|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
42-398 |
2.33e-92 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 287.20 E-value: 2.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 42 QEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLYESELADARRVLDETARERARLQIEIGKV 121
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 122 QAELEEARKSakkregeltvaqgrvkdleslfhrseaeLATALSDKQGLETEVAELRaqlakaedghavakKQLEKETLM 201
Cdd:pfam00038 81 RLAAEDFRQK----------------------------YEDELNLRTSAENDLVGLR--------------KDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 202 RVDLENRCQSLQEELAFSKSVFEE--EVRETRRRHERRLVEVDSSRQQEydfkMAQALEDLRSQHDEQVRLYRVELEQTY 279
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEevRELQAQVSDTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 280 QAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHELEEALAGERDKFRKMLDAKEQEMTE 359
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 1245684410 360 VRDAMQQQLAEYQELLDIKLALDMEISAYRKLLEGEEER 398
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
465-569 |
2.31e-19 |
|
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: 83.63 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 465 ATGVVNIDEVDPEG-----RFVRLKNSSDKDQSLGNWRIKRQVlegeDIAYKFTPKYVLRAGQTVTVWAAG----AGATH 535
Cdd:pfam00932 3 ATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDAS----GGTYTFPNGTTLAPGQTVVVWTGSgtnsATAGY 78
|
90 100 110
....*....|....*....|....*....|....
gi 1245684410 536 SPPSTLVWKSQtnwgpgeSFRTALVSADGEEVAV 569
Cdd:pfam00932 79 WGPSNAVWNNG-------GDAVALYDANGELVDS 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
94-398 |
1.75e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 94 ESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETE 173
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 174 VAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAfsksvfeeevreTRRRHERRLVEVDSSRQQEYDFKM 253
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA------------EAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 254 AQALEDLRSQHDEQVRLYRVE-LEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHI 332
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEeAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1245684410 333 HELEEALAGERDKFRKmLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDMEISAYRKLLEGEEER 398
Cdd:COG1196 466 AELLEEAALLEAALAE-LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-340 |
3.55e-11 |
|
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: 66.62 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 34 SPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVT----------TREVSGIKTLYESELADARRV 103
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleelSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 104 ldetARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAK 183
Cdd:TIGR02168 746 ----EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 184 AEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEEEVRETRRRHERrlvevdssrqqeydfkmAQALEDLRSQ 263
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-----------------LEALLNERAS 884
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1245684410 264 HDEQVRLYRVELEQTyQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASaaENHIHELEEALA 340
Cdd:TIGR02168 885 LEEALALLRSELEEL-SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEA 958
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-398 |
1.64e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 96 ELADARRVLD--ETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETE 173
Cdd:COG1196 217 ELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 174 VAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAfsksvfeeEVRETRRRHERRLVEVDSSRQQEydfkm 253
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE--------ELEEELEEAEEELEEAEAELAEA----- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 254 AQALEDLRSQHDEQVRLYRVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVEslsyqLLGLQKQASAAENHIH 333
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-----LEELEEALAELEEEEE 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1245684410 334 ELEEALAGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDMEISAYRKLLEGEEER 398
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-374 |
1.69e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 44 KEELRELndRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLYESeladarrvLDETARERARLQIEIGKVQA 123
Cdd:TIGR02168 219 KAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK--------LEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 124 ELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMRV 203
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 204 DLENRCQSLQEELAFSKSvfeeevretrrrherrlvEVDSSRQQEYdfkmaqaledlrsQHDEQVRLYRVELEqtyQAKL 283
Cdd:TIGR02168 369 ELESRLEELEEQLETLRS------------------KVAQLELQIA-------------SLNNEIERLEARLE---RLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 284 DNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAEnhihELEEALAGERDKFRKMLDAKEQEMTEVR-- 361
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE----EALEELREELEEAEQALDAAERELAQLQar 490
|
330
....*....|....
gi 1245684410 362 -DAMQQQLAEYQEL 374
Cdd:TIGR02168 491 lDSLERLQENLEGF 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-382 |
2.10e-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: 57.37 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 118 IGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEK 197
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 198 ETLMRVDLENRCQSLQEELAfsksvfEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEDLRSQHDEQVRLYRvELEQ 277
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLE------EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA-NLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 278 TYQAKLDNAKLLSDQND---KAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHELEEALAGERDKFRKmLDAKE 354
Cdd:TIGR02168 825 RLESLERRIAATERRLEdleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE-LSEEL 903
|
250 260
....*....|....*....|....*....
