|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
392-592 |
1.77e-76 |
|
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: 242.21 E-value: 1.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 392 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAC- 470
Cdd:pfam06818 1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 471 ------------------LKPALTPVDPAEPQdalATCESDEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVG 532
Cdd:pfam06818 81 eaellrekvgkleeevsgLREALSDVSPSGYE---SVYESDEAKEQRQE-------------------EADLGSLRREVE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 533 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 592
Cdd:pfam06818 139 RLRAELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
321-597 |
2.71e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRrslEQSEAAVAQQDKKQLQEEAARLmrQREELEDKVAACQKEQADFLPRIEETkwevcqkA 400
Cdd:COG1196 234 LRELEAELEELEAELEELE---AELEELEAELAELEAELEELRL--ELEELELELEEAQAEEYELLAELARL-------E 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 401 GEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKpaltpvdP 480
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE-------L 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 481 AEPQDALATCESDEAKMRRQAgvAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWL 560
Cdd:COG1196 375 AEAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270
....*....|....*....|....*....|....*..
gi 542133105 561 EEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRERGAA 597
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
322-596 |
1.57e-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: 64.31 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 322 QELEERLWEKEQEVAALR-RSLE------QSEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKW 394
Cdd:TIGR02168 216 KELKAELRELELALLVLRlEELReeleelQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 395 EVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKpa 474
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR-- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 475 ltpvdPAEPQDALATCESDEAKMRRQAGvAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAE 554
Cdd:TIGR02168 374 -----LEELEEQLETLRSKVAQLELQIA-SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 542133105 555 ERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRERGA 596
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
318-573 |
3.33e-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: 63.54 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 318 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQQDKK---------QLQEEAARLMRQREELEDKVAACQKEQADFLPR 388
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEleelsrqisALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 389 IEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPA 468
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 469 ACLKPALTPVDPAEPQDALATCESDEAKMRRQagVAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQ 548
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
250 260
....*....|....*....|....*
gi 542133105 549 GASFAEERRVWLEEKEKVIEYQKQL 573
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
319-597 |
3.61e-10 |
|
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: 63.16 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 319 ALIQELEE-RLWEKEQEVAALRRSLEQSEAAVA------QQDKKQLQEEAARLMRQREELEDKVAACQK----EQADFLP 387
Cdd:TIGR02169 215 ALLKEKREyEGYELLKEKEALERQKEAIERQLAsleeelEKLTEEISELEKRLEEIEQLLEELNKKIKDlgeeEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 388 RIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELP 467
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 468 AACLKPALTPVDPAEPQDAL--ATCESDEAKMRRQAGVAAAASLVSVDGEAE---AGGESGTRALRREVGRLQAELAAER 542
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLekLKREINELKRELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQE 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 542133105 543 RARERQGASFAEERRVWLEEKEKVIEYQK---QLQLSYVEMYQRNQQLERRLRERGAA 597
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKelsKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
318-564 |
3.38e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 318 SALIQELEERLWEKEQEVAALRRSLE-----------------------QSEAAVAQQDKKQLQEEAARLMRQREELEDK 374
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEelqkelyalaneisrleqqkqilRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 375 VAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSS 454
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 455 KQASLELGEGELPAACLKPALTPVDPAEPqdalatcESDEAKMRRQAGVAAAASLvsvdGEAEAGGESGTRALRREVGRL 534
Cdd:TIGR02168 419 LQQEIEELLKKLEEAELKELQAELEELEE-------ELEELQEELERLEEALEEL----REELEEAEQALDAAERELAQL 487
|
250 260 270
....*....|....*....|....*....|
gi 542133105 535 QAELAAERRARERQGASFAEERRVWLEEKE 564
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
310-447 |
4.78e-08 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 56.19 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 310 AACSPPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQQDK---------KQLQEEAARLMRQREELEDKVAAcqK 380
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKeikklessiKQVEEELEELKEQNEELEKQYKV--K 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 381 EQA-DFLPRIEE--------------------TKWEVCQKA--GEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRAS 437
Cdd:pfam05667 390 KKTlDLLPDAEEniaklqalvdasaqrlvelaGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEE 469
|
170
....*....|...
