|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
33-277 |
5.01e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 33 ELKNTERTQKLQEEKIKSEAEALERREQNLKN--IEDTYDQKLKTELLKYQLELKDDYITRTNKLLEEERKNKEKTIHLQ 110
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 111 EELTVINSKKEELSKSVKHMKEVELELESVKAQflAISKQNHLLNEKVREMSDYSQLKEEKVELQAQNKLLKLQLEETRN 190
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 191 ENLRLLDRITqpppELVIFQKELQKTEKAMELEHKDFETHRQALEKQLQSEIENSAQLRTQIAEYDASVKRLTVQVAELK 270
Cdd:COG1196 422 ELEELEEALA----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
....*..
gi 1907203673 271 SQLKQTQ 277
Cdd:COG1196 498 EAEADYE 504
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
24-199 |
5.61e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.94 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 24 FLRRRILWKELKNTERTQKLQEEKIKSEAEALeRREQNLKniedtydqkLKTELLKYQLELKDDYITRTNKLLEEERKNK 103
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAI-KKEALLE---------AKEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 104 EKTIHLQEELTVINSKKEELSKSVKHMKEVELELESVKAqflaisKQNHLLNEKVREMSDYSQLKEEkvelQAQNKLLKL 183
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEE------ELEELIEEQLQELERISGLTAE----EAKEILLEK 162
|
170
....*....|....*.
gi 1907203673 184 QLEETRNENLRLLDRI 199
Cdd:PRK12704 163 VEEEARHEAAVLIKEI 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-281 |
6.09e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 32 KELKNTERTQKLQEEKIKS---EAEALERREQNLKNIEDTYdQKLKTELLKYQLELKDDYITRTNKLLEEERKNKEKTIH 108
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAElekALAELRKELEELEEELEQL-RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 109 LQEELTVINSKKEELSKSVKHMKEVELELESVKAQFLAISKQNHLLNEKVREMSD-YSQLKEEKVELQAQNKLLKLQLEE 187
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeLTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 188 TRNENLRLLDRITQPPPELVIFQKELQKTEKAMELEHKDFETH---RQALEKQLQSEIENSAQLRTQIAEYDASVKRLTV 264
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlneRASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250
....*....|....*..
gi 1907203673 265 QVAELKSQLKQTQIALE 281
Cdd:TIGR02168 916 ELEELREKLAQLELRLE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
25-286 |
8.87e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 25 LRRRILWKELKNTERTQKLQEEKIKSEAEALERREQNLKNIEDTYDQkLKTELLKYQLELKD------DYITRTNKLLEE 98
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEaqaeeyELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 99 ERKNKEKTIHLQEELT-----------VINSKKEELSKSVKHMKEVELELESVKAQFLAISKQNHLLNEKVRE-MSDYSQ 166
Cdd:COG1196 304 IARLEERRRELEERLEeleeelaeleeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 167 LKEEKVELQAQNKLLKLQLEETRNENLRLLDRitqpppelvifQKELQKTEKAMELEHKDFETHRQALEKQLQSEIENSA 246
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLER-----------LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907203673 247 QLRTQIAEYDASVKRLTVQVAELKSQLKQTQIALENEVYR 286
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-277 |
3.61e-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: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 71 QKLKTELLKYQLELkddYITRTNKLLEEERKNKEKTIHLQEELTVINSKKEELSKSVKhmkEVELELESVKAQFLAISKQ 150
Cdd:TIGR02168 216 KELKAELRELELAL---LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE---ELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 151 NHLLNEKVREM-SDYSQLKEEKVELQAQNKLLKLQLEETRNENLRLLDRITQPPPELVIFQKELQKTE---KAMELEHKD 226
Cdd:TIGR02168 290 LYALANEISRLeQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEaelEELEAELEE 369
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907203673 227 FETHRQALEKQLQSEIENSAQLRTQIAEYDASVKRLTVQVAELKSQLKQTQ 277
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-256 |
