|
Name |
Accession |
Description |
Interval |
E-value |
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
238-489 |
5.06e-43 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 162.54 E-value: 5.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 238 QLKESLKEVQLERDEYAEHLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVP-- 315
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 316 SEVE------LQHLRKELERVAGELQAQVEYNQRISLLNEGQKERLREQEERLQEQQERLPEQEERL------------- 376
Cdd:pfam15070 81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILedmqsdratisra 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 377 --------QQLAEPQNSFKELNNEN---KSVLQLEQQVK--------ELQEKLG-------------------------- 411
Cdd:pfam15070 161 lsqnrelkEQLAELQNGFVKLTNENmelTSALQSEQHVKkelakklgQLQEELGelketlelksqeaqslqeqrdqylah 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 412 -----------------------------------------------------KERLEAASQQKQQLTAQLSLMALPGEG 438
Cdd:pfam15070 241 lqqyvaayqqlasekeelhkqyllqtqlmdrlqheevqgkvaaemarqelqetQERLEALTQQNQQLQAQLSLLANPGEG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1370466513 439 DGgghLDSE--GEEAPRPIPSIPQDLESREAMVAFFKSAGASAQEKQAQLQEQ 489
Cdd:pfam15070 321 DG---LESEeeEEEAPRPSLSIPEDFESREAMVAFFNSALAQAEEERAELRRQ 370
|
|
| GM130_C |
pfam19046 |
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ... |
629-668 |
8.50e-19 |
|
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.
Pssm-ID: 465957 Cd Length: 46 Bit Score: 80.12 E-value: 8.50e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1370466513 629 SPHDNPTAQPIV------QDHQEHPGLGSNCCVPFFCWAWLPRRRR 668
Cdd:pfam19046 1 SPPENPTAQQIMqllpeiQNPQEHPGLGSNPCIPFFYRADENDEVK 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-418 |
9.01e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 107 QLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSL 186
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 187 QRKGELERALSAVTATQKKKAERfssrsKARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKgerARWQQ 266
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEE-----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---ELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 267 RMRKMSQEVcSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVPSEVELQhlRKELERVAGELQAQVEYNQRISL 346
Cdd:COG1196 388 LLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE--EALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370466513 347 LNEGQKERLREQEerlqeqqerlpEQEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQEKLGKERLEAA 418
Cdd:COG1196 465 LAELLEEAALLEA-----------ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-351 |
1.77e-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: 61.23 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 107 QLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSL 186
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 187 QRKGELERALSAVTATQKKKAERFssrskARMEWKLEQSMREQALLKAQLT---QLKESLKEVQLERDEYAEHLKGERAR 263
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEEL-----AELEEKLEELKEELESLEAELEeleAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 264 WQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKL-----KHQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQAQV 338
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250
....*....|...
gi 1370466513 339 EYNQRISLLNEGQ 351
Cdd:TIGR02168 471 EEAEQALDAAERE 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
115-428 |
2.04e-09 |
|
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: 60.85 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 115 LKQQNKQVEhQLEEEKKANNEKQKAEREL-EVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSLQRKGELE 193
Cdd:TIGR02169 193 IDEKRQQLE-RLRREREKAERYQALLKEKrEYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 194 RALSAVTATQKKKAERFSSRSKARM---EWKLEQSMREQALLKAQLTQLKESLKEVQLERDEY---AEHLKGERARWQQR 267
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKIgelEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaeIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 268 MRKMSQEVCSLKKE------------KKHDKYRVE--KLERSLSKLKHQMAEplppeppavpSEVELQHLRKELERVAGE 333
Cdd:TIGR02169 352 RDKLTEEYAELKEEledlraeleevdKEFAETRDElkDYREKLEKLKREINE----------LKRELDRLQEELQRLSEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 334 LQaqvEYNQRISLLNEGQKERLREQEERLQEQQerlpEQEERLQQLAEpqnsfkELNNENKSVLQLEQQVKELQEKLGKE 413
Cdd:TIGR02169 422 LA---DLNAAIAGIEAKINELEEEKEDKALEIK----KQEWKLEQLAA------DLSKYEQELYDLKEEYDRVEKELSKL 488
|
330
....*....|....*
gi 1370466513 414 RLEAASQQKQQLTAQ 428
Cdd:TIGR02169 489 QRELAEAEAQARASE 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
110-303 |
2.44e-08 |
|
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: 56.70 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 110 NTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSLQRK 189
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 190 GELERALSAVTATQKKKAER------FSSRSKARMEWKLE----------QSMREQALLKAQLTQLKESLKEVQLERDEY 253
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1370466513 254 AEHLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQM 303
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
228-428 |
7.36e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.52 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 228 EQALLKAQLTQLKESLKEVQLERDEyAEHLKGERARWQQRMRKMSQEVCSLKKE------KKHDKYRVEKLERSLSKLKH 301
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEE-TEQLKQQLAQAPAKLRQAQAELEALKDDndeetrETLSTLSLRQLESRLAQTLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 302 QMAEPLPPEPPAVPSEVELQhlrKELERVAGELQAQVEYNQRI-SLLNEGQkerlreqeerlQEQQERLPEQEERL---Q 377
Cdd:PRK11281 136 QLQNAQNDLAEYNSQLVSLQ---TQPERAQAALYANSQRLQQIrNLLKGGK-----------VGGKALRPSQRVLLqaeQ 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370466513 378 QLAEPQNSFKELNNENKSVLQ----------------LEQQVKELQEKLGKERLEAASQQKQQLTAQ 428
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNTQLQdllqkqrdyltariqrLEHQLQLLQEAINSKRLTLSEKTVQEAQSQ 268
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
115-349 |
5.86e-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: 43.17 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 115 LKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSLQRKGELER 194
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 195 ALSAVTATqkkkaerfssrskarmewkLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERARWQQRMRKMSQE 274
Cdd:pfam05483 297 ELEDIKMS-------------------LQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370466513 275 VCSLKKEKKHDKYRVEKLERSLS----KLKHQMAEPLPPEPPAVPSEVELQhlrkELERVAGELQAQVEYNQRISLLNE 349
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNNKEVELE----ELKKILAEDEKLLDEKKQFEKIAE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-330 |
8.24e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 104 KVSQLKNTIKSLKQ-QNKQVEHQLEEEKKANNEKQKAERE---LEVQIQRLN--IQKGK-LNTDLYHTKRSLRYFEEESK 176
Cdd:PRK03918 494 ELIKLKELAEQLKElEEKLKKYNLEELEKKAEEYEKLKEKlikLKGEIKSLKkeLEKLEeLKKKLAELEKKLDELEEELA 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 177 DLAVRLQHSL--------QRKGELE----RALSAVTATQKKKAERfssRSKARMEWKLEQSMREQALLKAQLTQLKESLK 244
Cdd:PRK03918 574 ELLKELEELGfesveeleERLKELEpfynEYLELKDAEKELEREE---KELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 245 EVQLERDEyaehlkGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPpavpsevELQHLR 324
Cdd:PRK03918 651 ELEKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK-------ELEKLE 717
|
....*.
