|
Name |
Accession |
Description |
Interval |
E-value |
| NUDE_C |
pfam04880 |
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ... |
165-340 |
1.32e-53 |
|
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.
Pssm-ID: 461464 [Multi-domain] Cd Length: 169 Bit Score: 174.98 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 165 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVEAERTD 234
Cdd:pfam04880 1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 235 TAVQATgsvpSTPIAHRGPSSSLNtpgSFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNLVYDQSP 314
Cdd:pfam04880 81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145
|
170 180
....*....|....*....|....*.
gi 2462549449 315 NRtggpasgRSSKNRDGGERRPSSTS 340
Cdd:pfam04880 146 SR-------RGNSRSLYGSRPPTKFA 164
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
59-218 |
2.80e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 59 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEgyrQISALEDDLAQTKAIK 138
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 139 DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQE 218
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-221 |
2.98e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAI 137
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 138 KDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQ 217
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
....
gi 2462549449 218 EKPR 221
Cdd:COG1196 489 AAAR 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-217 |
5.59e-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: 58.14 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRMELE-TIKKFEVQHSEGYRQISALEDDLAQTKA 136
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEaQIEQLKEELKALREALDELRAELTLLNE 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 137 -------IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 209
Cdd:TIGR02168 818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
....*...
gi 2462549449 210 ELAVQQKQ 217
Cdd:TIGR02168 898 ELSEELRE 905
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
59-236 |
1.50e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 59 QRAENTQEELREFQEGSREYeAELETQLQQIETRNRDLLSENNRLRMELETIKKfEVQHSEGYRQISALEDDLAQTKAIK 138
Cdd:COG4717 71 KELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 139 DQLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAF-----LESELDEKENLLESVQRLKDEARDLRQEL-A 212
Cdd:COG4717 149 EELEERLEELRELEEELEELEAE----LAELQEELEELLEQLSLateeeLQDLAEELEELQQRLAELEEELEEAQEELeE 224
|
170 180
....*....|....*....|....
gi 2462549449 213 VQQKQEKPRTPMPSSVEAERTDTA 236
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEA 248
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-219 |
3.99e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAI 137
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 138 KDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAVQQKQ 217
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
..
gi 2462549449 218 EK 219
Cdd:COG1196 409 EE 410
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
62-219 |
1.01e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 62 ENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRL---RMELETIKKFEVQ--HSEGYRQISALEDDLAQTKA 136
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQN 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 137 IKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAI-ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 215
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKK----ELTNSESENSEKQRELeEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
....
gi 2462549449 216 KQEK 219
Cdd:TIGR04523 405 KLNQ 408
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-216 |
1.16e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAI 137
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549449 138 KDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 216
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-219 |
1.26e-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: 53.91 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 59 QRAENTQEELREFQEGS-----REYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQ 133
Cdd:TIGR02168 213 ERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 134 TKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQEL-- 211
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELes 372
|
....*...
gi 2462549449 212 AVQQKQEK 219
Cdd:TIGR02168 373 RLEELEEQ 380
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
42-218 |
1.30e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 42 SEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGY 121
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 122 RQISALEDDLAQTKAikdQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 201
Cdd:COG1196 386 EELLEALRAAAELAA---QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170
....*....|....*..
gi 2462549449 202 DEARDLRQELAVQQKQE 218
Cdd:COG1196 463 ELLAELLEEAALLEAAL 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-219 |
1.64e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKfEVQHSEgyRQISALEDDLAQTKAI 137
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE-ELEEAE--AELAEAEEALLEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 138 KDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQ 217
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
..
gi 2462549449 218 EK 219
Cdd:COG1196 454 LE 455
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-232 |
1.72e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 59 QRAENTQEELREFQEGSREYEAELETQLQQIE-TRNRDLLSENNRLRMELET--------IKKFEVQHSE-GYRQISALE 128
Cdd:COG4913 265 AAARERLAELEYLRAALRLWFAQRRLELLEAElEELRAELARLEAELERLEArldalreeLDELEAQIRGnGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 129 DDLAQTKAIKDQLQkyiRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEN----LLESVQRLKDEA 204
Cdd:COG4913 345 REIERLERELEERE---RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRREL 421
|
170 180
....*....|....*....|....*...
gi 2462549449 205 RDLRQELAVQQKQekpRTPMPSSVEAER 232
Cdd:COG4913 422 RELEAEIASLERR---KSNIPARLLALR 446
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-219 |
1.84e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 43 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYR 122
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 123 QISALEDDLAQTKAIKDQLQKYIRELEQANDDLE-RAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 201
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLeRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
170
....*....|....*...
gi 2462549449 202 DEARDLRQELAVQQKQEK 219
Cdd:COG1196 460 ALLELLAELLEEAALLEA 477
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
51-219 |
2.66e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 51.60 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 51 KDLAMTYKQRAENTQEELREFQEGSREYeaelETQLQQIETRNRDLLSENNRL--RMELETIKKfevqhsegyrQISALE 128
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTEKD----QTALETLEKALKDLLTDEGGAiaRKEIKDLQK----------ELEKLN 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 129 DDLAqtKAIKDQLQKYIRELEQANDDLERAKR------ATIMSLEDFEQRLNQAIE-----RNAF--LESELDEKENLLE 195
Cdd:cd22656 193 EEYA--AKLKAKIDELKALIADDEAKLAAALRliadltAADTDLDNLLALIGPAIPaleklQGAWqaIATDLDSLKDLLE 270
|
170 180
....*....|....*....|....