gi 542133105 438 LREKEE---QLLS 447
Cdd:pfam05667 470 AKQKEElykQLVA 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
319-568 |
5.96e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 319 ALIQELEERLWEKEQEVAALRRSL--EQSEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKwev 396
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA--- 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 397 cQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQAS--LELGEGELPAACLKPA 474
Cdd:COG1196 449 -EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVA 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 475 LTPVDPAEPQDALATCESD--EAKMRRQAGVAAAAslvsVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASF 552
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAA----IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
250
....*....|....*.
gi 542133105 553 AEERRVWLEEKEKVIE 568
Cdd:COG1196 604 VASDLREADARYYVLG 619
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
319-448 |
8.61e-08 |
|
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: 53.39 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQ------QDKKQL-----QEEAARLMRQREELEDKVAACQKEQADFLP 387
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEvearikKYEEQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELME 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133105 388 RIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREK-EEQLLSL 448
Cdd:COG1579 118 RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLAL 179
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-540 |
9.85e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQQDK---------KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEE 391
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldelraelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 392 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACL 471
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542133105 472 KPALTPVDPAEPQDALATCESDEAKMrrqagvaaaaslvsvDGEAEAGGESGTRALRREVGRLQAELAA 540
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTLEE---------------AEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
339-568 |
1.32e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 339 RRSLEQSEAAVAQQDKKQLQEEAARLMRQREELEDKVAAC--QKEQA-DFLPRIEETKWEVCQKAGEISLLKQQLKDSQA 415
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYeeQREQArETRDEADEVLEEHEERREELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 416 DVSQKLSEivglRSQLREgraSLREKEEQLLSLRDSFSSKQASLELGEGELPAAclkpaltpvdpAEPQDALATCESDEA 495
Cdd:PRK02224 266 TIAETERE----REELAE---EVRDLRERLEELEEERDDLLAEAGLDDADAEAV-----------EARREELEDRDEELR 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133105 496 KMRRQAGVAAAASLVSVDGEAEAGGESGTRA--LRREVGRLQAELAAERRARerqgasfaEERRVWLEEKEKVIE 568
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAeeLREEAAELESELEEAREAV--------EDRREEIEELEEEIE 394
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
319-455 |
7.67e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAV--AQQDKKQLQEEAARLMRQREELEDK---------VAACQKEQADFLP 387
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELedLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542133105 388 RIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 455
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
321-452 |
1.34e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRS------LEQsEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkW 394
Cdd:COG4913 663 VASAEREIAELEAELERLDASsddlaaLEE-QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA--A 739
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 542133105 395 EVCQKAGEISLLKQQLKdsQADVSQKLSEIV-GLRSQLREGRASLREKEEQLLSLRDSF 452
Cdd:COG4913 740 EDLARLELRALLEERFA--AALGDAVERELReNLEERIDALRARLNRAEEELERAMRAF 796
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
321-559 |
3.28e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLEQSEAAVA---------QQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIee 391
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAalarriralEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 392 tkwevcQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRA-SLREKEEQLLSLRDSFSSKQASLELGEGELpaac 470
Cdd:COG4942 114 ------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAeELRADLAELAALRAELEAERAELEALLAEL---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 471 lkpaltpvdpAEPQDALAtcesdEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAerRARERQGA 550
Cdd:COG4942 184 ----------EEERAALE-----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA--AAERTPAA 246
|
....*....