gi 1370466513 325 KELERV 330
Cdd:PRK03918 718 KALERV 723
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
238-489 |
5.06e-43 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 162.54 E-value: 5.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 238 QLKESLKEVQLERDEYAEHLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVP-- 315
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 316 SEVE------LQHLRKELERVAGELQAQVEYNQRISLLNEGQKERLREQEERLQEQQERLPEQEERL------------- 376
Cdd:pfam15070 81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILedmqsdratisra 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 377 --------QQLAEPQNSFKELNNEN---KSVLQLEQQVK--------ELQEKLG-------------------------- 411
Cdd:pfam15070 161 lsqnrelkEQLAELQNGFVKLTNENmelTSALQSEQHVKkelakklgQLQEELGelketlelksqeaqslqeqrdqylah 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 412 -----------------------------------------------------KERLEAASQQKQQLTAQLSLMALPGEG 438
Cdd:pfam15070 241 lqqyvaayqqlasekeelhkqyllqtqlmdrlqheevqgkvaaemarqelqetQERLEALTQQNQQLQAQLSLLANPGEG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1370466513 439 DGgghLDSE--GEEAPRPIPSIPQDLESREAMVAFFKSAGASAQEKQAQLQEQ 489
Cdd:pfam15070 321 DG---LESEeeEEEAPRPSLSIPEDFESREAMVAFFNSALAQAEEERAELRRQ 370
|
|
| GM130_C |
pfam19046 |
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ... |
629-668 |
8.50e-19 |
|
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.
Pssm-ID: 465957 Cd Length: 46 Bit Score: 80.12 E-value: 8.50e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1370466513 629 SPHDNPTAQPIV------QDHQEHPGLGSNCCVPFFCWAWLPRRRR 668
Cdd:pfam19046 1 SPPENPTAQQIMqllpeiQNPQEHPGLGSNPCIPFFYRADENDEVK 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-418 |
9.01e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 107 QLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSL 186
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 187 QRKGELERALSAVTATQKKKAERfssrsKARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKgerARWQQ 266
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEE-----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---ELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 267 RMRKMSQEVcSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVPSEVELQhlRKELERVAGELQAQVEYNQRISL 346
Cdd:COG1196 388 LLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE--EALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370466513 347 LNEGQKERLREQEerlqeqqerlpEQEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQEKLGKERLEAA 418
Cdd:COG1196 465 LAELLEEAALLEA-----------ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-351 |
1.77e-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: 61.23 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 107 QLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSL 186
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 187 QRKGELERALSAVTATQKKKAERFssrskARMEWKLEQSMREQALLKAQLT---QLKESLKEVQLERDEYAEHLKGERAR 263
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEEL-----AELEEKLEELKEELESLEAELEeleAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 264 WQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKL-----KHQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQAQV 338
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250
....*....|...
gi 1370466513 339 EYNQRISLLNEGQ 351
Cdd:TIGR02168 471 EEAEQALDAAERE 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
115-428 |
2.04e-09 |
|
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: 60.85 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 115 LKQQNKQVEhQLEEEKKANNEKQKAEREL-EVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSLQRKGELE 193
Cdd:TIGR02169 193 IDEKRQQLE-RLRREREKAERYQALLKEKrEYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 194 RALSAVTATQKKKAERFSSRSKARM---EWKLEQSMREQALLKAQLTQLKESLKEVQLERDEY---AEHLKGERARWQQR 267
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKIgelEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaeIEELEREIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 268 MRKMSQEVCSLKKE------------KKHDKYRVE--KLERSLSKLKHQMAEplppeppavpSEVELQHLRKELERVAGE 333
Cdd:TIGR02169 352 RDKLTEEYAELKEEledlraeleevdKEFAETRDElkDYREKLEKLKREINE----------LKRELDRLQEELQRLSEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 334 LQaqvEYNQRISLLNEGQKERLREQEERLQEQQerlpEQEERLQQLAEpqnsfkELNNENKSVLQLEQQVKELQEKLGKE 413
Cdd:TIGR02169 422 LA---DLNAAIAGIEAKINELEEEKEDKALEIK----KQEWKLEQLAA------DLSKYEQELYDLKEEYDRVEKELSKL 488
|
330
....*....|....*
gi 1370466513 414 RLEAASQQKQQLTAQ 428
Cdd:TIGR02169 489 QRELAEAEAQARASE 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-511 |
2.57e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 103 VKVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRL 182
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 183 QHSLQRKGELERALSAVTATQKKKAERFSSRSKARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERA 262
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 263 RWQQRMRKMSQEVCSLKKEKKHDKYR--VEKLERSLSKLKHQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQAQVEY 340
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEeaAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 341 NQRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQEKLGKERLEAASQ 420
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 421 QKQQLTAQLSLMALPGEGDGGGHL-DSEGEEAPRPIPSIPQDLESREAMVAFFKSAGASAQEKQAQLQEQSGFMDHLEEK 499
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLvASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
410
....*....|..