gi 1245684410 355 QEMTEVRDAMQQQLAEYQELL-DIKLALD 382
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLaQLELRLE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
85-400 |
2.19e-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: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 85 EVSGIKTlYESELADARRVLDETARERARLQIEIGKVQAELEEARK-----------SAKKREGELTVAQGRVKDLESLF 153
Cdd:TIGR02169 161 EIAGVAE-FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRerekaeryqalLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 154 HRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETlmrvdlENRCQSLQEELAFSKSvfeeevretRRR 233
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEA---------EIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 234 HERRLVEVDSSRQQEYDFKMAQALEDLRSQH------DEQVRLYRVELEQtYQAKLDNAK-----LLSD--QNDKAAHAA 300
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLaeieelEREIEEERKRRDK-LTEEYAELKeeledLRAEleEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 301 REELKEARMRVE-------SLSYQLLGLQKQASAAENHIHELEEALAGERDKfrkmLDAKEQEMTEVRDAMQQQLAEYQE 373
Cdd:TIGR02169 384 RDELKDYREKLEklkreinELKRELDRLQEELQRLSEELADLNAAIAGIEAK----INELEEEKEDKALEIKKQEWKLEQ 459
|
330 340
....*....|....*....|....*..
gi 1245684410 374 LLDIKLALDMEISAYRKLLEGEEERLK 400
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELS 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
127-399 |
3.31e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 127 EARKSAKKREGELTVAqgRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLE 206
Cdd:COG1196 217 ELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 207 NRCQSLQEELAFSKSvfEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEDLRSQhDEQVRLYRVELEQTyQAKLDNA 286
Cdd:COG1196 295 AELARLEQDIARLEE--RRRELEERLEELEEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEA-EEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 287 KLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHELEEALAGERDKfrkmLDAKEQEMTEVRDAMQQ 366
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA----LAELEEEEEEEEEALEE 446
|
250 260 270
....*....|....*....|....*....|...
gi 1245684410 367 QLAEYQELLDIKLALDMEISAYRKLLEGEEERL 399
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
126-399 |
1.25e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 126 EEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMRVDL 205
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 206 ENRCQSLQEELAfsksvfeeevretrrrherrlvevdssrqqEYDFKMAQALEDLrsqHDEQVRLYRVELE-QTYQAKLD 284
Cdd:TIGR02168 746 EERIAQLSKELT------------------------------ELEAEIEELEERL---EEAEEELAEAEAEiEELEAQIE 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 285 NAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHELEEALAGERdkfrkmldAKEQEMTEVRDAM 364
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS--------EDIESLAAEIEEL 864
|
250 260 270
....*....|....*....|....*....|....*
gi 1245684410 365 QQQLAEYQELLDIKLALDMEISAYRKLLEGEEERL 399
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
81-375 |
1.02e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 81 VTTREVSGIKTLYESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAEL 160
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 161 ATALSDKQGLETEVAELRAQLAK-----AEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVfeeevretRRRHE 235
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKEleariEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEE--------VSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 236 RRLVEVDSSRQQEYDFKmaQALEDLRsQHDEQVRLYRVELEQTYQAKLDNakllsDQNDKAAHAarEELKEARMRVESLS 315
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEK--EYLEKEI-QELQEQRIDLKEQIKSIEKEIEN-----LNGKKEELE--EELEELEAALRDLE 881
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1245684410 316 YQLLGLQKQASAAENHIHELEEA---LAGERDKFRKMLdakeQEMTEVRDAMQQQLAEYQELL 375
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKieeLEAQIEKKRKRL----SELKAKLEALEEELSEIEDPK 940
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
100-406 |
1.83e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 100 ARRVLDETARER-ARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELatalsDKQGLETEVAELR 178
Cdd:COG4913 600 SRYVLGFDNRAKlAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 179 AQLAKAEDGH---AVAKKQLEKETLMRVDLENRCQSLQEELAfsksvfeeevretrrrherrlvEVDSSRQQeydfkMAQ 255
Cdd:COG4913 675 AELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIG----------------------RLEKELEQ-----AEE 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 256 ALEDLRSQHDEQVRLYRVELEQTYQAKLDNAkLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAA-ENHIHE 334
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAA-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETAD 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 335 LEEALAGERDkFRKMLDA-KEQEMTEVRDAMQQQLAE--YQELLDIKLALDMEISAYRKLLE-----------GEEERLK 400
Cdd:COG4913 807 LDADLESLPE-YLALLDRlEEDGLPEYEERFKELLNEnsIEFVADLLSKLRRAIREIKERIDplndslkripfGPGRYLR 885
|
....*.
