|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
451-647 |
1.18e-71 |
|
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: 230.65 E-value: 1.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 451 VCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAC----- 525
Cdd:pfam06818 5 VCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKneael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 526 --------------LKPALTPVDPAEPQdalATCESDEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVGRLQA 591
Cdd:pfam06818 85 lrekvgkleeevsgLREALSDVSPSGYE---SVYESDEAKEQRQE-------------------EADLGSLRREVERLRA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1917203494 592 ELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 647
Cdd:pfam06818 143 ELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
351-623 |
3.54e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGcSGKLQQVARRAQRAQQGLQLQVLRLQQDK 430
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEE-LEELAEELLEALRAAAELAAQLEELEEAE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 431 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 510
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 511 QASLEL-----GEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRALRRE 585
Cdd:COG1196 490 AARLLLlleaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1917203494 586 ------------VGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIE 623
Cdd:COG1196 570 kagratflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-676 |
1.25e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgKLQQVARRAQRAqqglQLQVLRLQQ 428
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQA----EEYELLAELARL----EQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 429 DKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFS 508
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 509 SKQASLELGEGELpaaclkpaltpvdpAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAggESGTRALRREVGR 588
Cdd:COG1196 390 EALRAAAELAAQL--------------EELEEAEEALLERLERLEEELEELEEALAELEEEEEEE--EEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 589 LQAELAAERRARERQGASFAEERRVWLEEKEKVIEyQKQLQLSYVEMYQRNQQLERRLRERGAAGGASTPTPQHGEEkkA 668
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL--I 530
|
....*...
gi 1917203494 669 WTPSRLER 676
Cdd:COG1196 531 GVEAAYEA 538
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-628 |
1.49e-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: 64.69 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 348 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGCSGKLQQVARRAQRAQQGLQLQvlrlq 427
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKEL----- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 428 qdkKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSF 507
Cdd:TIGR02168 757 ---TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 508 SSKQASLELGEGELpaaclkpALTPVDPAEPQDALATCESDEAKMRRQagVAAAASLVSVDGEAEAGGESGTRALRREVG 587
Cdd:TIGR02168 834 AATERRLEDLEEQI-------EELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1917203494 588 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQL 628
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-555 |
7.41e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQGcSGKLQQVARRAQRAQQGLQLQVLRLQQDK 430
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKA-LREALDELRAELTLLNEE-AANLRERLESLERRIAATERRLEDLEEQI 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 431 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSsk 510
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-- 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1917203494 511 QASLELGEGELPAACLKPALTPVDPAEPQDALA---TCESDEAKMRRQ 555
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAlenKIEDDEEEARRR 973
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-649 |
1.12e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQ 428
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 429 DKKQLQEEAARLMRQREELEDKvcqkageiSLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFS 508
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLE--------GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 509 SKQASLELGE------GELPAACLKPALTPVDPAEPQD-----ALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGE- 576
Cdd:COG1196 559 AAAAIEYLKAakagraTFLPLDKIRARAALAAALARGAigaavDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRr 638
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917203494 577 -SGTRALRREV-----GRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRER 649
Cdd:COG1196 639 aVTLAGRLREVtlegeGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-619 |
8.37e-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: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 348 SALIQELEERLWEKEQEVAALRRSLEQSEAAVaQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLQ 427
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 428 QDKK---QLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLR 504
Cdd:TIGR02168 334 ELAEelaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 505 DSFSSKQASLELGEGELPAACLKPALTPVDPAEPqdalatcESDEAKMRRQAGVAAAASLvsvdGEAEAGGESGTRALRR 584
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAELEELEE-------ELEELQEELERLEEALEEL----REELEEAEQALDAAER 482
|
250 260 270
....*....|....*....|....*....|....*
gi 1917203494 585 EVGRLQAELAAERRARERQGASFAEERRVWLEEKE 619
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
349-503 |
1.03e-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: 53.39 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQ---GCSGKLQQVarRAQRAQQGLQLQVLR 425
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEArikKYEEQLGNV--RNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917203494 426 LQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREK-EEQLLSL 503
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLAL 179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-652 |
2.11e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 350 LIQELEERLwekeqevAALRRsleQSEAAV-AQVLEERQKAWERELAELRqgcsgklqqvaRRAQRAqqglqlQVLRLQQ 428
Cdd:COG1196 194 ILGELERQL-------EPLER---QAEKAErYRELKEELKELEAELLLLK-----------LRELEA------ELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 429 DKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFS 508
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 509 SKQASLELGEGELPAAC-----LKPALtpvdpAEPQDALATCES-------------------DEAKMRRQAGVAAAASL 564
Cdd:COG1196 327 ELEEELEELEEELEELEeeleeAEEEL-----EEAEAELAEAEEalleaeaelaeaeeeleelAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 565 VSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLER 644
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
....*...