gi 1370466513 500 ADLSELVEKEEL 511
Cdd:COG1196 660 GSLTGGSRRELL 671
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-437 |
6.59e-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: 59.30 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 112 IKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKlnTDLYHTKRSlryfEEESKDLAVRLQHSLQRKGE 191
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEK--AERYKELKA----ELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 192 LERALSAVTATQKKKAErfSSRSKARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEyaehLKGERARWQQRMRKM 271
Cdd:TIGR02168 241 LEELQEELKEAEEELEE--LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----LEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 272 SQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQAQVE-YNQRISLLNEG 350
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 351 QKERLREQEerlqeqqerlpEQEERLQQLAEPQNSFKELNNENKSVLQlEQQVKELQEKLGKERLEAASQQKQQLTAQLS 430
Cdd:TIGR02168 395 IASLNNEIE-----------RLEARLERLEDRRERLQQEIEELLKKLE-EAELKELQAELEELEEELEELQEELERLEEA 462
|
....*..
gi 1370466513 431 LMALPGE 437
Cdd:TIGR02168 463 LEELREE 469
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
110-303 |
2.44e-08 |
|
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: 56.70 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 110 NTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSLQRK 189
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 190 GELERALSAVTATQKKKAER------FSSRSKARMEWKLE----------QSMREQALLKAQLTQLKESLKEVQLERDEY 253
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1370466513 254 AEHLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQM 303
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
108-410 |
6.88e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 108 LKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSLQ 187
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 188 RKGELERALSAVTAtQKKKAERFSSRSKARMEWKLEQSMREQ-ALLKAQLTQLKESLKEVQLERdEYAEHlkgERARWQQ 266
Cdd:TIGR02169 766 RIEELEEDLHKLEE-ALNDLEARLSHSRIPEIQAELSKLEEEvSRIEARLREIEQKLNRLTLEK-EYLEK---EIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 267 RMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQAQVE-YNQRIS 345
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEkKRKRLS 920
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370466513 346 LLNEgqkerlreqeerlqeqqeRLPEQEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQEKL 410
Cdd:TIGR02169 921 ELKA------------------KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-431 |
7.22e-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: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 141 RELEVQIQRLNIQKGK------LNTDLYHTKRSLRYFEEESKDLAVRLQHSLQRKGELERALSAVTATQKKKAERFSSRS 214
Cdd:COG1196 196 GELERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 215 KARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEYA---EHLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEK 291
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEerlEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 292 LERSLSKLKHQMAEPLPPEPPavpsevELQHLRKELERVAGELQAQVEYNQRISLLNEGQKERLREQEERLQEQQErlpE 371
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAE------AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE---L 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 372 QEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQEKLGKERLEAASQQKQQLTAQLSL 431
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-426 |
7.33e-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: 52.75 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 104 KVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEkQKAERE-LEVQIQRLNIQKGKLntdlyhtKRSLRYFEEESKDLAVRL 182
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAE-AEAEIEeLEAQIEQLKEELKAL-------REALDELRAELTLLNEEA 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 183 QHSLQRKGELERALSAvtatqKKKAERFSSRSKARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERA 262
Cdd:TIGR02168 820 ANLRERLESLERRIAA-----TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 263 RWQQRMRKmsqevcslkkekkhdkyrVEKLERSLSKLKHqmaeplppeppavpsevELQHLRKELERVAGELQ-AQVEYN 341
Cdd:TIGR02168 895 ELEELSEE------------------LRELESKRSELRR-----------------ELEELREKLAQLELRLEgLEVRID 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 342 QRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLaepQNSFKELNNENKSVLQleqqvkELQEKlgKERLEAASQQ 421
Cdd:TIGR02168 940 NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL---ENKIKELGPVNLAAIE------EYEEL--KERYDFLTAQ 1008
|
....*
gi 1370466513 422 KQQLT 426
Cdd:TIGR02168 1009 KEDLT 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
221-431 |
8.06e-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: 52.37 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 221 KLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERARWQQrmrkMSQEVCSLKKEKKHDKYRVEKLERSLSKLK 300
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 301 HQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQAQVE-YNQRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQL 379
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466513 380 AEPQNSFKELNNE----NKSVLQLEQQVKELQEKLGK--ERLEAASQQKQQLTAQLSL 431
Cdd:TIGR02168 834 AATERRLEDLEEQieelSEDIESLAAEIEELEELIEEleSELEALLNERASLEEALAL 891
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
94-428 |
1.70e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 94 LAVVPDSRSVKVSQLKNTIKSLKQQNKQVEHQLEEEKKA----NNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLR 169
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQraslKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 170 YFEEESK--DLAVRLQHSLQRKGELERALSAVTATQKKKAERFSSRSKARMEWKLEQSMREQALLKAQLTQLKESLKEVQ 247