gi 542133105 551 SFAEERRVW 559
Cdd:COG4942 247 GFAALKGKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
347-608 |
3.74e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 347 AAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVG 426
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 427 LRSQLREGRASLREkeeqllSLRDSFSSKQASLelgegelpaacLKPALTPVDPAEPQDALATCESDEAKMRRQAG--VA 504
Cdd:COG4942 95 LRAELEAQKEELAE------LLRALYRLGRQPP-----------LALLLSPEDFLDAVRRLQYLKYLAPARREQAEelRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 505 AAASLVSVDGEAEAGGESgTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQlsyvemyQRN 584
Cdd:COG4942 158 DLAELAALRAELEAERAE-LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALI 229
|
250 260
....*....|....*....|....
gi 542133105 585 QQLERRLRERGAAGGASTPTPQHG 608
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
321-593 |
5.03e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQQDKKQLQEEAA-----RLMRQREELEDKVAACQ--KEQADFLPRIEETK 393
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRedleeLIAERRETIEEKRERAEelRERAAELEAEAEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 394 WEVCQKA--------GEISLLKQQLK--DSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGE 463
Cdd:PRK02224 557 REAAAEAeeeaeearEEVAELNSKLAelKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERK 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 464 GELPAAclkpaltpVDPAepqdalatcESDEAKMRRQagvAAAASLVSVDGEAEAGGESGTRaLRREVGRLQAELAAERR 543
Cdd:PRK02224 637 RELEAE--------FDEA---------RIEEAREDKE---RAEEYLEQVEEKLDELREERDD-LQAEIGAVENELEELEE 695
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 542133105 544 ARERQGAsfAEERRVWLEEkekVIEYQKQLQLSY----VEMYQRN-QQLERRLRE 593
Cdd:PRK02224 696 LRERREA--LENRVEALEA---LYDEAEELESMYgdlrAELRQRNvETLERMLNE 745
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
321-545 |
7.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkwevcqka 400
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE--------- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 401 geislLKQQLKDSQADvsqklsEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAClkpaltpvdp 480
Cdd:COG4913 328 -----LEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR---------- 386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133105 481 AEPQDALATCESDEAKMRRQAGVAAAASlvsvdgeaeaggesgtRALRREVGRLQAELAAERRAR 545
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAAL----------------RDLRRELRELEAEIASLERRK 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
319-449 |
7.21e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQQDKKQLQeeaaRLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQ 398
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 542133105 399 KAGEISLLKQQLKDSQADVSQKLSEI----VGLRSQLREGRASLREKEEQLLSLR 449
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALeealAEAEAALRDLRRELRELEAEIASLE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
314-594 |
9.87e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 314 PPSPSALIQELEERLWE---KEQEVAALRRSLEQSEAAV--AQQDKKQLQEEAARLMRQRE--ELEDKVAACQKEQADFL 386
Cdd:COG4717 66 PELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELeeLEAELEELREELEKLEKLLQllPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 387 PRIEETKWEVC---QKAGEISLLKQQLKDSQADVSQKLSEI-VGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELG 462
Cdd:COG4717 146 ERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 463 EGELPAAclkpaltpvdpAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRALRREVG---------- 532
Cdd:COG4717 226 EEELEQL-----------ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllallfllla 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133105 533 RLQAELAAERRARERQGASFAEERRVWLEEKEKV---IEYQKQLQLSYVEMYQRNQQLERRLRER 594
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREAEEL 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
329-594 |
1.47e-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: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 329 WEKEQEVAALRRsleqsEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQK-EQADFlpriEETKWEVCQKagEISLLK 407
Cdd:COG4913 606 FDNRAKLAALEA-----ELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSW----DEIDVASAER--EIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 408 QQLKDSQADvSQKLSEivgLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAclKPALTPVDPAEPQDAL 487
Cdd:COG4913 675 AELERLDAS-SDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL--QDRLEAAEDLARLELR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 488 ATCEsdeaKMRRQAGVAAAASLVSVDGEAEaggesgTRALRREVGRLQAELaaeRRARERQGASFAEERRVWLEEKEKVI 567
Cdd:COG4913 749 ALLE----ERFAAALGDAVERELRENLEER------IDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLP 815
|
250 260
....*....|....*....|....*...