gi 1917203494 645 RLRERGAA 652
Cdd:COG1196 482 LLEELAEA 489
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
351-510 |
6.47e-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: 51.08 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLqqDK 430
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIKRLEL----EIEEVEARIKKYEEQLGNVRNNK--EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 431 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 510
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-649 |
1.51e-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: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 355 EERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgkLQQVARRAQraqqglqlqvlrlqqDKKQLQ 434
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEA-LEAELDALQERREALQR-----LAEYSWDEI---------------DVASAE 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 435 EEAARLMRQREELEDkvcqKAGEISLLKQQLKDSQADvsqkLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASL 514
Cdd:COG4913 668 REIAELEAELERLDA----SSDDLAALEEQLEELEAE----LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 515 ELGEGELPAACLKPALtpvdPAEPQDALatcesdEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVGRLQAELa 594
Cdd:COG4913 740 EDLARLELRALLEERF----AAALGDAV------ERELRENL-------------------EERIDALRARLNRAEEEL- 789
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1917203494 595 aeRRARERQGASFAEERRVWLEEKEKVIEYQKQL-QLSYVEMYQRNQQLERRLRER 649
Cdd:COG4913 790 --ERAMRAFNREWPAETADLDADLESLPEYLALLdRLEEDGLPEYEERFKELLNEN 843
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-614 |
1.97e-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: 50.53 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 339 FAACSPPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQG 418
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALAR----RIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 419 LQLQvlrlqqdKKQLQEEAARLMRQREELED--KVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRA-SLRE 495
Cdd:COG4942 85 LAEL-------EKEIAELRAELEAQKEELAEllRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAeELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 496 KEEQLLSLRDSFSSKQASLELGEGELpaaclkpaltpvdpAEPQDALAtcesdEAKMRRQAGVAAAASLVSVDGEAEAGG 575
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAEL--------------EEERAALE-----ALKAERQKLLARLEKELAELAAELAEL 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 1917203494 576 ESGTRALRREVGRLQAELAAerRARERQGASFAEERRVW 614
Cdd:COG4942 219 QQEAEELEALIARLEAEAAA--AAERTPAAGFAALKGKL 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-648 |
2.23e-06 |
|
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: 51.21 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRqgcsGKLQQVARRAQRAQQglqlqvlrlqqDK 430
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL-EEEIEELQ----KELYALANEISRLEQ-----------QK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 431 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRA-------SLREKEEQLLSL 503
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleelesRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 504 RDSFSSKQASLELGEGELpaaclkpaltpvdpaEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRALR 583
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEI---------------ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917203494 584 REvgrLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQlSYVEMYQRNQQLERRLRE 648
Cdd:TIGR02168 450 EE---LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSEGVKA 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
434-652 |
4.53e-06 |
|
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: 50.06 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 434 QEEAARLMRQRE--ELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQ 511
Cdd:TIGR02168 667 KTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 512 ASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKmrRQAGVAAAASLVSVDGEAEAGGESGTRALRREVGRLQA 591
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917203494 592 ELAAERRARERQGASFAEERRVWLEEKEKVIEY--------------QKQLQLSYVEMYQRNQQLERRLRERGAA 652
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLaaeieeleelieelESELEALLNERASLEEALALLRSELEEL 899
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
351-620 |
7.39e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQ---GLQLQVLRLQ 427
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRD----RLEECRVAAQAHNEeaeSLREDADDLE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 428 QDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQA---DVSQKLSEIVGLRSQLREGRASLREKEEqllSLR 504
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgDAPVDLGNAEDFLEELREERDELREREA---ELE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 505 DSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGvAAAASLVSVDGEAEAGGESGTRALRR 584
Cdd:PRK02224 433 ATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE-DLEEEVEEVEERLERAEDLVEAEDRI 511
|
250 260 270
....*....|....*....|....*....|....*.
