|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
45-401 |
2.23e-95 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 295.29 E-value: 2.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 45 QEKEELRELNDRLAHYIDRVRALELENDRLLLKISEKEEVTTREVSGIKALYESELADARRVLDETARERARLQIEIGKL 124
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 125 RAELDEVNKSAKKRegeltvaqgrvkdleslfhrsevelaaaLSDKRGLESDVAELRaqlakaedghavakKQLEKETLM 204
Cdd:pfam00038 81 RLAAEDFRQKYEDE----------------------------LNLRTSAENDLVGLR--------------KDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 205 RVDLENRCQSLQEELDFRKSVFEE--EVRETRRRHERRLVEVDSSRQQEydfkMAQALEELRSQHDEQVRLYKLELEQTY 282
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEevRELQAQVSDTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 283 QAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERDKFRKMLDAKEQEMTE 362
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 388240801 363 MRDVMQQQLAEYQELLDVKLALDMEINAYRKLLEGEEER 401
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
468-576 |
1.95e-21 |
|
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 89.40 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 468 ASASGSVSIEEIDLEG-----KFVQLKNNSDKDQSLGNWRIKRQVLEgeeiAYKFTPKYILRAGQMVTVWAAG----AGV 538
Cdd:pfam00932 1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWTGSgtnsATA 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 388240801 539 AHSPPSTLVWKGQSSWgtgesfrTVLVNADGEEVAMRT 576
Cdd:pfam00932 77 GYWGPSNAVWNNGGDA-------VALYDANGELVDSVG 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
44-413 |
9.47e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 9.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 44 LQEKEELRELNDRLAHYidrvRALELENDRLLLKISEKEEVttrevsgiKALYESELADARRVLDETARERARLQIEIGK 123
Cdd:COG1196 218 LKEELKELEAELLLLKL----RELEAELEELEAELEELEAE--------LEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 124 LRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQLEKETL 203
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 204 MRVDLENRCQSLQEELD-FRKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEELRSQHDEQVRLYKLELEQty 282
Cdd:COG1196 366 ALLEAEAELAEAEEELEeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA-- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 283 QAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERDKFRKMLDAKEQEM-T 361
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlA 523
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 388240801 362 EMRDVMQQQLAEYQELLDVKLALDMEINAYRKLLEGEEERLKLSPSPSSRVT 413
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-383 |
2.38e-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: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 47 KEELRELndRLAHYIDRVRALELENDRLLLKISEKEEVTTREVSGIKALYESeladarrvLDETARERARLQIEIGKLRA 126
Cdd:TIGR02168 219 KAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK--------LEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 127 ELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQLEKETLMRV 206
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 207 DLENRCQSLQEELDFRKSvfeeevretrrrherrlvevdssrqqeydfKMAQALEELRSQHDEQVRLyKLELEQTYQAKl 286
Cdd:TIGR02168 369 ELESRLEELEEQLETLRS------------------------------KVAQLELQIASLNNEIERL-EARLERLEDRR- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 287 dsAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQ---ASAAEDRIRELEEAMAGERDKFRKMLDAKEQEMTEM 363
Cdd:TIGR02168 417 --ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEElerLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
330 340
....*....|....*....|
gi 388240801 364 RDVMQQQLAEYQELLDVKLA 383
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALLKN 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
129-402 |
4.19e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 129 DEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQLEKETLMRVDL 208
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 209 ENRCQSLQEEL-DFRKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEELRSQHDE---QVRLYKLEL------ 278
Cdd:TIGR02168 746 EERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraELTLLNEEAanlrer 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 279 EQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERDKfrkmLDAKEQ 358
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE----LEELSE 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 388240801 359 EMTEMRDVMQQQLAEYQELLDVKLALDMEINAYRKLLEGEEERL 402
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-377 |
1.81e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 37 SPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLKISEKEEVT----------TREVSGIKALYESELADARRV 106
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleelSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 107 LDETAR---ERARLQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLF--------------HRSEVELAAALSD 169
Cdd:TIGR02168 746 EERIAQlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalrealdelraelTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 170 KRGLESDVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELDfrksvfeeevretrrrherrlvevdssrq 249
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE----------------------------- 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 250 qeydfkmaqALEELRSQHDEQVRLYKLELEQTyQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQAS 329
Cdd:TIGR02168 877 ---------ALLNERASLEEALALLRSELEEL-SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 388240801 330 aaEDRIRELEEAMA------GERDKFRKMLDAKEQEMTEMRDVMQQQLAEYQEL 377
Cdd:TIGR02168 947 --EEYSLTLEEAEAlenkieDDEEEARRRLKRLENKIKELGPVNLAAIEEYEEL 998
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-403 |
5.17e-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: 56.23 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 88 EVSGIkALYESELADARRVLDETARERARLQIEIGKLRAELDEVNK-----------SAKKREGELTVAQGRVKDLESLF 156
Cdd:TIGR02169 161 EIAGV-AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRerekaeryqalLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 157 HRSEVELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQLEKETlmrvdlENRCQSLQEELdfrksvfeeEVRETRRR 236
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKI---------GELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 237 HERRLVEVDSSRQQEYDFKMAQALEEL-----------RSQHDEQVRLYKLELE-QTYQAKLDSAKLSSDQNDKAASAAR 304
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIdkllaeieeleREIEEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 305 EELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERDKFRKMLDAK---EQEMTEMRDVMQQQLAEYQELLDVK 381
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADL 464
|
330 340
....*....|....*....|..
