElmsthelekkeleenFEKLRLSLQDQVDTLTFQSQSLRDRA--- 416
Cdd:COG3096 555 LEELLAELEA---------------QLEELEEQAAE---------------AVEQRSELRQQLEQLRARIKELAARApaw 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463760 417 RRFEEALRKnTEEQLEIALAPYQHLEEDMkslkqvlemknQQIHEQEKKI-LELEKLAEKNIILEEKIQVLQQ 488
Cdd:COG3096 605 LAAQDALER-LREQSGEALADSQEVTAAM-----------QQLLEREREAtVERDELAARKQALESQIERLSQ 665
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
254-499 |
5.10e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 254 KELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGwQQQAELQELEERLQLQfEAEMARLQEehgdQLLSIR 333
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-ALARRIRALEQELAAL-EAELAELEK----EIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 334 CQHQEQVEDLtASHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeleeNFEKLRLSLQDQVDTLTFQSQSLR 413
Cdd:COG4942 97 AELEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ------------YLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 414 DrarrfeealrknTEEQLEIALAPYQHLEEDMKSLKQVLEmknQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQNEDL 493
Cdd:COG4942 164 A------------LRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAE---LAAELAELQQEAEEL 225
|
....*.
gi 1370463760 494 KARIDQ 499
Cdd:COG4942 226 EALIAR 231
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
410-534 |
6.29e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 410 QSLRDRARRFEEALRKNTEEQLEIALapyQHLEEDMKSLKQVLEmknQQIHEQEKKILELEK-LAEKNIILEEKIQVLQQ 488
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL---LEAKEEIHKLRNEFE---KELRERRNELQKLEKrLLQKEENLDRKLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1370463760 489 QNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR-TNEE 534
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGlTAEE 154
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
443-535 |
6.61e-04 |
|
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: 42.70 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 443 EDMKSLKQVLEMKNQQIHEQ-EKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKE 521
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRElEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
90
....*....|....
gi 1370463760 522 TQEKKRLSRTNEEL 535
Cdd:TIGR04523 425 EKEIERLKETIIKN 438
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
243-524 |
7.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 243 FRKNESALVKEKELSIELANIRDEV-AFHTAKCEKLQKEKEELERRF---EDEVKRLGwQQQAELQELEERLQLqFEAEM 318
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLkKYNLEELEKKAEEYEKLKEKLiklKGEIKSLK-KELEKLEELKKKLAE-LEKKL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 319 ARLQEEHGDQLLSIRCQHQEQVEDLtashDAALLEMENNHTVAITILQDDHDHKVQElmsthelekkeleENFEKLRLSL 398
Cdd:PRK03918 566 DELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLELKDAEKELEREE-------------KELKKLEEEL 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 399 QDQVDTLTFQSQSLRDRARRFEEALRKNTEEQleialapYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNII 478
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSEEE-------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370463760 479 LEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQE 524
Cdd:PRK03918 702 ELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGE 747
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
398-535 |
8.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 398 LQDQVDTLTFQSQSLRDRARRFEEALRKnteeqLEIALAPYQHLEEdMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNI 477
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEK-----LEKLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463760 478 ILEEKIQVLQQQNEDLKARIDQNTVVT-RQLSEENANLQEYVEKETQEKKRLSRTNEEL 535
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
192-534 |
8.92e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 192 PDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAIcgfDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHT 271
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA---ESLREDADDLEERAEELREEAAELESELEEAREAVEDRR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 272 AKCEKLQKEKEELERRFEDEVKRLGWQQ--------------------QAELQELEERLqlqfeAEMARLQEE------- 324
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEdfleelreerdelrereaelEATLRTARERV-----EEAEALLEAgkcpecg 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 325 -------HGDQLLSIRcqhqEQVEDLTASHDAALLEMENnhtvaitiLQDDHDhKVQELMSTHEL--EKKELEENFEKLR 395
Cdd:PRK02224 459 qpvegspHVETIEEDR----ERVEELEAELEDLEEEVEE--------VEERLE-RAEDLVEAEDRieRLEERREDLEELI 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 396 LSLQDQVDTLTFQSQSLRDRArrfeEALRKNTEEQLEIAlapyQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEK 475
Cdd:PRK02224 526 AERRETIEEKRERAEELRERA----AELEAEAEEKREAA----AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL 597
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463760 476 NIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEEN---ANLQEYVEKETQEKKRLSRTNEE 534
Cdd:PRK02224 598 LAAIADAEDEIERLREKREALAELNDERRERLAEKRerkRELEAEFDEARIEEAREDKERAE 659
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
426-532 |
9.35e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 426 NTEEQLEIALAPYQHLEEDMKSLKQVL-----EMKNQQIHEQEKKILEL-EKLAEKNIILEEKiQVLQQQNEDLKARIDQ 499
Cdd:PRK11281 198 QAEQALLNAQNDLQRKSLEGNTQLQDLlqkqrDYLTARIQRLEHQLQLLqEAINSKRLTLSEK-TVQEAQSQDEAARIQA 276
|
90 100 110
....*....|....*....|....*....|...