gi 1917203494 585 EVGRLQAELAAERRARERQGasfAEERRVWLEEKEK 620
Cdd:PRK02224 512 ERLEERREDLEELIAERRET---IEEKRERAEELRE 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
344-649 |
7.48e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 344 PPSPSALIQELEERLWEKEQEVAALRRSLEQSEAavaqvLEERQKAWERELAELRQGCSGKLQQVARRAQRAqqglqlqv 423
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEE-----LEEELEELEAELEELREELEKLEKLLQLLPLYQ-------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 424 lrlqqDKKQLQEEAARLMRQREELEDKVC---QKAGEISLLKQQLKDSQADVSQKLSEI-VGLRSQLREGRASLREKEEQ 499
Cdd:COG4717 133 -----ELEALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 500 LLSLRDSFSSKQASLELGEGELPAAclkpaltpvdpAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGT 579
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQL-----------ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 580 RALRREVG----------RLQAELAAERRARERQGASFAEERRVWLEEKEKV---IEYQKQLQLSYVEMYQRNQQLERRL 646
Cdd:COG4717 277 GVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREA 356
|
...
gi 1917203494 647 RER 649
Cdd:COG4717 357 EEL 359
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
352-652 |
7.54e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 352 QELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWE--RELAELRQgcsgKLQQVARRAQRAqQGLQLQVLRLQQD 429
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPlyQELEALEA----ELAELPERLEEL-EERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 430 KKQLQEEAARLMRQREELEDKVC-QKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRD--- 505
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeer 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 506 ---------------SFSSKQASLELGEGELPA---------ACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAA 561
Cdd:COG4717 245 lkearlllliaaallALLGLGGSLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 562 ASLVSVDGEAEAGGESG-------TRALRREVGRLQAELAAERRARERQ------GASFAEERRVWLEEKEKVIEYQKQL 628
Cdd:COG4717 325 LAALGLPPDLSPEELLElldrieeLQELLREAEELEEELQLEELEQEIAallaeaGVEDEEELRAALEQAEEYQELKEEL 404
|
330 340
....*....|....*....|....
gi 1917203494 629 QlsyvemyQRNQQLERRLRERGAA 652
Cdd:COG4717 405 E-------ELEEQLEELLGELEEL 421
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-515 |
1.31e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQV----------------------LEERQKAWERELAELRQGcSGKLQ 406
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIAELEAELERLDAS-SDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 407 QVARRAQRAQQglqlqvlrlqqDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 486
Cdd:COG4913 689 ALEEQLEELEA-----------ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
170 180
....*....|....*....|....*....
gi 1917203494 487 REGRASLREKEEQLLSLRDSFSSKQASLE 515
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAE 786
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
345-655 |
2.39e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 345 PSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQGLQLQVL 424
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQL-EEELEQARS----ELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 425 RLQQDKKQL---QEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLL 501
Cdd:COG4372 95 ELAQAQEELeslQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 502 SLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRA 581
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917203494 582 LRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRERGAAGGA 655
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAalELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
354-500 |
3.08e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 354 LEERLWEKEQEVAALRRSLEQseaavaqvLEERQKAWERELAELRQgcsgKLQQVARR---AQRAQQGLQLQVLRLQQDK 430
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEE--------VDKEFAETRDELKDYRE----KLEKLKREineLKRELDRLQEELQRLSEEL 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 431 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQL 500
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-525 |
4.59e-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: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAqqglqlqvlrlqq 428
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRR------------- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 429 dkKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFS 508
Cdd:COG4913 362 --ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
170 180
....*....|....*....|....*
gi 1917203494 509 SKQ--------ASLELGEGELPAAC 525
Cdd:COG4913 440 ARLlalrdalaEALGLDEAELPFVG 464
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
340-502 |
4.74e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.56 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 340 AACSPPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQ------KAWERELAELRQGCSGKLQQVARRAQ 413
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKklessiKQVEEELEELKEQNEELEKQYKVKKK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 414 RAQQGlqlqvlrlqqdkKQLQEEAARLMRQREELEDKVCQKAGE-----ISLLKQ--QLKDSQA----DVSQKLSEIVGL 482
Cdd:pfam05667 392 TLDLL------------PDAEENIAKLQALVDASAQRLVELAGQwekhrVPLIEEyrALKEAKSnkedESQRKLEEIKEL 459
|
170 180
....*....|....*....|...
