|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
153-608 |
1.06e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEKSRMEASyLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQ 232
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEE-LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 233 QHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDE 312
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 313 KNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTY--EKAKQKDQLA 390
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleAALAAALQNI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 391 IQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEA 470
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 471 ADGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEAD 550
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 22208850 551 dwKQELARLQQLHRQELERCQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRS 608
Cdd:COG1196 712 --AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-716 |
1.78e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 152 GEVDKRLHQLKTQlATLTSSLATVTQEKSRMEASYLADKKKmkqDLEDASNKAEEERARLEGELKGLQEQIAETKARLIT 231
Cdd:COG1196 196 GELERQLEPLERQ-AEKAERYRELKEELKELEAELLLLKLR---ELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 232 QQHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREalagrayAAEQMEGFELQTKQLTREVEELKSELQAIRD 311
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-------LEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 312 EknqpdprLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTyEKAKQKDQLAI 391
Cdd:COG1196 345 E-------LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-EEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 392 QKLKERILQLDLENKTLALAAssrspLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLcdleimpssEAA 471
Cdd:COG1196 417 ERLEEELEELEEALAELEEEE-----EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL---------AEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 472 DGEKATALYYQQELKQLKEEFERYkmrAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLScEELEHQHQQEADD 551
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGF---LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA-AALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 552 WKQELARLQQLHRQELERCQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPA 631
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 632 DTSSSDSLTQALQLAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHREEVAALQSHIEKNIR 711
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
....*
gi 22208850 712 DQSRE 716
Cdd:COG1196 719 EELEE 723
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
157-708 |
1.34e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 157 RLHQLKTQLATLTSSLATVTQEksrmeasyLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDR 236
Cdd:COG1196 233 KLRELEAELEELEAELEELEAE--------LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 237 AQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQp 316
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 317 dpRLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKE 396
Cdd:COG1196 384 --LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 397 RILQLDLENKTLALAASSRSPLDSHGEESSLDVnvLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKA 476
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLL--LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 477 TALYYQQELKQLKEEFERYKMRAQVVLKSKntKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQEL 556
Cdd:COG1196 540 LEAALAAALQNIVVEDDEVAAAAIEYLKAA--KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 557 ARLQQLHRQELERCQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPADTSSS 636
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22208850 637 DSLTQALQLAAANEPTFFLYAEQL--ARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHREEVAALQSHIEK 708
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELeeEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| GRIP |
pfam01465 |
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ... |
717-760 |
1.59e-13 |
|
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.
Pssm-ID: 460221 [Multi-domain] Cd Length: 44 Bit Score: 65.07 E-value: 1.59e-13
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 22208850 717 GANLEYLKNIIYRFLTLPDSLGRQQTLTAILTILHFSPEEKQVI 760
Cdd:pfam01465 1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
207-534 |
5.99e-12 |
|
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: 69.70 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 207 ERARLEGELKGLQEQIAETKARLIT--QQHDRAQEQ------------SDHALMLRELQKLLQEERTQRQDLELRLEETR 272
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAElrKELEELEEEleqlrkeleelsRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 273 EALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQqemrktalAEDQL 352
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE--------RLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 353 RQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKErilQLDLENKTLALAASSRSPLDSHGEESSLDVNVL 432
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES---ELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 433 KDKMEKLKRLLQVA-ARKSQVTLDVEKLcdleimpsseaadgekatalyyQQELKQLKEEF-ERYKMRAQVVLKSKNTKD 510
Cdd:TIGR02168 907 ESKRSELRRELEELrEKLAQLELRLEGL----------------------EVRIDNLQERLsEEYSLTLEEAEALENKIE 964
|
330 340
....*....|....*....|....
gi 22208850 511 GnlgkELEAAQEQLAELKEKYISL 534
Cdd:TIGR02168 965 D----DEEEARRRLKRLENKIKEL 984
|
|
| Grip |
smart00755 |
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245; |
717-762 |
6.10e-11 |
|
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
Pssm-ID: 197860 Cd Length: 46 Bit Score: 58.00 E-value: 6.10e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 22208850 717 GANLEYLKNIIYRFLTLPDSLgRQQTLTAILTILHFSPEEKQVIMR 762
Cdd:smart00755 1 EANFEYLKNVLLQFLTLRESE-RETLLPVISTVLQLSPEEMQKLLE 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
204-598 |
1.51e-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: 65.09 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 204 AEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQEERtqrqdLELRLEETREALAgrayaae 283
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYE-----GYELLKEKEALER------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 284 QMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRV 363
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 364 AALENQIsevsellgtyekakQKDQLAIQKLKERILQLDLENKTLALAassrspLDSHGEEssldVNVLKDKMEKLKRLL 443
Cdd:TIGR02169 318 EDAEERL--------------AKLEAEIDKLLAEIEELEREIEEERKR------RDKLTEE----YAELKEELEDLRAEL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 444 QVAARKSQVTLDVEKlcdleimpsseaadgekatalYYQQELKQLKEEFE---RYKMRAQVVLKSKNTKDGNLGKELEAA 520
Cdd:TIGR02169 374 EEVDKEFAETRDELK---------------------DYREKLEKLKREINelkRELDRLQEELQRLSEELADLNAAIAGI 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22208850 521 QEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLhRQELERCQldfrDRTLKLEEELHKQRDRALAVLTE 598
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-KEEYDRVE----KELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-398 |
2.53e-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: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEKSRMEASyLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARL--I 230
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkaL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 231 TQQHDRAQEQsdhalmLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGfelQTKQLTREVEELKSELQAIR 310
Cdd:TIGR02168 802 REALDELRAE------LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE---DIESLAAEIEELEELIEELE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 311 DEknqpdprLQELQEEaarlkshfQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLA 390
Cdd:TIGR02168 873 SE-------LEALLNE--------RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
....*...
gi 22208850 391 IQKLKERI 398
Cdd:TIGR02168 938 IDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-439 |
3.29e-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: 63.92 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 156 KRLHQLKTQLATLTSSLATVTQEKSRMEASyLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHD 235
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 236 RAQEQSDhalmLRELQKLLQEERTQRQDLELRLEETREALAGrayAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQ 315
Cdd:TIGR02168 311 LANLERQ----LEELEAQLEELESKLDELAEELAELEEKLEE---LKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 316 PDPRLQELQEEAARLKSHFQaqlQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKdqlAIQKLK 395
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIE---RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE---LQEELE 457
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 22208850 396 ERILQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKL 439
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
165-390 |
4.24e-10 |
|
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: 62.47 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 165 LATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHA 244
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 245 LMLRELQKLLQEERTQRQDLELRL------------------EETREALAGRAYAAEQMEGFELQTKQLTREVEELKSEL 306
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 307 QAIRDEKNQPDPRLQELQEEAARLKSHFQ------AQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTY 380
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAerqkllARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
250
....*....|
gi 22208850 381 EKAKQKDQLA 390
Cdd:COG4942 247 GFAALKGKLP 256
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
258-619 |
5.45e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 258 RTQRQDLELRLEETREALAgRAYA-----AEQMEGFELQTKQ------LTREVEELKSELQAIRDEKNQpdPRLQELQEE 326
Cdd:COG1196 171 KERKEEAERKLEATEENLE-RLEDilgelERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELE--AELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 327 AARLKSHfQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENK 406
Cdd:COG1196 248 LEELEAE-LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 407 TLALAassrspLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKlcdleimpSSEAADGEKATALYYQQELK 486
Cdd:COG1196 327 ELEEE------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA--------ELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 487 QLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLHRQE 566
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 22208850 567 LERcqldfRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALASGLPGRR 619
Cdd:COG1196 473 ALL-----EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
152-722 |
5.78e-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: 63.15 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 152 GEVDKRLHQLKTQLATLTSSLATVTQEKSRMEAS-------------YLADKKKMKQDLEDASNKAEEERARLEGELKGL 218
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERlanlerqleeleaQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 219 QEQIAETKA-------RLITQQHDRAQEQSDHALMLRELQKL---LQEERTQRQDLELRLEETREALAGRAYAAEQMEGF 288
Cdd:TIGR02168 357 EAELEELEAeleelesRLEELEEQLETLRSKVAQLELQIASLnneIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 289 ELQTKqlTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALEN 368
Cdd:TIGR02168 437 ELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 369 Q--ISEVSELLGTYEKAKQKDQLAIQK-LKERILQLDLENKTLALAA-----------SSRSPLDS--HGEESSLDVNVL 432
Cdd:TIGR02168 515 QsgLSGILGVLSELISVDEGYEAAIEAaLGGRLQAVVVENLNAAKKAiaflkqnelgrVTFLPLDSikGTEIQGNDREIL 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 433 KDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMpsseAADGEKATALyyqqeLKQLKEEF-----ERYKMRAQVVL---- 503