gi 1245684410 401 LSPSPS 406
Cdd:COG4913 886 LEARPR 891
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-398 |
3.92e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 44 KEELRELNDRLAHYIDRVRALELENDRLLLRISE----KEEV--TTREVSGIKTLYESELADARRVLDETARERARLQIE 117
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARREEledrDEELrdRLEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 118 IGKVQAELEEARKSAKKREG-------ELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAV 190
Cdd:PRK02224 365 AAELESELEEAREAVEDRREeieeleeEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 191 AKKQLEketlmrvdlENRCQSLQEELAFSKSVfeeevretrrrherrlVEVDSSRQQEYdfKMAQALEDLRSQHDE-QVR 269
Cdd:PRK02224 445 AEALLE---------AGKCPECGQPVEGSPHV----------------ETIEEDRERVE--ELEAELEDLEEEVEEvEER 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 270 LYR----VELEQTYQAKLDNAKLLSDQNDKaahaAREELKEARMRVESLSYQLLGLQKQASAAENHIHELEEALAGERDK 345
Cdd:PRK02224 498 LERaedlVEAEDRIERLEERREDLEELIAE----RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1245684410 346 FrKMLDAKEQEMTEVRDAmqqqLAEYQELLDIKLALDMEISAYRKLLEGEEER 398
Cdd:PRK02224 574 V-AELNSKLAELKERIES----LERIRTLLAAIADAEDEIERLREKREALAEL 621
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
94-217 |
2.29e-05 |
|
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: 46.07 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 94 ESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDK--QGLE 171
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQ 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1245684410 172 TEVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELA 217
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-345 |
3.12e-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: 46.68 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 104 LDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAK 183
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 184 aedghavakkqlEKETLMRVDLENRCQSLQEELAFSKSVFEEEVRETRRRHERRLVEVDSSRQQEYDfKMAQALEDLRSQ 263
Cdd:COG4942 102 ------------QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-ADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 264 HDEQVRLYRVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARmrveslsyQLLGLQKQASAAENHIHELEEALAGER 343
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA--------ELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 1245684410 344 DK 345
Cdd:COG4942 241 ER 242
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
101-398 |
4.10e-05 |
|
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: 46.21 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 101 RRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQ 180
Cdd:pfam19220 33 IEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 181 LAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEEL-AFSKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMA----- 254
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEENKALREEAqAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAaelae 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 255 -----QALEDLRSQHDEQVRlyrvELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAE 329
Cdd:pfam19220 193 ltrrlAELETQLDATRARLR----ALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEAR 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1245684410 330 NHIHELEEA----------LAGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDMEISAYRKLLEGEEER 398
Cdd:pfam19220 269 NQLRDRDEAiraaerrlkeASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEER 347
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
40-377 |
7.87e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 40 RLQEKE-ELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLY-ESELADARRV---LDETARERARL 114
Cdd:COG4913 611 KLAALEaELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaEREIAELEAElerLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 115 QIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSD-KQGLETEVAELRAQLAKAedghavakk 193
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLaRLELRALLEERFAAALGD--------- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 194 qlEKETLMRVDLENRCQSLQEELAfsksvfeeevretrrRHERRLVEVDSSRQQEYDFKMAQALEDLRSQHD---EQVRL 270
Cdd:COG4913 762 --AVERELRENLEERIDALRARLN---------------RAEEELERAMRAFNREWPAETADLDADLESLPEylaLLDRL 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 271 YRVELEQtYQAKLDNAKLLSDQNDKA--AHAAREELKEARMRVESLSYQLLGLQKQasaAENHIH-ELEEALAGERDKFR 347
Cdd:COG4913 825 EEDGLPE-YEERFKELLNENSIEFVAdlLSKLRRAIREIKERIDPLNDSLKRIPFG---PGRYLRlEARPRPDPEVREFR 900
|
330 340 350
....*....|....*....|....*....|.