gi 1917203494 483 RSQLREGRASLREKEE---QLLS 502
Cdd:pfam05667 460 REKIKEVAEEAKQKEElykQLVA 482
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
430-623 |
8.29e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 430 KKQLQEEAARLMRQREELEdkvcqkagEISLLKQQLKDSQADVSQKLSEivglRSQLREgraSLREKEEQLLSLRDSFSS 509
Cdd:PRK02224 233 RETRDEADEVLEEHEERRE--------ELETLEAEIEDLRETIAETERE----REELAE---EVRDLRERLEELEEERDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 510 KQASLELGEGELPAAclkpaltpvdpAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRA--LRREVG 587
Cdd:PRK02224 298 LLAEAGLDDADAEAV-----------EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeeLREEAA 366
|
170 180 190
....*....|....*....|....*....|....*.
gi 1917203494 588 RLQAELAAERRARerqgasfaEERRVWLEEKEKVIE 623
Cdd:PRK02224 367 ELESELEEAREAV--------EDRREEIEELEEEIE 394
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
377-663 |
8.43e-05 |
|
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: 45.53 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 377 AAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQraqqglqlqvlrlqqdkkQLQEEAARLMRQREELEDKVCQKAG 456
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQ----EIAELEKELA------------------ALKKEEKALLKQLAALERRIAALAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 457 EISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREkeeqllSLRDSFSSKQASLelgegelpaacLKPALTPVDPA 536
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE------LLRALYRLGRQPP-----------LALLLSPEDFL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 537 EPQDALATCESDEAKMRRQAG--VAAAASLVSVDGEAEAGGESgTRALRREVGRLQAELAAERRARERQGASFAEERRVW 614
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQAEelRADLAELAALRAELEAERAE-LEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1917203494 615 LEEKEKVIEYQKQLQlsyvemyQRNQQLERRLRERGAAGGASTPTPQHG 663
Cdd:COG4942 212 AAELAELQQEAEELE-------ALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
351-521 |
1.06e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQqglqlqvlrlqqdk 430
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL-KEELEDLRA----ELEEVDKEFAETR-------------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 431 kqlqeeaARLMRQREELEDkvcqkageislLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 510
Cdd:TIGR02169 385 -------DELKDYREKLEK-----------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
170
....*....|.
gi 1917203494 511 QASLELGEGEL 521
Cdd:TIGR02169 447 ALEIKKQEWKL 457
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
344-600 |
1.28e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 344 PPSPSALIQELEE---RLWEKEQEVAALRRSLEQSEAAVAQVlEERQKAWEReLAELRQGCSGKLQQVARRAQRAQQGLQ 420
Cdd:COG4913 220 EPDTFEAADALVEhfdDLERAHEALEDAREQIELLEPIRELA-ERYAAARER-LAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 421 LqvlrlqqdkkQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADvsqklsEIVGLRSQLREGRASLREKEEQL 500
Cdd:COG4913 298 E----------ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 501 LSLRDSFSSKQASLELGEGELPAAClkpaltpvdpAEPQDALATCESDEAKMRRQAGVAAAASlvsvdgeaeaggesgtR 580
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALR----------AEAAALLEALEEELEALEEALAEAEAAL----------------R 415
|
250 260
....*....|....*....|
gi 1917203494 581 ALRREVGRLQAELAAERRAR 600
Cdd:COG4913 416 DLRRELRELEAEIASLERRK 435
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
351-500 |
1.65e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSLEQ----SEAAVAQ---VLE---------ERQKAWERELAELRQGCSgkLQQVARRAQ- 413
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQklsvADAARRQfekAYElvckiagevERSQAWQTARELLRRYRS--QQALAQRLQq 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 414 -RAQQGLQLQVLRLQQDKKQLQEEAARlmRQREELEDkvcqkAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRAS 492
Cdd:COG3096 517 lRAQLAELEQRLRQQQNAERLLEEFCQ--RIGQQLDA-----AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
....*...