Cdd:TIGR00618 599 LTEKLSEaeDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 248 LERDEYAEHLKGERARWQQRM-RKMSQEVCSLKKEKKHDKYRvEKLERSLSKLKHQMAEPlppeppavpsEVELQHLRKE 326
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLaQCQTLLRELETHIEEYDREF-NEIENASSSLGSDLAAR----------EDALNQSLKE 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 327 LERVAGE-LQAQVEYNQRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKE--------LNNENKSVL 397
Cdd:TIGR00618 748 LMHQARTvLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeipsdediLNLQCETLV 827
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1370466513 398 QLEQQVKELQEKLGK---------ERLEAASQQKQQLTAQ 428
Cdd:TIGR00618 828 QEEEQFLSRLEEKSAtlgeithqlLKYEECSKQLAQLTQE 867
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
228-428 |
7.36e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.52 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 228 EQALLKAQLTQLKESLKEVQLERDEyAEHLKGERARWQQRMRKMSQEVCSLKKE------KKHDKYRVEKLERSLSKLKH 301
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEE-TEQLKQQLAQAPAKLRQAQAELEALKDDndeetrETLSTLSLRQLESRLAQTLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 302 QMAEPLPPEPPAVPSEVELQhlrKELERVAGELQAQVEYNQRI-SLLNEGQkerlreqeerlQEQQERLPEQEERL---Q 377
Cdd:PRK11281 136 QLQNAQNDLAEYNSQLVSLQ---TQPERAQAALYANSQRLQQIrNLLKGGK-----------VGGKALRPSQRVLLqaeQ 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370466513 378 QLAEPQNSFKELNNENKSVLQ----------------LEQQVKELQEKLGKERLEAASQQKQQLTAQ 428
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNTQLQdllqkqrdyltariqrLEHQLQLLQEAINSKRLTLSEKTVQEAQSQ 268
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
93-425 |
1.03e-05 |
|
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: 48.81 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 93 ELAVVPDSRSVKVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEvqiqRLNIQKGKLNTDLYHTKRSLRYFE 172
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE----YYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 173 EESKDLAVRLQHSLQRKGELERALSAV---TATQKKKAERFSSRSKARMEWKLEQSMREQALLKAQLTQLKESLKEVQLE 249
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKeeeKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 250 rdeyAEHLKGERARWQQRMRKMSQEVCSLKKEKK-HDKYRVEKLERSLSKLKHQMAEPLPPEPPAVPSEVELQHLRKELE 328
Cdd:pfam02463 316 ----LKESEKEKKKAEKELKKEKEEIEELEKELKeLEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 329 RVAGELQAQVEYNQRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQE 408
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
330
....*....|....*..
gi 1370466513 409 KLGKERLEAASQQKQQL 425
Cdd:pfam02463 472 DLLKETQLVKLQEQLEL 488
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
104-417 |
1.85e-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: 48.09 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 104 KVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQ 183
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 184 HSLQRKGELERALSAVTATQKKKAERFSSRSKarmewkleqsmrEQALLKAQLTQLKESLKEVQLERDEYAEHLKGERAR 263
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTN------------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 264 W---QQRMRKMSQEVCSLKKEKKHDKYRVEKLER--SLSKLKHQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQAQV 338
Cdd:TIGR04523 484 LeqkQKELKSKEKELKKLNEEKKELEEKVKDLTKkiSSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 339 -EYNQRISLLNEGQKERLREQEerlqeqqerlpEQEERLQQL-AEPQNSFKELNNENKSVLQLEQQVKELQEKlgKERLE 416
Cdd:TIGR04523 564 dEKNKEIEELKQTQKSLKKKQE-----------EKQELIDQKeKEKKDLIKEIEEKEKKISSLEKELEKAKKE--NEKLS 630
|
.
gi 1370466513 417 A 417
Cdd:TIGR04523 631 S 631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-510 |
2.34e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 109 KNTIKSLKQQNKQVEhQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFE--EESKDLAVRLQHSL 186
Cdd:COG4717 67 ELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 187 QRKGELERALSAVTATQKKKAERfsSRSKARMEWKLEQSMREQALLK-AQLTQLKESLKEVQLERdeyaEHLKGERARWQ 265
Cdd:COG4717 146 ERLEELEERLEELRELEEELEEL--EAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRL----AELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 266 QRMRKMSQEVCSLKKEK--KHDKYRVEKLERSL--------------SKLKHQMAEPLPPEPPAVPSEVELQHLRKELER 329
Cdd:COG4717 220 EELEELEEELEQLENELeaAALEERLKEARLLLliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 330 VAGELQAQVEYNQRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKsVLQLEQQVKELQEK 409
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 410 LGKERLEA------ASQQKQQLTAQLSLM--ALPGEGDGGGHLDSEGEEAprpipSIPQDLESREAMVAFFKSAGASAQE 481
Cdd:COG4717 379 AGVEDEEElraaleQAEEYQELKEELEELeeQLEELLGELEELLEALDEE-----ELEEELEELEEELEELEEELEELRE 453
|
410 420
....*....|....*....|....*....
gi 1370466513 482 KQAQLQEQsgfMDHLEEKADLSELVEKEE 510
Cdd:COG4717 454 ELAELEAE---LEQLEEDGELAELLQELE 479
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
107-430 |
3.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 107 QLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNT-----DLYHTKRSLRYFEEESKDLAVR 181
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgrelTEEHRKELLEEYTAELKRIEKE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 182 LQHSLQRKGELERALSAVTATQKKKAERFSSRSKARmewkleqsmreqallkaQLTQLKESLKEVQLERDEYAEHlkgER 261
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-----------------QLKELEEKLKKYNLEELEKKAE---EY 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 262 ARWQQRMRKMSQEVCSLKKEKKhdkyRVEKLERSLSKLKHQMAEPlppeppavpsEVELQHLRKELERVAGELQAQVE-- 339
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDEL----------EEELAELLKELEELGFESVEELEer 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 340 -------YNQRISLLNEGQKERlreqeerlqeqqerlpEQEERLQQLA-EPQNSFKELNNENKSVLQLEQQVKELQEKLG 411
Cdd:PRK03918 594 lkelepfYNEYLELKDAEKELE----------------REEKELKKLEeELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
330
....*....|....*....