gi 388240801 382 LALDMEINAYRKLLEGEEERLK 403
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELS 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-404 |
2.86e-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: 53.92 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 84 VTTREVSGIKALYESELADARRVLDETARERARLQIEIGKLRAELDEVNKSAKKREGELTVAQ--------------GRV 149
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeieqleqeeeklkERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 150 KDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAE----------DGHAVAKKQLEKETL--MRVDLENRCQSLQE 217
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEealndlearlSHSRIPEIQAELSKLeeEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 218 ELDFR--KSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQaLEELRSQHDE-QVRLYKLEleqtyqAKLDSAKLSSD 294
Cdd:TIGR02169 820 KLNRLtlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK-KEELEEELEElEAALRDLE------SRLGDLKKERD 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 295 QNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGER---------DKFRKMLDAKEQEMTEMRD 365
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELQRVEEEIRALEP 972
|
330 340 350
....*....|....*....|....*....|....*....
gi 388240801 366 VMQQQLAEYQElldVKLALDmEINAYRKLLEGEEERLKL 404
Cdd:TIGR02169 973 VNMLAIQEYEE---VLKRLD-ELKEKRAKLEEERKAILE 1007
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
104-402 |
4.96e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.30 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 104 RRVLDETARERARLQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQ 183
Cdd:pfam19220 33 IEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 184 LAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELD-FRKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMA----- 257
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEENKALREEAQaAEKALQRAEGELATARERLALLEQENRRLQALSEEQAaelae 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 258 -----QALEELRSQHDEQVRLYKLEL--EQTYQAKLDSaklssdQNDKAASAAREELKEARMRLESLSYQLSGLQKQASA 330
Cdd:pfam19220 193 ltrrlAELETQLDATRARLRALEGQLaaEQAERERAEA------QLEEAVEAHRAERASLRMKLEALTARAAATEQLLAE 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388240801 331 AEDRIRELEEAMAGERDKFR---KMLDAKEQEMTEMRDVMQQQLAEYQELLDVKLALDMEINAYRKLLEGEEERL 402
Cdd:pfam19220 267 ARNQLRDRDEAIRAAERRLKeasIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAAL 341
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-367 |
6.16e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 47 KEELRELNDRLAHYIDRVRALELENDRLLLKISEKEEVTTR------EVSGIKALYESELADARRVLDETARERARLQ-- 118
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQlskeltELEAEIEELEERLEEAEEELAEAEAEIEELEaq 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 119 -----IEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAEDGHAV 193
Cdd:TIGR02168 791 ieqlkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 194 AKKQLEKETLMRVDLENRCQSLQEELD-----FRKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEELRSQH- 267
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEelseeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYs 950
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 268 ---DEQVRLYKLELEQTYQAKldsAKLSSDQNDKAA-----SAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELE 339
Cdd:TIGR02168 951 ltlEEAEALENKIEDDEEEAR---RRLKRLENKIKElgpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
330 340
....*....|....*....|....*...