Cdd:TIGR02168 595 KNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV----VDDLDNALEL-----AKKLRPGYrivtlDGDLVRPGGVItggs 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 504 KSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLHRQ-ELERCQLDFRDRTLKLE 582
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQL 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 583 EELHKQRDRALAVLTEK------DLELEQLRSVALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQL----AAANEPT 652
Cdd:TIGR02168 746 EERIAQLSKELTELEAEieeleeRLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeAANLRER 825
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22208850 653 FFLYAEQLARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHREEVAALQSH-IEKNIRDQSREGANLEY 722
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERASLEEALALLRSEL 896
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
193-386 |
7.37e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 193 MKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLIT--QQH---DRAQEQSDHALMLRELQKLLQEERTQRQDLELR 267
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNglvDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 268 LEETREALA-GRAYAAEQMEGFELQtkQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTA 346
Cdd:COG3206 242 LAALRAQLGsGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 22208850 347 LAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQK 386
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
188-600 |
1.27e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 188 ADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLELR 267
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA 1413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 268 LEETREALAGRAYAAEQMEGFELQTK-QLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRKTA 346
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 347 LAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESS 426
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 427 LDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADgEKATALYYQQELKQLKEEFEryKMRAQVVLKSK 506
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK-IKAEELKKAEEEKKKVEQLK--KKEAEEKKKAE 1650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 507 NTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELAR-LQQLHRQELERCQldfRDRTLKLEEEL 585
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKK---KAEELKKAEEE 1727
|
410
....*....|....*
gi 22208850 586 HKQRDRALAVLTEKD 600
Cdd:PTZ00121 1728 NKIKAEEAKKEAEED 1742
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
153-441 |
3.68e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKMKQdLEDASNKAEEERARLEGELKGLQEQIAETKARLITQ 232
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 233 QHDRAQ-EQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAE-----------QMEGFELQTKQLTREVE 300
Cdd:TIGR02169 778 EEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekeiqelqeQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 301 ELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQaQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTY 380
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERD-ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22208850 381 EKAKQKDQ------LAIQKLKERILQLDLENKTLAlAASSRSPLDShgEESSLDVNVLKDKMEKLKR 441
Cdd:TIGR02169 937 EDPKGEDEeipeeeLSLEDVQAELQRVEEEIRALE-PVNMLAIQEY--EEVLKRLDELKEKRAKLEE 1000
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-615 |
1.46e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 191 KKMKQDLEDASNKAEEERARLEGELKGLQEQIaetkarlitqqhDRAQEQSDHALMLRELQKllQEERTQRQDLELRLEE 270
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELERQL------------KSLERQAEKAERYKELKA--ELRELELALLVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 271 TREALAGRAYAAEQMEGfelQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEaarlkshfQAQLQQEMRKtalaed 350
Cdd:TIGR02168 237 LREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLEVSELEEEIEELQKE--------LYALANEISR------ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 351 qLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQL--DLENKTLALAASSRSPLDSHGEESSLD 428
Cdd:TIGR02168 300 -LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELkeELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 429 VNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMpsseaadgekatalyyQQELKQLKEEFERYKMRAQvvLKSKNT 508
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR----------------RERLQQEIEELLKKLEEAE--LKELQA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 509 KDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLHRQELERCQLDFRDRTLKLEEELHKQ 588
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
410 420
....*....|....*....|....*..
gi 22208850 589 RDRALAVLTEKDLELEQLRSVALASGL 615
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAALGGRL 547
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
155-434 |
2.24e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 155 DKRLHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERAR-------LEGELKGLQEQIAETKA 227
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekigeLEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 228 RLITQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQ 307
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 308 AIRDEKNQPDPRLQELQEEAARLKShfqAQLQQEMRKTALAEDQLRQQSQVEEQR--VAALENQISEVSELLGTYEKAKQ 385
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSE---ELADLNAAIAGIEAKINELEEEKEDKAleIKKQEWKLEQLAADLSKYEQELY 472
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 22208850 386 KDQLAIQKLKERILQLDLEnktLALAASSRSPLDSHGEESSLDVNVLKD 434
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRE---LAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
162-721 |
3.10e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.35 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 162 KTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQS 241
Cdd:pfam15921 291 RSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 242 DHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDE-KNQPDPRL 320
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQM 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 321 QELQEEAARLK--SHFQAQLQ--QEMRKTALAEDQLRQQSQVEEQRVaalenqISEVSELLGTYEKAKQKDQLAIQKLKE 396
Cdd:pfam15921 451 AAIQGKNESLEkvSSLTAQLEstKEMLRKVVEELTAKKMTLESSERT------VSDLTASLQEKERAIEATNAEITKLRS 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 397 RIlqlDLENKTLALAASSrsplDSHGEESSLDVNVLKDKMEKLKRLLQVAARKsqvtldveklcdLEIMPSSEAADGEKA 476
Cdd:pfam15921 525 RV---DLKLQELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVIEILRQQ------------IENMTQLVGQHGRTA 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 477 TALyyQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLgKELEAAQEQLAELKEKYI---SLRL-SCEELEHQHQQEADDW 552
Cdd:pfam15921 586 GAM--QVEKAQLEKEINDRRLELQEFKILKDKKDAKI-RELEARVSDLELEKVKLVnagSERLrAVKDIKQERDQLLNEV 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 553 KQELARLQQLhRQELERCQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSVALASGLPGRRSpvGGGGPGDPAD 632
Cdd:pfam15921 663 KTSRNELNSL-SEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA--MGMQKQITAK 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 633 TSSSDSLTQALQ-----LAAANEPTFFLYAEQLA-RKEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHRE---EVAALQ 703
Cdd:pfam15921 740 RGQIDALQSKIQfleeaMTNANKEKHFLKEEKNKlSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEvalDKASLQ 819
|
570
....*....|....*....
gi 22208850 704 -SHIEKNIRDQSREGANLE 721
Cdd:pfam15921 820 fAECQDIIQRQEQESVRLK 838
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
197-332 |
6.09e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 197 LEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALA 276
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 22208850 277 GRAYAAEqmEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKS 332
Cdd:COG4913 373 LPLPASA--EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-370 |
9.16e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 195 QDLEDASNKAEEERARLEGELKGLQEQIAETKARLitQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREA 274
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERR--EALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 275 LAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEA-ARLKSHFQAQLQQEMRKTALAE--DQ 351
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArLELRALLEERFAAALGDAVERElrEN 770
|
170
....*....|....*....
gi 22208850 352 LRQQSQVEEQRVAALENQI 370
Cdd:COG4913 771 LEERIDALRARLNRAEEEL 789
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
484-608 |
9.38e-07 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 51.30 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 484 ELKQLKEEFERYKMRAQVVLKSK-----NTKDGN-----------------LGKELEAAQEQLAELKEKYISLRLSCEEL 541
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKekliaSLKEGSgvegldsstaltleleeLRQERDLLREEIQKLRGQIQQLRTELQEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22208850 542 EHQHQQEADDWKQELARLQ----------QLHRQELERCQLDFRdrtlKLEEELHKQRDRALAVLTEKDLELEQLRS 608
Cdd:pfam09787 81 EAQQQEEAESSREQLQELEeqlatersarREAEAELERLQEELR----YLEEELRRSKATLQSRIKDREAEIEKLRN 153
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
206-608 |
1.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 206 EERARLEGELKGLQEQIAETKArlITQQHDRAQEQsdhalmLRELQKLLQEERTQRQDLElRLEETREALAGRAYAAEQM 285
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE--LQEELEELEEE------LEELEAELEELREELEKLE-KLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 286 EGFELQTKQLTREVEELKSELQAIRDEKNQpdprLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAA 365
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAE----LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 366 LENQISEVSELLGTYEKAKQKDQLAiQKLKERILQLDLENKTLALAASSRSPLDSH-----------GEESSLDVNVLKD 434
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlflvlGLLALLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 435 KMEKLKRLLQVAARKSQVTLDVEKLCDL--EIMPSSEAADGEKATALYYQQELKQLKEEFERYK--MRAQVVLKSKNTKD 510
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELlaALGLPPDLSPEELLELLDRIEELQELLREAEELEeeLQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 511 GNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQ-QLHRQELERCQldfrdrtlKLEEELHKQR 589
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELEELE--------EELEELEEEL 448
|
410
....*....|....*....
gi 22208850 590 DRALAVLTEKDLELEQLRS 608
Cdd:COG4717 449 EELREELAELEAELEQLEE 467
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
162-588 |
2.34e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 162 KTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQeqiAETKARLItQQHDRAQEQS 241
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE---AKKKAEEK-KKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 242 DHALMLRELQKLLQEERtQRQDLELRLEETREALAGRAYAAEQMEGFELQTK--QLTREVEELKSELQAirdEKNQPDPR 319
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEA---KKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 320 LQELQEEAARLKSHFQAQLQQEMRKTALAE--DQLRQQSQVEE-QRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKE 396
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKkaDELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 397 RILQLDLENKTLALAASSRSPLDSHGEESSLDVNVlKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKA 476
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE-KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 477 TALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQ-QEADDWKQE 555
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaEEAKKDEEE 1755
|
410 420 430
....*....|....*....|....*....|...