gi 2462549449 196 SVQRlkDEARDLRQELAVQQKQEK 219
Cdd:cd22656 271 DDIS--KIPAAILAKLELEKAIEK 292
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
44-218 |
2.72e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 44 EEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSegyRQ 123
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL---AE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 124 ISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDE 203
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170
....*....|....*
gi 2462549449 204 ARDLRQELAVQQKQE 218
Cdd:COG1196 377 AEEELEELAEELLEA 391
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
80-231 |
2.90e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 80 AELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHsEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAK 159
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549449 160 R---ATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAE 231
Cdd:COG4913 692 EqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
80-219 |
3.10e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 80 AELETQLQQIETRNRDLLSENNRLRMELETIK----KFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYI------RELE 149
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEarleAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549449 150 QANDDLERAKRAtIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQ-RLKDEARDLRQELAVQQKQEK 219
Cdd:COG1579 93 ALQKEIESLKRR-ISDLEDEILELMERIEE---LEEELAELEAELAELEaELEEKKAELDEELAELEAELE 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
58-242 |
4.09e-07 |
|
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: 51.30 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQT--- 134
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 135 -----------------------------KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLES 185
Cdd:COG4942 113 lyrlgrqpplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549449 186 ELDEKENLLesvQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGS 242
Cdd:COG4942 193 LKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
58-284 |
6.75e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEV-QHSEGyrqISALEDDLAQTKA 136
Cdd:COG3883 50 NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVlLGSES---FSDFLDRLSALSK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 137 IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 216
Cdd:COG3883 127 IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549449 217 QEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISA 284
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
36-217 |
6.81e-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: 51.60 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 36 SGKTFSSEEEEANYWKDLAMTyKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIKKFEV 115
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI----SALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 116 QHSEGYRQISALEDDLAQtkaikdQLQKYIRELEQANDDLERAKRatimSLEDFEQRLNQAIERNAFLESELDEKEnllE 195
Cdd:TIGR02168 744 QLEERIAQLSKELTELEA------EIEELEERLEEAEEELAEAEA----EIEELEAQIEQLKEELKALREALDELR---A 810
|
170 180
....*....|....*....|..
gi 2462549449 196 SVQRLKDEARDLRQELAVQQKQ 217
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERR 832
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
59-212 |
8.84e-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: 51.22 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 59 QRAENTQEELREFQEGSREYEA-ELETQLQQIETRNRDLLSENNRLRMELEtikKFEVQHSEGYRQISALEDDLAQ-TKA 136
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGyELLKEKEALERQKEAIERQLASLEEELE---KLTEEISELEKRLEEIEQLLEElNKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 137 IKD-------QLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELD-----------EKENLLESVQ 198
Cdd:TIGR02169 281 IKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereieeerkRRDKLTEEYA 360
|
170
....*....|....
gi 2462549449 199 RLKDEARDLRQELA 212
Cdd:TIGR02169 361 ELKEELEDLRAELE 374
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-212 |
9.41e-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: 50.83 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 44 EEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIKKfevqhsegyrQ 123
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV----AQLELQIASLNN----------E 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 124 ISALEDDLAQtkaIKDQLQKYIRELEQANDDLERAKRATI-MSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKD 202
Cdd:TIGR02168 402 IERLEARLER---LEDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
170
....*....|
gi 2462549449 203 EARDLRQELA 212
Cdd:TIGR02168 479 AAERELAQLQ 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
79-222 |
9.55e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 79 EAELETQLQQIETRNRDLLSENNRLRMELE-TIKKFEVQHSEgYRQisaLEDDLAQTKAIKDQLQKYIRELEQANDDLER 157
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEeELKEAEEKEEE-YAE---LQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549449 158 AKRA--TIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRT 222
Cdd:COG4717 124 LLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-212 |
1.06e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLaqTKAI 137
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAE 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549449 138 KDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELA 212
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-219 |
1.24e-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: 50.45 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 33 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLlsenNRLRMELETIK- 111
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEa 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 112 ---------------KFEVQHSEGYRQISALEDDLAQTKAIKDQLQK-------YIRELE-------QANDDLERAKRAT 162
Cdd:TIGR02169 787 rlshsripeiqaelsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKeiqelqeQRIDLKeqiksieKEIENLNGKKEEL 866
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549449 163 IMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 219
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
45-217 |
1.29e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 45 EEANYWKDLAmtykqraENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKF--EVQHSEGYR 122
Cdd:PRK04863 424 ERAKQLCGLP-------DLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIagEVSRSEAWD 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 123 QISALEDDLAQTKAIKDQLQKY---IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 199
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQLrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
170
....*....|....*...
gi 2462549449 200 LKDEARDLRQELAVQQKQ 217
Cdd:PRK04863 573 SVSEARERRMALRQQLEQ 590
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
59-247 |
1.47e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 59 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAIK 138
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 139 DQLQKYIRELEQANDDLERAKRAT-IMSLEDFEQ--RLNQAIER-NAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 214
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlLLSPEDFLDavRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|...
gi 2462549449 215 QKQEKPRTPMPSSVEAERTDTAVQATGSVPSTP 247
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELA 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-219 |
1.65e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 66 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISAledDLAQTKAIKDQLQKYI 145
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549449 146 RELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 219
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-218 |
1.75e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 67 ELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIR 146
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 147 ELEQAND-------DLERAKRATIMSLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQ 215
Cdd:TIGR02168 355 SLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIerleARLERLEDRRERLQQEIEELLKKLEEAE 434
|
...
gi 2462549449 216 KQE 218
Cdd:TIGR02168 435 LKE 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-219 |
2.12e-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: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 55 MTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQT 134
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 135 KAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ 214
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
....*
gi 2462549449 215 QKQEK 219
Cdd:TIGR02168 924 LAQLE 928
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-219 |
3.26e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 69 REFQEGSREYEAELetQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIREL 148
Cdd:COG1196 216 RELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549449 149 EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQEK 219
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-212 |
3.86e-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: 48.90 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAI 137
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 138 KDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL------------ESVQRLKDEAR 205
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenkieDDEEEARRRLK 975
|
....*..
gi 2462549449 206 DLRQELA 212
Cdd:TIGR02168 976 RLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-207 |
4.22e-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: 48.90 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 44 EEEANYWKDLamtyKQRAENTQEELREFQEGSREYEAE----------LETQLQQIETRNRDLLSENNRLRMELETIKKF 113
Cdd:TIGR02168 361 EELEAELEEL----ESRLEELEEQLETLRSKVAQLELQiaslnneierLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 114 EVQhsegyRQISALEDDLAQTKAIKDQLQkyiRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENL 193
Cdd:TIGR02168 437 ELQ-----AELEELEEELEELQEELERLE---EALEELREELEEAEQA----LDAAERELAQLQARLDSLERLQENLEGF 504
|
170
....*....|....
