|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
378-570 |
3.85e-80 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 251.07 E-value: 3.85e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 378 TQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKN 457
Cdd:pfam06818 1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 458 EAELLREKVNLLEQELLELRAQAAlhrDAAPLGPPGIGLTFS--------EDIPALQRELDRLRAELKEERQGHDQMSSG 529
Cdd:pfam06818 81 EAELLREKVGKLEEEVSGLREALS---DVSPSGYESVYESDEakeqrqeeADLGSLRREVERLRAELREERQRRERQASS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 23618893 530 FQHERLVWKEEKEKVIQYQKQLQQSYLAMYQRNQRLEKALQ 570
Cdd:pfam06818 158 FEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-591 |
6.89e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 262 TIQELEQKLLQRETALQKLQRSFDEKefasgqtfEERPRRTRDELECLEPKSKLkpasqksqrtqqvlqlqvlqLQQEKR 341
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEEL--------EEELEQLRKELEELSRQISA--------------------LRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 342 QLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDTR 421
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 422 GKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELLELRAQAALHrdaaplgppgigltfSED 501
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---------------LNE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 502 IPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQsylAMYQRNQRLEK--ALQQLARGDIAG 579
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG---LEVRIDNLQERlsEEYSLTLEEAEA 958
|
330
....*....|..
gi 23618893 580 EPFEIDLEGADI 591
Cdd:TIGR02168 959 LENKIEDDEEEA 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
339-574 |
9.57e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLK 418
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 419 DTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELLELRAQAALHRDAAplgppgigltf 498
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL----------- 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23618893 499 sediPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYLAMYQRNQRLEKALQQLAR 574
Cdd:COG1196 431 ----AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-467 |
1.77e-05 |
|
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: 48.13 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 263 IQELEQKLLQRETALQKLQRSFDEKEfASGQTFEERPRRTRDELECLEPKSKLKPASQKSQRtqqvlqlqvlQLQQEKRQ 342
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELE-AQLEELESKLDELAEELAELEEKLEELKEELESLE----------AELEELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 343 LRQELESLMKEQdlletklrsyEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSL-----KAQL 417
Cdd:TIGR02168 366 ELEELESRLEEL----------EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAEL 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 23618893 418 KDTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVN 467
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
341-583 |
1.19e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKEsqmeVNAKASEILSLKAQLKDT 420
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 421 RGKLEGMELKTQDLESALRTKGLELEvcenELQRKKNEAELLREKVNLLEQELLELRaqaalhrdaaplgppgiglTFSE 500
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIE----ELEEKVKELKELKEKAEEYIKLSEFYE-------------------EYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 501 DIPALQRELDRLRAELKEERQGHDQMSSgfQHERLVWKEEKEKVIQYQKQLQQSYLAMYQRNQRLEKALQQLaRGDIAGE 580
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERL-KKRLTGL 384
|
...