gi 1917203494 493 LREKEEQL 500
Cdd:COG3096 590 LRARIKEL 597
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
352-649 |
2.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 352 QELEERLWEKEQEVAALRRSLEQSEAA-VAQVLEERQKAWE-RELAELRQGCSGKLQQVARRA---QRAQQGLQLQVLRL 426
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKAdEAKKAEEAKKADEaKKAEEAKKADEAKKAEEKKKAdelKKAEELKKAEEKKK 1565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 427 QQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRaSLREKEEQLLSLRDS 506
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE-EEKKKVEQLKKKEAE 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 507 FSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAK----MRRQAGVAAAASLVSVDGEAEAGGESGTRAl 582
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKaaeaLKKEAEEAKKAEELKKKEAEEKKKAEELKK- 1723
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917203494 583 RREVGRLQAELAAERRARERQGAsfaEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQ-LERRLRER 649
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAvIEEELDEE 1788
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
432-646 |
4.17e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 432 QLQEEAA-RLMRQREELEDKvcqkagEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 510
Cdd:TIGR02168 206 ERQAEKAeRYKELKAELREL------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 511 QASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTraLRREVGRLQ 590
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE--LKEELESLE 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203494 591 AELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQL-----QLSYVEmyQRNQQLERRL 646
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnnEIERLE--ARLERLEDRR 416
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
344-490 |
4.81e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 344 PPSPSALIQELEerlwekeQEVAALRRSLEQ--SEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQL 421
Cdd:PRK11448 137 PEDPENLLHALQ-------QEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203494 422 QVLRLQQDKKQLQEEAARLMRQREELEDKvcqkageisLLKQQLKDS--QADvSQKLSEIVGLRSQlrEGR 490
Cdd:PRK11448 210 TSQERKQKRKEITDQAAKRLELSEEETRI---------LIDQQLRKAgwEAD-SKTLRFSKGARPE--KGR 268
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
431-676 |
5.38e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 431 KQLQEEAARLMRQREELEDKVcQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 510
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFI-KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 511 QASLELGEGELPAacLKPALtpvdpAEPQDALATCESDEAKMRRQAGvaaaaSLVSVDGEAEAGGE---------SGTRA 581
Cdd:PRK03918 244 EKELESLEGSKRK--LEEKI-----RELEERIEELKKEIEELEEKVK-----ELKELKEKAEEYIKlsefyeeylDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 582 LRREVGRLQAELAA-ERRARErqgASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRergaaggastptp 660
Cdd:PRK03918 312 IEKRLSRLEEEINGiEERIKE---LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE------------- 375
|
250
....*....|....*.
gi 1917203494 661 QHGEEKKAWTPSRLER 676
Cdd:PRK03918 376 RLKKRLTGLTPEKLEK 391
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
347-504 |
8.53e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 347 PSALIQELEERLWEKEQEVAALRRSLEQ--SEAAVAQVLEERQKAWER----ELAELRQGCSGKLQQVARRAQRA----- 415
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEEleEELQLEELEQEIAALLAEagveDEEELRAALEQAEEYQELKEELEeleeq 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 416 --QQGLQLQVLRLQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADvsQKLSEivgLRSQLREGRASL 493
Cdd:COG4717 411 leELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAE---LLQELEELKAEL 485
|
170
....*....|.