5.79e-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: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 26 RRRILWKELKNTERTQKLQEEKIKSEAEALERREQNLKNIEDTyDQKLKTELLKYQLELKDdyitrtnkLLEEERKNKEK 105
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE-LEELEEELEELEEELEE--------AEEELEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 106 TIHLQEELTVINSKKEELSKSVKHMKEVELELESVKAQFLAisKQNHLLNEKVREMSDYSQLKEEKVELQAQNKLLKLQL 185
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA--QLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907203673 186 EETRNENLRLLDRITQpppelviFQKELQKTEKAMELEHKDFETHRQALEKQLQSEIENSAQLRTQIAEYD 256
Cdd:COG1196 438 EEEEEALEEAAEEEAE-------LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-275 |
2.30e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 38 ERTQKLQEEK-----IKSEAEALERREQNLKN-IED--TYDQKLKTELLKYQLELKDdyitrtnklLEEERKNKEKTIH- 108
Cdd:TIGR02169 706 ELSQELSDASrkigeIEKEIEQLEQEEEKLKErLEEleEDLSSLEQEIENVKSELKE---------LEARIEELEEDLHk 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 109 LQEELtviNSKKEELSKSvkHMKEVELELESVKAQFLAISKQ-NHLLNEKVREMSDYSQLKEEKVELQAQNKLLKLQLEE 187
Cdd:TIGR02169 777 LEEAL---NDLEARLSHS--RIPEIQAELSKLEEEVSRIEARlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 188 TRNENLRLLDRITQPPPELvifqKELQKTEKAMELEHKDFETHRQALEKQLQSEIENSAQLRTQIAEYDASVKRLTVQVA 267
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEEL----EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
....*...
gi 1907203673 268 ELKSQLKQ 275
Cdd:TIGR02169 928 ALEEELSE 935
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-264 |
2.39e-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: 48.13 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 32 KELKNTERTQKLQEEKIKSEAEALERREQNLKNIEDtYDQKLKTELLKYQLEL-------------------KDDYITRT 92
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRL-EVSELEEEIEELQKELyalaneisrleqqkqilreRLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 93 NKLLEEER-KNKEKTIHLQEELTVINSKKEELSKSVKHMKEvelELESVKAQFLAISKQNHLLNEKVREM-SDYSQLKEE 170
Cdd:TIGR02168 318 LEELEAQLeELESKLDELAEELAELEEKLEELKEELESLEA---ELEELEAELEELESRLEELEEQLETLrSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 171 KVELQAQNKLLKLQLEETRNENLRLLDRITQPPPELVIFQKELQKT---EKAMELEH--KDFETHRQALEKQLQSEIENS 245
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAeleELEEELEElqEELERLEEALEELREELEEAE 474
|
250
....*....|....*....
gi 1907203673 246 AQLRTQIAEYDASVKRLTV 264
Cdd:TIGR02168 475 QALDAAERELAQLQARLDS 493
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
60-262 |
3.61e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.14 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 60 QNLKNIEDTYdQKLKTEllKYQLELKDdyITRTNKLLEEERKNKEKTI------HLQEELTVINSKKEEL----SKSVKH 129
Cdd:PRK04778 230 DQLQELKAGY-RELVEE--GYHLDHLD--IEKEIQDLKEQIDENLALLeeldldEAEEKNEEIQERIDQLydilEREVKA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 130 MKEVELELESVKAQFLAISKQNHLLNEKVREMSDYSQLKEEkvELQAQNKLLKlQLEETRNENLRLLDRI---TQPPPEL 206
Cdd:PRK04778 305 RKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNES--ELESVRQLEK-QLESLEKQYDEITERIaeqEIAYSEL 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907203673 207 VIFQKELQKTEKAMELEHKDFETHRQALEKQLQSEIENSAQLRTQIAEydasVKRL 262
Cdd:PRK04778 382 QEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHE----IKRY 433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
93-283 |
4.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 93 NKLLEEERKNKEKTIHLQEELTVINSKKEELSKSVKHMKEVELELESVKAQFLAISKQNHLLNEKVREMSDYSQLKE--- 169
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyq 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 170 EKVELQAQNKLLKLQLEETRNENLRLLDRITQpppeLVIFQKELQKTEKAMELEHKDFethRQALEKQLQSEIENSAQLR 249
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQL---SLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|....