gi 388240801 340 EAMageRDKFRKMLDAKEQEMTEMRDVM 367
Cdd:TIGR02168 1028 REA---RERFKDTFDQVNENFQRVFPKL 1052
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
36-396 |
1.35e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 36 LSPTRLSRLQEKEELRELNDRLAH---YIDRVRALELENDRLLLKISEKEEVTTREVSGIKALYESELADARRVLDETAR 112
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 113 ERARLQIEIGKLRAELDEVNKSAKKREGELTVAQ--GRVKDLESLFhRSEVELAAALSDKRGLES------DVAELRAQL 184
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLL-LIAAALLALLGLGGSLLSliltiaGVLFLVLGL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 185 AKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEEldfrksvfeeeVRETRRRHERRLVEVDSSRQQEYDFKMAQALEELR 264
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEE-----------ELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 265 SQHDEQVRLYKLELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAA---------EDRI 335
Cdd:COG4717 355 EAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlealdeeelEEEL 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 388240801 336 RELEEAMAGERDKFRKMLDAK---EQEMTEMR--DVMQQQLAEYQELLDVKLALDMEINAYRKLLE 396
Cdd:COG4717 435 EELEEELEELEEELEELREELaelEAELEQLEedGELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
107-348 |
1.59e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 107 LDETARERARLQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAK 186
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 187 aedghavakkqlEKETLMRVDLENRCQSLQEELDFrksVFEEEVRETRRRHERRLVEVDSSRQQEYDfKMAQALEELRSQ 266
Cdd:COG4942 102 ------------QKEELAELLRALYRLGRQPPLAL---LLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 267 HDEQvrlykLELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGER 346
Cdd:COG4942 166 RAEL-----EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 388240801 347 DK 348
Cdd:COG4942 241 ER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
49-403 |
1.70e-05 |
|
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: 48.30 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 49 ELRELNDRLAHYIDRVRALELENDRLLLKISEKeevTTREVSGIkalyESELADARRVLD-ETARERARLQIEIGKLRAE 127
Cdd:pfam12128 355 ELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ---NNRDIAGI----KDKLAKIREARDrQLAVAEDDLQALESELREQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 128 LDEVNKSAKKREGELTVAQGRVKDL-----------------ESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAEDG 190
Cdd:pfam12128 428 LEAGKLEFNEEEYRLKSRLGELKLRlnqatatpelllqlenfDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 191 HAVAKKQLEKetlmrvdLENRCQSLQEEL----------------DFRKSVFEEEVRETRRRHERRLVEVDSSRQQEY-- 252
Cdd:pfam12128 508 LRQASRRLEE-------RQSALDELELQLfpqagtllhflrkeapDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELnl 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 253 -----DFKMAQALEELrsQHDEQVRLYKLELEQTYQAKLDSAKLSSDQ----------NDKAASAAREELKEARMRLESL 317
Cdd:pfam12128 581 ygvklDLKRIDVPEWA--ASEEELRERLDKAEEALQSAREKQAAAEEQlvqangelekASREETFARTALKNARLDLRRL 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 318 SYQLSGLQKQAS--------AAEDRIRELEEAMAGERDKFRKMLDAKEQEMTEMRDVMQQQLAEYQELLDVKLA-LDMEI 388
Cdd:pfam12128 659 FDEKQSEKDKKNkalaerkdSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLAlLKAAI 738
|
410
....*....|....*
gi 388240801 389 NAYRKLLEGEEERLK 403
Cdd:pfam12128 739 AARRSGAKAELKALE 753
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-379 |
2.45e-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: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 43 RLQEKE-ELRELNDRLAHYIDRVRALELENDRL---LLKISEKEEVTTREVSGIKALYE-SELADARRVLDETARERARL 117
Cdd:COG4913 611 KLAALEaELAELEEELAEAEERLEALEAELDALqerREALQRLAEYSWDEIDVASAEREiAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 118 QIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKR-GLESDVAELRAQLAKAedghavakk 196
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAALGD--------- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 197 qlEKETLMRVDLENRCQSLQEELDfrksvfeeevretrrRHERRLVEVDSSRQQEYDFKMAQALEELRSQHDEQVRLYKL 276
Cdd:COG4913 762 --AVERELRENLEERIDALRARLN---------------RAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRL 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 277 E---LEQtYQAKLDSAKLSSDQNDKA--ASAAREELKEARMRLESLSYQLSGLQKQasaAEDRIR-ELEEAMAGERDKFR 350
Cdd:COG4913 825 EedgLPE-YEERFKELLNENSIEFVAdlLSKLRRAIREIKERIDPLNDSLKRIPFG---PGRYLRlEARPRPDPEVREFR 900
|
330 340 350
....*....|....*....|....*....|
gi 388240801 351 KML-DAKEQEMTEMRDVMQQQLAEYQELLD 379
Cdd:COG4913 901 QELrAVTSGASLFDEELSEARFAALKRLIE 930
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
47-382 |
3.09e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 47 KEELRELNDRLAHYIDRVRALELENDRLLLKIS--EKEEVTTREV------------SGIKALYESelADARRVLDETAR 112
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARREelEDRDEELRDRleecrvaaqahnEEAESLRED--ADDLEERAEELR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 113 ERAR-LQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAEDGH 191
Cdd:PRK02224 363 EEAAeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 192 AVAKKQLEK----------ETLMRVDLENRCQSLQEELDFRKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALE 261
Cdd:PRK02224 443 EEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLE 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 262 ELRSQHD----------EQVRLYKLELEQTYQAKLDSAKLSSDQNDKAASAA------REELKEARMRLESLSYQLSGLQ 325
Cdd:PRK02224 523 ELIAERRetieekreraEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVaelnskLAELKERIESLERIRTLLAAIA 602
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388240801 326 KQASAAEdRIRELEEAMAGERDKFRKMLDAKEQEMTEMRDVMQ-----------QQLAEYQELLDVKL 382
Cdd:PRK02224 603 DAEDEIE-RLREKREALAELNDERRERLAEKRERKRELEAEFDearieearedkERAEEYLEQVEEKL 669
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
103-414 |
1.97e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 103 ARRVLDETARER-ARLQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELaaalsDKRGLESDVAELR 181
Cdd:COG4913 600 SRYVLGFDNRAKlAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 182 AQLAKAEDGH---AVAKKQLEKETLMRVDLENRCQSLQEELDfrksvfeeevretrrrherrlvEVDSSRQQeydfkMAQ 258
Cdd:COG4913 675 AELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIG----------------------RLEKELEQ-----AEE 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 259 ALEELRSQHDEQVRLYKLELEQTYQAKLDSAkLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAA-EDRIRE 337
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAA-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETAD 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 338 LEEAMAGERDkFRKMLDA-KEQEMTEMRDVMQQQLAE--YQELLDVKLALDMEINAYRKLLE-----------GEEERLK 403
Cdd:COG4913 807 LDADLESLPE-YLALLDRlEEDGLPEYEERFKELLNEnsIEFVADLLSKLRRAIREIKERIDplndslkripfGPGRYLR 885
|
330
....*....|.