gi 1917203494 494 REKEEQLLSLR 504
Cdd:COG4717 486 RELAEEWAALK 496
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
351-658 |
1.39e-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: 42.25 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQGC------SGKLQQVARRAQRAQQGLQLQVL 424
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEAR-LEAAEEEVDSLKSQLADYQQALdvqqtrAIQYQQAVQALEKARALCGLPDL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 425 rlqqDKKQLQEEAARLMRQREELEDKVCQkageislLKQQLKDSQADVSQ------KLSEIVG----------LRSQLRE 488
Cdd:COG3096 435 ----TPENAEDYLAAFRAKEQQATEEVLE-------LEQKLSVADAARRQfekayeLVCKIAGeversqawqtARELLRR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 489 GRaSLREKEEQLLSLRDSFS------SKQASLElgegELPAACLKPALTPVDPAEpqdalatcESDEAKMRRQAGVAAAA 562
Cdd:COG3096 504 YR-SQQALAQRLQQLRAQLAeleqrlRQQQNAE----RLLEEFCQRIGQQLDAAE--------ELEELLAELEAQLEELE 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 563 SLVSVDGEAEAGGESGTRALRREVGRLQAE----LAAERRA---RERQGASFAEERRVwLEEKEKVIEYQKQLQLSYVEM 635
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAARapawLAAQDALerlREQSGEALADSQEV-TAAMQQLLEREREATVERDEL 649
|
330 340
....*....|....*....|...
gi 1917203494 636 YQRNQQLERRLRERGAAGGASTP 658
Cdd:COG3096 650 AARKQALESQIERLSQPGGAEDP 672
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
348-581 |
1.46e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 348 SALIQELEERLWEKEQEVAALRRSLEQSEAAvaqvLEERQKAWERELAEL-RQGCSGK--------------------LQ 406
Cdd:COG3883 50 NEEYNELQAELEALQAEIDKLQAEIAEAEAE----IEERREELGERARALyRSGGSVSyldvllgsesfsdfldrlsaLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 407 QVARRAQRAQQGLQLQVLRLQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 486
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 487 REGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVS 566
Cdd:COG3883 206 AAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGG 285
|
250
....*....|....*
gi 1917203494 567 VDGEAEAGGESGTRA 581
Cdd:COG3883 286 AGGAGGGGGGGGAAS 300
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
346-508 |
1.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 346 SPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLR 425
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQD----RLEAAEDLARLELRALLEERFA 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 426 LQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLL----KQQLKDSQADVSQKLSEIVGLRSQLREGRAS-LREKEEQL 500
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEELERAmrafNREWPAETADLDADLESLPEYLALLDRLEEDgLPEYEERF 836
|
....*...
gi 1917203494 501 LSLRDSFS 508
Cdd:COG4913 837 KELLNENS 844
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
347-646 |
2.04e-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: 41.03 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 347 PSALIqeLEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKA---WERELAELRQGCsGKLQQVARRAQRAQQGLQLQV 423
Cdd:pfam07888 27 PRAEL--LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDreqWERQRRELESRV-AELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 424 LRLQQDKKQLQEEAARLMRQRE-------ELED-------KVCQKAGEISLLKQQLK--------------DSQADVSQK 475
Cdd:pfam07888 104 KELSASSEELSEEKDALLAQRAahearirELEEdiktltqRVLERETELERMKERAKkagaqrkeeeaerkQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 476 LSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQasLELGEGELPAACLKPALTPVDPAepQDALATCESDEAKMRRQ 555
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT--QKLTTAHRKEAENEALLEELRSL--QERLNASERKVEGLGEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 556 AGVAAA-------------------------ASLVSVDGEAEAGGESGT------------RALRREVGRLQAELAAERR 598
Cdd:pfam07888 260 LSSMAAqrdrtqaelhqarlqaaqltlqladASLALREGRARWAQERETlqqsaeadkdriEKLSAELQRLEERLQEERM 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917203494 599 ARERQGASFAEER---RVWLEEKEKVIEYQK-----------QLQLSYVEMYQRNQQLERRL 646
Cdd:pfam07888 340 EREKLEVELGREKdcnRVQLSESRRELQELKaslrvaqkekeQLQAEKQELLEYIRQLEQRL 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
351-503 |
2.63e-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: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSL------EQSEAAVAQV--LEERQKAWERELAELRQgcsgKLQQVarRAQRAQQGLQLQ 422
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNglvdlsEEAKLLLQQLseLESQLAEARAELAEAEA----RLAAL--RAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 423 VLRLQQDKKQLQEEAARLMRQREELEDK-------VCQKAGEISLLKQQLKDSQADVSQKL-SEIVGLRSQLREGRASLR 494
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLeAELEALQAREASLQAQLA 337
|
....*....