gi 23618893 581 PFE 583
Cdd:PRK03918 385 TPE 387
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
263-467 |
6.78e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 263 IQELEqKLLQRETALQKLQRSfDEKEFASG----QTFEERPRRTRDELECLEPK----SKLKPASQKSQRTQQVLQLQVL 334
Cdd:PRK03918 178 IERLE-KFIKRTENIEELIKE-KEKELEEVlreiNEISSELPELREELEKLEKEvkelEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 335 QLQQEKRQLRQELESLMKEQDLLETKLRSYE--REKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILS 412
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23618893 413 LKAQLKDTRGKLEGMELKTQDLESALRT------------------KGLELEVCENELQRKKNEAELLREKVN 467
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkkrlTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
220-463 |
7.07e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 220 QDSNMMSLKALSFSDGGSKLAHPGKVEKGSSCVRSPLS-------TDECTIQELEQKLLQRETALQKLQRSFDEKEFASG 292
Cdd:pfam15921 570 QIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkilkdKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 293 QTFEERP------RRTRDELECLEP-----KSKLKPASQKSQRTQQVLQLQVLQLQQEKRQLRQELESL----------- 350
Cdd:pfam15921 650 DIKQERDqllnevKTSRNELNSLSEdyevlKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMegsdghamkva 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 351 --MKEQ--------DLLETKLRSYEREKTNfapALEETQWEVCQKSGeislLKQQLKESQMEVNAKASEILSLKAQLKDT 420
Cdd:pfam15921 730 mgMQKQitakrgqiDALQSKIQFLEEAMTN---ANKEKHFLKEEKNK----LSQELSTVATEKNKMAGELEVLRSQERRL 802
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 23618893 421 RGKLEGMELktqdlesALRTKGLELEVCENELQRKKNEAELLR 463
Cdd:pfam15921 803 KEKVANMEV-------ALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
378-570 |
3.85e-80 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 251.07 E-value: 3.85e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 378 TQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKN 457
Cdd:pfam06818 1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 458 EAELLREKVNLLEQELLELRAQAAlhrDAAPLGPPGIGLTFS--------EDIPALQRELDRLRAELKEERQGHDQMSSG 529
Cdd:pfam06818 81 EAELLREKVGKLEEEVSGLREALS---DVSPSGYESVYESDEakeqrqeeADLGSLRREVERLRAELREERQRRERQASS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 23618893 530 FQHERLVWKEEKEKVIQYQKQLQQSYLAMYQRNQRLEKALQ 570
Cdd:pfam06818 158 FEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-591 |
6.89e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 262 TIQELEQKLLQRETALQKLQRSFDEKefasgqtfEERPRRTRDELECLEPKSKLkpasqksqrtqqvlqlqvlqLQQEKR 341
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEEL--------EEELEQLRKELEELSRQISA--------------------LRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 342 QLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDTR 421
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 422 GKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELLELRAQAALHrdaaplgppgigltfSED 501
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---------------LNE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 502 IPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQsylAMYQRNQRLEK--ALQQLARGDIAG 579
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG---LEVRIDNLQERlsEEYSLTLEEAEA 958
|
330
....*....|..
gi 23618893 580 EPFEIDLEGADI 591
Cdd:TIGR02168 959 LENKIEDDEEEA 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
339-574 |
9.57e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLK 418
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 419 DTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELLELRAQAALHRDAAplgppgigltf 498
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL----------- 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23618893 499 sediPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYLAMYQRNQRLEKALQQLAR 574
Cdd:COG1196 431 ----AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
339-573 |
1.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLK 418
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 419 DTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNllEQELLELRAQAALHRdaaplgppgigltF 498
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE--RLEARLERLEDRRER-------------L 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23618893 499 SEDIPALQRELDRL-RAELKEERQGHDQMSSGFQHERLVWKEEKEKViqyQKQLQQSYLAMYQRNQRLEKALQQLA 573
Cdd:TIGR02168 420 QQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEEL---REELEEAEQALDAAERELAQLQARLD 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-574 |
1.22e-07 |
|
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: 54.00 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLK 418
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 419 DTRGKLEGMELKTQDLEsalRTKGLELEVCENELQRKKNEAELLREKVNlleqellELRAQAalhrdaaplgppgigltf 498
Cdd:COG4942 101 AQKEELAELLRALYRLG---RQPPLALLLSPEDFLDAVRRLQYLKYLAP-------ARREQA------------------ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23618893 499 sEDIPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYLAMYQRNQRLEKALQQLAR 574
Cdd:COG4942 153 -EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
263-592 |
1.42e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 263 IQELEQKLLQRETALQKLQRSFDEKEfasgQTFEERPRRTRD--ELECLEPKSKLkpASQKSQRTQQVLQLqvlqlqqek 340
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIE----QLLEELNKKIKDlgEEEQLRVKEKI--GELEAEIASLERSI--------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDT 420
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 421 RGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELLELRAQaalhrdaaplgppgigltfse 500
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE--------------------- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 501 dIPALQRELDRLRAELKEERQghdqmssgfQHERLvwKEEKEKVIQYQKQLQQSYlamyqrnQRLEKALQQLARGDIAGE 580
Cdd:TIGR02169 450 -IKKQEWKLEQLAADLSKYEQ---------ELYDL--KEEYDRVEKELSKLQREL-------AEAEAQARASEERVRGGR 510
|
330
....*....|..