gi 22208850 556 LARLQQLHRQELERCQLDFRDRTLKLEEELHKQ 588
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-608 |
2.81e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 152 GEVDKRLHQLKTQLATLTSSLATVTQEKSRMEA--SYLADKKKMKQDLEdASNKAEEERAR--------LEGELKGLQEQ 221
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEElkEEIEELEKELESLE-GSKRKLEEKIReleerieeLKKEIEELEEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 222 IAETKarlitqqhdraqEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGrayaaeqmegfelqtkqltreVEE 301
Cdd:PRK03918 282 VKELK------------ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING---------------------IEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 302 LKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQaqlqqemrktaLAEDQLRQQSQVEEQRVAALENQISEVSELLGTYE 381
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEERHE-----------LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 382 KAKQKDQLAIQKLKERILQLDLENKTLALAASS-----------RSPLDSHG-----EESSLDVNVLKDKMEKLKRLLQv 445
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcGRELTEEHrkellEEYTAELKRIEKELKEIEEKER- 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 446 AARKSQVTLDVEKLCDLEIMPSSEAADG----EKATALYYQQELKQLKEEFERYKMRA------QVVLKSKNTKDGNLGK 515
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQlkelEEKLKKYNLEELEKKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 516 ELEAAQEQLAELKEKYISLRlscEELEHQHQQEADDWKQELARLQQLHRQELErcQLDFRDRTLKLEEELHKQR---DRA 592
Cdd:PRK03918 557 KLAELEKKLDELEEELAELL---KELEELGFESVEELEERLKELEPFYNEYLE--LKDAEKELEREEKELKKLEeelDKA 631
|
490
....*....|....*.
gi 22208850 593 LAVLTEKDLELEQLRS 608
Cdd:PRK03918 632 FEELAETEKRLEELRK 647
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-540 |
4.09e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAET------- 225
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaee 1481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 226 --KARLITQQHDRAQEQSDHALMLRELQKLLQE----ERTQRQDLELRLEETREALAGRAyAAEQMEGFELQTKQLTREV 299
Cdd:PTZ00121 1482 akKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkaEEAKKADEAKKAEEAKKADEAKK-AEEKKKADELKKAEELKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 300 EELKSELQAIRDE--KNQPDPRLQELQ-------EEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQI 370
Cdd:PTZ00121 1561 EEKKKAEEAKKAEedKNMALRKAEEAKkaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 371 SEVSELLGTYEKAKQKDQLAIQKLKERilQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKS 450
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEA--KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 451 QVTLDVEKLCDLEIMPSSEAADGEKATAlyyqQELKQLKEEferyKMRAQVVLKSKNTKDGNLGKELEAAQEQlaELKEK 530
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKA----EEAKKDEEE----KKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEE 1788
|
410
....*....|
gi 22208850 531 YISLRLSCEE 540
Cdd:PTZ00121 1789 DEKRRMEVDK 1798
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
177-610 |
4.20e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 177 QEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARlitQQHDRAQEQSDHALMLRELQKLLQE 256
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARK---AEDARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 257 ERTQRQDLELRLEETREALAGRAyAAEQMEGFELQTKQLTREVEELKSELQAIRDE---KNQPDPRLQELQEEAARLKSH 333
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARK-AEEVRKAEELRKAEDARKAEAARKAEEERKAEearKAEDAKKAEAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 334 FQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLaiqKLKERILQLDlENKTLALAAS 413
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA---KKAEEKKKAD-EAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 414 SRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDleimPSSEAADGEKATALYYQQELKQLKEEfe 493
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE----EKAEAAEKKKEEAKKKADAAKKKAEE-- 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 494 rykMRAQVVLKSKNTKDGNLGKEL---EAAQEQLAELKEKYISLRlSCEEL-----EHQHQQEADDWKQELARLQQLHRQ 565
Cdd:PTZ00121 1390 ---KKKADEAKKKAEEDKKKADELkkaAAAKKKADEAKKKAEEKK-KADEAkkkaeEAKKADEAKKKAEEAKKAEEAKKK 1465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 22208850 566 ELERCQLDfrdrTLKLEEELHKQRDRALAVLTEKDLELEQLRSVA 610
Cdd:PTZ00121 1466 AEEAKKAD----EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
153-338 |
4.26e-06 |
|
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: 48.77 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEksrmeasyLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAetkarlitq 232
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDE--------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 233 qhdRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDE 312
Cdd:COG1579 77 ---KYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|....*.
gi 22208850 313 KNQpdpRLQELQEEAARLKSHFQAQL 338
Cdd:COG1579 154 LEA---ELEELEAEREELAAKIPPEL 176
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
153-400 |
5.02e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEKSRMEASylaDKKKMKQDLEDASNKAEEER-ARLEGELKGLQEQIAETKARLIT 231
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEALKDD---NDEETRETLSTLSLRQLESRlAQTLDQLQNAQNDLAEYNSQLVS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 232 QQH--DRAQEQSDHAlmlrelQKLLQEERTQRQDLELRLEETREALAGRaYAAEQmEGFELQTKQLTREVE---ELKSEL 306
Cdd:PRK11281 154 LQTqpERAQAALYAN------SQRLQQIRNLLKGGKVGGKALRPSQRVL-LQAEQ-ALLNAQNDLQRKSLEgntQLQDLL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 307 QAIRDEKNQpdpRLQELQEeaarlkshfQAQLQQEmrktALAEDQLRQ-QSQVEEQRVAALENQISEVSELlgtyekakq 385
Cdd:PRK11281 226 QKQRDYLTA---RIQRLEH---------QLQLLQE----AINSKRLTLsEKTVQEAQSQDEAARIQANPLV--------- 280
|
250
....*....|....*.
gi 22208850 386 KDQLAI-QKLKERILQ 400
Cdd:PRK11281 281 AQELEInLQLSQRLLK 296
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
152-376 |
5.99e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 152 GEVDKRLHQLKTQLATLTSSLATVTQ-EKSRMEASYLADKKKMKQDL-EDASNKAEEERARLEGELKGLQEQIAETKarl 229
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDlVEAEDRIERLEERREDLEELiAERRETIEEKRERAEELRERAAELEAEAE--- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 230 itQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAI 309
Cdd:PRK02224 555 --EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22208850 310 RDEKNQ-----PDPRLQELQEEAARLKShFQAQLQQEMRKTALAEDQLrqqsqveEQRVAALENQISEVSEL 376
Cdd:PRK02224 633 RERKREleaefDEARIEEAREDKERAEE-YLEQVEEKLDELREERDDL-------QAEIGAVENELEELEEL 696
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-401 |
7.31e-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: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 196 DLEDASNKAEEERARLEgELKGLQEQIAETKARLITQQHDRAQEQSDHA-LMLRELQKLLQEERTQRQDLELRLEETREA 274
Cdd:COG4913 239 RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 275 LAGrayAAEQMEGFELQTKQL-TREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKShfqaqlqqemrKTALAEDQLR 353
Cdd:COG4913 318 LDA---LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGL-----------PLPASAEEFA 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22208850 354 QQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQL 401
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
200-542 |
1.80e-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: 48.53 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 200 ASNKAEEERAR-----LEGELKGLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQEERTQRQdlelRLEETREA 274
Cdd:TIGR02169 670 RSEPAELQRLRerlegLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE----RLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 275 LagrayaaeqmegfelqtKQLTREVEELKSELQAIRDEKNQPDPRLQELQEE----AARLKSHFQAQLQQEMRK------ 344
Cdd:TIGR02169 746 L-----------------SSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlEARLSHSRIPEIQAELSKleeevs 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 345 ---------------TALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLa 409
Cdd:TIGR02169 809 riearlreieqklnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL- 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 410 laASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLD----VEKLCDLEIMPSSEAADGEKAtalyyQQEL 485
Cdd:TIGR02169 888 --KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEelseIEDPKGEDEEIPEEELSLEDV-----QAEL 960
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 486 KQLKEE---FERYKMRAQvvlkskntkdgnlgKELEAAQEQLAELKEKYISLRLSCEELE 542
Cdd:TIGR02169 961 QRVEEEiraLEPVNMLAI--------------QEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
486-721 |
2.75e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 486 KQLKEEFERYKMRAQVV-LKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLhR 564
Cdd:COG1196 216 RELKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL-L 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 565 QELERCQLDfRDRTLKLEEELHKQRDRALAVLTEKDLELEQLRSvALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQ 644
Cdd:COG1196 295 AELARLEQD-IARLEERRRELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22208850 645 LAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEvevhQLQDRLLEEGERHREEVAALQSHIEKNIRDQSREGANLE 721
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELE----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
153-409 |
2.83e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEKSRmeasyLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLitq 232
Cdd:COG4913 665 SAEREIAELEAELERLDASSDDLAALEEQ-----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL--- 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 233 qhDRAqeqsdhalmlrelqkllqeERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDE 312
Cdd:COG4913 737 --EAA-------------------EDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 313 KNQPDP-RLQELQEEAARLkSHFQAQLQQemrktaLAEDQL-RQQSQVEEQRvaaLENQISEVSELLGTYEKakqkdqlA 390
Cdd:COG4913 796 FNREWPaETADLDADLESL-PEYLALLDR------LEEDGLpEYEERFKELL---NENSIEFVADLLSKLRR-------A 858
|
250
....*....|....*....