gi 1370466513 412 KERLEAASQQKQQLTAQLS 430
Cdd:PRK03918 658 EEEYEELREEYLELSRELA 676
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
190-434 |
3.08e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 190 GELERALSAVtATQKKKAERFssrskarMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEyaehLKGERARWQQRMR 269
Cdd:COG1196 196 GELERQLEPL-ERQAEKAERY-------RELKEELKELEAELLLLKLRELEAELEELEAELEE----LEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 270 KMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPlppeppavpsEVELQHLRKELERVAGELQaqvEYNQRISLLNE 349
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARL----------EQDIARLEERRRELEERLE---ELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 350 GQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQEKLGKERLEAASQQKQQLTAQL 429
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
....*
gi 1370466513 430 SLMAL 434
Cdd:COG1196 411 ALLER 415
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
73-412 |
1.11e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 73 IHGESPTSSATLKDLESPCQELavvpDSRSVKVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNI 152
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKEL----EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 153 QKGK------LNTDLYHTKRSLRYFEEESKDLAVRLQHSLQRKGELERALSAVTATQKKKAErfSSRSKARMEWKLEQSM 226
Cdd:PRK03918 288 LKEKaeeyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE--LEKRLEELEERHELYE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 227 REQAlLKAQLTQLKESLKEVQLER-DEYAEHLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSK------- 298
Cdd:PRK03918 366 EAKA-KKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgre 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 299 ---------LKHQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQAQVEYNQRISLLNEGQKERLREQEERLQEQQERL 369
Cdd:PRK03918 445 lteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA 524
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1370466513 370 PEQEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQEKLGK 412
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-299 |
1.33e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 102 SVKVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLR----YFEEESKD 177
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleeQLETLRSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 178 LAVRLQHSLQRKGELERALSAVTATQKKKaERFSSRSKARMEWKLEQSMREqalLKAQLTQLKESLKEVQLERDEYAEHL 257
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRR-ERLQQEIEELLKKLEEAELKE---LQAELEELEEELEELQEELERLEEAL 463
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1370466513 258 KgeraRWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKL 299
Cdd:TIGR02168 464 E----ELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
186-428 |
1.53e-04 |
|
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: 45.11 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 186 LQRKGELERALSAVTATQKKKAERFSSRSKARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERARWQ 265
Cdd:pfam17380 312 VERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 266 QRMRkmsQEVCSLKKEKKHDKYRveklERSLSKLKHQMAEPLPPEPPAVPSEVEL--QHLRKELERVAGELQAQVEYNQR 343
Cdd:pfam17380 392 ERVR---QELEAARKVKILEEER----QRKIQQQKVEMEQIRAEQEEARQREVRRleEERAREMERVRLEEQERQQQVER 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 344 ISLLNEGQKerlreqeerlQEQQERlpEQEERLQQLAEPQNSF---KELnNENKSVLQLEQQVKELQEKLGKERLEAASQ 420
Cdd:pfam17380 465 LRQQEEERK----------RKKLEL--EKEKRDRKRAEEQRRKileKEL-EERKQAMIEEERKRKLLEKEMEERQKAIYE 531
|
....*...
gi 1370466513 421 QKQQLTAQ 428
Cdd:pfam17380 532 EERRREAE 539
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
104-430 |
1.78e-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: 44.63 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 104 KVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQ 183
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 184 hslQRKGELEralsavtATQKKKAERFSSRSK---ARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDeyaeHLKGE 260
Cdd:TIGR04523 292 ---QLKSEIS-------DLNNQKEQDWNKELKselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT----NSESE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 261 RARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLS----KLKHQMAEPLPPEPPAVPSEVELQHLRKELERVageLQA 336
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdlesKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL---KET 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 337 QVEYNQRISLLNEG--------------QKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKsvlQLEQQ 402
Cdd:TIGR04523 435 IIKNNSEIKDLTNQdsvkeliiknldntRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK---ELEEK 511
|
330 340 350
....*....|....*....|....*....|
gi 1370466513 403 VKELQEK--LGKERLEAASQQKQQLTAQLS 430
Cdd:TIGR04523 512 VKDLTKKisSLKEKIEKLESEKKEKESKIS 541
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
106-424 |
4.22e-04 |
|
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: 43.57 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 106 SQLKNTIKSLKQQNKQVEHQLEEEK----KANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVR 181
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLSDLEstvsQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 182 LQHSLQRKGELERALSAVTATQKKKAERFSSRS------KARMEWKLEQSMREQALLKAQLT----QLKESLKEVQLERD 251
Cdd:pfam15921 379 LQKLLADLHKREKELSLEKEQNKRLWDRDTGNSitidhlRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 252 --EYAEHLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKlKHQMAEPLPPEPPAVPSEV-----ELQHLR 324
Cdd:pfam15921 459 slEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEATNAEITKLRSRVdlklqELQHLK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 325 KE---LERVAGELQA----QVEYNQRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKEL----NNEN 393
Cdd:pfam15921 538 NEgdhLRNVQTECEAlklqMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFkilkDKKD 617
|
330 340 350
....*....|....*....|....*....|....*..
gi 1370466513 394 KSVLQLEQQVKELQ-EKL-----GKERLEAASQQKQQ 424
Cdd:pfam15921 618 AKIRELEARVSDLElEKVklvnaGSERLRAVKDIKQE 654
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
104-520 |
5.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 104 KVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDlAVRLQ 183
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK-ADEAK 1450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 184 HSLQRKGELERALSavTATQKKKAERFSSRSKARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERAR 263
Cdd:PTZ00121 1451 KKAEEAKKAEEAKK--KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 264 WQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVPSEVELqhLRKELERVAGELQAQVEYNQR 343
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE--AKKAEEARIEEVMKLYEEEKK 1606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 344 ISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNN--ENKSVLQLEQQVKELQEKLGKERLEAASQQ 421
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaeEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 422 KQQLTAQLSLMAlpGEGDGGGHLDSEGEEAPRPIPSIPQDLESREAMVAFFKSAGASAQEKQAQLQEQSGfmdhleEKAD 501
Cdd:PTZ00121 1687 EKKAAEALKKEA--EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE------EKKK 1758
|
410
....*....|....*....