gi 542133105 568 EYQKQL-QLSYVEMYQRNQQLERRLRER 594
Cdd:COG4913 816 EYLALLdRLEEDGLPEYEERFKELLNEN 843
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
320-434 |
2.32e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 320 LIQELEE---RLWEKEQEVAALRRSLEQSEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLP--RIEETKW 394
Cdd:PRK00409 521 LIASLEElerELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKelRQLQKGG 600
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 542133105 395 EVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREG 434
Cdd:PRK00409 601 YASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
318-565 |
4.06e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 318 SALIQELEERLWEKEQEVAALRRSLEQSEAAV--AQQDKKQLQEEAARLMRQREELEDKVAACQKEqadflprIEETKWE 395
Cdd:PRK02224 306 DADAEAVEARREELEDRDEELRDRLEECRVAAqaHNEEAESLREDADDLEERAEELREEAAELESE-------LEEAREA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 396 VCQKAGEISLLKQQLKDSQA---DVSQKLSEIVGLRSQLREGRASLREKEEqllSLRDSFSSKQASLELGEGELPAACLK 472
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRErfgDAPVDLGNAEDFLEELREERDELREREA---ELEATLRTARERVEEAEALLEAGKCP 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 473 PALTPVDPAEPQDALATCESDEAKMRRQAGvAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGasf 552
Cdd:PRK02224 456 ECGQPVEGSPHVETIEEDRERVEELEAELE-DLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRET--- 531
|
250
....*....|...
gi 542133105 553 AEERRVWLEEKEK 565
Cdd:PRK02224 532 IEEKRERAEELRE 544
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
315-460 |
4.41e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 315 PSPSALIQELEERLWEKEQEVAALRRSLEQ--SEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEET 392
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQlrEELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542133105 393 KWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLE 460
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
330-444 |
4.83e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 330 EKE-QEVAALRRSLEQSEAAVAQQDKK---QLQEEAARLM---RQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGE 402
Cdd:pfam01576 383 ESEnAELQAELRTLQQAKQDSEHKRKKlegQLQELQARLSeseRQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD 462
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 542133105 403 ISLLKQQLKDSQA----DVSQKLSEIVGLRsQLREGRASLREKEEQ 444
Cdd:pfam01576 463 VSSLESQLQDTQEllqeETRQKLNLSTRLR-QLEDERNSLQEQLEE 507
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
319-470 |
7.62e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQ----------QDKKQLQEEAARLMRQREELEDKVAAcQKEQADFL-- 386
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDEleaqirgnggDRLEQLEREIERLERELEERERRRAR-LEALLAALgl 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 387 --PRIEETKWEVCQKAGEislLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQ-------- 456
Cdd:COG4913 374 plPASAEEFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLlalrdala 450
|
170
....*....|....
gi 542133105 457 ASLELGEGELPAAC 470
Cdd:COG4913 451 EALGLDEAELPFVG 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
388-597 |
2.25e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 388 RIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELP 467
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 468 AACLKPALTPVDPAEPQDALATCESDEAKmrRQAGVAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARER 547
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542133105 548 QGASFAEERRVWLEEKEKVIEY--------------QKQLQLSYVEMYQRNQQLERRLRERGAA 597
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLaaeieeleelieelESELEALLNERASLEEALALLRSELEEL 899
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
316-426 |
3.97e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 316 SPSALIQELEERLWEKEQEVAALRRslEQSEAAvaqqdkkqlQEEAARLMRQREELEDKVAACQ---KEQADFLPRIEET 392
Cdd:COG0542 408 SKPEELDELERRLEQLEIEKEALKK--EQDEAS---------FERLAELRDELAELEEELEALKarwEAEKELIEEIQEL 476
|
90 100 110
....*....|....*....|....*....|....*..
gi 542133105 393 KWEVCQKAGEISLLKQQLKDSQADVSQK---LSEIVG 426
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELaplLREEVT 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
316-430 |
4.46e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 316 SPSALIQELEERLWEKEQEVAALRRSLEQseaavAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFL-PRIEETKW 394
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDE-----LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFA 756
|
90 100 110
....*....|....*....|....*....|....*....