gi 2462549449 194 LESVQRLKDEARDL 207
Cdd:TIGR02168 505 SEGVKALLKNQSGL 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
65-218 |
4.42e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 65 QEELREFQEGS-----REYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAIKD 139
Cdd:COG1196 219 KEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549449 140 QLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQE 218
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
58-225 |
4.73e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAI 137
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 138 KDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESEL--DEKENLLESVQRLKDEARDLRQELAVQQ 215
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELqaLSEAEAEQALDELLKEANRNAEKEEELA 203
|
170
....*....|
gi 2462549449 216 KQEKPRTPMP 225
Cdd:COG4372 204 EAEKLIESLP 213
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
53-221 |
5.16e-06 |
|
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: 48.58 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 53 LAMTYKQRAENTQEELREFQ-EGSREYEAELE-TQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDD 130
Cdd:pfam17380 342 MAMERERELERIRQEERKRElERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 131 LAQTKAIKDQL-QKYIRELEQanddlERAKRATIMSLEDFEQRlnQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 209
Cdd:pfam17380 422 MEQIRAEQEEArQREVRRLEE-----ERAREMERVRLEEQERQ--QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR 494
|
170
....*....|..
gi 2462549449 210 ELAVQQKQEKPR 221
Cdd:pfam17380 495 KILEKELEERKQ 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
56-227 |
5.20e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 56 TYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDL--LSENNRLRMEL--ETIKKFeVQHSEGYRQIS-ALEDD 130
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyrLGRQPPLALLLspEDFLDA-VRRLQYLKYLApARREQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 131 LAQTKAIKDQLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLESELDEKENLLES-VQRLKDEARDLRQ 209
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEA 227
|
170
....*....|....*...
gi 2462549449 210 ELAVQQKQEKPRTPMPSS 227
Cdd:COG4942 228 LIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
58-217 |
5.25e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQtkaI 137
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---Q 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 138 KDQLQKYIRELEQANddlERAKRATIMSLEDFeqrlNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQ 217
Cdd:COG4942 103 KEELAELLRALYRLG---RQPPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
58-205 |
7.74e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEG--YRQISALEDDLAQTK 135
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 136 AIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEAR 205
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELA 169
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-204 |
1.22e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 43 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEA-----------------ELETQLQQIETRNRDLLSENNRLRM 105
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdlesrlgdlkkerdELEAQLRELERKIEELEAQIEKKRK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 106 ELETIKkfeVQHSEGYRQISALEDDLAQTKAIK------DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIER 179
Cdd:TIGR02169 918 RLSELK---AKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
170 180
....*....|....*....|....*
gi 2462549449 180 NAFLESELDEKENLLESVQRLKDEA 204
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-222 |
1.28e-05 |
|
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: 47.36 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 33 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEA---ELETQLQQIETRNRDLLSENNRLRMELET 109
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESkrsELRRELEELREKLAQLELRLEGLEVRIDN 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 110 IKKfevQHSEGYRqiSALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQrLNqaiERNAFLESELDE 189
Cdd:TIGR02168 941 LQE---RLSEEYS--LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEE-LK---ERYDFLTAQKED 1011
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462549449 190 ----KENLLESVQRLKDEARDLRQELAVQQKQEKPRT 222
Cdd:TIGR02168 1012 lteaKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
126-217 |
1.29e-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: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 126 ALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEAR 205
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIA 93
|
90
....*....|..
gi 2462549449 206 DLRQELAVQQKQ 217
Cdd:COG4942 94 ELRAELEAQKEE 105
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-219 |
1.74e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 48 NYWKDLA---MTYKQRAENTQEELR---EFQEGSREYEAELETQLQQI---ETRNRDLLSENNRLRMELETIKKFEVQHS 118
Cdd:PRK03918 162 NAYKNLGeviKEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREIneiSSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 119 EGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLE-RAKRatimsLEDFEQRLNQAIERNAFLESELDEKENLLESV 197
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEeKVKE-----LKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180
....*....|....*....|..
gi 2462549449 198 QRLKDEARDLRQELAVQQKQEK 219
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEE 338
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
72-221 |
2.07e-05 |
|
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: 46.87 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 72 QEGSREYEAELETQLQQIETRNRDL-----LSENNRLRME--LETIKKF--EVQHSEGY-------RQISALEDDLAQTK 135
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELeqklsVADAARRQFEkaYELVCKIagEVERSQAWqtarellRRYRSQQALAQRLQ 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 136 AIKDQLqkyiRELEQANDDLERAKRatimSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 215
Cdd:COG3096 516 QLRAQL----AELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
....*.
gi 2462549449 216 KQEKPR 221
Cdd:COG3096 588 EQLRAR 593
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-223 |
2.60e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 66 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYI 145
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 146 ReLEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLES-------------ELDEKENLLESVQRLKDEARDLRQELA 212
Cdd:PRK03918 297 K-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeerleelkkklkELEKRLEELEERHELYEEAKAKKEELE 375
|
170
....*....|.
gi 2462549449 213 VQQKQEKPRTP 223
Cdd:PRK03918 376 RLKKRLTGLTP 386
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
58-202 |
3.72e-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: 44.53 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSE--NNRlrmELETIKKfEVQHSEgyRQISALEDDLAQTK 135
Cdd:COG1579 44 EARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNvrNNK---EYEALQK-EIESLK--RRISDLEDEILELM 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549449 136 AIKDQLQKYIRE----LEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDekENLLESVQRLKD 202
Cdd:COG1579 117 ERIEELEEELAEleaeLAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP--PELLALYERIRK 185
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
37-204 |
4.12e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 37 GKTFSSEEEEANYWKDLAMTYKQRAENTQ----EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIkk 112
Cdd:COG5185 289 KQFENTKEKIAEYTKSIDIKKATESLEEQlaaaEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI-- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 113 fevqhsEGYRQISALEDDLaqtKAIKDQLQKYIRELEQANDDlerAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEN 192
Cdd:COG5185 367 ------VGEVELSKSSEEL---DSFKDTIESTKESLDEIPQN---QRGYAQEILATLEDTLKAADRQIEELQRQIEQATS 434
|
170
....*....|..