gi 23618893 581 PFEIDLeGADIP 592
Cdd:TIGR02169 511 AVEEVL-KASIQ 521
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
265-572 |
5.27e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 265 ELEQKLLQRetALQKLQRSFDEKEFASGQTFEERPRRTRDELECLEPKSKLKPASQKSQRtqqvlqlqvlqlqqEKRQLR 344
Cdd:pfam07888 30 ELLQNRLEE--CLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE--------------ELRQSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 345 QELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDTRGKL 424
Cdd:pfam07888 94 EKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 425 EGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQE-LLELRAQAALHRDAAPLGPPGIGLTFSED-I 502
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlTTAHRKEAENEALLEELRSLQERLNASERkV 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23618893 503 PALQREL-------DRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYLAMYQRNQRLEKALQQL 572
Cdd:pfam07888 254 EGLGEELssmaaqrDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRL 330
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-543 |
1.80e-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: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETqwevcqksgEISLLKQQLKESQMEVNAKASEILSLKAQLKDT 420
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 421 RGKLEGMELKTQDLESALrtKGLELEVCENELQRKKNEAELLREKVNLLEQELLELRAQAALhrdaaplgppgigLTFSE 500
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-------------RDLES 882
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23618893 501 DIPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEK 543
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
263-516 |
5.48e-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: 49.68 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 263 IQELEQKLLQRETALQKLQRSFDEKEFASGQtfeerprrTRDELECLEPKsklkpasqksqrtqqvlqlqvlQLQQEKRQ 342
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHK--------LEEALNDLEAR----------------------LSHSRIPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 343 LRQELESLMKEQDLLETKLRSYEREktnfapaLEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDTRG 422
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQK-------LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 423 KLEGMELKTQDLESALrtKGLELEVCE-----NELQRKKNEAELLREKVNlLEQELLELRAQAALHRDAAPLGPPGIGLT 497
Cdd:TIGR02169 869 ELEELEAALRDLESRL--GDLKKERDEleaqlRELERKIEELEAQIEKKR-KRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
250 260
....*....|....*....|..
gi 23618893 498 FSE---DIPALQRELDRLRAEL 516
Cdd:TIGR02169 946 IPEeelSLEDVQAELQRVEEEI 967
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-579 |
1.59e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFApALEETQWE---VCQKSGEISLLKQQLKEsqmeVNAKASEILSLKA 415
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDeidVASAEREIAELEAELER----LDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 416 QLKDTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELLELRAQAALHRDAaplgPPGIG 495
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV----ERELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 496 LTFSEDIPALQRELDRLRAELKEERQGHDQmssGFQHERLVWKEEKEKVIQYQK---QLQQSYLAMYQrnQRLEKALQQL 572
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAFNR---EWPAETADLDADLESLPEYLAlldRLEEDGLPEYE--ERFKELLNEN 843
|
....*..
gi 23618893 573 ARGDIAG 579
Cdd:COG4913 844 SIEFVAD 850
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-467 |
1.77e-05 |
|
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: 48.13 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 263 IQELEQKLLQRETALQKLQRSFDEKEfASGQTFEERPRRTRDELECLEPKSKLKPASQKSQRtqqvlqlqvlQLQQEKRQ 342
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELE-AQLEELESKLDELAEELAELEEKLEELKEELESLE----------AELEELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 343 LRQELESLMKEQdlletklrsyEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSL-----KAQL 417
Cdd:TIGR02168 366 ELEELESRLEEL----------EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAEL 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 23618893 418 KDTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVN 467
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-540 |
3.72e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 339 EKRQLRQELESLMKEQDLLETKLRSY--EREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEV--------NAKAS 408
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELdeleaqirGNGGD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 409 EILSLKAQLKDTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNlleqellelRAQAALHRDAAP 488
Cdd:COG4913 339 RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE---------EELEALEEALAE 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 23618893 489 LGppgigltfsEDIPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEE 540
Cdd:COG4913 410 AE---------AALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
341-451 |
8.80e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 341 RQLRQELESLMKEQDLLetklrSYERektnfapaLEETQWEVCQKSGEISLLKQQLKESQmevnAKASEILSLKAQLKDT 420
Cdd:COG0542 421 EQLEIEKEALKKEQDEA-----SFER--------LAELRDELAELEEELEALKARWEAEK----ELIEEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|...