gi 1907203673 250 TQIAEYDASVKRLTVQVAELKSQLKQTQIALENE 283
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-271 |
9.26e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 26 RRRILWKELKNTERTQKLQEEKIKSEAEALERREQNLKNIEDTYDQKLKTELLKYQLELKDDYITRTNKLLEEERKNKEK 105
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 106 tihLQEELTVINSKKEELSKSVKHMKEVELELESVKAQFLAISKQNHLLNEKV-------REMSDYSQLKEEKVELQAQN 178
Cdd:PRK03918 257 ---LEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLdelreieKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 179 KLLKLQLEETRNENLRLLDRITQPPPELVIFQKELQKTEKAMELEHKDFETHRQALEKQLQS------EIENS-AQLRTQ 251
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEElekakeEIEEEiSKITAR 413
|
250 260
....*....|....*....|
gi 1907203673 252 IAEYDASVKRLTVQVAELKS 271
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKK 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-282 |
1.25e-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: 45.40 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 45 EEKIKSEAEALERREQNLKNIEDTYdqKLKTELLKYQLELKDDYITRTNKLLEEERKNKEKTIHLQEELTVINS------ 118
Cdd:TIGR04523 39 EKKLKTIKNELKNKEKELKNLDKNL--NKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSeikndk 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 119 -----KKEELSKSVKHMKEVELELESVKAQFLAISKQNHLLNEKvremsdYSQLKEEKVELQAQNKLLKLQLEETRNENL 193
Cdd:TIGR04523 117 eqknkLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK------YNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 194 RLLDRITQPPPELVIFQKELQKtEKAMELEHKDFETHRQALEKQLQSEIENSAQLRTQIAEYDASVKRLTVQVAELKSQL 273
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQK-NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
....*....
gi 1907203673 274 KQTQIALEN 282
Cdd:TIGR04523 270 SEKQKELEQ 278
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
32-274 |
1.26e-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: 45.40 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 32 KELKNTERTQKLQEEKIKSEAEALERREQNLKNIEDTYDQKLKTelLKYQLELKDDYITRtnkLLEEERKNKEKTIHLQE 111
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK--LQQEKELLEKEIER---LKETIIKNNSEIKDLTN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 112 ELTVINSKKEELSKSVKHMKEvelELESVKAQflaISKQNHLLNEKVREM----SDYSQLKEEKVELQAQNKLLKLQLEE 187
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLET---QLKVLSRS---INKIKQNLEQKQKELkskeKELKKLNEEKKELEEKVKDLTKKISS 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 188 TRNENLRLLDRITqpppelvifQKELQKTEKAMELEHKDFETHRQALEKQLQSEIENSAQLRTQIAEYDASVKRLTVQVA 267
Cdd:TIGR04523 522 LKEKIEKLESEKK---------EKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
....*..
gi 1907203673 268 ELKSQLK 274
Cdd:TIGR04523 593 QKEKEKK 599
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
44-288 |
1.86e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 44 QEEKIKSEAEALERREQNLKNIEDTYDQ-KLKTELLKYQLELKDDYITRTNKLLEEerknkektihLQEELTVINSKKEE 122
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAAlKKEEKALLKQLAALERRIAALARRIRA----------LEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 123 LSKSVKHMKEvelelesvkaqflAISKQNHLLNEKVREMSDYSQLKEEKVELQAQN-----KLLKLqLEETRNENLRLLD 197
Cdd:COG4942 88 LEKEIAELRA-------------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDfldavRRLQY-LKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 198 RITQPPPELVIFQKELQKTEKAMELEHKDFETHRQALEKQLQSEIENSAQLRTQIAEYDASVKRLTVQVAELKSQLKQTQ 277
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|.