gi 22208850 391 IQKLKERILQLdleNKTLA 409
Cdd:COG4913 859 IREIKERIDPL---NDSLK 874
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-576 |
3.44e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 156 KRLHQLKTQLATLTSSLATVTQEKSRMEasyladKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAEtkarlitqqhd 235
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLE------KLLQLLPLYQELEALEAELAELPERLEELEERLEE----------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 236 raqeqsdhalmLRELQKLLQEERTQRQDLELRLEETREALagRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQ 315
Cdd:COG4717 158 -----------LRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 316 PDPRLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLK 395
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 396 ERILQLDLENKTLALAASS-RSPLDSHGEESSLDVNVLKDKMEKLKRLL-QVAARKSQVTLDVEKLCDLEIMPSSEAADG 473
Cdd:COG4717 305 EELQALPALEELEEEELEElLAALGLPPDLSPEELLELLDRIEELQELLrEAEELEEELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 474 EKATALYYQ-QELKQLKEEFERYKMR-----AQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQ 547
Cdd:COG4717 385 EELRAALEQaEEYQELKEELEELEEQleellGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420
....*....|....*....|....*....
gi 22208850 548 EADDwkQELARLQQLHRQELERCQLDFRD 576
Cdd:COG4717 465 LEED--GELAELLQELEELKAELRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-716 |
4.63e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 157 RLHQLKTQLATLTSSLATVTQEKSRMEASyLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDR 236
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 237 AQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELK-------SELQAI 309
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlskyeQELYDL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 310 RDEKNQPDPRLQELQEEAARLKSHFQAqLQQEMRKTALAED-----------QLRQQSQVEEQRVAALE----NQISEVs 374
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARA-SEERVRGGRAVEEvlkasiqgvhgTVAQLGSVGERYATAIEvaagNRLNNV- 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 375 eLLGTYEKAKQkdqlAIQKLKERILQ----LDLeNKTlalaASSRSPLDSHGEESSLDV--------------------- 429
Cdd:TIGR02169 553 -VVEDDAVAKE----AIELLKRRKAGratfLPL-NKM----RDERRDLSILSEDGVIGFavdlvefdpkyepafkyvfgd 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 430 NVLKDKMEKLKRLLqvaARKSQVTLDVEKLCDLEIMP-SSEAADGEKATALYYQQELKQLKEEFERYKmRAQVVLKSKNT 508
Cdd:TIGR02169 623 TLVVEDIEAARRLM---GKYRMVTLEGELFEKSGAMTgGSRAPRGGILFSRSEPAELQRLRERLEGLK-RELSSLQSELR 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 509 KdgnLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQLHRQ--ELERCQLDFRDRTLKLEEELH 586
Cdd:TIGR02169 699 R---IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEieNVKSELKELEARIEELEEDLH 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 587 KQRDrALAVLTEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTFFLYAE-QLARKEV 665
Cdd:TIGR02169 776 KLEE-ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeQIKSIEK 854
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 22208850 666 EITSLRKQKHRLEVEVHQLQDRLLEEGERH------REEVAALQSHIEKNIRDQSRE 716
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRDELEAQLRELERKIEELEAQ 911
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
152-607 |
5.59e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 152 GEVDKRLHQlktQLATLTSSLATVTQEKSRMEAsylaDKKKMKQDLEDASNKAEEERARLEgELKGLQEQIAETkarlit 231
Cdd:PRK02224 198 EKEEKDLHE---RLNGLESELAELDEEIERYEE----QREQARETRDEADEVLEEHEERRE-ELETLEAEIEDL------ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 232 qqhdraqeQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQ---- 307
Cdd:PRK02224 264 --------RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrv 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 308 ----------AIRDEKNQPDPRLQELQEEAARLKSHFQ-AQLQQEMRKTALAEdqLRQQSQVEEQRVAALENQISEVSEL 376
Cdd:PRK02224 336 aaqahneeaeSLREDADDLEERAEELREEAAELESELEeAREAVEDRREEIEE--LEEEIEELRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 377 LGTYEKAKQKdqlAIQKLKEriLQLDLEN------KTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLK----RLLQVA 446
Cdd:PRK02224 414 LEELREERDE---LREREAE--LEATLRTarerveEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEeleaELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 447 ARKSQVTLDVEKLCDLEIMPS------------SEAADGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLG 514
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEAEDrierleerredlEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 515 KELEAAQE---QLAELKEKYISLRLSCEELE--HQHQQEADDWKQELARLQQLHRQELERCQlDFRDRTLKLE------- 582
Cdd:PRK02224 569 EAREEVAElnsKLAELKERIESLERIRTLLAaiADAEDEIERLREKREALAELNDERRERLA-EKRERKRELEaefdear 647
|
490 500
....*....|....*....|....*.
gi 22208850 583 -EELHKQRDRALAVLTEKDLELEQLR 607
Cdd:PRK02224 648 iEEAREDKERAEEYLEQVEEKLDELR 673
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
154-325 |
5.81e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 154 VDKRLHQLKTQLATLTSSLATvTQEKSRMEASYladKKKMKQDLEDASNkAEEERARLEGELKGLQEQIAETKARLITQQ 233
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRLRQ-QQRAERLLAEF---CKRLGKNLDDEDE-LEQLQEELEARLESLSESVSEARERRMALR 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 234 HDRAQEQSDHalmlRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEEL---KSELQAIR 310
Cdd:PRK04863 586 QQLEQLQARI----QRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELaarKQALDEEI 661
|
170
....*....|....*....
gi 22208850 311 DEKNQP----DPRLQELQE 325
Cdd:PRK04863 662 ERLSQPggseDPRLNALAE 680
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
512-691 |
7.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 512 NLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQ----EADDWKQELARLQQlHRQELERCQLDFRDRTLKLEEElhk 587
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLER-ELEERERRRARLEALLAALGLP--- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 588 qrdralAVLTEKDLELEQLRSVALASGLPGRRSPVGGGGPGDPAdtsssdsltqalQLAAANEptfflyaeQLARKEVEI 667
Cdd:COG4913 375 ------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA------------ALRDLRR--------ELRELEAEI 428
|
170 180
....*....|....*....|....
gi 22208850 668 TSLRKQKHRLEVEVHQLQDRLLEE 691
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEA 452
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
251-397 |
1.44e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 251 QKLLQEERTqRQDLELrleetrEALAGRAYAAEQMEGFELQTKQ-LTREVEELKSELQAIRDEKNqpdpRLQELQEEAAR 329
Cdd:PRK09039 41 QFFLSREIS-GKDSAL------DRLNSQIAELADLLSLERQGNQdLQDSVANLRASLSAAEAERS----RLQALLAELAG 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22208850 330 LKSHFQAQLQQEMRKTAlAEDQL--RQQSQVE--EQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKER 397
Cdd:PRK09039 110 AGAAAEGRAGELAQELD-SEKQVsaRALAQVEllNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRR 180
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-581 |
1.50e-04 |
|
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: 45.34 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 193 MKQDLEDASNKAEEERARLEGELKGLQEQIAETKARL--ITQQHDRAQEQSDHALMLRELQKLLQEERTQrqdlELRLEE 270
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHayLTQKREAQEEQLKKQQLLKQLRARIEELRAQ----EAVLEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 271 TREALAGRAYAAEQMEGFELQTkQLTREVEELKSELQAIRDEknqpdpRLQELQEEAARLKSHFQAQLQQEMRKTALA-E 349
Cdd:TIGR00618 282 TQERINRARKAAPLAAHIKAVT-QIEQQAQRIHTELQSKMRS------RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 350 DQLRQQSQVEEQRVAALENQISEVSELLgTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHgeessldV 429
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQHTLTQHIH-TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQ-------L 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 430 NVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKatalyyqQELKQLKEEFERYKMRAQVVLKSKNTK 509
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE-------QQLQTKEQIHLQETRKKAVVLARLLEL 499
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22208850 510 DGN----LGKELEAAQE-QLAELKEKYISLRLSCEELEHQHQQEADDWKQELARLQQlHRQELERCQLDFRDRTLKL 581
Cdd:TIGR00618 500 QEEpcplCGSCIHPNPArQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLKEQMQEIQQSFSIL 575
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
298-541 |
1.70e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 298 EVEELKSELQAIRDEKnqPDPRLQELQEEAARLKSHFqaqlqqEMRKTALAEdqlrqqsqVEEQRVAALENQISEVSELL 377
Cdd:PRK05771 32 HIEDLKEELSNERLRK--LRSLLTKLSEALDKLRSYL------PKLNPLREE--------KKKVSVKSLEELIKDVEEEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 378 GTYEKAkqkdqlaIQKLKERILQLDLENKTLALAASSRSPLdshgeeSSLDVnvlkdKMEKLKRLLQVAARKSQVTLDVE 457
Cdd:PRK05771 96 EKIEKE-------IKELEEEISELENEIKELEQEIERLEPW------GNFDL-----DLSLLLGFKYVSVFVGTVPEDKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 458 KLCDLEIMPS---SEAADGEKATAL------YYQQELKQLKE-EFERYKM----RAQVVLKSKNTKDGNLGKELEAAQEQ 523
Cdd:PRK05771 158 EELKLESDVEnveYISTDKGYVYVVvvvlkeLSDEVEEELKKlGFERLELeeegTPSELIREIKEELEEIEKERESLLEE 237
|
250
....*....|....*...