gi 1370463760 500 NTVVTRQLsEENANLQEYVEKETQEKKRLSRTN 532
Cdd:PRK11281 277 NPLVAQEL-EINLQLSQRLLKATEKLNTLTQQN 308
|
|
| CCDC14 |
pfam15254 |
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ... |
426-543 |
1.15e-03 |
|
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing protein 14 (CCDC14) is a domain of unknown function. This family of proteins is found in eukaryotes. Proteins in this family are typically between 301 and 912 amino acids in length.
Pssm-ID: 464594 Cd Length: 857 Bit Score: 42.09 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 426 NTEEQLEIALApYQHLEEDMKSLKQVLEMKNQQIHEQEKKI---------LELEKLAEKNIILEEKIQVLQQQNEDLKAR 496
Cdd:pfam15254 378 NTNIQAEIALA-LQPLRSENAQLRRQLRILNQQLREQEKTEktsgsgdcnLELFSLQSLNMSLQNQLQESLKSQELLQSK 456
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1370463760 497 idqntvvtrqlseeNANLQEYVEKETQEKKRLSRT----NEELLWKLQTGD 543
Cdd:pfam15254 457 --------------NEELLKVIENQKEENKKLTKIfkekEQTLLENKQQFD 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
408-540 |
1.81e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 408 QSQSLRDRARRFEEALRKNTEE---QLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNII---LE 480
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEeKLEELRLEvseLE 280
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 481 EKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 540
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
254-535 |
1.85e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 254 KELSIELANIRDEVafhtakcEKLQKEKEELERRFE--DEVKRLGWQQQAELQELEERLQlQFEAEMARLQEEHGDQlls 331
Cdd:PRK03918 210 NEISSELPELREEL-------EKLEKEVKELEELKEeiEELEKELESLEGSKRKLEEKIR-ELEERIEELKKEIEEL--- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 332 ircqhQEQVEDLTAshdaalLEMENNHTVAITILQDDHDHKVQELmsthelekKELEENFEKLRLSLQDQVDTLTFQSQS 411
Cdd:PRK03918 279 -----EEKVKELKE------LKEKAEEYIKLSEFYEEYLDELREI--------EKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 412 LRDRARRFEEALRKNTEeqleiaLAPYQHLEEDMKSLKQVLE-----MKNQQIHEQEKKILELEK----LAEKNIILEEK 482
Cdd:PRK03918 340 LEELKKKLKELEKRLEE------LEERHELYEEAKAKKEELErlkkrLTGLTPEKLEKELEELEKakeeIEEEISKITAR 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 483 IQVLQQQNEDLKARIDQ-------NTVVTRQLSEENAnlQEYVEKETQEKKRLSRTNEEL 535
Cdd:PRK03918 414 IGELKKEIKELKKAIEElkkakgkCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEI 471
|
|
| PRK14954 |
PRK14954 |
DNA polymerase III subunits gamma and tau; Provisional |
63-200 |
2.16e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184918 [Multi-domain] Cd Length: 620 Bit Score: 41.08 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 63 GTMQYVVSFVWHLSLMLLRLICLVAGSTfgnEEQPVLKASLPSKDT-----PKGAGRVAPPASSSVTAPRRSLLPAPKST 137
Cdd:PRK14954 351 GELKFQFEYQFRFELALLRLIELVRNDG---GVAPSPAGSPDVKKKapepdLPQPDRHPGPAKPEAPGARPAELPSPASA 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463760 138 STPAGTKKDAQKDQDTNKPAVSSPKRVAASTTKLHSPGYPKQRTAAARNGFPPKPdPQAREAE 200
Cdd:PRK14954 428 PTPEQQPPVARSAPLPPSPQASAPRNVASGKPGVDLGSWQGKFMNFTRNGSRKQP-VQASSSD 489
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
97-199 |
2.93e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 97 PVLKASLPSKDTPKGAGRVAPPASSSVTAPRRslLPAPKSTSTPAGTKKDAQKDQDTNKPAVSSPKRVAASTTKLHSPGY 176
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRR--LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828
|
90 100
....*....|....*....|...