gi 388240801 404 LSPSPSSRVTV 414
Cdd:COG4913 886 LEARPRPDPEV 896
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-404 |
2.04e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 173 LESDVAELRAQLAKAEDGHAVAKKQLEKETLMRV----DLENRCQSLQEELDFRKSVFEEEVRETRRRHERrlVEVDSSR 248
Cdd:COG1196 198 LERQLEPLERQAEKAERYRELKEELKELEAELLLlklrELEAELEELEAELEELEAELEELEAELAELEAE--LEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 249 QQEYDFKMAQALEELRSQHDEQVRL-----YKLELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSG 323
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLeqdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 324 LQKQASAAEDRIRELEEAMAGERDKFRKMLDAKEQEMTEMRDVMQQQLAEYQELLDVKLALDMEINAYRKLLEGEEERLK 403
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
.
gi 388240801 404 L 404
Cdd:COG1196 436 E 436
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
64-402 |
2.59e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 64 VRALELENDRLLLKISEKEEVTTREvSGIKALYESelADARRVLDETAReraRLQIEIGKLRAELDEVNKSAKKREGELT 143
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAE-SDLEQDYQA--ASDHLNLVQTAL---RQQEKIERYQADLEELEERLEEQNEVVE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 144 VAQGRVKDLESLFHRSEVE---LAAALSD-KRGLesDVAELRA----------------------QLAKAEDGHAVAKKQ 197
Cdd:PRK04863 373 EADEQQEENEARAEAAEEEvdeLKSQLADyQQAL--DVQQTRAiqyqqavqalerakqlcglpdlTADNAEDWLEEFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 198 LEKETLMRVDLENRCQSLQEELDFRKSVFEEEVRETRRRHERRLVEVDSS--RQQEYDFKMAQALEELRSQHDEQVRlyK 275
Cdd:PRK04863 451 EQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVAREllRRLREQRHLAEQLQQLRMRLSELEQ--R 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 276 LELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERDKFRKMLDA 355
Cdd:PRK04863 529 LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAA 608
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 388240801 356 KE-----QEMTEMRDVMQQQLAEY-QELLDVKLALDME---INAYRKLLEGEEERL 402
Cdd:PRK04863 609 QDalarlREQSGEEFEDSQDVTEYmQQLLERERELTVErdeLAARKQALDEEIERL 664
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
46-200 |
2.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 46 EKEELRELNDRLAHYIDRVRALELENDRLLLKISEK----EEVTTREVSGIKALYES--ELADARRVLDETARERARLQI 119
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEE 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 120 EIGKLRAELDEVNKSAKKREGELtvaqgrvKDLESLFhrSEVELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQLE 199
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKEL-------EELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
.
gi 388240801 200 K 200
Cdd:PRK03918 698 K 698
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
44-443 |
4.97e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 44 LQEKEELRELNDRLAHYIDRVRALE-----LENDRLLLKISEKEEVTTREVSGIKALYESELADARRVLDETAR--ERAR 116
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADeakkkAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAK 1489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 117 LQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLE---SLFHRSEVELAAALSDKRGLESDVAElraQLAKAEDGHAV 193
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakkAEEAKKADEAKKAEEKKKADELKKAE---ELKKAEEKKKA 1566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 194 AKKQLEKEtlmrvdlenrcqslqeeldfRKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMaqalEELRSQHDEQVRL 273
Cdd:PTZ00121 1567 EEAKKAEE--------------------DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA----EEAKKAEEAKIKA 1622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 274 YKLELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQAS---AAEDRIRELEEAMAGERDKFR 350
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeakKAEEDEKKAAEALKKEAEEAK 1702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 351 KMLDAKEQEMTEMRDVMQQQLAEYQELLDVKLALDMEINAYRKLLEG---EEERLKLSPSPSSRVTVSRATSSSSGSLSA 427
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
410
....*....|....*.