gi 2462549449 193 LLESVQRLKDEA 204
Cdd:COG5185 435 SNEEVSKLLNEL 446
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
44-234 |
4.77e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 44 EEEANYWKDLamtyKQRAENTQEELREFQEGSREYE---AELETQLQQIETRNRDLLSENNRLRMELETiKKFEVQ---- 116
Cdd:TIGR04523 303 QKEQDWNKEL----KSELKNQEKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNSESENSEKQRELEE-KQNEIEklkk 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 117 HSEGYR--------QISALEDDLAQTKAIKDQLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAIERnafLESELD 188
Cdd:TIGR04523 378 ENQSYKqeiknlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK----EIERLKETIIKNNSEIKD---LTNQDS 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549449 189 EKENLLESVQRLKD-----------EARDLRQELAVQQKQEKPRTPMPSSVEAERTD 234
Cdd:TIGR04523 451 VKELIIKNLDNTREsletqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
53-221 |
5.72e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 53 LAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLA 132
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 133 QTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR--LKDEARDLRQE 210
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAEAEQA 184
|
170
....*....|.
gi 2462549449 211 LAVQQKQEKPR 221
Cdd:COG4372 185 LDELLKEANRN 195
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
80-195 |
6.94e-05 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.36 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 80 AELETQLQQIETRNRDLLSENNRLRMELETIKKfEV----QHSEGYRQISAledDLAQTKAIKDQLQKYIRELEQANDDL 155
Cdd:pfam13851 36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQE-EVeelrKQLENYEKDKQ---SLKNLKARLKVLEKELKDLKWEHEVL 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462549449 156 ERAKRATIMSLEDFEQRLNQAIE--------RNAFLESELDEKENLLE 195
Cdd:pfam13851 112 EQRFEKVERERDELYDKFEAAIQdvqqktglKNLLLEKKLQALGETLE 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
81-220 |
7.97e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 81 ELETQLQQIETR--NRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 158
Cdd:TIGR02168 217 ELKAELRELELAllVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549449 159 kratimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 220
Cdd:TIGR02168 297 -------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
60-217 |
1.22e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 60 RAENTQEELREFQEGSREYEAELETQLQQIETRnrdlLSENNRLrmeLETIKKFEV-QHSEGYRQISALEDDLAQTKAIK 138
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARER----VEEAEAL---LEAGKCPECgQPVEGSPHVETIEEDRERVEELE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 139 DQLQKYIRELEQANDDLERAKratimSLEDFEQRLNQAIERNAFLESELDEKENLLES----VQRLKDEARDLRQELAVQ 214
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEK 556
|
...
gi 2462549449 215 QKQ 217
Cdd:PRK02224 557 REA 559
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
28-220 |
1.52e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 28 SPVFTMEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIEtRNRDLLSENNRLRM-- 105
Cdd:COG5185 230 NIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFE-NTKEKIAEYTKSIDik 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 106 -----------ELETIKKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIR-----------------ELEQANDDLER 157
Cdd:COG5185 309 katesleeqlaAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKeeienivgevelsksseELDSFKDTIES 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549449 158 AKRatimslEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 220
Cdd:COG5185 389 TKE------SLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNE 445
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
58-289 |
1.59e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRM---------------ELETIKKFEVQHSEGYR 122
Cdd:COG3883 57 QAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYldvllgsesfsdfldRLSALSKIADADADLLE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 123 QISALEDDLAQTKA----IKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ 198
Cdd:COG3883 137 ELKADKAELEAKKAeleaKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 199 RLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTP 278
Cdd:COG3883 217 AAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
|
250
....*....|.
gi 2462549449 279 AARISALNIVG 289
Cdd:COG3883 297 GAASGGSGGGS 307
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-211 |
1.78e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 44 EEEANYWKDLAMTYKQRAENTQEELREFQE------GSREYEAELETQL-------QQIETRN--RDLLSENNRLRMEL- 107
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSklaelkERIESLERIRTLLaaiadaeDEIERLRekREALAELNDERRERl 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 108 ----ETIKKFEVQHSEGyrQISALEDDLAQTKAIKDQLQKYIRELEQANDDLErakrATIMSLEDFEQRLNQAIERNAFL 183
Cdd:PRK02224 630 aekrERKRELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQ----AEIGAVENELEELEELRERREAL 703
|
170 180
....*....|....*....|....*...
gi 2462549449 184 ESELDEKENLLESVQRLKDEARDLRQEL 211
Cdd:PRK02224 704 ENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
56-221 |
1.80e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 56 TYKQRAENTQEELREFQEGSREYE------------AELETQLQQIETRNRDLLSENNRLRMELETIKKfEVQHSEGYRQ 123
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVDlseeaklllqqlSELESQLAEARAELAEAEARLAALRAQLGSGPD-ALPELLQSPV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 124 ISALEDDLAQTKA-IKDQLQKY------IRELEQANDDLERAKRATI-MSLEDFEQRLNQAIERNAFLESELDEKENLLE 195
Cdd:COG3206 265 IQQLRAQLAELEAeLAELSARYtpnhpdVIALRAQIAALRAQLQQEAqRILASLEAELEALQAREASLQAQLAQLEARLA 344
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462549449 196 SVQRLKDEARDL-----------------RQELAVQQKQEKPR 221
Cdd:COG3206 345 ELPELEAELRRLerevevarelyesllqrLEEARLAEALTVGN 387
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
33-221 |
1.83e-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: 43.67 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 33 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREyeaELETQLQQIETRNRDLLSENNRLRMELETIKK 112
Cdd:pfam12128 641 ETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLN---SLEAQLKQLDKKHQAWLEEQKEQKREARTEKQ 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 113 FEVQHSEGYR--QISALEDDLA----QTKAIKDQLQK-YIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIER 179
Cdd:pfam12128 718 AYWQVVEGALdaQLALLKAAIAarrsGAKAELKALETwYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRY 797
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462549449 180 NAFLESE-LDEKENLLESVQRLKDEARDLRQELAVQQKQEKPR 221
Cdd:pfam12128 798 FDWYQETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-212 |
2.59e-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: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 43 EEEEANYWKDLAMtykQRAENTQEELREFqegsREYEAELETQLQQIETRNRDLLSENNRLRMELETIKK----FEVQHS 118
Cdd:TIGR02169 778 EEALNDLEARLSH---SRIPEIQAELSKL----EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEqridLKEQIK 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 119 EGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQaiernafLESELDEKENLLEsvq 198
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------LEAQIEKKRKRLS--- 920
|
170
....*....|....