gi 1245684410 348 KML-DAKEQEMTEVRDAMQQQLAEYQELLDI 377
Cdd:COG4913 901 QELrAVTSGASLFDEELSEARFAALKRLIER 931
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
42-217 |
9.66e-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: 45.44 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 42 QEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLY-------------------------ESE 96
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshsripeiqaelskleeevsriEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 97 LADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAE 176
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1245684410 177 LRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELA 217
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
76-401 |
1.16e-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: 45.35 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 76 SEKEEVTTREVSGIkTLYESELADARRVLDETARERARLQIEIGKVQ-AELEEARKSAKKREGELTVAQGRVKDLESLFH 154
Cdd:pfam02463 151 KPERRLEIEEEAAG-SRLKRKKKEALKKLIEETENLAELIIDLEELKlQELKLKEQAKKALEYYQLKEKLELEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 155 RSEAELATALSDKQGLETEVAELRAQLAKAEDghavAKKQLEKETLMRVDLENRCQSLQEELAfsKSVFEEEVRETRRRH 234
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIE----KEEEKLAQVLKENKEEEKEKKLQEEEL--KLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 235 ERRLVEVDSSRQQEYDFKMAQALEDLRSQ--------------HDEQVRLYRVELEQTYQAKLDNAKLLSDQNDKAAHAA 300
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKekeeieelekelkeLEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 301 REELKEARMRVESLSYQLLGLQKQASaaenhIHELEEALAGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLA 380
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEKEAQL-----LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
330 340
....*....|....*....|.
gi 1245684410 381 LDMEISAYRKLLEGEEERLKL 401
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQL 479
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
43-197 |
1.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 43 EKEELRELNDRLAHYIDRVRALELENDRLLLRISEK----EEVTTREVSGIKTLYES--ELADARRVLDETARERARLQI 116
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEE 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 117 EIGKVQAELEEARKSAKKREGELtvaqgrvKDLESLFhrSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLE 196
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKEL-------EELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
.
gi 1245684410 197 K 197
Cdd:PRK03918 698 K 698
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
61-399 |
1.71e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 61 VRALELENDRLLLRISEKEEVTTREvSGIKTLYESelADARRVLDETAReraRLQIEIGKVQAELEEARKSAKKREGELT 140
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAE-SDLEQDYQA--ASDHLNLVQTAL---RQQEKIERYQADLEELEERLEEQNEVVE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 141 VAQGRVKDLESLFHRSEAE---LATALSD-KQGLEteVAELRA----------------------QLAKAEDGHAVAKKQ 194
Cdd:PRK04863 373 EADEQQEENEARAEAAEEEvdeLKSQLADyQQALD--VQQTRAiqyqqavqalerakqlcglpdlTADNAEDWLEEFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 195 LEKETLMRVDLENRCQSLQEelafSKSVFEEEVRETRRRHErrlvEVDSS----------RQQEYDFKMAQALEDLRSQH 264
Cdd:PRK04863 451 EQEATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAG----EVSRSeawdvarellRRLREQRHLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 265 DEQVRlyRVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHELE---EALAG 341
Cdd:PRK04863 523 SELEQ--RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQariQRLAA 600
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1245684410 342 ERDKFRKMLDAKEQ--EMTEVRDAMQQQLAEY-QELLDIKLALDME---ISAYRKLLEGEEERL 399
Cdd:PRK04863 601 RAPAWLAAQDALARlrEQSGEEFEDSQDVTEYmQQLLERERELTVErdeLAARKQALDEEIERL 664
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
45-374 |
4.42e-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: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 45 EELRELNDRLAHY----IDRVRALELENDRLLLRISEKEEVTTREvSGIKTLYESELADARRVldetaRERARLQIEIGK 120
Cdd:COG3096 278 NERRELSERALELrrelFGARRQLAEEQYRLVEMARELEELSARE-SDLEQDYQAASDHLNLV-----QTALRQQEKIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 121 VQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAE---LATALSD-KQGLetEVAELRA-QLAKAEDGHAVAKKQL 195
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEvdsLKSQLADyQQAL--DVQQTRAiQYQQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 196 EKETLMRVDLENRCQSLQEELAfsksvfeeevretrrrherrlvEVDSS-RQQEYDFKMAQAledLRSQHDEQVRLYR-- 272
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQ----------------------QATEEvLELEQKLSVADA---ARRQFEKAYELVCki 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 273 ---VELEQTYQAkldnAK-LLSDQNDKAAHAARE-----ELKEARMRVES---LSYQLLGLQKQASAAENHIHELEEALA 340
Cdd:COG3096 485 ageVERSQAWQT----AReLLRRYRSQQALAQRLqqlraQLAELEQRLRQqqnAERLLEEFCQRIGQQLDAAEELEELLA 560
|
330 340 350
....*....|....*....|....*....|....*...