gi 388240801 428 TGRLGRSKRKRLEVEE 443
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDK 1798
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
48-376 |
5.30e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 48 EELRELNDRLAHY----IDRVRALELENDRLLLKISEKEEVTTREvSGIKALYESELADARRVldetaRERARLQIEIGK 123
Cdd:COG3096 278 NERRELSERALELrrelFGARRQLAEEQYRLVEMARELEELSARE-SDLEQDYQAASDHLNLV-----QTALRQQEKIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 124 LRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVE---LAAALSD-KRGLesDVAELRA-QLAKAEDGHAVAKKQL 198
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEvdsLKSQLADyQQAL--DVQQTRAiQYQQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 199 EKETLMRVDLENRCQSLQEELDfrksvfeeevretrrrherrlvEVDSS-RQQEYDFKMAQAleeLRSQHDEQVRLYKle 277
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQ----------------------QATEEvLELEQKLSVADA---ARRQFEKAYELVC-- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 278 leqtyqaKLDSAKLSSDqndkAASAAREELKEARmRLESLSYQLSGLQKQASAAEDRIRELEEA----------MAGERD 347
Cdd:COG3096 483 -------KIAGEVERSQ----AWQTARELLRRYR-SQQALAQRLQQLRAQLAELEQRLRQQQNAerlleefcqrIGQQLD 550
|
330 340
....*....|....*....|....*....
gi 388240801 348 KfRKMLDAKEQEMTEMRDVMQQQLAEYQE 376
Cdd:COG3096 551 A-AEELEELLAELEAQLEELEEQAAEAVE 578
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-355 |
5.62e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 45 QEKEELRELNDRLAHYIDRVRALELENDRLLLKISEKEEVTTREVSGIKALYESelaDARRVLDETARERARLQIEIGKL 124
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 125 RAELDEVNKSAKKREGELTVAQGRVKDLESLF-----HRSEVELAAALS--DKRGLESDVAELRAQLAKAEDGHAVAKKQ 197
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRidlkeQIKSIEKEIENLngKKEELEEELEELEAALRDLESRLGDLKKE 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 198 LEKETLMRVDLENRCQSLQEELDFRKSVFEEEVRETrrrherrlvEVDSSRQQEYDFKMAQALEELRSQHD-EQVRLYKL 276
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL---------EALEEELSEIEDPKGEDEEIPEEELSlEDVQAELQ 961
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 388240801 277 ELEQTYQAkLDSAKLssdqndkaasAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAmagERDKFRKMLDA 355
Cdd:TIGR02169 962 RVEEEIRA-LEPVNM----------LAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK---KREVFMEAFEA 1026
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
43-367 |
7.22e-04 |
|
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: 42.65 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 43 RLQEKEELRELNDRLAHYIDRVRalELENDRLLLKISEKEEV------TTREVSGIKALYESELADARRVLDETARERAR 116
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLE--ELKLQELKLKEQAKKALeyyqlkEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 117 LQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKK 196
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 197 QLEKETLMRVDLENrcqslqeeldFRKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEELRSQHDEQVRLYKL 276
Cdd:pfam02463 329 ELKKEKEEIEELEK----------ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 277 ELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERDKFRKMLDAK 356
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330
....*....|.
gi 388240801 357 EQEMTEMRDVM 367
Cdd:pfam02463 479 LVKLQEQLELL 489
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
43-345 |
7.85e-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: 42.63 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 43 RLQEK-----EELRELNDRLAHYIDRVRALELENDRLllkiSEKEEVTTREVSGIKalyeSELADARRVLDE-------- 109
Cdd:COG3096 344 RQQEKieryqEDLEELTERLEEQEEVVEEAAEQLAEA----EARLEAAEEEVDSLK----SQLADYQQALDVqqtraiqy 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 110 ----TARERARLQIEIGKL------------RAELDEVNKSAKKREGELTVAQGRVKDLESLFH-----RSEVELAAALS 168
Cdd:COG3096 416 qqavQALEKARALCGLPDLtpenaedylaafRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiAGEVERSQAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 169 DKRGLESDVAELRAQLAKAED---GHAVAKKQLEKETLMRVDLENRCQSLQEELDFRKSVFEEEVRETRRRHErrlVEVD 245
Cdd:COG3096 496 TARELLRRYRSQQALAQRLQQlraQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE---LEEQ 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 246 SSRQQEYDFKMAQALEELRSQHDE-----------QVRLYKLElEQTYQAKLDSAKLSSD-----QNDKAASAAREELKE 309
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRARIKElaarapawlaaQDALERLR-EQSGEALADSQEVTAAmqqllEREREATVERDELAA 651
|
330 340 350
....*....|....*....|....*....|....*.