gi 1907203673 278 IALENEVYRNP 288
Cdd:COG4942 234 AEAAAAAERTP 244
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
132-278 |
6.34e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.73 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 132 EVELELESVKAQFLAISKQNHLLNEKVREMSDYSQLKEEKVELQAQNKLLKLQLEetRNENLRLLDRITQpppelvifqk 211
Cdd:COG1566 80 DLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELE--RYQALYKKGAVSQ---------- 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907203673 212 elQKTEKAmELEHKDFETHRQALEKQLQsEIENSAQLRTQIAEYDASVKRLTVQVAELKSQLKQTQI 278
Cdd:COG1566 148 --QELDEA-RAALDAAQAQLEAAQAQLA-QAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTI 210
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
140-281 |
8.93e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 140 VKAQFL---AISKQNHLLNEKVREMSDYSQLkeekvelqaqnkllkLQLEETRNENLRllDRITQPPPELVIFQKE---L 213
Cdd:PRK09039 38 VVAQFFlsrEISGKDSALDRLNSQIAELADL---------------LSLERQGNQDLQ--DSVANLRASLSAAEAErsrL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907203673 214 QKTEKAMELEHKDFETHRQALEKQLQSEIENSAQLRTQIAeydasvkRLTVQVAELKSQLKQTQIALE 281
Cdd:PRK09039 101 QALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVE-------LLNQQIAALRRQLAALEAALD 161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-281 |
9.39e-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: 42.75 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 11 NLKELVKQKMKpsfLRRRILWKElKNTERTQKLQEEKIKSEAEALERREQNLKNIEDTYDQK---LKTELLKYQLELKDd 87
Cdd:TIGR02169 231 EKEALERQKEA---IERQLASLE-EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrVKEKIGELEAEIAS- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 88 yITRTNKLLEEERKNKEKTIHLQEELtvINSKKEELSKSVKHMKEVELELESVKAQFLAISKQNHLLNEKVREMSdySQL 167
Cdd:TIGR02169 306 -LERSIAEKERELEDAEERLAKLEAE--IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD--KEF 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 168 KEEKVEL-QAQNKLLKLQLEetRNENLRLLDRITQPPPELVIFQKELQKTEKAMELEHKDFETHRQALEKQLQSEIENSA 246
Cdd:TIGR02169 381 AETRDELkDYREKLEKLKRE--INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
250 260 270
....*....|....*....|....*....|....*
gi 1907203673 247 QLRTQIAEYDASVKRLTVQVAELKSQLKQTQIALE 281
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
3-196 |
9.75e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 3 RNWLSSRMNLKELVkQKMKpSFLRRRILWKELKNTERTQKLQE---------EKIKSEAEALERREQNLKNIEDTYDQKL 73
Cdd:PRK05771 46 RKLRSLLTKLSEAL-DKLR-SYLPKLNPLREEKKKVSVKSLEElikdveeelEKIEKEIKELEEEISELENEIKELEQEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 74 KT-ELLKY-----QLELKDDYITRTNKLLEEERKNKEKTIHLQEELTVINSKKEE----LSKSVKHMKEVELELEsvKAQ 143
Cdd:PRK05771 124 ERlEPWGNfdldlSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvVVVLKELSDEVEEELK--KLG 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907203673 144 FLAISkqnhlLNEKVREMSDYSQLKEEKVELQAQNKLLKLQLEETRNENLRLL 196
Cdd:PRK05771 202 FERLE-----LEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEEL 249
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-283 |
1.49e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 131 KEVELELESVKAQfLAISKQNHLLNEKVREMSDYSQLKEEKVELQAQNKLLKLQLEETRNENLRLLDRITQpppelviFQ 210
Cdd:COG1196 216 RELKEELKELEAE-LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE-------AQ 287
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907203673 211 KELQKTEKAMElehkdfethrqALEKQLQSEIENSAQLRTQIAEYDASVKRLTVQVAELKSQLKQTQIALENE 283
Cdd:COG1196 288 AEEYELLAELA-----------RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
60-262 |