gi 1245684410 341 gERDKFRKMLDAKEQEMTEVRDAMQQQL----AEYQEL 374
Cdd:COG3096 561 -ELEAQLEELEEQAAEAVEQRSELRQQLeqlrARIKEL 597
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
168-401 |
4.77e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 168 QGLETEVAELRAQLAKAEDGHAVAKKQLEKETLmrVDLENRCQSLQEELAfsksvfEEEVRETRRRHERRLVEVDSSRQQ 247
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAEL--EELEAELEELEAELA------ELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 248 EYDFKMAQALEDLRSQHDEQVrlyrvELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASA 327
Cdd:COG1196 288 AEEYELLAELARLEQDIARLE-----ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1245684410 328 AENHIHELEEALAGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDMEISAYRKLLEGEEERLKL 401
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-340 |
5.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 96 ELADARRVLDETARERARLQiEIGKVQAELEEARksAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVA 175
Cdd:COG4913 236 DLERAHEALEDAREQIELLE-PIRELAERYAAAR--ERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 176 ELRAQLAKAEDGHAVAKKQLEKETLMRVD-LENRCQSLQEELAfsksvfeeevretrrrherrlvEVDSSRQQeydfkMA 254
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELE----------------------ERERRRAR-----LE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 255 QALEDLRSQHDEQVRLYrVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHE 334
Cdd:COG4913 366 ALLAALGLPLPASAEEF-AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
|
....*.
gi 1245684410 335 LEEALA 340
Cdd:COG4913 445 LRDALA 450
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
123-353 |
7.47e-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: 42.90 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 123 AELEEARKSAKKREGELtVAQGRvKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHA-VAKKQLEKETLM 201
Cdd:pfam12128 275 ASRQEERQETSAELNQL-LRTLD-DQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIeTAAADQEQLPSW 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 202 RVDLENRCQSLQEELAFSKSV---FEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQ---------ALED-LRSQHDEQV 268
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVtakYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQlavaeddlqALESeLREQLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 269 RLYRVELEQtYQAKLDNAKLLSDQ-------------NDKAAHAAREELKEARMRVESLSYQLLGLQK---QASAAENHI 332
Cdd:pfam12128 433 LEFNEEEYR-LKSRLGELKLRLNQatatpelllqlenFDERIERAREEQEAANAEVERLQSELRQARKrrdQASEALRQA 511
|
250 260
....*....|....*....|.
gi 1245684410 333 HELEEALAGERDKFRKMLDAK 353
Cdd:pfam12128 512 SRRLEERQSALDELELQLFPQ 532
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
42-182 |
8.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 42 QEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGI----KTLYESELADARRVLDETARERARLQIE 117
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1245684410 118 IGKVQAELEEARKSAKKREGEltvAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLA 182
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
75-397 |
8.78e-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: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 75 ISEKEEVTTREVSGIKTLYESE-------LADARRVL---DETARERARLQIEIGKVQAELEEARKSAKKRegeltvaqg 144
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEklknielTAHCDKLLlenKELTQEASDMTLELKKHQEDIINCKKQEERM--------- 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 145 rVKDLESLfHRSEAELATAL-SDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVF 223
Cdd:pfam05483 533 -LKQIENL-EEKEMNLRDELeSVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 224 EEEVRETRRRHERRLVEvdSSRQQEYDFKMAQ---ALEDLRSQHDEQVRLYRVELEQTyqaKLDNAKLLsDQNDKAAHAA 300
Cdd:pfam05483 611 EELHQENKALKKKGSAE--NKQLNAYEIKVNKlelELASAKQKFEEIIDNYQKEIEDK---KISEEKLL-EEVEKAKAIA 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 301 REEL---KEARMRVESLSYQLLGLQkqasaaENHIHELEEALAgERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQ-ELLD 376
Cdd:pfam05483 685 DEAVklqKEIDKRCQHKIAEMVALM------EKHKHQYDKIIE-ERDSELGLYKNKEQEQSSAKAALEIELSNIKaELLS 757
|
330 340
....*....|....*....|.