gi 388240801 310 ARMRLESlsyQLSGLQKQASAAEDRIRELEEAMAGE 345
Cdd:COG3096 652 RKQALES---QIERLSQPGGAEDPRLLALAERLGGV 684
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
44-400 |
9.92e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 44 LQEKEELRELNDRLAHYIDRVRALELENDrLLLKISEKE----EVTTREVSGIKALYESELADARRVLDETARERARLQI 119
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIAEELKGKEQELI-FLLQAREKEihdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 120 EIGKLRAELDEVNKSAKKREGELTVAQGRV-----------KDLESLfHRSEVELAAAL-SDKRGLESDVAELRAQLAKA 187
Cdd:pfam05483 493 HCDKLLLENKELTQEASDMTLELKKHQEDIinckkqeermlKQIENL-EEKEMNLRDELeSVREEFIQKGDEVKCKLDKS 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 188 EDGHAVAKKQLEKETLMRVDLENRCQSLQEELDFRKSVFEEEVRETRRRHERRLVEvdSSRQQEYDFKMAQALEELRSQH 267
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE--NKQLNAYEIKVNKLELELASAK 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 268 DEQVrlyklELEQTYQAKLDSAKLSSD----QNDKAASAAREEL---KEARMRLESLSYQLSGLQKQASAAEDRIRElee 340
Cdd:pfam05483 650 QKFE-----EIIDNYQKEIEDKKISEEklleEVEKAKAIADEAVklqKEIDKRCQHKIAEMVALMEKHKHQYDKIIE--- 721
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388240801 341 amagERDKFRKMLDAKEQEMTEMRDVMQQQLAEYQ-ELLDVKLALDMEINAYRKLLEGEEE 400
Cdd:pfam05483 722 ----ERDSELGLYKNKEQEQSSAKAALEIELSNIKaELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
79-446 |
9.99e-04 |
|
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: 42.27 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 79 SEKEEVTTREVSGIkALYESELADARRVLDETARERARLQIEIGKL-RAELDEVNKSAKKREGELTVAQGRVKDLESLFH 157
Cdd:pfam02463 151 KPERRLEIEEEAAG-SRLKRKKKEALKKLIEETENLAELIIDLEELkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 158 RSEVELAAALSDKRGLESDVAELRAQLAKAEDghavAKKQLEKETLMRVDLENRCQSLQEELdfRKSVFEEEVRETRRRH 237
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIE----KEEEKLAQVLKENKEEEKEKKLQEEE--LKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 238 ERRLVEVDSSRQQEYDFKMAQALE-----------ELRSQHDEQVRLYKLELEQTYQAKLDSAKLSSDQNDKAASAARE- 305
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEkelkkekeeieELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLEs 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 306 ELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERdkfRKMLDAKEQEMTEMRDVMQQQLAEYQELLDVKLALD 385
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEE---KKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388240801 386 MEINAYRKLLEGEEERLKLSPSPSSRVTVSRATSSSSGSLSATGRLGRSKRKRLEVEEPLG 446
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
43-381 |
1.01e-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: 42.41 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 43 RLQEKEELRELNDRLAHyidrvraLELENDRLLLKISEKE---EVTTREVSGIKALyeseLADARRVLDETARERARLQI 119
Cdd:pfam15921 529 KLQELQHLKNEGDHLRN-------VQTECEALKLQMAEKDkviEILRQQIENMTQL----VGQHGRTAGAMQVEKAQLEK 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 120 EIGKLRAELDEVNKSAKKREGELTVAQGRVKDLEslfhRSEVELAAALSDKRGLESDVAELRAQLakaedghavakkqLE 199
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLE----LEKVKLVNAGSERLRAVKDIKQERDQL-------------LN 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 200 KETLMRVDLenrcQSLQEELDFRKSVFEEEVRETRRRHERRLVEVDSSRQQeydfkMAQALEELRSQHDEQVRLYKLELE 279
Cdd:pfam15921 661 EVKTSRNEL----NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE-----LEQTRNTLKSMEGSDGHAMKVAMG 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 280 QTYQAKLDSAKLSSDQN-----DKAASAAREELKEARMRLESLSYQLSGL--QKQASAAE-DRIRELEEAMAGERDKFRK 351
Cdd:pfam15921 732 MQKQITAKRGQIDALQSkiqflEEAMTNANKEKHFLKEEKNKLSQELSTVatEKNKMAGElEVLRSQERRLKEKVANMEV 811
|
330 340 350
....*....|....*....|....*....|....*
gi 388240801 352 MLDAKEQEMTEMRDVMQQQLAE-----YQELLDVK 381