gi 1370466513 502 LSELVEKEELGFFQYYRER 520
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEK 1777
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
115-349 |
5.86e-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: 43.17 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 115 LKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSLQRKGELER 194
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 195 ALSAVTATqkkkaerfssrskarmewkLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERARWQQRMRKMSQE 274
Cdd:pfam05483 297 ELEDIKMS-------------------LQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370466513 275 VCSLKKEKKHDKYRVEKLERSLS----KLKHQMAEPLPPEPPAVPSEVELQhlrkELERVAGELQAQVEYNQRISLLNE 349
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNNKEVELE----ELKKILAEDEKLLDEKKQFEKIAE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
84-430 |
6.25e-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: 43.09 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 84 LKDLESPCQELAVVPDSRSVKVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQ--------------KAERELEVQIQR 149
Cdd:TIGR04523 220 ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleqnnkkikeleKQLNQLKSEISD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 150 LNIQKGK-------------------LNTDLYHTKRSLRYFEEESKDLAVRLQHS----LQRKGELERALSAVTATQKKK 206
Cdd:TIGR04523 300 LNNQKEQdwnkelkselknqekkleeIQNQISQNNKIISQLNEQISQLKKELTNSesenSEKQRELEEKQNEIEKLKKEN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 207 AERFSSRSKARMEWK-LEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERARWQQRMRKMSQEVCSLKKE-KKH 284
Cdd:TIGR04523 380 QSYKQEIKNLESQINdLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIiKNL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 285 DKYR------VEKLERSLSKLKHqmaeplppeppavpsevELQHLRKELERVAGELQaqvEYNQRISLLNEGQKERLREQ 358
Cdd:TIGR04523 460 DNTResletqLKVLSRSINKIKQ-----------------NLEQKQKELKSKEKELK---KLNEEKKELEEKVKDLTKKI 519
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370466513 359 EERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKSVlQLEQQVKELQEKLGK-----ERLEAASQQKQQLTAQLS 430
Cdd:TIGR04523 520 SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE-NLEKEIDEKNKEIEElkqtqKSLKKKQEEKQELIDQKE 595
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-330 |
8.24e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 104 KVSQLKNTIKSLKQ-QNKQVEHQLEEEKKANNEKQKAERE---LEVQIQRLN--IQKGK-LNTDLYHTKRSLRYFEEESK 176
Cdd:PRK03918 494 ELIKLKELAEQLKElEEKLKKYNLEELEKKAEEYEKLKEKlikLKGEIKSLKkeLEKLEeLKKKLAELEKKLDELEEELA 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 177 DLAVRLQHSL--------QRKGELE----RALSAVTATQKKKAERfssRSKARMEWKLEQSMREQALLKAQLTQLKESLK 244
Cdd:PRK03918 574 ELLKELEELGfesveeleERLKELEpfynEYLELKDAEKELEREE---KELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 245 EVQLERDEyaehlkGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPpavpsevELQHLR 324
Cdd:PRK03918 651 ELEKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK-------ELEKLE 717
|
....*.
gi 1370466513 325 KELERV 330
Cdd:PRK03918 718 KALERV 723
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
121-275 |
1.00e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 121 QVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSLQRKGEL--ERALSA 198
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 199 VT---ATQKKKAERFSSRSKARMEwKLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLKGERARWQQRMRKMSQEV 275
Cdd:COG1579 94 LQkeiESLKRRISDLEDEILELME-RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
156-416 |
1.34e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 156 KLNTDLYhtkrslRYFEEESKDLAVRLQHSLQRkgeleralsavTATQKKKAERFSSRSKARMEWKleQSMREQAL---- 231
Cdd:PHA02562 170 KLNKDKI------RELNQQIQTLDMKIDHIQQQ-----------IKTYNKNIEEQRKKNGENIARK--QNKYDELVeeak 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 232 -LKAQLTQLKESLKEVQLERDEYAEHLKgeraRWQQRMRKMSQEVCSLKKE----KKHD-----KYRVEKLERSLSKLKH 301
Cdd:PHA02562 231 tIKAEIEELTDELLNLVMDIEDPSAALN----KLNTAAAKIKSKIEQFQKVikmyEKGGvcptcTQQISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 302 QMaeplppeppavpseVELQH-LRKELErvagelqAQVEYNQRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLA 380
Cdd:PHA02562 307 KL--------------KELQHsLEKLDT-------AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKA 365
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370466513 381 EPQNSFKELNNENKSVLQLEQQVKELQEKLGKERLE 416
Cdd:PHA02562 366 AIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
99-489 |
1.44e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 99 DSRSVKVSQLKNTIKSLKQQNK-QVEHQLEEEKKANNEKQKAErELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKD 177
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVS-SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 178 LAVRLQhslqrkgELERALSAVTAtqkkKAERFSSRSKARMEwKLEQSMREQALLKAQLTQLkESLKEVQLERDEYAEHL 257
Cdd:pfam15921 501 LTASLQ-------EKERAIEATNA----EITKLRSRVDLKLQ-ELQHLKNEGDHLRNVQTEC-EALKLQMAEKDKVIEIL 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 258 KgerarwqQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAeplppeppavpsevELQHLRKELERVAGELQAQ 337
Cdd:pfam15921 568 R-------QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ--------------EFKILKDKKDAKIRELEAR 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 338 VE--YNQRISLLNEGQKERLREQEErlqeqqerlpeQEERLQQLAEPQNSFKELNN--ENKSVLQ--LEQQVKELQEKLG 411
Cdd:pfam15921 627 VSdlELEKVKLVNAGSERLRAVKDI-----------KQERDQLLNEVKTSRNELNSlsEDYEVLKrnFRNKSEEMETTTN 695
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466513 412 KERLEAASQQKQQLTAQLSLMALPGegdGGGHLDSEGEEAPRPIPSIPQDLESREAMVAFFKSAGASAQEKQAQLQEQ 489
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSMEG---SDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE 770
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
100-433 |
1.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 100 SRSVKVSQLKNTIKSLKQQNKQVEHQLEEEKkannEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRY-FEEESKDL 178
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELE----ERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 179 AVRLQHSLQRKGELERALSAVTATQKKKAERFSSRSKARMEWKLEQSMREQALLKAQLTQLkESLKEVQLERDEYAEHLK 258
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 259 G----------ERARWQQRMRK-MSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVPSEVELQHLRKEL 327
Cdd:COG4717 277 GvlflvlgllaLLFLLLAREKAsLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 328 ERVAGELQAQVEYNQRISLLNEGQkerlREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKSVL------QLEQ 401
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAG----VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdeeELEE 432
|
330 340 350
....*....|....*....|....*....|....