gi 22208850 524 LAELKEKYISLRLSCEEL 541
Cdd:PRK05771 238 LKELAKKYLEELLALYEY 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
153-329 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLitq 232
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL--- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 233 qhdrAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALagrayaaeqmegfelqtKQLTREVEELKSELQAIRDE 312
Cdd:COG4913 376 ----PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL-----------------RDLRRELRELEAEIASLERR 434
|
170
....*....|....*..
gi 22208850 313 KNQPDPRLQELQEEAAR 329
Cdd:COG4913 435 KSNIPARLLALRDALAE 451
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
321-549 |
1.84e-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: 44.37 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 321 QELQEEAARLKshfqaQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERI-- 398
Cdd:COG4942 20 DAAAEAEAELE-----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIae 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 399 LQLDLENKTLALAASSRSpLDSHGEESSLDVNVLKDKMEKLKRLLQ-----VAARKSQVTLDVEKLCDLEimpsseaadG 473
Cdd:COG4942 95 LRAELEAQKEELAELLRA-LYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELA---------A 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22208850 474 EKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQHQQEA 549
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
204-703 |
1.84e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 204 AEEERARLEGELKGLQEQIAETKARL--ITQQHDRAQEQSDhalmlrELQKLLQEERTQRQDLELRLEETREALAGRAYA 281
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIerYEEQREQARETRD------EADEVLEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 282 AEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHfQAQLQQEMRKTALAEDQLRQQSQVEEQ 361
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 362 RVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLE----NKTLALAASSRSPLDSHGEESSLDVNVLKDKME 437
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 438 KLKRLLQVAA---RKSQVTLDVEKlC-----DLEIMPSSEAADGEKATALYYQQELKQLKEEFERYKMRAqvvlkskntk 509
Cdd:PRK02224 430 ELEATLRTARervEEAEALLEAGK-CpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERL---------- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 510 dgNLGKELEAAQEQLAELKEKyislRLSCEELEHQHQQEADDWKQELARLqqlhrqelercqldfRDRTLKLEEELHKQR 589
Cdd:PRK02224 499 --ERAEDLVEAEDRIERLEER----REDLEELIAERRETIEEKRERAEEL---------------RERAAELEAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 590 DRAlavlTEKDLELEQLRSVALAsgLPGRRSpvggggpgdpADTSSSDSLTQALQLAAAneptfflyaeqLARKEVEITS 669
Cdd:PRK02224 558 EAA----AEAEEEAEEAREEVAE--LNSKLA----------ELKERIESLERIRTLLAA-----------IADAEDEIER 610
|
490 500 510
....*....|....*....|....*....|....
gi 22208850 670 LRKQKHRLEVEVHQLQDRLLEEGERHREEVAALQ 703
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFD 644
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
191-607 |
2.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 191 KKMKQDLEDASNKAEEERARLEGELKGLQEQIaetkarlitqqhdraQEQSDHALMLRELQKLLQEERTQRQDLELRLEE 270
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERI---------------KELEEKEERLEELKKKLKELEKRLEELEERHEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 271 TREALAgrayAAEQMEgfELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHfQAQLQQEMR--KTALA 348
Cdd:PRK03918 364 YEEAKA----KKEELE--RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE-IKELKKAIEelKKAKG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 349 EDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLD 428
Cdd:PRK03918 437 KCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 429 VNVLKDKMEKLKRLLqvaarksqvtldvEKLCDLEIMPSSEAADGEKAtalyyqQELKQLKEEFERYKMRAQVVLKSKNT 508
Cdd:PRK03918 517 LEELEKKAEEYEKLK-------------EKLIKLKGEIKSLKKELEKL------EELKKKLAELEKKLDELEEELAELLK 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 509 KDGNLG----KELEAAQEQLAELKEKYISLRLSCEELEHQH------QQEADDWKQELARLQ---QLHRQELERCQLDFR 575
Cdd:PRK03918 578 ELEELGfesvEELEERLKELEPFYNEYLELKDAEKELEREEkelkklEEELDKAFEELAETEkrlEELRKELEELEKKYS 657
|
410 420 430
....*....|....*....|....*....|..
gi 22208850 576 DRTLKLEEELHKQRDRALAVLTEKDLELEQLR 607
Cdd:PRK03918 658 EEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
215-413 |
2.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 215 LKGLQEQIAETKARLitqqhDRAQEQsdhalmLRELQKLLQEERTQRQDLElRLEETREAlagrayaaeqmegfELQTKQ 294
Cdd:COG4913 612 LAALEAELAELEEEL-----AEAEER------LEALEAELDALQERREALQ-RLAEYSWD--------------EIDVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 295 LTREVEELKSELQAIRDeknqPDPRLQELQEEAarlkshfqAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVS 374
Cdd:COG4913 666 AEREIAELEAELERLDA----SSDDLAALEEQL--------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
170 180 190
....*....|....*....|....*....|....*....
gi 22208850 375 ELLGTYEKAKQKDQLAiqKLKERILQLDLENKTLALAAS 413
Cdd:COG4913 734 DRLEAAEDLARLELRA--LLEERFAAALGDAVERELREN 770
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
214-606 |
2.82e-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: 44.56 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 214 ELKGLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLEL---RLEETREALAgrayAAEQMEGFEL 290
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAasdHLNLVQTALR----QQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 291 QTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFqAQLQQemrktALAEDQLRQ-QSQveeQRVAALEN- 368
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL-ADYQQ-----ALDVQQTRAiQYQ---QAVQALEKa 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 369 -QISEVSELL-----GTYEKAKQKDQLAIQKLkerilqLDLENKtLALAASSRSPLD---------SHGEESSLDVNVLK 433
Cdd:COG3096 426 rALCGLPDLTpenaeDYLAAFRAKEQQATEEV------LELEQK-LSVADAARRQFEkayelvckiAGEVERSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 434 DKMEKLKRLLQVAARKSQVTLdveKLCDLEIMPSSEAADGEKATALYYQQELK-QLKEEFERYKMRAQVvlkskntkdgn 512
Cdd:COG3096 499 ELLRRYRSQQALAQRLQQLRA---QLAELEQRLRQQQNAERLLEEFCQRIGQQlDAAEELEELLAELEA----------- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 513 lgkELEAAQEQLAELKEKYISLRLSCEELEHQHQQ---EADDWKQELARLQQLHRQ---ELERCQ--LDFRDRTLKLEEE 584
Cdd:COG3096 565 ---QLEELEEQAAEAVEQRSELRQQLEQLRARIKElaaRAPAWLAAQDALERLREQsgeALADSQevTAAMQQLLERERE 641
|
410 420
....*....|....*....|..
gi 22208850 585 LHKQRDRALAVLTEKDLELEQL 606
Cdd:COG3096 642 ATVERDELAARKQALESQIERL 663
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
260-537 |
3.52e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 260 QRQDLELRLEETREALagrayaaeqmEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARlkshfqAQLQ 339
Cdd:COG3206 162 LEQNLELRREEARKAL----------EFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL------SELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 340 QEMRktalaedQLRQQSQVEEQRVAALENQISEVSELLgtyekAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPld 419
Cdd:COG3206 226 SQLA-------EARAELAEAEARLAALRAQLGSGPDAL-----PELLQSPVIQQLRAQLAELEAELAELSARYTPNHP-- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 420 shgeesslDVNVLKDKMEKLKRLLQVAARKSQVTLDVEklcdleimpsseaADGEKATALYYQQELKQLKEEFERYKmRA 499
Cdd:COG3206 292 --------DVIALRAQIAALRAQLQQEAQRILASLEAE-------------LEALQAREASLQAQLAQLEARLAELP-EL 349
|
250 260 270
....*....|....*....|....*....|....*...
gi 22208850 500 QVVLKskntkdgNLGKELEAAQEQLAELKEKYISLRLS 537
Cdd:COG3206 350 EAELR-------RLEREVEVARELYESLLQRLEEARLA 380
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
153-531 |
3.53e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEKSRmEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQ 232
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 233 QHDRAQEQSDHALMLRELQKLLQEE---RTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTRE----------- 298
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAallEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagava 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 299 -------------------------VEELKSELQAIRDEKNQPDPRLQEL-----------QEEAARLKSHFQAQLQQEM 342
Cdd:COG1196 528 vligveaayeaaleaalaaalqnivVEDDEVAAAAIEYLKAAKAGRATFLpldkiraraalAAALARGAIGAAVDLVASD 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 343 RKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDS-- 420
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAer 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 421 -HGEESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEFERYKMRA 499
Cdd:COG1196 688 lAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
410 420 430
....*....|....*....|....*....|....*....