Cdd:pfam15921 812 ALDKASLQFAECQDIIQRQEQEsvrlkLQHTLDVK 846
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
97-381 |
1.50e-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: 41.70 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 97 ESELADARRVLDETARERARLQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESD 176
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTR 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 177 VAELraqlakaEDGHAVAKKQLEKETLMRVDLENRCQSLQEELdfrksvfeeevretrrrherrlveVDSSRQQEYDFKM 256
Cdd:pfam01576 491 LRQL-------EDERNSLQEQLEEEEEAKRNVERQLSTLQAQL------------------------SDMKKKLEEDAGT 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 257 AQALEELRsqhdeqvRLYKLELEQTYQaKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQK------QASA 330
Cdd:pfam01576 540 LEALEEGK-------KRLQRELEALTQ-QLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKkqkkfdQMLA 611
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388240801 331 AEDRI-------RELEEAMAGERDKFRKMLDAKEQEMTEMRD----VMQQQLAEYQELLDVK 381
Cdd:pfam01576 612 EEKAIsaryaeeRDRAEAEAREKETRALSLARALEEALEAKEelerTNKQLRAEMEDLVSSK 673
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
45-201 |
1.86e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 45 QEKEELRELNDRLAHYIDRVRALELENDRLLLKiSEKEEVTTRevsgiKALYESELADARRVLDETARERA--------R 116
Cdd:COG4913 269 ERLAELEYLRAALRLWFAQRRLELLEAELEELR-AELARLEAE-----LERLEARLDALREELDELEAQIRgnggdrleQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 117 LQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKK 196
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
....*
gi 388240801 197 QLEKE 201
Cdd:COG4913 423 ELEAE 427
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
42-356 |
1.98e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 42 SRLQEKEELRELNDRLAhyIDRVRALELENDRLLLKISEKEEVTTREVSGIKALYESELADARRvLDETARERARLQIEI 121
Cdd:pfam12128 216 SRLNRQQVEHWIRDIQA--IAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASR-QEERQETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 122 GKLRaelDEVNKSAKKREGELTVAQGRVKDLESlfhrsevELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQLEKE 201
Cdd:pfam12128 293 RTLD---DQWKEKRDELNGELSAADAAVAKDRS-------ELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEER 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 202 TLMrvdLENRCQSLQEELDFRKSVFEEEVRETRRRHERRLVEV--DSSRQQEYDFKMAQALE-ELRSQHDEQVRLYKLEL 278
Cdd:pfam12128 363 LKA---LTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIreARDRQLAVAEDDLQALEsELREQLEAGKLEFNEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 279 EQTYQA------KLDSAKLSSD------QNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAM---A 343
Cdd:pfam12128 440 YRLKSRlgelklRLNQATATPElllqleNFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLeerQ 519
|
330
....*....|...
gi 388240801 344 GERDKFRKMLDAK 356
Cdd:pfam12128 520 SALDELELQLFPQ 532
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
40-184 |
2.90e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 40 RLSRLQEK-EELRELND----RLAHYIDRVRALElendrlllkiSEKEEVTTREVSGIKALYESELADARRVLDETARER 114
Cdd:PRK02224 607 EIERLREKrEALAELNDerreRLAEKRERKRELE----------AEFDEARIEEAREDKERAEEYLEQVEEKLDELREER 676
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 115 ARLQIEIGKLRAELDEVNKSAKKREGeltvAQGRVKDLESLFhrSEVElaaalsdkrGLESDVAELRAQL 184
Cdd:PRK02224 677 DDLQAEIGAVENELEELEELRERREA----LENRVEALEALY--DEAE---------ELESMYGDLRAEL 731
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
277-370 |
2.95e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 277 ELEQTyQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEamagERDKFRKMLDAK 356
Cdd:COG4942 28 ELEQL-QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----EIAELRAELEAQ 102
|
90
....*....|....