gi 542133105 395 EVCQKAGEISL---LKQQLKDSQADVSQKLSEIVGLRSQ 430
Cdd:COG4913 757 AALGDAVERELrenLEERIDALRARLNRAEEELERAMRA 795
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
321-457 |
5.08e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.82 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLEQSEaavaqQDK----------KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIE 390
Cdd:pfam13851 56 NKRLTEPLQKAQEEVEELRKQLENYE-----KDKqslknlkarlKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFE 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542133105 391 ETKWEVCQKAG-EISLLKQQLKDSQADVSQK---LSEIVglrsqlreGRASLREKEEQLLS--LRDSFSSKQA 457
Cdd:pfam13851 131 AAIQDVQQKTGlKNLLLEKKLQALGETLEKKeaqLNEVL--------AAANLDPDALQAVTekLEDVLESKNQ 195
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
319-412 |
5.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 319 ALIQELEERLwEKEQEVAALRRSLEQ----SEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIE--ET 392
Cdd:COG4717 389 AALEQAEEYQ-ELKEELEELEEQLEEllgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEE 467
|
90 100
....*....|....*....|
gi 542133105 393 KWEVCQKAGEISLLKQQLKD 412
Cdd:COG4717 468 DGELAELLQELEELKAELRE 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
318-469 |
5.52e-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: 42.83 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 318 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQQdKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVC 397
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQ-KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133105 398 QKAGEIsllkQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAA 469
Cdd:COG4942 147 ARREQA----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
338-593 |
5.81e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 338 LRRSLEQSEAAVAQQDKKQLQ--EEAARLMRQREELEDKVAACQKEQADFlPRIEETkwevcqkageislLKQQL---KD 412
Cdd:PRK10929 28 ITQELEQAKAAKTPAQAEIVEalQSALNWLEERKGSLERAKQYQQVIDNF-PKLSAE-------------LRQQLnneRD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 413 SQADVSQKLS------EIVGLRSQLREGRASLREKEEQLLSLRDSFS-----SKQASLELGEGELPAACLKPALTPVdpA 481
Cdd:PRK10929 94 EPRSVPPNMStdaleqEILQVSSQLLEKSRQAQQEQDRAREISDSLSqlpqqQTEARRQLNEIERRLQTLGTPNTPL--A 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 482 EPQDALatcesdeakmrRQAGVAAAASLVSvdgEAEAGGESGTRalRREVGRLQAELAAERRAR--------------ER 547
Cdd:PRK10929 172 QAQLTA-----------LQAESAALKALVD---ELELAQLSANN--RQELARLRSELAKKRSQQldaylqalrnqlnsQR 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 542133105 548 QgasfaEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRE 593
Cdd:PRK10929 236 Q-----REAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQ 276
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
321-451 |
6.51e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLE----QSEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETkwev 396
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNGlvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL---- 259
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133105 397 cQKAGEISLLKQQLKDSQADVSQKLS-------EIVGLRSQLREGRASLREKEEQLLSLRDS 451
Cdd:COG3206 260 -LQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEA 320
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-577 |
9.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 339 RRSLEQSEAAVAQ-QDKKQLQEEAARLMRQREELEDKVAACQK-----EQADFLpRIEETKWEVCQKAGEISLLKQQLKD 412
Cdd:COG4913 221 PDTFEAADALVEHfDDLERAHEALEDAREQIELLEPIRELAERyaaarERLAEL-EYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 413 SQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSlrdsfsSKQASLELGEGELPAAclkpaltpvdpaepQDALATCES 492
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRG------NGGDRLEQLEREIERL--------------ERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 493 DEAKMRRQAGVAaaaslvsvdGEAEAGGESGTRALRREVGRLQAELAAER-RARERQGASFAEERRVW--LEEKEKVIEY 569
Cdd:COG4913 360 RRARLEALLAAL---------GLPLPASAEEFAALRAEAAALLEALEEELeALEEALAEAEAALRDLRreLRELEAEIAS 430
|
....*...