gi 1370463760 177 PKQRTAAARNGFPPKPDPQAREA 199
Cdd:PHA03247 2829 PPPTSAQPTAPPPPPGPPPPSLP 2851
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
426-540 |
2.97e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 38.37 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 426 NTEEQLEIALAPYQHLEEDMKSLKQVLEmknQQIHEQEKKIlELEKLAEKNiiLEEKIQVLQQQNEDLKARIDQNTVVTR 505
Cdd:pfam09744 33 NVLELLESLASRNQEHNVELEELREDNE---QLETQYEREK-ALRKRAEEE--LEEIEDQWEQETKDLLSQVESLEEENR 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370463760 506 QLSEENANLQEyvEKETQEKKRLSRTNE---ELLWKLQ 540
Cdd:pfam09744 107 RLEADHVSRLE--EKEAELKKEYSKLHEretEVLRKLK 142
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
191-535 |
3.97e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 191 KPDPQAREAERQLVlRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFH 270
Cdd:pfam01576 212 KLEGESTDLQEQIA-ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 271 TAKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQfeaemARLQEE---HGDQLLSIRCQHQEQVEDLTASH 347
Cdd:pfam01576 291 EKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELK-----KALEEEtrsHEAQLQEMRQKHTQALEELTEQL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 348 DAA------------LLEMENNHTVA----ITILQDDHDHK-------VQELMSTHELEkkeleenfEKLRLSLQDQVDT 404
Cdd:pfam01576 366 EQAkrnkanlekakqALESENAELQAelrtLQQAKQDSEHKrkklegqLQELQARLSES--------ERQRAELAEKLSK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 405 LTFQSQSLRDRARRFEEALRKNTEE--QLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILE-LEKLAEKNIILEE 481
Cdd:pfam01576 438 LQSELESVSSLLNEAEGKNIKLSKDvsSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEqLEEEEEAKRNVER 517
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463760 482 KIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQ-------EKKRLSRTNEEL 535
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQqleekaaAYDKLEKTKNRL 578
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
284-512 |
4.10e-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: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 284 LERRFEDEVKRLGWQQQaELQELEERLQlQFEAEMARLQEEHG------------DQLLSIRCQH---QEQVEDLTASHD 348
Cdd:COG3206 166 LELRREEARKALEFLEE-QLPELRKELE-EAEAALEEFRQKNGlvdlseeaklllQQLSELESQLaeaRAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 349 AALLEMENNHTVAITILQDDhdhKVQELMSthelekkeleeNFEKLRLSLQDQVDTLTFQS---QSLRDRARRFEEALRK 425
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSP---VIQQLRA-----------QLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 426 NTEEQLEIALAPYQHLEEDMKSLKQVLEmknqqihEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQnTVVTR 505
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLA-------QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE-ARLAE 381
|
....*..
gi 1370463760 506 QLSEENA 512
Cdd:COG3206 382 ALTVGNV 388
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
451-541 |
4.14e-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: 40.00 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 451 VLEMKNQQIHEQEKKILELEKlaeKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR 530
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKK---QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
90
....*....|.