gi 388240801 357 EQEMTEMRDVMQQQ 370
Cdd:COG4942 103 KEELAELLRALYRL 116
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
104-404 |
3.50e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 104 RRVLDETarERARlQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEvELAAALSDKRGLEsdvaelRAQ 183
Cdd:pfam17380 315 RRKLEEA--EKAR-QAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQE-EIAMEISRMRELE------RLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 184 LAKAEDGHAVaKKQLEKETLMRVDLENRCQSLQEELDFRKSVFEeevretrrrherrlvEVDSSRQQEydfkmAQALEEL 263
Cdd:pfam17380 385 MERQQKNERV-RQELEAARKVKILEEERQRKIQQQKVEMEQIRA---------------EQEEARQRE-----VRRLEEE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 264 RSQHDEQVRLYKLELEQTY------QAKLDSAKLSSDQNDKAASAARE--------ELKEARMRLESLSYQLSGLQKQAS 329
Cdd:pfam17380 444 RAREMERVRLEEQERQQQVerlrqqEEERKRKKLELEKEKRDRKRAEEqrrkilekELEERKQAMIEEERKRKLLEKEME 523
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388240801 330 AAEDRIRELEEAMAGERDKfrkmldAKEQEMTEMRDVMQQQLAEYQELLDVKlALDMEINAYRKLLEGEEERLKL 404
Cdd:pfam17380 524 ERQKAIYEEERRREAEEER------RKQQEMEERRRIQEQMRKATEERSRLE-AMEREREMMRQIVESEKARAEY 591
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
57-365 |
3.99e-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: 40.49 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 57 LAHYIDRVRALELENDRLLLKISEKEEVTTREVSGIKALYESELADARRVLDETARERARLQIEIGKLRAELDEVNKsak 136
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR--- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 137 kregeltVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAK-AEDGHAVAKK-QLEKETLMRV---DLENR 211
Cdd:pfam15921 339 -------MYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlLADLHKREKElSLEKEQNKRLwdrDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 212 --CQSLQEELDFRKsvfeeevretrrRHERRLVEVDSSRQQEYDFKMAQALEELRSQHDEqvrlykLELEQTYQAKLDSA 289
Cdd:pfam15921 412 itIDHLRRELDDRN------------MEVQRLEALLKAMKSECQGQMERQMAAIQGKNES------LEKVSSLTAQLEST 473
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 388240801 290 KlssdqndKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIreleEAMAGERDKFRKMLDAKEQEMTEMRD 365
Cdd:pfam15921 474 K-------EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI----EATNAEITKLRSRVDLKLQELQHLKN 538
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
299-412 |
5.06e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 299 AASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERDKFRKmLDAKEQEMTEMRDVMQQQL---AEYQ 375
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIklsEFYE 303
|
90 100 110
....*....|....*....|....*....|....*..
gi 388240801 376 ELLDVKLALDMEINAYRKLLEGEEERLKLSPSPSSRV 412
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
42-225 |
5.30e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 42 SRLQEKEELRELNDRLAHYIDRVRALELENDRLLLKISEKEEVTTREVSGIKALyESELADARRVLDETARERARLQIEI 121
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-EQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 122 GKLRAELDEVNKSAKKregeltvaQGRVKDLESLFHRSEVELAAALSD-----KRGLESDVAELRAQLAKAEDGHAVAKK 196
Cdd:COG4942 100 EAQKEELAELLRALYR--------LGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEA 171
|
170 180
....*....|....*....|....*....
gi 388240801 197 QLEKETLMRVDLENRCQSLQEELDFRKSV 225
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKL 200
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
40-383 |
6.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 40 RLSRLQEKEELRELND-RLAHYIDRVRALELENDRLLLKISEKEEVttREVSGIKALYESELADARRVLDETARERARLQ 118
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEaRMAHFARRQAAIKAEEARKADELKKAEEK--KKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 119 IEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEvELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQL 198
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE-EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 199 EKETLMRVDLENRCQSLQEELDFRKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAqalEELRSQHDEQVRLYKLEL 278
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA---EEAKKKAEEAKKADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 279 EQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERDKFRKMLDAKE- 357
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEl 1557
|
330 340
....*....|....*....|....*.
gi 388240801 358 QEMTEMRDVMQQQLAEYQELLDVKLA 383
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
99-343 |
8.33e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 99 ELADARRVLDETARERARLQieigklraELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKrgLESDVA 178
Cdd:COG4913 236 DLERAHEALEDAREQIELLE--------PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE--LRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 179 ELRAQLAKAEDGHAVAKKQLE--KETLMRVDLEnRCQSLQEELDfrksvfeeevretrrRHERRLVEVDSSRQQeydfkM 256
Cdd:COG4913 306 RLEAELERLEARLDALREELDelEAQIRGNGGD-RLEQLEREIE---------------RLERELEERERRRAR-----L 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 257 AQALEELRSQHDEQVRLYKlELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIR 336
Cdd:COG4913 365 EALLAALGLPLPASAEEFA-ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
....*..
gi 388240801 337 ELEEAMA 343
Cdd:COG4913 444 ALRDALA 450
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
98-340 |
9.60e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 98 SELADARRVLDETARERARLQIEIGKLRAELDEVnKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDV 177
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 178 AELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELDFRKSVFEEEVRETRRRHerrlvEVDSSRQQEYDFkma 257
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAED-----EIERLREKREAL--- 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240801 258 QALEELRSQHDEQVRLYKLELEqtyqAKLDSAKLSSDQNDKAAsaAREELKEARMRLESLSYQLSGLQKQASAAEDRIRE 337
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELE----AEFDEARIEEAREDKER--AEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
...
gi 388240801 338 LEE 340
Cdd:PRK02224 693 LEE 695
|
|
| |