gi 22208850 500 QvvLKSKNTKDGNLGK-------ELEAAQEQLAELKEKY 531
Cdd:COG1196 768 E--LERLEREIEALGPvnllaieEYEELEERYDFLSEQR 804
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
157-325 |
3.80e-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: 44.17 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 157 RLHQLKTQLATLTSSLATvtQEKSRMEASYLAdkKKMKQDLEDASNkAEEERARLEGELKGLQEQIAETKARLITQQHD- 235
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQ--QQNAERLLEEFC--QRIGQQLDAAEE-LEELLAELEAQLEELEEQAAEAVEQRSELRQQl 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 236 -----RAQEQSDHALMLRELQKLLQEERTQrqdLELRLEETREALAGRAYAAEQmegfELQTKQLTREVEELKSELQAIR 310
Cdd:COG3096 588 eqlraRIKELAARAPAWLAAQDALERLREQ---SGEALADSQEVTAAMQQLLER----EREATVERDELAARKQALESQI 660
|
170
....*....|....*....
gi 22208850 311 DEKNQP----DPRLQELQE 325
Cdd:COG3096 661 ERLSQPggaeDPRLLALAE 679
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
195-386 |
4.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 195 QDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQhdraQEQSDHALMLRELQKLLQEERTQRQDLELRLEETRea 274
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAK----TELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 275 lagrayAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQemRKTALAEDQlRQ 354
Cdd:COG1579 87 ------NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE--LDEELAELE-AE 157
|
170 180 190
....*....|....*....|....*....|..
gi 22208850 355 QSQVEEQRvAALENQISEvsELLGTYEKAKQK 386
Cdd:COG1579 158 LEELEAER-EELAAKIPP--ELLALYERIRKR 186
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
154-374 |
4.30e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 154 VDKRLHQLKTQLATLTSSLATVTQE-------KSRMEASYLADKKKMKQ-DLEDASNKAEEERARLEgELKGLQEQIAET 225
Cdd:PRK04863 440 AEDWLEEFQAKEQEATEELLSLEQKlsvaqaaHSQFEQAYQLVRKIAGEvSRSEAWDVARELLRRLR-EQRHLAEQLQQL 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 226 KARLITQQHDRAQEQSDHALmLRELQKLLQEERTQRQDLELRLEETREALAG----RAYAAEQMEGFELQTKQLTREVEE 301
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERL-LAEFCKRLGKNLDDEDELEQLQEELEARLESlsesVSEARERRMALRQQLEQLQARIQR 597
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22208850 302 LKSelQAirdeknqpdPRLQELQEEAARLKSHFQA------QLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVS 374
Cdd:PRK04863 598 LAA--RA---------PAWLAAQDALARLREQSGEefedsqDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS 665
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
176-613 |
4.40e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 176 TQEKSRMEAsYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQ 255
Cdd:pfam12128 272 TLIASRQEE-RQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 256 EERTQRQDLELRLEETREALAGRAYAAEQMEgfELQTKQLTREVEELKSELQAIRDEKnqpdprlqELQEEAARlkSHFQ 335
Cdd:pfam12128 351 SWQSELENLEERLKALTGKHQDVTAKYNRRR--SKIKEQNNRDIAGIKDKLAKIREAR--------DRQLAVAE--DDLQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 336 AQ-----LQQEMRKTALAEDQLRQQSQVEEQRVaaLENQISEVSELLGTYEKAKQKDQLAIQKL-KERILQLDLENKTLA 409
Cdd:pfam12128 419 ALeselrEQLEAGKLEFNEEEYRLKSRLGELKL--RLNQATATPELLLQLENFDERIERAREEQeAANAEVERLQSELRQ 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 410 LAASSRSPLDSHGEESsLDVNVLKDKMEKLKRLLQVAAR------KSQV---------TLDVEKLCDLEIMPSSEAADGE 474
Cdd:pfam12128 497 ARKRRDQASEALRQAS-RRLEERQSALDELELQLFPQAGtllhflRKEApdweqsigkVISPELLHRTDLDPEVWDGSVG 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 475 KATALY----------------YQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSC 538
Cdd:pfam12128 576 GELNLYgvkldlkridvpewaaSEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDL 655
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22208850 539 EELEHQHQQEADDWKQELARLQQLHRQELERCQLDFRDRTLKLEEELHKQRDRALAVLTEKD---LELEQLRSVALAS 613
Cdd:pfam12128 656 RRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQaywQVVEGALDAQLAL 733
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
155-303 |
5.18e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 155 DKRLHQLKTQLATLTSSLATVTQEKSRMEASYLAdkkkmkqdLEDASNKAEEERARLEGELKGLQEQI--AETKARLITQ 232
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVAN--------LRASLSAAEAERSRLQALLAELAGAGaaAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22208850 233 QHDRAQEQSDHALMLRE-LQKLLQEERTQRQDLE--LRLEETREALAGRAYAAeqmEGFELQTKqLTREVEELK 303
Cdd:PRK09039 124 ELDSEKQVSARALAQVElLNQQIAALRRQLAALEaaLDASEKRDRESQAKIAD---LGRRLNVA-LAQRVQELN 193
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
174-530 |
5.95e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 174 TVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERArLEGELKGLQEQIAETKARLITQQHDRAQEqsdhalmLRELQKL 253
Cdd:PLN02939 90 STSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQL-SDFQLEDLVGMIQNAEKNILLLNQARLQA-------LEDLEKI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 254 LQEERTQRQD---LELRLEETREALagrAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARL 330
Cdd:PLN02939 162 LTEKEALQGKiniLEMRLSETDARI---KLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 331 KSHFQAqLQQEMRKTALAEDQLrqqSQVEEQRvAALENQISEV-SELLGTYEKAKQKDQLAIQKLKERILQL-DLENKTL 408
Cdd:PLN02939 239 KDDIQF-LKAELIEVAETEERV---FKLEKER-SLLDASLRELeSKFIVAQEDVSKLSPLQYDCWWEKVENLqDLLDRAT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 409 ALAASSRSPLDSHGEessldvnvLKDKMEKLKRLLQVAarksqvtlDVEKLCD--LEIMpsseaadgekatalyyQQELK 486
Cdd:PLN02939 314 NQVEKAALVLDQNQD--------LRDKVDKLEASLKEA--------NVSKFSSykVELL----------------QQKLK 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 22208850 487 QLKEEFER--YKMRAQVVLKSKNTKDgnlgkeleaAQEQLAELKEK 530
Cdd:PLN02939 362 LLEERLQAsdHEIHSYIQLYQESIKE---------FQDTLSKLKEE 398
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
293-377 |
7.18e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 293 KQLTREVEELKSELQAIRDEKNQPD-PRLQELQEEAARLKSHFQAQLQQ-EMRKTALAEDQ-LRQQSQVEEQRVAALENQ 369
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASfERLAELRDELAELEEELEALKARwEAEKELIEEIQeLKEELEQRYGKIPELEKE 493
|
....*...
gi 22208850 370 ISEVSELL 377
Cdd:COG0542 494 LAELEEEL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-721 |
8.27e-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: 43.12 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEKSRMEASyLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQ 232
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAE-LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 233 QHDRAQEQSDHALMLRELQKLLQE-ERTQRQDLELRLEETREALAGrayAAEQMEGFELQTKQLTREVEELKSELQAIRD 311
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEE---LQEELERLEEALEELREELEEAEQALDAAER 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 312 EKNQPDPRLQELQEEAARLKSHFQ--AQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISE----------------- 372
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEgvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGrlqavvvenlnaakkai 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 373 -------------------------------------------------------VSELLGTY----------EKAKQKD 387
Cdd:TIGR02168 563 aflkqnelgrvtflpldsikgteiqgndreilkniegflgvakdlvkfdpklrkaLSYLLGGVlvvddldnalELAKKLR 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 388 QL---------------------------------AIQKLKERI--LQLDLENKTLALAA---------SSRSPLDSHGE 423
Cdd:TIGR02168 643 PGyrivtldgdlvrpggvitggsaktnssilerrrEIEELEEKIeeLEEKIAELEKALAElrkeleeleEELEQLRKELE 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 424 ESSLDVNVLKDKMEKLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEFERYKMRAQvvl 503
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK--- 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 504 kskntkdgNLGKELEAAQEQLAELKEKYISLRLSCEelehQHQQEADDWKQELARLQQLHRQ---ELERCQLDFRDRTlK 580
Cdd:TIGR02168 800 --------ALREALDELRAELTLLNEEAANLRERLE----SLERRIAATERRLEDLEEQIEElseDIESLAAEIEELE-E 866
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 581 LEEELHKQRDRALAVLTEKDLELEQLRSvalasglpgrrspvggGGPGDPADTSSSDSLTQALQlaaaneptfflyaEQL 660
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRS----------------ELEELSEELRELESKRSELR-------------REL 917
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22208850 661 ARKEVEITSLRKQKHRLEVEVHQLQDRLLEEGERHREEVAALQSHIEKNIRDQSREGANLE 721
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
155-390 |
1.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 155 DKRLHQLKTQLATLTSSLATVTQEKSRMEASYladkkkmkQDLEDASNKAEEERARLEGELKGLQEQIAETKARLitqqh 234
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL--------EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 235 DRAQEQsdhalmLRELQKLLQEERTQRQDLELRLE-ETREALAGRAYAAEQMEGFEL----QTKQLTREVEELKSELQAI 309
Cdd:COG3883 82 EERREE------LGERARALYRSGGSVSYLDVLLGsESFSDFLDRLSALSKIADADAdlleELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 310 RDEknqpdprLQELQEEAARLKSHFQAQLQQemrKTALAeDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQL 389
Cdd:COG3883 156 LAE-------LEALKAELEAAKAELEAQQAE---QEALL-AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
.