gi 2462549449 199 RLKDEARDLRQELA 212
Cdd:TIGR02169 921 ELKAKLEALEEELS 934
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
33-219 |
3.17e-04 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 41.66 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 33 MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREF--QEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETI 110
Cdd:PRK14160 1 MEKECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIekEEIIEDSEESNEVKIEELKDENNKLKEENKKLENELEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 111 KKFEVQHS---EGYRQISALEDDLAQTKAIKDQLQKYIRELeqanDDLERAKrATIMSLEDFEQRLNQAIE--RNAF--- 182
Cdd:PRK14160 81 KDRLLRTVaeyDNYRKRTAKEKEGIYSDACEDVLKELLPVL----DNLERAA-AVEGSVEDLKKGIEMTVKqfKTSLekl 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462549449 183 ----LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 219
Cdd:PRK14160 156 gveeISTEGEFDPNLHNAVMHVEDENYGENEIVEVFQKGYK 196
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
66-218 |
3.48e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 66 EELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEddlAQTKAIKDQLQKYI 145
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELK---KQNNQLKDNIEKKQ 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549449 146 RELEQANDDLERAkratimsledfEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQ------QKQE 218
Cdd:TIGR04523 239 QEINEKTTEISNT-----------QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnnQKEQ 306
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
65-227 |
3.48e-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: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 65 QEELREFQEGSREYEAELEtQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYR---QISALE---DDLAQTKAIK 138
Cdd:COG4913 616 EAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEleaELERLDassDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 139 DQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIER--------NAFLESELDEK--------------ENLLES 196
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlaRLELRALLEERfaaalgdaverelrENLEER 774
|
170 180 190
....*....|....*....|....*....|.
gi 2462549449 197 VQRLKDEARDLRQELAVQQKQEKPRTPMPSS 227
Cdd:COG4913 775 IDALRARLNRAEEELERAMRAFNREWPAETA 805
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
54-203 |
3.83e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 54 AMTYKQRAENTQEElrEFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQ 133
Cdd:PRK12704 51 AEAIKKEALLEAKE--EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549449 134 TKA-IKDQLQKYIRELEQ-ANDDLERAKRATIMSLEDfEQRLNQA-----IERNAFLESELDEKENLLESVQRLKDE 203
Cdd:PRK12704 129 KEEeLEELIEEQLQELERiSGLTAEEAKEILLEKVEE-EARHEAAvlikeIEEEAKEEADKKAKEILAQAIQRCAAD 204
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
57-219 |
3.96e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 57 YKQRAENTQEELREFQEGSREYEAELETQLQQIETRN---RDLLSENNRLRMELETIKKFEVQHSEgyrQISALEDdlaQ 133
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNseiKDLTNQDSVKELIIKNLDNTRESLET---QLKVLSR---S 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 134 TKAIKDQLQKYIRELEQANDDLERAKRATIMS---LEDFEQRLNQAIERNAFLESELDEKENLLESvqrLKDEARDLRQE 210
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISD---LEDELNKDDFE 553
|
170
....*....|....*.
gi 2462549449 211 L-------AVQQKQEK 219
Cdd:TIGR04523 554 LkkenlekEIDEKNKE 569
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
169-224 |
4.45e-04 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 40.72 E-value: 4.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549449 169 FEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPM 224
Cdd:COG3166 43 LQGQIAQQQARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQSRPPW 98
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
51-233 |
5.23e-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: 42.02 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 51 KDLAMTYKQRAENTQEELR----EFQEGSREYE----------AELEtQLQQIETRNRDLLSENNRLRMELETIKKFEvQ 116
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKiitmELQKKSSELEemtkfknnkeVELE-ELKKILAEDEKLLDEKKQFEKIAEELKGKE-Q 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 117 HSEGYRQISALE--DDLAQTKAIKDQLQKYIRELEQANDDLERAKRATI--------MSLEDFE------------QRLN 174
Cdd:pfam05483 440 ELIFLLQAREKEihDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIeltahcdkLLLENKEltqeasdmtlelKKHQ 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 175 QAIERNAFLESE-LDEKENLLESVQRLKDEARDLRQELavQQKQEKPRTPMPSSVEAERT 233
Cdd:pfam05483 520 EDIINCKKQEERmLKQIENLEEKEMNLRDELESVREEF--IQKGDEVKCKLDKSEENARS 577
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
80-265 |
7.21e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.25 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 80 AELETQLQQIETRNRDLLSENNRLRMEletIKKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAK 159
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAE---LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 160 -RATI--MSLEDF-EQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQekprtpmPSSVEAERTDT 235
Cdd:pfam00529 131 vLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQ-------IAEAEAELKLA 203
|
170 180 190
....*....|....*....|....*....|
gi 2462549449 236 AVQATGSVPSTPIAHRGPSSSLNTPGSFRR 265
Cdd:pfam00529 204 KLDLERTEIRAPVDGTVAFLSVTVDGGTVS 233
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
58-217 |
8.47e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKfevqhsegyrQISALEDDLAQTkai 137
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE----------ELEQLEEELEQA--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 138 KDQLQKYIRELEQANDDLERAKRatimSLEDFEQRLNQAIERNAFLESELD----EKENLLESVQRLKDEARDLRQELAV 213
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQA----ELAQAQEELESLQEEAEELQEELEelqkERQDLEQQRKQLEAQIAELQSEIAE 147
|
....
gi 2462549449 214 QQKQ 217
Cdd:COG4372 148 REEE 151
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
76-112 |
1.02e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 40.97 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2462549449 76 REYEAELETQLQQIETRNRDLLSENNRLRMELETIKK 112
Cdd:PRK03992 7 EERNSELEEQIRQLELKLRDLEAENEKLERELERLKS 43
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-207 |
1.26e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAI 137
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549449 138 KDQLQKYIRELEQANDDLERAKRATIMSLEDFEqrlnQAIERNAFLESELD----EKENLLESVQRLKDEARDL 207
Cdd:COG1196 759 PPDLEELERELERLEREIEALGPVNLLAIEEYE----ELEERYDFLSEQREdleeARETLEEAIEEIDRETRER 828
|
|
| PRKG1_interact |
pfam15898 |
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ... |
128-207 |
1.39e-03 |
|
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.