gi 1370466513 402 QVKELQEKL--GKERLEAASQQKQQLTAQLSLMA 433
Cdd:COG4717 433 ELEELEEELeeLEEELEELREELAELEAELEQLE 466
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
108-418 |
1.82e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 108 LKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNiqkgKLNTDLYHTKRSLRYFEEESKDLAvrlqhslQ 187
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN----EISSELPELREELEKLEKEVKELE-------E 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 188 RKGELEralsavtatQKKKAERFSSRSKARMEWKLEQSMREQALLKAQLTQLKE---SLKEVQLERDEYAEhLKGERARW 264
Cdd:PRK03918 236 LKEEIE---------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkELKELKEKAEEYIK-LSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 265 QQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKhqmaeplppeppavpsevELQHLRKELERVAGELQAQVE-YNQR 343
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLE------------------ELKKKLKELEKRLEELEERHElYEEA 367
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370466513 344 ISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEpqnsfkELNNENKSVLQLEQQVKELQEKLgkERLEAA 418
Cdd:PRK03918 368 KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE------EISKITARIGELKKEIKELKKAI--EELKKA 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-247 |
1.91e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 84 LKDLESPCQELAVVPDSRSVKVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNtdlyh 163
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE----- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 164 tkRSLRYFEEESKDLAVRLQhsLQRKGELERALSAVTATQKKKAERFssrskARMEWKLEQSMREQALLKAQLTQLKESL 243
Cdd:TIGR02168 414 --DRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEEL-----ERLEEALEELREELEEAEQALDAAEREL 484
|
....
gi 1370466513 244 KEVQ 247
Cdd:TIGR02168 485 AQLQ 488
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
104-424 |
1.92e-03 |
|
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: 41.54 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 104 KVSQLKNTIKSLKQQNKQVEHQLEEEK-----------KANNE---KQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLR 169
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNKdkinklnsdlsKINSEiknDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 170 YFEEESKDLAVRLQHSLQRKGELERALSAV-TATQKKKAERFSSRSK-ARMEWKL---EQSMREQALLKAQLTQLKE--- 241
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELENELNLLeKEKLNIQKNIDKIKNKlLKLELLLsnlKKKIQKNKSLESQISELKKqnn 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 242 SLKE-VQLERDEYAEhLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEK-------LERSLSKLKHQMAEPLPPEPPA 313
Cdd:TIGR04523 229 QLKDnIEKKQQEINE-KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkkikeLEKQLNQLKSEISDLNNQKEQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 314 VPSEV--ELQHLRKELErvagELQAQV-EYNQRISLLNEgqkerlrEQEERLQEQQERLPEQEERLQQLAEPQNSFKELN 390
Cdd:TIGR04523 308 WNKELksELKNQEKKLE----EIQNQIsQNNKIISQLNE-------QISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
330 340 350
....*....|....*....|....*....|....*...
gi 1370466513 391 NENKSVLQ----LEQQVKELQEKLGKErlEAASQQKQQ 424
Cdd:TIGR04523 377 KENQSYKQeiknLESQINDLESKIQNQ--EKLNQQKDE 412
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
106-281 |
2.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 106 SQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAEREL---EVQIQRLNIQKGKLNTDLYHTKRSLRYFEE--ESKDLAV 180
Cdd:COG3883 37 AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaEAEIEERREELGERARALYRSGGSVSYLDVllGSESFSD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 181 RLQHSLqrkgelerALSAVTATQKKKAERFSS--RSKARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEYAEHLK 258
Cdd:COG3883 117 FLDRLS--------ALSKIADADADLLEELKAdkAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180
....*....|....*....|...
gi 1370466513 259 GERARWQQRMRKMSQEVCSLKKE 281
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAA 211
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
84-432 |
2.37e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 84 LKDLESPCQELAVVPDSRSVKVSQLKNTIKSLKQQNKQVEHQLEEEKkanNEKQKAERELEVQIQRLNIQKgKLNTDLYH 163
Cdd:TIGR00606 718 LKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK---NDIEEQETLLGTIMPEEESAK-VCLTDVTI 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 164 TKRslryFEEESKDLAVRLQHSLQRKGELERALSaVTATQKKKAERFSSRSKARMEWKLEQSMREQAllKAQLTQLKESL 243
Cdd:TIGR00606 794 MER----FQMELKDVERKIAQQAAKLQGSDLDRT-VQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ--QEQIQHLKSKT 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 244 KEVQLERDEYAEHLKgERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEP-LPPEPPAVPSEVELQH 322
Cdd:TIGR00606 867 NELKSEKLQIGTNLQ-RRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELiSSKETSNKKAQDKVND 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 323 LRKELERVAGELQAQVEYNQ----RISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKSVLQ 398
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQdgkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK 1025
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1370466513 399 LEQQVKELQEKL-------GKERLEAASQQKQQLTAQLSLM 432
Cdd:TIGR00606 1026 RENELKEVEEELkqhlkemGQMQVLQMKQEHQKLEENIDLI 1066
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
92-424 |
2.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 92 QELAVVPDSRSVKVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKgklNTDLYHTKRSLRYF 171
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK---KAEEARIEEVMKLY 1601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 172 EEESKDLAVRLqhslqRKGELERalsaVTATQKKKAERFSSRSKARMEWKLEQSMREQALLKAQLtqlKESLKEVQLERD 251
Cdd:PTZ00121 1602 EEEKKMKAEEA-----KKAEEAK----IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE---ENKIKAAEEAKK 1669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 252 EYAEHLKGERARWQQRMRKMSQEVCslkKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVPSEVELQHLRKELERVA 331
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEAL---KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 332 GELQAQVEYNQRISLLNEGQKERLREQEERLQ---------EQQERLPEQEERLQQLAEPQNSFKELNNENKSVLQLEQQ 402
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEavieeeldeEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKE 1826
|
330 340
....*....|....*....|....*..