gi 1370463760 531 TNEELLWKLQT 541
Cdd:TIGR04523 282 KIKELEKQLNQ 292
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
252-471 |
4.54e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 252 KEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLG--WQQQAELQELEERLQLQFE--AEMARLQEEHGD 327
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEehEERREELETLEAEIEDLREtiAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 328 QLLSircqHQEQVEDLtashdaallEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDqvdtLTF 407
Cdd:PRK02224 280 EVRD----LRERLEEL---------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA----HNE 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463760 408 QSQSLRDRARRFEEALRKNTEEQLEialapyqhLEEDMKSLKQVLEMKNQQIHEQEKKILELEK 471
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAE--------LESELEEAREAVEDRREEIEELEEEIEELRE 398
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-536 |
4.92e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 392 EKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALA------PYQHLEEDMKSLKQVLEMKNQQIHEQEKK 465
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrleqQKQILRERLANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463760 466 ILEL-EKLAEkniiLEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEyvEKETQEKKRLSRTNEELL 536
Cdd:TIGR02168 332 LDELaEELAE----LEEKLEELKEELESLEAELEELEAELEELESRLEELEE--QLETLRSKVAQLELQIAS 397
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
392-511 |
5.49e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 392 EKLRLSLQDQVDTLTFQSQSLRDRARRFEEALrknteEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKK------ 465
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERL-----EELEERLEELRELEEELEELEAELAELQEELEELLEQlslate 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1370463760 466 ------ILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEEN 511
Cdd:COG4717 192 eelqdlAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
195-535 |
5.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 195 QAREAERQLVLRLKERCEQQTRQLGVAQGELKRAIcgfDALAVATQHFFRKNESALVKEK--ELSIELANIRDEVAFHT- 271
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREEL---EKLEKLLQLLPLYQELEALEAElaELPERLEELEERLEELRe 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 272 --AKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQ------LQFEAEMARLQEEHGDqllsIRCQHQEQVEDL 343
Cdd:COG4717 161 leEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEelqqrlAELEEELEEAQEELEE----LEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 344 TASHDAALLEMENNHTVAITIlqddhdhkVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEAL 423
Cdd:COG4717 237 EAAALEERLKEARLLLLIAAA--------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 424 RKNTEEQLEIA-----LAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQN----EDLK 494
Cdd:COG4717 309 ALPALEELEEEeleelLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGvedeEELR 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1370463760 495 ARIDQN----------TVVTRQLSEENANLQEYVEKETQE--KKRLSRTNEEL 535
Cdd:COG4717 389 AALEQAeeyqelkeelEELEEQLEELLGELEELLEALDEEelEEELEELEEEL 441
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
260-541 |
6.07e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 260 LANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQA-ELQELEERLQLQfEAEMARLQEEhgdqlLSIRCQHQE 338
Cdd:TIGR00618 221 KQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkQLRARIEELRAQ-EAVLEETQER-----INRARKAAP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 339 QVEdltasHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeLEENFEKLRLSLQDQVDTL-TFQSQSLRDRAR 417
Cdd:TIGR00618 295 LAA-----HIKAVTQIEQQAQRIHTELQSKMRSRAKLLM---------KRAAHVKQQSSIEEQRRLLqTLHSQEIHIRDA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 418 RFEEALRKnteEQLEIALAPYQHLeedmKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARI 497
Cdd:TIGR00618 361 HEVATSIR---EISCQQHTLTQHI----HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ 433
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370463760 498 D---QNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQT 541
Cdd:TIGR00618 434 ElqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
|
| FAM76 |
pfam16046 |
FAM76 protein; This family of proteins is functionally uncharacterized. This family of ... |
441-514 |
6.65e-03 |
|
FAM76 protein; This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 233 and 341 amino acids in length.
Pssm-ID: 464993 [Multi-domain] Cd Length: 303 Bit Score: 39.00 E-value: 6.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463760 441 LEEDMKSLKQVLEMKNQQIHEQEKKILELE-KLAEKNIILEEKIQVLQQQNEDlkaRIDQNTVVTRQLSEENANL 514
Cdd:pfam16046 227 LKEQIASLQKQLAQKDQQLLEKDKQITELKaKHFTKERELRNKMKTMEKEHED---KVEQLQIKIRSLLKEVATL 298
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
287-543 |
7.20e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 287 RFEDEVKRLGWQQQ---AELQELEERLQlQFEAEMARLQEEHgDQLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAIT 363
Cdd:TIGR00618 532 RGEQTYAQLETSEEdvyHQLTSERKQRA-SLKEQMQEIQQSF-SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 364 ILQDDHDHKVQELMSTHELEKKELEENFEK----LRLSLQDQVDTLTFQSQSLRDRARRFEEALRKnteEQLEIALAPYQ 439
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQelalKLTALHALQLTLTQERVREHALSIRVLPKELL---ASRQLALQKMQ 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 440 HLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniileekiqvLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVE 519
Cdd:TIGR00618 687 SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE----------IENASSSLGSDLAAREDALNQSLKELMHQARTVL 756
|
250 260
....*....|....*....|....