gi 1245684410 377 IKLALDMEISAYRKLLEGEEE 397
Cdd:pfam05483 758 LKKQLEIEKEEKEKLKMEAKE 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
37-181 |
9.53e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 37 RLSRLQEK-EELRELND----RLAHYIDRVRALELENDRLllRISEKEEVTTRevsgiktlYESELADARRVLDETARER 111
Cdd:PRK02224 607 EIERLREKrEALAELNDerreRLAEKRERKRELEAEFDEA--RIEEAREDKER--------AEEYLEQVEEKLDELREER 676
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 112 ARLQIEIGKVQAELEEaRKSAKKREGELtvaQGRVKDLESLFHRSEAelatalsdkqgLETEVAELRAQL 181
Cdd:PRK02224 677 DDLQAEIGAVENELEE-LEELRERREAL---ENRVEALEALYDEAEE-----------LESMYGDLRAEL 731
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
96-386 |
1.76e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 96 ELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVA 175
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 176 ELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEEEVRETRRRHERRLVEVDSSRQQEYDfKMAQ 255
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN-RNAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 256 ALEDLRSQHDEQVRLYRVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHEL 335
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1245684410 336 EEALAGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDMEIS 386
Cdd:COG4372 278 LEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-400 |
2.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 37 RLSRLQEK--EELRELNDRLAHYIDRVRAL-----ELENDRLLLR-ISEKEEVTTREVSGIKTlYESELADARRVLDETA 108
Cdd:PRK03918 297 KLSEFYEEylDELREIEKRLSRLEEEINGIeerikELEEKEERLEeLKKKLKELEKRLEELEE-RHELYEEAKAKKEELE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 109 RERARLQI-EIGKVQAELEEARKSAKKREGELTVAQGRVKDLES---------------------------------LFH 154
Cdd:PRK03918 376 RLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKeikelkkaieelkkakgkcpvcgrelteehrkeLLE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 155 RSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMR--VDLENRCQSLQ-EELAFSKSVFEEEVRETR 231
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlKELEEKLKKYNlEELEKKAEEYEKLKEKLI 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 232 RRHERRL-VEVDSSRQQEYDFKMAQALEDLRSQHDEQVRLYRVELEQTYQAKLDNAKLLsdQNDKAAHAAREELKEARMR 310
Cdd:PRK03918 536 KLKGEIKsLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERL--KELEPFYNEYLELKDAEKE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 311 VESLSYQLLGLQKQASAAENHIHELEEALagerDKFRKMLDAKEQEMTEvrdamqqqlAEYQELLDIKLALDMEISAYRK 390
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRL----EELRKELEELEKKYSE---------EEYEELREEYLELSRELAGLRA 680
|
410
....*....|
gi 1245684410 391 LLEGEEERLK 400
Cdd:PRK03918 681 ELEELEKRRE 690
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
33-200 |
2.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 33 LSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLyeselaDARRVLDETARERA 112
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE------EELRAALEQAEEYQ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 113 RLQIEIGKVQAELEEARKSAKKREGELTVAQgrvkdLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAK 192
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
....*...