Pssm-ID: 464927 [Multi-domain] Cd Length: 102 Bit Score: 37.67 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 128 EDDLAQTKAIKDQLQKYIRELEQANDDLERA---------KRATIMSLEDFEQRlnqAIERNAF-LESELDEKENLLESV 197
Cdd:pfam15898 7 EEELQENERLKRKLQDAQQELAELKSQLERLtqqrqesfsDRSSLLETEKREKR---ALERKISeMEEELKVLEDLRAEN 83
|
90
....*....|
gi 2462549449 198 QRLKDEARDL 207
Cdd:pfam15898 84 QRLKDENGAL 93
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
62-216 |
1.45e-03 |
|
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: 40.86 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 62 ENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIkKFEVQHSEGYRQisALEDDLAQTKAIKDQL 141
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDI-KMSLQRSMSTQK--ALEEDLQIATKTICQL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 142 QKyirELEQANDDLERAK----------RATIMSLEDF----EQRLNQAIERNAFLESELDEKENLLESVQRLKD----E 203
Cdd:pfam05483 330 TE---EKEAQMEELNKAKaahsfvvtefEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnkevE 406
|
170
....*....|...
gi 2462549449 204 ARDLRQELAVQQK 216
Cdd:pfam05483 407 LEELKKILAEDEK 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
58-216 |
1.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREyeaELETQLQQIETRNRDLLSENN---RLRMELETIKKFEvqhsegyRQISALEDDLAQT 134
Cdd:PRK03918 569 EEELAELLKELEELGFESVE---ELEERLKELEPFYNEYLELKDaekELEREEKELKKLE-------EELDKAFEELAET 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 135 KAIKDQLQKYIRELEQANDDLE-RAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAV 213
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEE---LEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
...
gi 2462549449 214 QQK 216
Cdd:PRK03918 716 LEK 718
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
58-222 |
1.82e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNR--DLLSENNRLRMELETIKKFEVQHSEGYRQISALEddLAQTK 135
Cdd:pfam02463 148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLE--LEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 136 AIKDQLQKYIRELEQANDDLERAKRATIMSLedfEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 215
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELLRDEQEEIESS---KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
....*..
gi 2462549449 216 KQEKPRT 222
Cdd:pfam02463 303 LKLERRK 309
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
60-218 |
1.86e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 60 RAENTQEELrefqEGSREYEAELetqLQQIETRNRDLLSENNRLRMELEtikKFEVQHSEGYRQISALEDDLAQTKAIKD 139
Cdd:pfam07888 28 RAELLQNRL----EECLQERAEL---LQAQEAANRQREKEKERYKRDRE---QWERQRRELESRVAELKEELRQSREKHE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549449 140 QLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLEsvqRLKDEARdlrqELAVQQKQE 218
Cdd:pfam07888 98 ELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE---RMKERAK----KAGAQRKEE 169
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
43-216 |
1.86e-03 |
|
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: 40.48 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 43 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETR-------NRDLLSENNRLRMELETIKKFEV 115
Cdd:pfam05483 86 EAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKleeeiqeNKDLIKENNATRHLCNLLKETCA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 116 QHSEGYRQISALEDDLAQTKA-IKDQLQKYIRELEQANDDLERAKRATIMSL-----------EDFEQRLNQAIERNAFL 183
Cdd:pfam05483 166 RSAEKTKKYEYEREETRQVYMdLNNNIEKMILAFEELRVQAENARLEMHFKLkedhekiqhleEEYKKEINDKEKQVSLL 245
|
170 180 190
....*....|....*....|....*....|...
gi 2462549449 184 ESELDEKENLLESVQRLKDEARDLRQELAVQQK 216
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTK 278
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
122-217 |
1.87e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 122 RQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAfLESELDEKENLLES----- 196
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREA----LQRLAEYSWDEIDVAS-AEREIAELEAELERldass 684
|
90 100
....*....|....*....|...
gi 2462549449 197 --VQRLKDEARDLRQELAVQQKQ 217
Cdd:COG4913 685 ddLAALEEQLEELEAELEELEEE 707
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
52-239 |
1.89e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 39.42 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 52 DLAMTYKQRAENTQEELREFQegsREYEAELETQLQqiETRNRDLLSENNRLRMELET--IKKF-------EVQHSEGYR 122
Cdd:pfam17045 74 ELVAKYEQQLQKLQEELSKLK---RSYEKLQRKQLK--EAREEAKSREEDRSELSRLNgkLEEFrqkslewEQQRLQYQQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 123 QISALEddlAQTKAIKDQL-----QKYIRELEQANDDLErAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL-ES 196
Cdd:pfam17045 149 QVASLE---AQRKALAEQSsliqsAAYQVQLEGRKQCLE-ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELgDS 224
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462549449 197 VQRLKDEARDLRQELAVQQKQEKPRtpmpsSVEAERTDTAVQA 239
Cdd:pfam17045 225 NRKLLEEQQRLLEELRMSQRQLQVL-----QNELMELKATLQS 262
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-216 |
2.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 42 SEEEEanywKDLAMTYKQRAENTQEELREFQEGSREYEAE---LETQLQQIET--RNRDLLSENNRLRMELETIKKFEV- 115
Cdd:PRK03918 446 TEEHR----KELLEEYTAELKRIEKELKEIEEKERKLRKElreLEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELe 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 116 QHSEGYR-----------QISALEDDLAQTKAIKDQLQKYIRELEQANDDLE----RAKRATIMSLEDFE---QRLNQAI 177
Cdd:PRK03918 522 KKAEEYEklkekliklkgEIKSLKKELEKLEELKKKLAELEKKLDELEEELAellkELEELGFESVEELEerlKELEPFY 601
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462549449 178 ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 216
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
173-235 |
2.02e-03 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 39.58 E-value: 2.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549449 173 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVqqKQEKPRTPMPSSVEAERTDT 235
Cdd:PRK13922 71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNL--KESLDYQFITARVISRSPDP 131
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
53-219 |
2.25e-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: 40.16 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 53 LAMTYKQRA-ENTQEELREFQEGSREYEAELETQLQqieTRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDL 131
Cdd:pfam01576 485 LNLSTRLRQlEDERNSLQEQLEEEEEAKRNVERQLS---TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 132 AQTKAIKDQLQKYIRELEQANDDLERA---KRATIMSLEDFEQRLNQ--AIERNAFL---------ESELDEKENLLESV 197
Cdd:pfam01576 562 EEKAAAYDKLEKTKNRLQQELDDLLVDldhQRQLVSNLEKKQKKFDQmlAEEKAISAryaeerdraEAEAREKETRALSL 641
|
170 180
....*....|....*....|..