gi 1370466513 403 -----VKELQEKLGKERLEAASQQKQQ 424
Cdd:PTZ00121 1827 medsaIKEVADSKNMQLEEADAFEKHK 1853
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
92-422 |
3.90e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 92 QELAVVPDSRSVKVSQLKNTIKSLKQQNK-QVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLN-TDLYHTKRSLR 169
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEARKaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEeARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 170 YFEEESKdlavRLQHSLQRKGELERALSAVTATQKKKAERFSSRSKarmewklEQSMREQALLKAQLTQLK-ESLKEVQL 248
Cdd:PTZ00121 1271 AIKAEEA----RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE-------EAKKADEAKKKAEEAKKKaDAAKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 249 ERDEYAEHLKGERARWQQRMRKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKHQMAEPLPPEPPAVPSEvELQHlRKELE 328
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKK-AAAAK 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 329 RVAGELQAQVEYNQRIsllNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNN---ENKSVLQLEQQVKE 405
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKA---DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaeEAKKADEAKKKAEE 1494
|
330
....*....|....*..
gi 1370466513 406 LQEKLGKERLEAASQQK 422
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKK 1511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
140-342 |
6.61e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 140 ERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSLQRKGELERALSAVTATQKKKAERFSSRSKARME 219
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 220 WKLEQSMREqalLKAQLTQLKESLKEVQLERDEYAEhLKGERARWQQRMRKMSQEVCSLKKEKKHDKYrvEKLERSLSKL 299
Cdd:COG4717 128 LPLYQELEA---LEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATE--EELQDLAEEL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1370466513 300 KHQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQAQVEYNQ 342
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
79-421 |
6.78e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 79 TSSATLKDLESPCQeLAVVPDSRSVKVSQLKNTIKSLKQQnKQVEHQLEEEKKANNEKQKAERELEVQIQRLNiqkgkln 158
Cdd:TIGR00618 200 TLRSQLLTLCTPCM-PDTYHERKQVLEKELKHLREALQQT-QQSHAYLTQKREAQEEQLKKQQLLKQLRARIE------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 159 tdlyhtkrslRYFEEESKDLAVRLQHSLQRKGELERALSAVTATQKKKAERFSSRSKARMEWKLEQSMREQALLKAQLtq 238
Cdd:TIGR00618 271 ----------ELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQS-- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 239 lkESLKEVQLERDEYAEHLKGERARWQQRMRKmsQEVCSLKKEKKHDKYRVEKLERSLSKLKhqmaeplppeppavPSEV 318
Cdd:TIGR00618 339 --SIEEQRRLLQTLHSQEIHIRDAHEVATSIR--EISCQQHTLTQHIHTLQQQKTTLTQKLQ--------------SLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 319 ELQHLRKELERVAGELQAQVEYNQRISLLNEGQKERLREQEERLQEQQERLPEQEERLQQLAEPQNSFKELNNENKSVLQ 398
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
330 340
....*....|....*....|...
gi 1370466513 399 LEQQVKELQEKLGKERLEAASQQ 421
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEP 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
215-431 |
7.92e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 215 KARMEWKLEQSMREQALLKAQLTQLKESLKEVQLERDEY-AEH----LKGERARWQQRMRKMSQEVCSLKKEKkhdkyrv 289
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFrQKNglvdLSEEAKLLLQQLSELESQLAEARAEL------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 290 EKLERSLSKLKHQMAEPLPPEPPAVPSEVeLQHLRKELERVAGELQAQV-----EYNQRISLLNEGQKERLREQEERLQE 364
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSarytpNHPDVIALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370466513 365 QQERLPEQEERLQQLAEPQNSFKELNNENKSVLQLEQQVKELQEKL--GKERLEAASQQKQQLTAQLSL 431
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVevARELYESLLQRLEEARLAEAL 383
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-281 |
8.72e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 104 KVSQLKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRlniQKGKLNTDLyhtkrslryfEEESKDLAVRLQ 183
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG---NGGDRLEQL----------EREIERLERELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 184 HSLQRKGELERALSAVTATQKKKAERFSSRSKARMEWkLEQSMREQALLKAQLTQLKESLKEVQLERDEyaehLKGERAR 263
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL-LEALEEELEALEEALAEAEAALRDLRRELRE----LEAEIAS 430
|
170
....*....|....*...
gi 1370466513 264 WQQRMRKMSQEVCSLKKE 281
Cdd:COG4913 431 LERRKSNIPARLLALRDA 448
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
192-301 |
9.32e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 192 LERALSAVTATQKKKAERFSSRSKARMEWKLEQSMREQALLKAQLTQLK---ESLKEVQLERDEYAEHLKGE--RARWQQ 266
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEaevEELEAELEEKDERIERLERElsEARSEE 457
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1370466513 267 RM--------RKMSQEVCSLKKEKKHDKYRVEKLERSLSKLKH 301
Cdd:COG2433 458 RReirkdreiSRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
108-222 |
9.81e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466513 108 LKNTIKSLKQQNKQVEHQLEEEKKANNEKQKAERELEVQIQRLNIQKGKLNTDLYHTKRSLRYFEEESKDLAVRLQHSLQ 187
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
90 100 110
....*....|....*....|....*....|....*
gi 1370466513 188 RKGELERALSAVTATQKKKAERFSSRSKARMEWKL 222
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| |