gi 1370463760 520 KETQEKKrlSRTNEELLWKLQTGD 543
Cdd:TIGR00618 757 KARTEAH--FNNNEEVTAALQTGA 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
271-496 |
7.24e-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: 38.98 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 271 TAKCEKLQKEKEELERRFEDEVKRLGWQQ------QAELQELEERLQL------QFEAEMARLQEEHGD---QLLSIRCQ 335
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKkeekalLKQLAALERRIAAlarrirALEQELAALEAELAElekEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 336 HQEQVEDLtASHDAALLEMENNHTVAITILQDDHDHKVQELMsthelekkeleeNFEKLRLSLQDQVDTLTFQSQSLRDR 415
Cdd:COG4942 99 LEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ------------YLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 416 ARRFEEAlRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKniiLEEKIQVLQQQNEDLKA 495
Cdd:COG4942 166 RAELEAE-RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE---LEALIARLEAEAAAAAE 241
|
.
gi 1370463760 496 R 496
Cdd:COG4942 242 R 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
178-534 |
8.53e-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: 39.05 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 178 KQRTAAARNGFPPKPDPQAREAErqlvlrLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHffrknESALVKEKELS 257
Cdd:pfam12128 401 KIREARDRQLAVAEDDLQALESE------LREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATA-----TPELLLQLENF 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 258 IELAN-IRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLG------WQQQAELQELEERLQ------LQFEAEMARLQEE 324
Cdd:pfam12128 470 DERIErAREEQEAANAEVERLQSELRQARKRRDQASEALRqasrrlEERQSALDELELQLFpqagtlLHFLRKEAPDWEQ 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 325 HGDQLLSIRCQHQeqvEDLTASHDAALLEMENN-HTVAITILQDDHDHKVQelmsthelekkeleenfekLRLSLQDQVD 403
Cdd:pfam12128 550 SIGKVISPELLHR---TDLDPEVWDGSVGGELNlYGVKLDLKRIDVPEWAA-------------------SEEELRERLD 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 404 TLTFQSQSLRDRARRFEEAL---RKNTEEQ---LEIALAPYQHLEEDMKSL---KQVLEMKNQQIHEQEKKIL--ELEKL 472
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLvqaNGELEKAsreETFARTALKNARLDLRRLfdeKQSEKDKKNKALAERKDSAneRLNSL 687
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463760 473 -AEKNIILEEKIQVLQQQNEDLK----ARIDQNTVVTRQLSEENANLQEYVEK-ETQEKKRLSRTNEE 534
Cdd:pfam12128 688 eAQLKQLDKKHQAWLEEQKEQKReartEKQAYWQVVEGALDAQLALLKAAIAArRSGAKAELKALETW 755
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
195-496 |
9.27e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 195 QAREAErQLVLRLKERC--------EQQTR--QLGVAQGELKRA--ICGFDALAV----ATQHFFRKNESALVK-----E 253
Cdd:PRK04863 384 RAEAAE-EEVDELKSQLadyqqaldVQQTRaiQYQQAVQALERAkqLCGLPDLTAdnaeDWLEEFQAKEQEATEellslE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 254 KELSI-ELANIRDEVAFHTAKC-------EKLQKEKEELERRFEDEVKRLGWQQQ--AELQELEERLQLQFEAEmaRLQE 323
Cdd:PRK04863 463 QKLSVaQAAHSQFEQAYQLVRKiagevsrSEAWDVARELLRRLREQRHLAEQLQQlrMRLSELEQRLRQQQRAE--RLLA 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 324 EHGdQLLSIRCQHQEQVEDLTASHDAALlemennhtvaitilqDDHDHKVQELmsthelekkeleenfEKLRLSLQDQVD 403
Cdd:PRK04863 541 EFC-KRLGKNLDDEDELEQLQEELEARL---------------ESLSESVSEA---------------RERRMALRQQLE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463760 404 TLTFQSQSLRDRARRFEEAlrKNTEEQLeialapYQHLEEDMKSLKQVLE-MKNQQIHEQEkkilelekLAEKNIILEEK 482
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAA--QDALARL------REQSGEEFEDSQDVTEyMQQLLERERE--------LTVERDELAAR 653
|
330
....*....|....
gi 1370463760 483 IQVLQQQNEDLKAR 496
Cdd:PRK04863 654 KQALDEEIERLSQP 667
|
|
| |