gi 1917203494 495 EKEEQLLSL 503
Cdd:COG3206 338 QLEARLAEL 346
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
430-646 |
2.81e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 430 KKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLK--DSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLrdsf 507
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 508 sskQASLELGEGELPAACLKPALtpvdpAEPQDALATCESDEAKMRRQAG------VAAAASLVSVDgeaeaggesgtRA 581
Cdd:COG3206 246 ---RAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTpnhpdvIALRAQIAALR-----------AQ 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917203494 582 LRREVGRLQAELAAERRARERQGASFAEErrvwLEEKEKVIEYQKQLQLSYVEMyQRNQQLERRL 646
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQ----LAQLEARLAELPELEAELRRL-EREVEVAREL 366
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
581-649 |
2.83e-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: 38.72 E-value: 2.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203494 581 ALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRER 649
Cdd:smart00935 29 KRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKElqKKVQEFQRKQQKLQQDLQKRQQEELQKILDK 99
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
431-521 |
4.40e-03 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 39.01 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 431 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQK------LSEIVGLRSQLREGRASLREKEEQLLSLR 504
Cdd:pfam14662 18 QKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEklleeeLEDLKLIVNSLEEARRSLLAQNKQLEKEN 97
|
90
....*....|....*..
gi 1917203494 505 DSFSSKQASLELGEGEL 521
Cdd:pfam14662 98 QSLLQEIESLQEENKKN 114
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
433-521 |
4.75e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 39.30 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 433 LQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQA------DVSQKLSEIVGLRSQLREGRASLREK---------- 496
Cdd:pfam15294 138 LKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKeqgakkDVKSNLKEISDLEEKMAALKSDLEKTlnastalqks 217
|
90 100
....*....|....*....|....*.
gi 1917203494 497 -EEQLLSLRDSFSSKQASLELGEGEL 521
Cdd:pfam15294 218 lEEDLASTKHELLKVQEQLEMAEKEL 243
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
351-522 |
4.81e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.94 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSLEQ-------SEAAVAQVLEERQKAWERELAELRqgcsGKLQQVARRAQRAQQGlqlqv 423
Cdd:COG5185 372 LSKSSEELDSFKDTIESTKESLDEipqnqrgYAQEILATLEDTLKAADRQIEELQ----RQIEQATSSNEEVSKL----- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 424 lrlqqdKKQLQEEAARLMRQREELED-KVCQKAGEISL-LKQQLKDSQADVSQKLSEIVGLRSQLREGRASLrekEEQLL 501
Cdd:COG5185 443 ------LNELISELNKVMREADEESQsRLEEAYDEINRsVRSKKEDLNEELTQIESRVSTLKATLEKLRAKL---ERQLE 513
|
170 180
....*....|....*....|.
gi 1917203494 502 SLRDSFSSKQASLELGEGELP 522
Cdd:COG5185 514 GVRSKLDQVAESLKDFMRARG 534
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
340-513 |
6.24e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 340 AACSPPSPSALIQELEErlwekeqevAALRRSLEQSEAAVAQVLEERQ------KAWERELAELRQgcsgKLQQVARRAQ 413
Cdd:PRK11281 31 SNGDLPTEADVQAQLDA---------LNKQKLLEAEDKLVQQDLEQTLalldkiDRQKEETEQLKQ----QLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 414 RAQQglqlqvlrlqqDKKQLQEEAARLMRQR------EELEDKVCQkageislLKQQLKDSQADVSQKLSEIVGLRSQLR 487
Cdd:PRK11281 98 QAQA-----------ELEALKDDNDEETRETlstlslRQLESRLAQ-------TLDQLQNAQNDLAEYNSQLVSLQTQPE 159
|
170 180
....*....|....*....|....*.