1.68e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.76 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 60 QNLKNIEDTYDQklkteLLKYQLELKDDYITRTNKLLEEERKNKEKTIH------LQEELTVINSKKEEL----SKSVKH 129
Cdd:pfam06160 211 DQLEELKEGYRE-----MEEEGYALEHLNVDKEIQQLEEQLEENLALLEnleldeAEEALEEIEERIDQLydllEKEVDA 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 130 MKEVELELESVKAQFLAISKQNHLLNEKVREMSDYSQLKEEKVELQaqnKLLKLQLEETRNENLRLLDRI---TQPPPEL 206
Cdd:pfam06160 286 KKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELERV---RGLEKQLEELEKRYDEIVERLeekEVAYSEL 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907203673 207 VIFQKELQKTEKAMELEHKDFETHRQALEKQLQSEIENSAQLRTQIAEydasVKRL 262
Cdd:pfam06160 363 QEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELRE----IKRL 414
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
33-289 |
1.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 33 ELKNTERTQKLQEEKIKSEAealeRREQNLKNIEDTYDQKLKTELLKYQLELKDDYITRTNKLLEEERKNKEKTIHLQEE 112
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEA----KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 113 ltvinSKKEELSKSVKHMKEVELELESVKAQFLAISKQNHLLNEKVREMSDYSQLKEEKVELQAQNKLLKLQLEETRNEN 192
Cdd:PTZ00121 1626 -----KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 193 LRLLDRITQPPPELVIFQKELQKTE-----KAMELEHKDFETHRQALEKQLQSEIENSAQLRTQIAEYDASVKRLTVQvA 267
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEeenkiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE-A 1779
|
250 260
....*....|....*....|..
gi 1907203673 268 ELKSQLKQTQIALENEVYRNPK 289
Cdd:PTZ00121 1780 VIEEELDEEDEKRRMEVDKKIK 1801
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-283 |
2.40e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 9 RMNLKELVKQKMKPSFLRRRI--LWKELKNTERTQKLQEEKIKSEAEALERREQNLKNIEDTYDQKLKTELLKyqlELKD 86
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELesLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS---EFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 87 DYITRTNKLLEEERKNKEKTIHLQEELTVINSKKEELSKSVKHMKEVELELESVKAQFLAISKQNHLLNEKVREMSDYSQ 166
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 167 LKEEKVElqAQNKLLKLQLEETRNENLRLLDRITQPPPELVIFQKELQKTEKA--------MELEhkdfETHRQALEKQL 238
Cdd:PRK03918 384 LTPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgRELT----EEHRKELLEEY 457
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907203673 239 QSEIENSAqlrtqiaeydASVKRLTVQVAELKSQLKQTQIALENE 283
Cdd:PRK03918 458 TAELKRIE----------KELKEIEEKERKLRKELRELEKVLKKE 492
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
46-249 |
2.75e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 46 EKIKSEAEALERREQNLKNIedtydQKLKTELlKYQLELKDDYITRTNKLLEEERKNKEKTIHLQEELTVINSKKEELSK 125
Cdd:PRK03918 148 EKVVRQILGLDDYENAYKNL-----GEVIKEI-KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 126 SVKHMKEVELELESVKAQFLAISKQNHLLNEKVREmsdysqLKEEKVELQAQNKLLKLQLEETRnENLRLLDRITQPPPE 205
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKRK------LEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEE 294
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907203673 206 LVIFQKELQKTEKA---MELEHKDFETHRQALEKQLQSEIENSAQLR 249
Cdd:PRK03918 295 YIKLSEFYEEYLDElreIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
78-285 |
3.28e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 78 LKYQLELKDDYITRTNKLLEEER-----------------KNKEKTIHLQEELTVINSKKEELSKSVKhmkEVELELESV 140
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLpelrkeleeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLA---EARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 141 KAQFLAISKQNHLLNEKVREMSD---YSQLKEEKVELQAQnkLLKLQLEETRNEnlrlldritqppPELVIFQKELQKTE 217