gi 23618893 421 RGKLEGMELKTQDLESALRTKG--LELEVCENE 451
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAplLREEVTEED 516
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
339-481 |
2.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLK--ESQM-------EVNAKASE 409
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLgnvrnnkEYEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23618893 410 ILSLKAQLKDTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELLELRAQAA 481
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
339-489 |
3.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEvcQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLK 418
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE--AELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23618893 419 DTRGKL-EGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELLELRAQAALHRDAAPL 489
Cdd:COG4717 174 ELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
343-440 |
3.97e-04 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 41.73 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 343 LRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEislLKQQLKESQMEVNAKASEILSLKAQLKDTRG 422
Cdd:pfam06785 95 LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLE---SEEQLAEKQLLINEYQQTIEEQRSVLEKRQD 171
|
90
....*....|....*...
gi 23618893 423 KLEGMELKTQDLESALRT 440
Cdd:pfam06785 172 QIENLESKVRDLNYEIKT 189
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-518 |
8.63e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 385 KSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLRE 464
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 23618893 465 KVNLLEQELLELRAQAALHRDAAPLGPPGIGltfsEDIPALQRELDRLRAELKE 518
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEP----PDLEELERELERLEREIEA 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
339-465 |
9.24e-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: 42.31 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 339 EKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLK 418
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 23618893 419 DTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREK 465
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
341-583 |
1.19e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKEsqmeVNAKASEILSLKAQLKDT 420
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 421 RGKLEGMELKTQDLESALRTKGLELEvcenELQRKKNEAELLREKVNLLEQELLELRaqaalhrdaaplgppgiglTFSE 500
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIE----ELEEKVKELKELKEKAEEYIKLSEFYE-------------------EYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 501 DIPALQRELDRLRAELKEERQGHDQMSSgfQHERLVWKEEKEKVIQYQKQLQQSYLAMYQRNQRLEKALQQLaRGDIAGE 580
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERL-KKRLTGL 384
|
...
gi 23618893 581 PFE 583
Cdd:PRK03918 385 TPE 387
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
264-554 |
1.44e-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: 41.88 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 264 QELEQKLLQRETALQKLQRSFDEKEF-------ASGQTFEERPRR---TRDELECLEPKSKLKPASQKSQRTQQVLQLQV 333
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDIlqreqatIDTRTSAFRDLQgqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 334 LQLQQEKRQLRQELESLMKEQDLLEtklrSYEREKTNFAPALEETQWEVCqksgeisllkqQLKESQMEVNAKASEILSL 413
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHL----QETRKKAVVLARLLELQEEPC-----------PLCGSCIHPNPARQDIDNP 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 414 KAqlkdTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELLElraqaalhrdaaplgppg 493
Cdd:TIGR00618 524 GP----LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR------------------ 581
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23618893 494 igltFSEDIPALQRELDRLRAELKEERQgHDQMSSGFQHERLVWKEEK---EKVIQYQKQLQQS 554
Cdd:TIGR00618 582 ----SKEDIPNLQNITVRLQDLTEKLSE-AEDMLACEQHALLRKLQPEqdlQDVRLHLQQCSQE 640
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
256-574 |
1.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 256 LSTDECTIQELEQKLLQRETALQKLQRSFDEKEFASGQTFEERPRRTRDELEclepksKLKPASQKSQRTQQVLQLQVLQ 335
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE------ELQQRLAELEEELEEAQEELEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 336 LQQEKRQLRQELESLMKEQDLLETK----------------------------------------LRSYEREKTNFAPAL 375
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 376 EETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDTRGKLEGMElktqDLESALRTKGLELEVCENELQRK 455