gi 2462549449 198 QRLKDEARDLRQELAVQQKQEK 219
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLR 663
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
73-221 |
2.34e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 73 EGSREYEAELETQLQQIETRNRDLLSENNRLrmelETIKKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQAN 152
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERA----EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 153 DDLE---RAKRA--------------TIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLkdeaRDLRQELAVQQ 215
Cdd:PRK02224 547 AELEaeaEEKREaaaeaeeeaeeareEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERL----REKREALAELN 622
|
....*.
gi 2462549449 216 KQEKPR 221
Cdd:PRK02224 623 DERRER 628
|
|
| GrpE |
pfam01025 |
GrpE; |
79-158 |
2.58e-03 |
|
GrpE;
Pssm-ID: 425996 [Multi-domain] Cd Length: 165 Bit Score: 38.36 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 79 EAELETQLQQIETRNRDLLSENNRLRMELETIKKFevqhsegyrqisaLEDDLAqtKAIKDQLQKYIRELEQANDDLERA 158
Cdd:pfam01025 13 IESLEEEIEELEKKIEELKEKLLRALAEFENLRKR-------------TEKEKE--EAKKFAIEKFAKDLLPVIDNLERA 77
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
56-217 |
2.89e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 56 TYKQRAENTQEELREFQEGSREYEAELETQLQQIEtrNRDLLSENNRLRMEL----ETIKKFEVQHSEGYRQISALED-- 129
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELaeldEEIERYEEQREQARETRDEADEvl 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 130 --------DLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 201
Cdd:PRK02224 244 eeheerreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD 323
|
170
....*....|....*.
gi 2462549449 202 DEARDLRQELAVQQKQ 217
Cdd:PRK02224 324 EELRDRLEECRVAAQA 339
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
80-217 |
3.04e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.23 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 80 AELETQ-------LQQIETRNRDLLSENNRLRMELETIKKFEVQhsegyrqisaLEDDLAQTKAIKDQLQKYIRELEQAN 152
Cdd:smart00787 126 ARLEAKkmwyewrMKLLEGLKEGLDENLEGLKEDYKLLMKELEL----------LNSIKPKLRDRKDALEEELRQLKQLE 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549449 153 DDLERAKRATIMSL-EDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQ 217
Cdd:smart00787 196 DELEDCDPTELDRAkEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
58-202 |
3.50e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.55 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELE----------TQLQQ---IETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQI 124
Cdd:COG3096 305 QYRLVEMARELEELSARESDLEQDYQaasdhlnlvqTALRQqekIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 125 SALEDDLaqtKAIKDQLQKYIRELE----------QANDDLERAKR---ATIMSLEDFEQRLNQAIERnaflESELDEKe 191
Cdd:COG3096 385 EAAEEEV---DSLKSQLADYQQALDvqqtraiqyqQAVQALEKARAlcgLPDLTPENAEDYLAAFRAK----EQQATEE- 456
|
170
....*....|.
gi 2462549449 192 nLLESVQRLKD 202
Cdd:COG3096 457 -VLELEQKLSV 466
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
14-210 |
3.84e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 14 KEIL-RHHATRRVISSPVFTMEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETR 92
Cdd:PRK02224 240 DEVLeEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 93 N------RDLLSE--------NNRLRMELETIKKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERA 158
Cdd:PRK02224 320 EdrdeelRDRLEEcrvaaqahNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462549449 159 KRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQE 210
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-212 |
4.65e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 59 QRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKKFEVQHSEGYRQISALEDDLAQtkAIK 138
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE--NLE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 139 DQLQKYIRELEQANDDLERAKR--------------ATIMSLEDFEQRLNQAIE----------RNAFLESELDEKENLL 194
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEdglpeyeerfKELLNENSIEFVADLL 852
|
170
....*....|....*...
gi 2462549449 195 esvQRLKDEARDLRQELA 212
Cdd:COG4913 853 ---SKLRRAIREIKERID 867
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
115-218 |
4.65e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 37.51 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 115 VQHSEGYRQISA-LEddlAQTKAIKDQLQKYIRELEQANDDLEraKRATIMSLEDFEQRlnqaiernaflESELDEKEnl 193
Cdd:COG2825 35 LQESPEGKAAQKkLE---KEFKKRQAELQKLEKELQALQEKLQ--KEAATLSEEERQKK-----------ERELQKKQ-- 96
|
90 100
....*....|....*....|....*
gi 2462549449 194 lesvQRLKDEARDLRQELAVQQKQE 218
Cdd:COG2825 97 ----QELQRKQQEAQQDLQKRQQEL 117
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
43-219 |
4.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 43 EEEEANYWKDLAMTYKQRAENTQEELREFQEGSREyEAELETQLQQIETRNRDLLSENNRLRMEL-----ETIKKFEVQH 117
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK-LAELEKKLDELEEELAELLKELEELGFESveeleERLKELEPFY 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 118 SEGYRQISA---LEDDLAQTKAIKDQLQKYIRELEQANDDLERAKR-----ATIMSLEDFEQRLNQAIERNAFLESELDE 189
Cdd:PRK03918 602 NEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKeleelEKKYSEEEYEELREEYLELSRELAGLRAE 681
|
170 180 190
....*....|....*....|....*....|
gi 2462549449 190 KENLLESVQRLKDEARDLRQELAVQQKQEK 219
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
123-218 |
5.62e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 37.22 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 123 QISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ---- 198
Cdd:pfam08614 58 LLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQdelv 137
|
90 100 110
....*....|....*....|....*....|....