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAE--LAELSARYTPNH------------PDVIALRAQIAALR 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907203673 218 KAMELEHKDFethRQALEKQLQSEIENSAQLRTQIAEYDASVKRLTVQVAELkSQLKQtQIALENEVY 285
Cdd:COG3206 305 AQLQQEAQRI---LASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL-RRLER-EVEVARELY 367
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
34-262 |
3.91e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 34 LKNTERTQKLQE-EKIKSEAEALERR----EQNL----KNIEDTYDQKLKTELLKYQLElkddyiTRTNKLLEEERKNKE 104
Cdd:PLN02939 146 LLNQARLQALEDlEKILTEKEALQGKinilEMRLsetdARIKLAAQEKIHVEILEEQLE------KLRNELLIRGATEGL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 105 KTIHLQEELTVINSKKEELSKSVKHMKEVELELESVKAQFLAISKQNHLLNEKVREM--------SDYSQLKE------- 169
Cdd:PLN02939 220 CVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELeskfivaqEDVSKLSPlqydcww 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 170 EKVE-LQ-----AQNKLLKLQLEETRNENLR-LLDRITQPPPELVIFQKELQKTEkAMELEHKDFETHRQALEKQLQSEI 242
Cdd:PLN02939 300 EKVEnLQdlldrATNQVEKAALVLDQNQDLRdKVDKLEASLKEANVSKFSSYKVE-LLQQKLKLLEERLQASDHEIHSYI 378
|
250 260
....*....|....*....|
gi 1907203673 243 ENSAQLrtqIAEYDASVKRL 262
Cdd:PLN02939 379 QLYQES---IKEFQDTLSKL 395
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-277 |
6.25e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 45 EEKIKSEAEALERREQNLKNIEDTYDQKLKtellkyQLELkddyitrtnklLEEERKNKEKTIHLQEEL-----TVINSK 119
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQ------QLER-----------LRREREKAERYQALLKEKreyegYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 120 KEELSKSV----KHMKEVELELESVKAQFLAISKQNHL-------LNEKVREMSD--YSQLKEEKVELQAQNKLLKLQLE 186
Cdd:TIGR02169 232 KEALERQKeaieRQLASLEEELEKLTEEISELEKRLEEieqlleeLNKKIKDLGEeeQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 187 ETRNENLRLLDRITQPPPELVIFQKELQKTEKAMELEHKDfethRQALEKQLQSEIENSAQLRTQIAEYDASVKRLTVQV 266
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250
....*....|.
gi 1907203673 267 AELKSQLKQTQ 277
Cdd:TIGR02169 388 KDYREKLEKLK 398
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
203-288 |
8.34e-03 |
|
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.
Pssm-ID: 464151 [Multi-domain] Cd Length: 295 Bit Score: 39.16 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 203 PPELVIFQKELQKTEKAMELEHKDfethrqALEKQLQseiensAQLRTQIAEYDASVKRLTVQVAELKSQLKQTQIALEN 282
Cdd:pfam14362 98 PLELKIFEKEIDRELLEIQQEEAD------AAKAQLA------AAYRARLAELEAQIAALDAEIDAAEARLDALQAEARC 165
|
....*.
gi 1907203673 283 EVYRNP 288
Cdd:pfam14362 166 ELDGTP 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-282 |
8.47e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 32 KELKNTERTQKL---QEEKIKSEAEALER---REQNLKNIEDTYDQ--KLKTELLKYQLE-LKDDYitrtnkllEEERKN 102
Cdd:PRK03918 459 AELKRIEKELKEieeKERKLRKELRELEKvlkKESELIKLKELAEQlkELEEKLKKYNLEeLEKKA--------EEYEKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 103 KEKTIHLQEELTVINSKKEELSKSVKHMKEVELELESVKaqflaiSKQNHLLNE-KVREMSDYSQLKEEKVELQ-AQNKL 180
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE------EELAELLKElEELGFESVEELEERLKELEpFYNEY 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203673 181 LKLQLEETRNEnlRLLDRITQPPPELVIFQKELQKTEKAMELEHKDFETHRQALEKQLQSEIENS-AQLRTQIAEYDASV 259
Cdd:PRK03918 605 LELKDAEKELE--REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEyLELSRELAGLRAEL 682
|
250 260
....*....|....*....|...
gi 1907203673 260 KRLTVQVAELKSQLKQTQIALEN 282
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEE 705
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