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE----ELEEELQLEELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 456 KNEAELLREKVNLLEQELLELRAQAALHRDAAPLGPPGIGLTFSEDIPALQRELDRLRAELKEERQGHDQMssgfqherl 535
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL--------- 451
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 23618893 536 vwKEEKEKVIQYQKQLQQS--YLAMYQRNQRLEKALQQLAR 574
Cdd:COG4717 452 --REELAELEAELEQLEEDgeLAELLQELEELKAELRELAE 490
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
343-574 |
2.12e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 343 LRQELESLMKEQDLLETKLRSYeREKTNFAPALEETQwevcQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDTRG 422
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEF-RQKNGLVDLSEEAK----LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 423 KLEgmELKTQDLESALRTKGLELEVCENELQRKKNEAellrekvnlleqellelraqaalhrdaaplgppgigltfSEDI 502
Cdd:COG3206 255 ALP--ELLQSPVIQQLRAQLAELEAELAELSARYTPN---------------------------------------HPDV 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23618893 503 PALQRELDRLRAELKEERQghdQMSSGFQHERLVWKEEKEkviQYQKQLQQsYLAMYQRNQRLEKALQQLAR 574
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQ---RILASLEAELEALQAREA---SLQAQLAQ-LEARLAELPELEAELRRLER 358
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
341-467 |
2.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 341 RQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDT 420
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 23618893 421 RGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVN 467
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
350-460 |
2.63e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 350 LMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKA---QLKDTRGKLEG 426
Cdd:pfam15905 161 LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEyitELSCVSEQVEK 240
|
90 100 110
....*....|....*....|....*....|....
gi 23618893 427 MELKTQDLESALRTKGLELEVCENELQRKKNEAE 460
Cdd:pfam15905 241 YKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS 274
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
263-458 |
4.10e-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: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 263 IQELEQKLLQRETALQKLQRSFDEKEFASGQTfEERPRRTRDELECLEPK-SKLKpaSQKSQRTQQVLQLQVLQLQQEKR 341
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN-NKKIKELEKQLNQLKSEiSDLN--NQKEQDWNKELKSELKNQEKKLE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 342 QLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQqlkesqmEVNAKASEILSLKAQLKDTR 421
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK-------ENQSYKQEIKNLESQINDLE 397
|
170 180 190
....*....|....*....|....*....|....*..
gi 23618893 422 GKLEGMELKTQDLESALRTKGLELEVCENELQRKKNE 458
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
445-574 |
4.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 445 LEVCENELQRKKNEAELLREKVNLLEQELLELRAQAALHRDAAplgppgiGLTFSE-DIPALQRELDRLRAELKEERQGH 523
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA-------EYSWDEiDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 23618893 524 DQMssgfqhERLvwKEEKEKVIQYQKQLQQSYLAMYQRNQRLEKALQQLAR 574
Cdd:COG4913 685 DDL------AAL--EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
262-574 |
5.65e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 262 TIQELEQKLLQRETALQKLQRSFDEKEfasgqTFEERPRRTRDELECLEpksklkpasqksqrtqqvlqlqvlqlqQEKR 341
Cdd:COG4372 36 ALFELDKLQEELEQLREELEQAREELE-----QLEEELEQARSELEQLE---------------------------EELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 342 QLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDTR 421
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 422 GKLEGMELKTQDLESALRTKGLelevcENELQRKKNEAELLREKVNLLEQELLELRAQAALHRDAAPLGPPGIGLTFSED 501
Cdd:COG4372 164 EELAALEQELQALSEAEAEQAL-----DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23618893 502 IPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYLAMYQRNQRLEKALQQLAR 574
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIG 311
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
388-583 |
6.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 388 EISLLKQQLKESQmevnAKASEILSLKAQLKDTRGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELlrekvn 467
Cdd:COG4717 72 ELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 468 lleqELLELRAQAALHRDAAplgppgiGLTFSEDIPALQRELDRLRAELKEERQGHDQMssgfQHERLV-WKEEKEKVIQ 546
Cdd:COG4717 142 ----AELPERLEELEERLEE-------LRELEEELEELEAELAELQEELEELLEQLSLA----TEEELQdLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*..