gi 542133105 570 QKQLQLSY 577
Cdd:COG4913 431 LERRKSNI 438
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
314-435 |
1.18e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 314 PPSPSALIQELeerlwekEQEVAALRRSLEQ--SEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEE 391
Cdd:PRK11448 137 PEDPENLLHAL-------QQEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE 209
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542133105 392 TKWEVCQKAGEIS----------------LLKQQLKDS--QADvSQKLSEIVGLRSQlrEGR 435
Cdd:PRK11448 210 TSQERKQKRKEITdqaakrlelseeetriLIDQQLRKAgwEAD-SKTLRFSKGARPE--KGR 268
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
320-459 |
1.32e-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: 41.93 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 320 LIQELEERLWEKEQEVAALRRSLEQSeaavaQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQK 399
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQK-----QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133105 400 AGEISLLKQQLKDSQADVSQKLSEIVGLR-----SQLREGRASLREKEEQLLSLRDSFSSKQASL 459
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKENLEKEIDEknkeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
323-591 |
1.70e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 323 ELEERLWEKEQEVAALRRSLEQSEAAV--AQQDKKQLQEEAARLMRQRE-------ELEDKVAACQKEQADFLPRIEETK 393
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYkeLSASSEELSEEKDALLAQRAahearirELEEDIKTLTQRVLERETELERMK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 394 WEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQasLELGEGELPAACLKP 473
Cdd:pfam07888 157 ERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT--QKLTTAHRKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 474 ALTPVDPAepQDALATCESDEAKMRRQAGVAAA-------------------------ASLVSVDGEAEAGGESGT---- 524
Cdd:pfam07888 235 LLEELRSL--QERLNASERKVEGLGEELSSMAAqrdrtqaelhqarlqaaqltlqladASLALREGRARWAQERETlqqs 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 525 --------RALRREVGRLQAELAAERRARERQGASFAEER---RVWLEEKEKVIEYQK-----------QLQLSYVEMYQ 582
Cdd:pfam07888 313 aeadkdriEKLSAELQRLEERLQEERMEREKLEVELGREKdcnRVQLSESRRELQELKaslrvaqkekeQLQAEKQELLE 392
|
....*....
gi 542133105 583 RNQQLERRL 591
Cdd:pfam07888 393 YIRQLEQRL 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
321-460 |
2.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLEQ-----------SEAAVAQQDKKQLQEEAARLMRQRE----------ELEDKVAACQ 379
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDAlqerrealqrlAEYSWDEIDVASAEREIAELEAELErldassddlaALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 380 KEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASL 459
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
.