gi 22208850 390 A 390
Cdd:COG3883 225 A 225
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
191-541 |
1.32e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 191 KKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKarlitQQHDRAQEQsdhalmLRELQKLLQEERTQRQDLELRLEE 270
Cdd:pfam01576 369 KRNKANLEKAKQALESENAELQAELRTLQQAKQDSE-----HKRKKLEGQ------LQELQARLSESERQRAELAEKLSK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 271 TREALAGRAYAAEQMEGfelQTKQLTREVEELKSELQAIrdeknqpdprlQELQEEAARLKSHFQAQLQQemrktaLAED 350
Cdd:pfam01576 438 LQSELESVSSLLNEAEG---KNIKLSKDVSSLESQLQDT-----------QELLQEETRQKLNLSTRLRQ------LEDE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 351 Q--LRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKE--RILQLDLENKTLALAASSRSpldshgeess 426
Cdd:pfam01576 498 RnsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEgkKRLQRELEALTQQLEEKAAA---------- 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 427 ldvnvlKDKMEKLKRLLQVAARKSQVTLDVEKlcdlEIMPSSEAADGEKATALyyqQELKQLKEEFERYKMRAQVVLKSK 506
Cdd:pfam01576 568 ------YDKLEKTKNRLQQELDDLLVDLDHQR----QLVSNLEKKQKKFDQML---AEEKAISARYAEERDRAEAEAREK 634
|
330 340 350
....*....|....*....|....*....|....*
gi 22208850 507 NTKDGNLGKELEAAQEQLAELKEKYISLRLSCEEL 541
Cdd:pfam01576 635 ETRALSLARALEEALEAKEELERTNKQLRAEMEDL 669
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
221-708 |
1.77e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 221 QIAETKARLITQQHDRAQEQSDHALMLRELQK-------LLQEERTQRQDLELRLE--ETREALAGRAYAaEQMEGFELQ 291
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKkasalkrQLDRESDRNQELQKRIRllEKREAEAEEALR-EQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 292 TKQLT---REVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHFQAQLQQEMRktalaedqLRQQSQVEEQRvaalen 368
Cdd:pfam05557 82 KKYLEalnKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEE--------LQERLDLLKAK------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 369 qISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLdVNVLKDKMEKLKRLlqvaar 448
Cdd:pfam05557 148 -ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKE-LERLREHNKHLNEN------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 449 KSQVTLDVEKLCDLEIMPSSEaaDGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDgNLGKELEAAQEQLAELK 528
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLERE--EKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPE-DLSRRIEQLQQREIVLK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 529 EKYISLRLSCEELEHQHQQEADDWKQELARLQQLhRQELERcQLDFRDRTLKLEEELHKQRDRALAVLTEKDLELEQlrS 608
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDL-NKKLKR-HKALVRRLQRRVLLLTKERDGYRAILESYDKELTM--S 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 609 VALASGLPGRRSPVGGGGPGDPADTSSSDSLTQAlqlaaanEPTFFLYAEQLARKEVEITSLRKQKHRLEV--------E 680
Cdd:pfam05557 373 NYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVA-------EEELGGYKQQAQTLERELQALRQQESLADPsyskeevdS 445
|
490 500
....*....|....*....|....*...
gi 22208850 681 VHQLQDRLLEEGERHREEVAALQSHIEK 708
Cdd:pfam05557 446 LRRKLETLELERQRLREQKNELEMELER 473
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
184-411 |
1.78e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 184 ASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLI-TQQHDRAQEqsDHALMLRELQKLLQEERTQRQ 262
Cdd:PRK10929 19 AATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLErAKQYQQVID--NFPKLSAELRQQLNNERDEPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 263 DLELRLeeTREALagrayaAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQpdprLQELQEEAARLKSHFQAQLQ-QE 341
Cdd:PRK10929 97 SVPPNM--STDAL------EQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQ----LPQQQTEARRQLNEIERRLQtLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 342 MRKTALAEDQL--------RQQSQVEEQRVAALE-NQISEVSEL-LGTYEKAKQKDQLAIQKLKERILQLDLENKTLALA 411
Cdd:PRK10929 165 TPNTPLAQAQLtalqaesaALKALVDELELAQLSaNNRQELARLrSELAKKRSQQLDAYLQALRNQLNSQRQREAERALE 244
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
209-569 |
2.08e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 209 ARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLEL---RLEETREALAgrayAAEQM 285
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAasdHLNLVQTALR----QQEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 286 EGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSHF----QAQLQQEMR-------KTALAE----- 349
Cdd:PRK04863 351 ERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyqQALDVQQTRaiqyqqaVQALERakqlc 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 350 --------------DQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQkdqlAIQKLKERILQLDLEN--KTLALAAS 413
Cdd:PRK04863 431 glpdltadnaedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQ----LVRKIAGEVSRSEAWDvaRELLRRLR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 414 SRSPLDSHGEESSLDVNVLKDKMEK---LKRLLQVAARKSQVTLDVEKLCD---------LEIMPSSEAADGEKATALyy 481
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEqlqeelearLESLSESVSEARERRMAL-- 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 482 QQELKQLKEEFERYKMRAQVVLKSK---NTKDGNLGKELEAAQ---EQLAELKEKYISLRLSCEELEHQHQQeaddWKQE 555
Cdd:PRK04863 585 RQQLEQLQARIQRLAARAPAWLAAQdalARLREQSGEEFEDSQdvtEYMQQLLERERELTVERDELAARKQA----LDEE 660
|
410
....*....|....
gi 22208850 556 LARLQQLHRQELER 569
Cdd:PRK04863 661 IERLSQPGGSEDPR 674
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
250-726 |
2.30e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 250 LQKLLQEERTQRQDLELRLEETREAlagrayaaeqmegFELQTKQLTREVEELKSELQAIRDEKN-QPDPRLQELQEEaA 328
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNEL-------------HEKQKFYLRQSVIDLQTKLQEMQMERDaMADIRRRESQSQ-E 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 329 RLKSHFQAQLQQEMRKTALAEDQLRQQS-QVEEQRVAAL--ENQISEVSELLGTYEKAKQKdqlaiqKLKERILQLDLEN 405
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNtQIEQLRKMMLshEGVLQEIRSILVDFEEASGK------KIYEHDSMSTMHF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 406 KTLALAASS-RSPLDSHGEESSLDVNVLKDKMEKLKRLLQ--VAARKSQVTLDVEKLC---DLEIMPSSEAADGEKATAL 479
Cdd:pfam15921 216 RSLGSAISKiLRELDTEISYLKGRIFPVEDQLEALKSESQnkIELLLQQHQDRIEQLIsehEVEITGLTEKASSARSQAN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 480 YYQQELKQLKEEferykmraqvvLKSKNTKDGNLGKELEAAQEQL-AELKEKYISLRLSCEELEHQ----------HQQE 548
Cdd:pfam15921 296 SIQSQLEIIQEQ-----------ARNQNSMYMRQLSDLESTVSQLrSELREAKRMYEDKIEELEKQlvlanselteARTE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 549 ADDWKQELARLQQLHRQELerCQLDFRDRTLKLEEELHKQ---RDRALAV--------LTEKDLELEQLRSV--ALASGL 615
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLL--ADLHKREKELSLEKEQNKRlwdRDTGNSItidhlrreLDDRNMEVQRLEALlkAMKSEC 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 616 PGRrspvggGGPGDPADTSSSDSLTQALQLAAANEPTfflyaEQLARKEVEitSLRKQKHRLEVEVHQLQDRL--LEEGE 693
Cdd:pfam15921 443 QGQ------MERQMAAIQGKNESLEKVSSLTAQLEST-----KEMLRKVVE--ELTAKKMTLESSERTVSDLTasLQEKE 509
|
490 500 510
....*....|....*....|....*....|....*..
gi 22208850 694 RHRE----EVAALQSHIEKNIRDQSREGANLEYLKNI 726
Cdd:pfam15921 510 RAIEatnaEITKLRSRVDLKLQELQHLKNEGDHLRNV 546
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
158-241 |
2.53e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 158 LHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKmKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRA 237
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAEAQQQE-LVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
....