gi 2462549449 199 --------------RLKDEARDLRQELaVQQKQE 218
Cdd:pfam08614 138 alqlqlnmaeeklrKLEKENRELVERW-MKRKGQ 170
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
32-175 |
6.40e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.07 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 32 TMEDSGKTFSSEEEEANywkDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIEtrnrdllsenNRLRMELETIK 111
Cdd:smart00787 155 GLKEDYKLLMKELELLN---SIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAK----------EKLKKLLQEIM 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549449 112 KFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQandDLERAKRATIMSLEDFEQRLNQ 175
Cdd:smart00787 222 IKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEK---KLEQCRGFTFKEIEKLKEQLKL 282
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
12-239 |
6.52e-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: 38.56 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 12 SRKEILRHHATRrvISSPVFTMEDSGKTFS------SEEEEANYWKDLAMT-YKQRAENTQEELREFQ-EGSREYEAELE 83
Cdd:pfam15921 472 STKEMLRKVVEE--LTAKKMTLESSERTVSdltaslQEKERAIEATNAEITkLRSRVDLKLQELQHLKnEGDHLRNVQTE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 84 TQLQQIETRNRDLLSEnnRLRMELETIKKFEVQH-----------SEGYRQISALEDDLAQTKAIKDQLQKYIRELEQAN 152
Cdd:pfam15921 550 CEALKLQMAEKDKVIE--ILRQQIENMTQLVGQHgrtagamqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 153 DDLE-------RAKRATIMSLEDFEQRLNQAIERNAFLESELDekeNLLESVQRLKDEARDLRQELAVQQKQEKPRTPMP 225
Cdd:pfam15921 628 SDLElekvklvNAGSERLRAVKDIKQERDQLLNEVKTSRNELN---SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSA 704
|
250
....*....|....
gi 2462549449 226 SSvEAERTDTAVQA 239
Cdd:pfam15921 705 QS-ELEQTRNTLKS 717
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
94-219 |
7.08e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 37.19 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 94 RDLLSENNRLRMELETIKKFEvQHSEgyRQISALEddlAQTKAIKDQLQKYIRELEQANDDLERAKRAtIMSLEDFEQRL 173
Cdd:pfam13851 22 RNNLELIKSLKEEIAELKKKE-ERNE--KLMSEIQ---QENKRLTEPLQKAQEEVEELRKQLENYEKD-KQSLKNLKARL 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462549449 174 NQAIERNAFLESELDEKENLLESVQRLKDEARDlRQELAVQQKQEK 219
Cdd:pfam13851 95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYD-KFEAAIQDVQQK 139
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
51-212 |
7.71e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 38.13 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 51 KDLAMTYKQRAEnTQEELREFQEGSREYEAE---LETQLQQIET--------------RNR---------------DLLS 98
Cdd:COG0497 158 EEYREAYRAWRA-LKKELEELRADEAERAREldlLRFQLEELEAaalqpgeeeeleeeRRRlsnaeklrealqealEALS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 99 EN--------NRLRMELETIkkfeVQHSEGYRQIS-ALEDDLAQTKAIKDQLQKYIRELEQandDLERakratimsLEDF 169
Cdd:COG0497 237 GGeggaldllGQALRALERL----AEYDPSLAELAeRLESALIELEEAASELRRYLDSLEF---DPER--------LEEV 301
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549449 170 EQRLNQ--------------AIERNAFLESELDEKENLLESVQRLKDEARDLRQELA 212
Cdd:COG0497 302 EERLALlrrlarkygvtveeLLAYAEELRAELAELENSDERLEELEAELAEAEAELL 358
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
81-231 |
7.96e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 38.13 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 81 ELETQLQQIETRNRDLLSENNRLRMELETIKKFE-------VQHSEGYRQISALEDDLAQTKAIKD-------QLQKYIR 146
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDdsgtpggKKYLLLQKQLEQLQEENFRLETARDdyrikceELEKEVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 147 ELEQANDDLERAKrATIMSLEDFEQRLNQAIERNAFLESeldekenLLESVQRLKDEARDLRQElaVQQKQEKPRTPMPS 226
Cdd:pfam05622 98 ELQHRNEELTSLA-EEAQALKDEMDILRESSDKVKKLEA-------TVETYKKKLEDLGDLRRQ--VKLLEERNAEYMQR 167
|
....*
gi 2462549449 227 SVEAE 231
Cdd:pfam05622 168 TLQLE 172
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
81-227 |
8.34e-03 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 37.63 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 81 ELETQLQQIETRNRDLlSENNRLRMELETIKKFEVQHSEGYRQI-SALEDDLAQTKAIKDQLQKYIRELEQANDDLERAK 159
Cdd:pfam15934 76 HQIKQLQSMITGYSDI-SENNRLKEEIHDLKQKNCVQARVVRKMgLELKGQEEQRVELCDKYESLLGSFEEQCQELKRAN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 160 RatimSLEDFEQRLNQaIERnafLESELDEKENLL-ESVQRLKD-EARDLRQELAVQQKQEKPRTPMPSS 227
Cdd:pfam15934 155 R----RVQSLQTRLSQ-VEK---LQEELRTERKILrEEVIALKEkDAKSNGRERALQDQLKCCQTEIEKS 216
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
59-189 |
8.62e-03 |
|
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: 38.12 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 59 QRAENTQEELREFQEGSREYEAEL----------ETQLQQIETRNRDLLSENNRLRMELETIKKfEVQHSEGYR-----Q 123
Cdd:pfam19220 90 ARLAKLEAALREAEAAKEELRIELrdktaqaealERQLAAETEQNRALEEENKALREEAQAAEK-ALQRAEGELatareR 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549449 124 ISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDE 189
Cdd:pfam19220 169 LALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEE 234
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
58-203 |
8.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.12 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549449 58 KQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRlrmelETIKKFEVQHSEGYRQISALEDDLAQTKAI 137
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEYLELSRELAGLRAELEELEKR 688
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549449 138 KDQLQKYIRELEQANDDLERAKratiMSLEDFEQRLNQAIE-RNAFLESELDEKENLLESVQRLKDE 203
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAK----KELEKLEKALERVEElREKVKKYKALLKERALSKVGEIASE 751
|
|
| |