gi 1245684410 193 KQLEKETL 200
Cdd:COG4717 474 LLQELEEL 481
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
33-374 |
2.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 33 LSPTRLSRLQEKEELRELNDRLAH---YIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLYESELADARRVLDETAR 109
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 110 ERARLQIEIGKVQAELEEARKSAKKREGELTVAQ--GRVKDLESLFhRSEAELATALSDKQGLE------TEVAELRAQL 181
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLL-LIAAALLALLGLGGSLLsliltiAGVLFLVLGL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 182 AKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFS-----------------------KSVFEEEVRETRRRHERRL 238
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEEllaalglppdlspeellelldriEELQELLREAEELEEELQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 239 VEVDSSRQQEYDFKMAQALEDLRS---QHDEQVRLYRV--ELEQTYQAKLDNAKLLSDQNDKAAhaAREELKEARMRVES 313
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEELRAaleQAEEYQELKEEleELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEE 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1245684410 314 LSYQLLGLQKQASAAENHIHELEEAlagerdkfrKMLDAKEQEMTEVRDAMQQQLAEYQEL 374
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEED---------GELAELLQELEELKAELRELAEEWAAL 495
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
42-196 |
3.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 42 QEKEELRELNDRLAHYIDRVRALELENDRLLLRiSEKEEVTTRevsgiKTLYESELADARRVLDETARERA--------R 113
Cdd:COG4913 269 ERLAELEYLRAALRLWFAQRRLELLEAELEELR-AELARLEAE-----LERLEARLDALREELDELEAQIRgnggdrleQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 114 LQIEIGKVQAELEEARKSAKKREGELTVAQGRV----KDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHA 189
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
....*..
gi 1245684410 190 VAKKQLE 196
Cdd:COG4913 423 ELEAEIA 429
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
95-337 |
3.35e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 95 SELADARRVLDETARERARLQIEIGKVQAELEEArKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEV 174
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 175 AELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEEEVRETRRRHerrlvEVDSSRQQEYDFkma 254
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAED-----EIERLREKREAL--- 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 255 QALEDLRSQHDEQVRLYRVELEqtyqAKLDNAKLLSDQNDKAAhaAREELKEARMRVESLSYQLLGLQKQASAAENHIHE 334
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELE----AEFDEARIEEAREDKER--AEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
...
gi 1245684410 335 LEE 337
Cdd:PRK02224 693 LEE 695
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
37-202 |
6.78e-03 |
|
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: 38.75 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 37 RLSRLQEKE-ELRELNDRLAHYIDRVRALELENDRLLLRISEKEEvttrEVSGIKTLY---ESELADARRVL--DETARE 110
Cdd:COG1579 8 ALLDLQELDsELDRLEHRLKELPAELAELEDELAALEARLEAAKT----ELEDLEKEIkrlELEIEEVEARIkkYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 111 RARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSD----KQGLETEVAELRAQLAKAED 186
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEELEA 163
|
170
....*....|....*.
gi 1245684410 187 GHAVAKKQLEKETLMR 202
Cdd:COG1579 164 EREELAAKIPPELLAL 179
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-400 |
9.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 42 QEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEevttrEVSGIKTLYEsELADARRVLDETARERARLQIEIgkv 121
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----KLLQLLPLYQ-ELEALEAELAELPERLEELEERL--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 122 qAELEEARKSAKKREGELTVAQGRVKDLESLF-HRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETL 200
Cdd:COG4717 156 -EELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 201 MRVDLENRcQSLQEE----------LAFSKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEDLRSQHDEQVRL 270
Cdd:COG4717 235 ELEAAALE-ERLKEArlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 271 YRVElEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHiHELEEALAGERDKFRKML 350
Cdd:COG4717 314 EELE-EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1245684410 351 DAKE--QEMTEVRDAMQQQLAEYQELLDIKLA------LDMEISAYRKLLEGEEERLK 400
Cdd:COG4717 392 EQAEeyQELKEELEELEEQLEELLGELEELLEaldeeeLEEELEELEEELEELEEELE 449
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
94-389 |
9.59e-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: 39.00 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 94 ESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETE 173
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTR 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 174 VAELraqlakaEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEEEVRETRRRHERR---LVEVDSSRQQEYD 250
Cdd:pfam01576 491 LRQL-------EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKkrlQRELEALTQQLEE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 251 FKMA------------QALEDLRSQHDEQVRLyrVELEQTYQAKLDNA----KLLSDQNDKAAHAAREELKEARMRVESL 314
Cdd:pfam01576 564 KAAAydklektknrlqQELDDLLVDLDHQRQL--VSNLEKKQKKFDQMlaeeKAISARYAEERDRAEAEAREKETRALSL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245684410 315 SYQLLGLQKQASAAENHIHELE---EALAGERD-------KFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDME 384
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRaemEDLVSSKDdvgknvhELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVN 721
|
....*
gi 1245684410 385 ISAYR 389
Cdd:pfam01576 722 MQALK 726
|
|
| |