gi 22208850 238 QEQS 241
Cdd:PRK11448 223 DQAA 226
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
158-588 |
3.64e-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: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 158 LHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERARlEGELKGLQEQIAETKARLITQQHDRA 237
Cdd:TIGR00618 405 LQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE-KIHLQESAQSLKEREQQLQTKEQIHL 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 238 QEQSDHALMLRELQkLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDeknqpd 317
Cdd:TIGR00618 484 QETRKKAVVLARLL-ELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK------ 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 318 pRLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKER 397
Cdd:TIGR00618 557 -QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 398 ILQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQVAA--RKSQVTLDVEKLCDLEIMPSSEAADGEK 475
Cdd:TIGR00618 636 QCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMqsEKEQLTYWKEMLAQCQTLLRELETHIEE 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 476 ATALYYQQE--------------------LKQLKEEFeRYKMRAQVVLKSKN----TKDGNLGKELEAAQEQLAELKEKY 531
Cdd:TIGR00618 716 YDREFNEIEnassslgsdlaaredalnqsLKELMHQA-RTVLKARTEAHFNNneevTAALQTGAELSHLAAEIQFFNRLR 794
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 22208850 532 ISLRLSCEELEHQHQQEADDWKQELARLQQLHRQELERCQLDFRDRTLKLEEELHKQ 588
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
150-498 |
4.42e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 150 AGGEVDKRLHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARL 229
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 230 ITQQHDRAQE-QSDHALMLRELQKLLQEERTQRQDLELRLEETREAL---AGRAYAAEQMEGFELQTKQLTREVEELKSE 305
Cdd:pfam02463 243 QELLRDEQEEiESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKllaKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 306 LQAIRDEKNQpdprLQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQ 385
Cdd:pfam02463 323 KKKAEKELKK----EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 386 KDQLAIQKLKERILQLDLENKTLALAASSRSPLDShGEESSLDVNVLKDKMEKLKRLLQvaarksqvTLDVEKLCDLEIM 465
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE-EEEESIELKQGKLTEEKEELEKQ--------ELKLLKDELELKK 469
|
330 340 350
....*....|....*....|....*....|...
gi 22208850 466 PSSEAADGEKATALYYQQELKQLKEEFERYKMR 498
Cdd:pfam02463 470 SEDLLKETQLVKLQEQLELLLSRQKLEERSQKE 502
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
281-413 |
5.50e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 39.83 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 281 AAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPrlqELQEEAAR-LKSHFQAQLQQEMRKTALAEDQLRQQS-QV 358
Cdd:COG3524 175 REDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDP---EATAEALLqLIATLEGQLAELEAELAALRSYLSPNSpQV 251
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 22208850 359 E--EQRVAALENQISEVSELLGTyekAKQKDQLAIQKLKERILQLDLENKTLALAAS 413
Cdd:COG3524 252 RqlRRRIAALEKQIAAERARLTG---ASGGDSLASLLAEYERLELEREFAEKAYTSA 305
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
299-401 |
5.70e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 299 VEELKSELQAIRDEKnqpdprLQELQEEAARLKSHFQ-------AQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQIS 371
Cdd:PRK12704 44 LEEAKKEAEAIKKEA------LLEAKEEIHKLRNEFEkelrerrNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
|
90 100 110
....*....|....*....|....*....|
gi 22208850 372 EVSELLGTYEKAKQKDQLAIQKLKERILQL 401
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
373-688 |
6.58e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 373 VSELLGTYEKAKQKDQLAiQKLKEriLQLDLENKTLALAASSRSPLDSHGEESSLDVNVLKDKMEKLKRLLQvaarKSQV 452
Cdd:TIGR02168 195 LNELERQLKSLERQAEKA-ERYKE--LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQ----ELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 453 TLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEEFERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYI 532
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 533 SLRLSCEELEHQHQQEADDWkQELARLQQLHRQELERCQLDFRDRTLKlEEELHKQRDRALAVLTEKDLELEQLRSVALA 612
Cdd:TIGR02168 348 ELKEELESLEAELEELEAEL-EELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22208850 613 sglpgrRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTfflyAEQLARKEVEITSLRKQKHRLEVEVHQLQDRL 688
Cdd:TIGR02168 426 ------LLKKLEEAELKELQAELEELEEELEELQEELERL----EEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
282-404 |
6.79e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.23 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 282 AEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQE-----------EAARLKSHFQAQLQQEMRKTALAEd 350
Cdd:smart00787 150 DENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQledeledcdptELDRAKEKLKKLLQEIMIKVKKLE- 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 22208850 351 QLRQQSQVEEQRVAALENQISEV----SELLGTYEKAKQKDQLAIQKLKERILQLDLE 404
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSELnteiAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSL 286
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
193-333 |
7.53e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 39.36 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 193 MKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQQHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETR 272
Cdd:pfam09787 73 LRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLR 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22208850 273 EALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQEEAARLKSH 333
Cdd:pfam09787 153 NQLTSKSQSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGE 213
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
192-325 |
7.58e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 39.74 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 192 KMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLitqqhDRAQEQSDhalmlRELQKLLQEERTQRQDLELRLEET 271
Cdd:COG1193 518 KLIEELERERRELEEEREEAERLREELEKLREELEEKL-----EELEEEKE-----EILEKAREEAEEILREARKEAEEL 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 22208850 272 REALagrayaaEQMEGFELQTKQLTREVEELKSELQAIRDEKNQPDPRLQELQE 325
Cdd:COG1193 588 IREL-------REAQAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPPEE 634
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
515-608 |
8.76e-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: 39.55 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 515 KELEAAQEQLAELKEKYISLRlscEELEHQHQQEAD---------DWkqeLARLQQLHRQE--LERCQLDFRDRTLKLEE 583
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEMA---RELEELSARESDleqdyqaasDH---LNLVQTALRQQekIERYQEDLEELTERLEE 365
|
90 100 110
....*....|....*....|....*....|.
gi 22208850 584 ------ELHKQRDRALAVLTEKDLELEQLRS 608
Cdd:COG3096 366 qeevveEAAEQLAEAEARLEAAEEEVDSLKS 396
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
298-687 |
8.92e-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: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 298 EVEELKSELQAIRDEKNQPDPRLQELQEEAARLKshfqaQLQQEMRKTALAEDQLRQQsqveeqrvaALENQISEVSELL 377
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAERYQ-----ALLKEKREYEGYELLKEKE---------ALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 378 GTYEKAKQKDQLAIQKLKERILQLDLENKTLALAassrspLDSHGEESSLDVnvlKDKMEKLKrlLQVAARKSQVTLDVE 457
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKK------IKDLGEEEQLRV---KEKIGELE--AEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 458 KLCDLEimpsseaadgekatalyyqQELKQLKEEFERYKMRAQvvlkSKNTKDGNLGKELEAAQEQLAELKEKYISLRLS 537
Cdd:TIGR02169 316 ELEDAE-------------------ERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 538 CEELEHQHQQEADDWKQELARLQQLHRQElercqldfrdrtlkleEELHKQRDRALAVLTEKDLELEQLRSvALASGLPG 617
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREI----------------NELKRELDRLQEELQRLSEELADLNA-AIAGIEAK 435
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 618 RRSPVGGGGPGDPADTSSSDSLTQALQLAAANEPTFFLYAEQLARKEVEITSLRKQKHRLEVEVHQLQDR 687
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
177-544 |
8.97e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 177 QEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAET-----KARLITQQHDRAQEQSDHALMLRELQ 251
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 252 kllqEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQltREVEELKSELQAIRDEKNQPDPRLQELQEEAARLK 331
Cdd:PTZ00121 1617 ----EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 332 SHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQLAIQKLKERILQLDLENKTLALA 411
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 412 ASSRSPLDSHGEEsSLDVNVLKDKMEkLKRLLQVAARKSQVTLDVEKLCDLEIMPSSEAADGEKATALYYQQELKQLKEE 491
Cdd:PTZ00121 1771 EEIRKEKEAVIEE-ELDEEDEKRRME-VDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADA 1848
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 22208850 492 FERYKMRAQVVLKSKNTKDGNLGKELEAAQEQLAELKEKYISLRLSCEELEHQ 544
Cdd:PTZ00121 1849 FEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
153-527 |
9.52e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 153 EVDKRLHQLKTQLATLTSSLATVTQEKSRMEASYLADKKKMKQDLEDASNKAEEERARLEGELKGLQEQIAETKARLITQ 232
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 233 QHDRAQEQSDHALMLRELQKLLQEERTQRQDLELRLEETREALAGRAYAAEQMEGFELQTKQLTREVEELKSELQAIRDE 312
Cdd:COG4717 240 ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 313 KNQPDPR----LQELQEEAARLKSHFQAQLQQEMRKTALAEDQLRQQSQVEEQRVAALENQISEVSELLGTYEKAKQKDQ 388
Cdd:COG4717 320 ELEELLAalglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22208850 389 LAiQKLKERILQLDLENKTLALAASSRSPLDSHGEESSLDVNvLKDKMEKLKRLLQVAARKSQVTLDVEKlcdleimpss 468
Cdd:COG4717 400 LK-EELEELEEQLEELLGELEELLEALDEEELEEELEELEEE-LEELEEELEELREELAELEAELEQLEE---------- 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22208850 469 eaaDGEKATALYYQQELKQLKEEFERYKMRAQVVLK-----SKNTKDGNLGKELEAAQEQLAEL 527
Cdd:COG4717 468 ---DGELAELLQELEELKAELRELAEEWAALKLALElleeaREEYREERLPPVLERASEYFSRL 528
|
|
| |