gi 23618893 547 YQKQLQQSYLAMYQRNQRLEKALQQLARGDIAGEPFE 583
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
263-467 |
6.78e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 263 IQELEqKLLQRETALQKLQRSfDEKEFASG----QTFEERPRRTRDELECLEPK----SKLKPASQKSQRTQQVLQLQVL 334
Cdd:PRK03918 178 IERLE-KFIKRTENIEELIKE-KEKELEEVlreiNEISSELPELREELEKLEKEvkelEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 335 QLQQEKRQLRQELESLMKEQDLLETKLRSYE--REKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILS 412
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23618893 413 LKAQLKDTRGKLEGMELKTQDLESALRT------------------KGLELEVCENELQRKKNEAELLREKVN 467
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkkrlTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
220-463 |
7.07e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 220 QDSNMMSLKALSFSDGGSKLAHPGKVEKGSSCVRSPLS-------TDECTIQELEQKLLQRETALQKLQRSFDEKEFASG 292
Cdd:pfam15921 570 QIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkilkdKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 293 QTFEERP------RRTRDELECLEP-----KSKLKPASQKSQRTQQVLQLQVLQLQQEKRQLRQELESL----------- 350
Cdd:pfam15921 650 DIKQERDqllnevKTSRNELNSLSEdyevlKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMegsdghamkva 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 351 --MKEQ--------DLLETKLRSYEREKTNfapALEETQWEVCQKSGeislLKQQLKESQMEVNAKASEILSLKAQLKDT 420
Cdd:pfam15921 730 mgMQKQitakrgqiDALQSKIQFLEEAMTN---ANKEKHFLKEEKNK----LSQELSTVATEKNKMAGELEVLRSQERRL 802
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 23618893 421 RGKLEGMELktqdlesALRTKGLELEVCENELQRKKNEAELLR 463
Cdd:pfam15921 803 KEKVANMEV-------ALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
244-574 |
8.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 244 KVEKGSSCVRSPLSTDECTIQELEQKLLQRETALQKLQ----------RSFDEKEFasgqtfEERPRRTRDELECLEpkS 313
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEEHR------KELLEEYTAELKRIE--K 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 314 KLKPASQKSQRTQQVLQLQVLQLQQEKRQLRqeLESLMKEQDLLETKLRSYEREKTNF-APALEETQWEVCQKSGEISLL 392
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAEQLKELEEKLKKYNLEELEKkAEEYEKLKEKLIKLKGEIKSL 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 393 KQQLKESQmEVNAKASEILSLKAQLKDTRGKLEG------------MELKTQDLESA------LRTKGLELEVCENELQR 454
Cdd:PRK03918 545 KKELEKLE-ELKKKLAELEKKLDELEEELAELLKeleelgfesveeLEERLKELEPFyneyleLKDAEKELEREEKELKK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23618893 455 KKNEAELLREKVNLLEQELLELRAQ-AALHRDAAPLGPPGIgltfSEDIPALQRELDRLRAELKEERQGHDQMSSGFqhE 533
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEEL----REEYLELSRELAGLRAELEELEKRREEIKKTL--E 697
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 23618893 534 RLvwKEEKEKVIQYQKQLqqsylamyqrnQRLEKALQQLAR 574
Cdd:PRK03918 698 KL--KEELEEREKAKKEL-----------EKLEKALERVEE 725
|
|
| |