gi 542133105 460 E 460
Cdd:COG4913 779 R 779
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
320-594 |
2.25e-03 |
|
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: 41.26 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 320 LIQELEERLWEKEQevaalRRSLEQSEAAVAQQDKKQ--LQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVc 397
Cdd:pfam17380 301 LRQEKEEKAREVER-----RRKLEEAEKARQAEMDRQaaIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEI- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 398 QKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLR-DSFSSKQASLELGEGELPAACLKPALt 476
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRaEQEEARQREVRRLEEERAREMERVRL- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 477 pvDPAEPQDALATCESDEAKMRRQagvaaaaslvSVDGEAEAGGESGTRALRREVgrLQAELAAERRA------------ 544
Cdd:pfam17380 454 --EEQERQQQVERLRQQEEERKRK----------KLELEKEKRDRKRAEEQRRKI--LEKELEERKQAmieeerkrklle 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 542133105 545 ---RERQGASFAEERRVWLEE---KEKVIEYQKQLQLSYVEMYQRNQQLERRLRER 594
Cdd:pfam17380 520 kemEERQKAIYEEERRREAEEerrKQQEMEERRRIQEQMRKATEERSRLEAMERER 575
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
321-597 |
2.50e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQQDKKQLQ---EEAARLMRQREELEDKVAACQKEQADflpriEETKWEVC 397
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQdlaEELEELQQRLAELEEELEEAQEELEE-----LEEELEQL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 398 QKAGEISLLKQQLKDSQADVSQkLSEIVGLRSqlregraslrekeeQLLSLRDSFSSKQASLELGEGELPAACLKPALTP 477
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLI-AAALLALLG--------------LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 478 VDPAEPQDALAtcESDEAKMRRQAGVAAAASLVSVDGEAEAGGESG-------TRALRREVGRLQAELAAERRARERQ-- 548
Cdd:COG4717 298 ASLGKEAEELQ--ALPALEELEEEELEELLAALGLPPDLSPEELLElldrieeLQELLREAEELEEELQLEELEQEIAal 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 542133105 549 ----GASFAEERRVWLEEKEKVIEYQKQLQlsyvemyQRNQQLERRLRERGAA 597
Cdd:COG4717 376 laeaGVEDEEELRAALEQAEEYQELKEELE-------ELEEQLEELLGELEEL 421
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
322-456 |
2.75e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 322 QELEERLWEKEQEVAALRRSLEQSEAAVA--QQDKKQLQEEAARLMRQREElEDKVAAcqkeqadflPRIEETKWEVCQK 399
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSplETFLEKDQQEKEELISSKET-SNKKAQ---------DKVNDIKEKVKNI 953
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 542133105 400 AGEISLLKQQLKDSQAD-VSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQ 456
Cdd:TIGR00606 954 HGYMKDIENKIQDGKDDyLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
310-588 |
3.10e-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: 40.72 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 310 AACSPPSPSALIQELEERLWEKEQEVAALRRSLEQ-SEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKEQadflPR 388
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYlTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ----ER 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 389 IEET-KWEvcqKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELP 467
Cdd:TIGR00618 286 INRArKAA---PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 468 AACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARER 547
Cdd:TIGR00618 363 VATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 542133105 548 QGASFAEERRvwlEEKEKVIEYQKqLQLSYVEMYQRNQQLE 588
Cdd:TIGR00618 443 CAAAITCTAQ---CEKLEKIHLQE-SAQSLKEREQQLQTKE 479
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
324-431 |
3.18e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 324 LEERLWEKEQEVAALRrslEQSEaavaqQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEI 403
Cdd:pfam10174 441 LEEALSEKERIIERLK---EQRE-----REDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSG 512
|
90 100
....*....|....*....|....*...
gi 542133105 404 SLLKQQLKDSQADVSQKLSEIVGLRSQL 431
Cdd:pfam10174 513 LKKDSKLKSLEIAVEQKKEECSKLENQL 540
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
321-466 |
3.24e-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: 40.77 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLEQSEAAVaQQDKKQLQ---EEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVC 397
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEI-EKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542133105 398 QKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGEL 466
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
526-594 |
3.26e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 3.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542133105 526 ALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRER 594
Cdd:smart00935 29 KRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKElqKKVQEFQRKQQKLQQDLQKRQQEELQKILDK 99
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
322-461 |
3.53e-03 |
|
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: 40.71 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 322 QELEERLWEKEQEVAALRRSLEQSEAAVAQQ------------DKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRI 389
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQRLRQQQNAERLLeefcqrigqqldAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542133105 390 EETKwevcQKAGEISLLKQQLKDSQaDVSQKLSEIVGL----RSQLREGRASLREKEEQLLSLRDSFSSKQASLEL 461