gi 1917203494 488 EGRASLREKEEQLLSLRDSFSSKQAS 513
Cdd:PRK11281 160 RAQAALYANSQRLQQIRNLLKGGKVG 185
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
352-648 |
6.50e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 352 QELE-----ERLWEKEQEVAALRRSLEQseaavaqvLEERQKAWERELAELRQgcsgkLQQVARRAQRAQQGLQLQVLRL 426
Cdd:PRK02224 459 QPVEgsphvETIEEDRERVEELEAELED--------LEEEVEEVEERLERAED-----LVEAEDRIERLEERREDLEELI 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 427 QQDKKQLQEE---AARLMRQREELE-----------------DKVCQKAGEISLLKQQLKDSQaDVSQKLSEIVGLRSQL 486
Cdd:PRK02224 526 AERRETIEEKrerAEELRERAAELEaeaeekreaaaeaeeeaEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADA 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 487 REGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAclkpaltpVDPAepqdalatcESDEAKMRRQagvAAAASLVS 566
Cdd:PRK02224 605 EDEIERLREKREALAELNDERRERLAEKRERKRELEAE--------FDEA---------RIEEAREDKE---RAEEYLEQ 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 567 VDGEAEAGGESGTRaLRREVGRLQAELAAERRARERQGAsfAEERRVWLEEkekVIEYQKQLQLSY----VEMYQRN-QQ 641
Cdd:PRK02224 665 VEEKLDELREERDD-LQAEIGAVENELEELEELRERREA--LENRVEALEA---LYDEAEELESMYgdlrAELRQRNvET 738
|
....*..
gi 1917203494 642 LERRLRE 648
Cdd:PRK02224 739 LERMLNE 745
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
350-649 |
7.51e-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: 39.72 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 350 LIQELEERLWEKEQevaalRRSLEQSEAAvAQVLEERQKAWERELAELRQGCSGKLQQVaRRAQRAQQGLQLQVLRLQQD 429
Cdd:pfam17380 301 LRQEKEEKAREVER-----RRKLEEAEKA-RQAEMDRQAAIYAEQERMAMERERELERI-RQEERKRELERIRQEEIAME 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 430 KKQLQEeAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRaslrekEEQLLSLRDSFSS 509
Cdd:pfam17380 374 ISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR------QREVRRLEEERAR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 510 KQASLELGEgelpaaclkpaltpvdpAEPQDALATCESDEAKMRRQagvaaaaslvSVDGEAEAGGESGTRALRREVgrL 589
Cdd:pfam17380 447 EMERVRLEE-----------------QERQQQVERLRQQEEERKRK----------KLELEKEKRDRKRAEEQRRKI--L 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917203494 590 QAELAAERRA---------------RERQGASFAEERRVWLEE---KEKVIEYQKQLQLSYVEMYQRNQQLERRLRER 649
Cdd:pfam17380 498 EKELEERKQAmieeerkrkllekemEERQKAIYEEERRREAEEerrKQQEMEERRRIQEQMRKATEERSRLEAMERER 575
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
432-521 |
8.12e-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: 37.99 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 432 QLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQ 511
Cdd:pfam08614 61 QLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQ 140
|
90
....*....|
gi 1917203494 512 ASLELGEGEL 521
Cdd:pfam08614 141 LQLNMAEEKL 150
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
350-515 |
8.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 350 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQkawerELAELRQGCSGKLQQVARRAQRAqqglqlqvLRLQQD 429
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-----ELEELKEEIEELEKELESLEGSK--------RKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 430 KKQLQEEAARLMRQREELEDKV---------CQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQL 500
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVkelkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170
....*....|....*
gi 1917203494 501 LSLRDSFSSKQASLE 515
Cdd:PRK03918 341 EELKKKLKELEKRLE 355
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
351-581 |
8.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQV------LEERQKAWERELAELRQ---GCSGKLQQVARRAQRAQQGLQL 421
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELqaeleaLQAEIDKLQAEIAEAEAeieERREELGERARALYRSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 422 QVL-----------RLQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGR 490
Cdd:COG3883 105 LDVllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203494 491 ASLREKEEQLLSLRDSFSSKQASLE--LGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVD 568
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAELAAAEaaAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
250
....*....|...
gi 1917203494 569 GEAEAGGESGTRA 581
Cdd:COG3883 265 AGAAAGAAGAGAA 277
|
|
| |