Cdd:COG3096 588 EQLR----ARIKELAARAPAWLAAQ-DALERLREQSGEaladSQEVTAAMQQLLEREREATVERDELAARKQALES 658
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
318-450 |
4.92e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 318 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQQDKKQLQEEAARLMRQREELEDKVAACQKeqadflpRIEETKwevc 397
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE-------RIERLE---- 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 542133105 398 qkaGEISLLKQQLKD---SQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRD 450
Cdd:COG2433 448 ---RELSEARSEERReirKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
318-466 |
5.17e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 38.37 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 318 SALIQELEERLwekEQEVAALRRSLEQSEAAVAQQDKKQLQEEAARLMRQREELedkvAACQKEQADFLPRIEETKwevc 397
Cdd:pfam08614 16 TALLEAENAKL---QSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREEL----AELYRSRGELAQRLVDLN---- 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542133105 398 qkaGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGEL 466
Cdd:pfam08614 85 ---EELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKL 150
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
321-466 |
5.54e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLEQSEAavaqqdkkqlqeEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKA 400
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDA------------DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542133105 401 GEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGEL 466
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
322-627 |
5.94e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 322 QELEERLWEKEQEVAALRRSleqSEAAVAQQDKKQLQE--EAARLMRQREELEDKV-----AACQKEQADFLPRIEETKw 394
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKA---EEAKKADEAKKKAEEakKADEAKKKAEEAKKKAdeakkAAEAKKKADEAKKAEEAK- 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 395 evcqKAGEISLLKQQLKDSQADVSQ--------KLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQA--------- 457
Cdd:PTZ00121 1523 ----KADEAKKAEEAKKADEAKKAEekkkadelKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeearieevm 1598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 458 SLELGEGELPAACLKPALTPVDPAE----------PQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRAL 527
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEelkkaeeekkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 528 RREVGRLQAELAAERRARERQGASFAEE-RRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRErgaaggASTPTPQ 606
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEElKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK------AEEAKKD 1752
|
330 340
....*....|....*....|.
gi 542133105 607 HGEEKKAWTPSRLERIESTEI 627
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEI 1773
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-459 |
7.68e-03 |
|
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: 39.67 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 350 AQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVC---QKAGEISLL-----------KQQLKDSQA 415
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSdasRKIGEIEKEieqleqeeeklKERLEELEE 744
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 542133105 416 DVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASL 459
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
351-591 |
7.69e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 351 QQDKKQLQEEAARLMRQR-EELEDKVAACQKEQADFLprieetkwevcQKAGEISLlkqqlkDSQADVSqkLSEIVGLRS 429
Cdd:COG3206 166 LELRREEARKALEFLEEQlPELRKELEEAEAALEEFR-----------QKNGLVDL------SEEAKLL--LQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 430 QLREGRASLREKEEQLLSLrdsfsskQASLELGEGELPAACLKPALtpvdpAEPQDALATCESDEAKMRRQAG------V 503
Cdd:COG3206 227 QLAEARAELAEAEARLAAL-------RAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTpnhpdvI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 504 AAAASLVSVDgeaeaggesgtRALRREVGRLQAELAAERRARERQGASFAEErrvwLEEKEKVIEYQKQLQLSYVEMyQR 583
Cdd:COG3206 295 ALRAQIAALR-----------AQLQQEAQRILASLEAELEALQAREASLQAQ----LAQLEARLAELPELEAELRRL-ER 358
|
....*...
gi 542133105 584 NQQLERRL 591
Cdd:COG3206 359 EVEVAREL 366
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
319-460 |
8.09e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQQDKKQLQEEAARLMRQREELEdkVAACQKEQADFLPRI----EETKW 394
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAgvedEEELR 388
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542133105 395 EVCQKAGEISLLKQQLKDSQADVSQKLSEIV---------GLRSQLREGRASLREKEEQLLSLRDSFSSKQASLE 460
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEellealdeeELEEELEELEEELEELEEELEELREELAELEAELE 463
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
321-446 |
9.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133105 321 IQELEERLWEKEQEVAALRRSLEQSEAavaqqDKKQLQEEAARLMRQREELEDKVAACQ--KEQADFLPRIEETKWEVCQ 398
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEE-----KIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLD 307
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 542133105 399 KAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREgrasLREKEEQLL 446
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELE 351
|
|
| |
