|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
199-555 |
1.75e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 199 ERLKEHIQSLETQIAKwnLqvkmnKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSA 278
Cdd:COG1196 189 ERLEDILGELERQLEP--L-----ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 279 SNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMEthgkNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKD 358
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLE----QDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 359 EVASVENELVELQEvekRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKVdgnySLLTKLSLEEE 438
Cdd:COG1196 338 ELEELEEELEEAEE---ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA----AQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 439 NHLIQLkcENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRER 518
Cdd:COG1196 411 ALLERL--ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330 340 350
....*....|....*....|....*....|....*..
gi 197927450 519 ALQMKisDLETELRKKNEEQNQLVGNMSTKAQHQDIC 555
Cdd:COG1196 489 AAARL--LLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-531 |
2.58e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 184 HDRLQLQIQKREVENERLKEHIQSLETQIAkwnlqvkmnkqeavavkeASRQKAEALKKASKVYRQRLRHFTGDIEQLTS 263
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIA------------------ELEKALAELRKELEELEEELEQLRKELEELSR 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 264 QIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLrkmethgknscEEILRKLHSLEDENEALN 343
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-----------AEAEAEIEELEAQIEQLK 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 344 IENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHEnkliINKKNTKLEKV 423
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEEL 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 424 DGNYSLLTKL--SLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEflKHSDLELREKAAECTaLSRQLEAALEE 501
Cdd:TIGR02168 872 ESELEALLNEraSLEEALALLRSELEELSEELRELESKRSELRRELEELRE--KLAQLELRLEGLEVR-IDNLQERLSEE 948
|
330 340 350
....*....|....*....|....*....|...
gi 197927450 502 GR---QKVSEEVEKMSSRERALQMKISDLETEL 531
Cdd:TIGR02168 949 YSltlEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
131-484 |
2.59e-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: 60.46 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 131 LLKDLSDSDSENRDLKKKVLEKETYIQELSCLFHNEKESALKANRFSQsvkvvhdRLQLQIQKREVENERLKEHIQSLET 210
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-------QLEERIAQLSKELTELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 211 QIAKWNLQvkmnKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIA 290
Cdd:TIGR02168 769 RLEEAEEE----LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 291 IEKTELEVQIETMKKQISHLLEdlrkmethgknSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVEL 370
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEE-----------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 371 QEVEKRQKALVEGYRTQVQKLEEAAAMVKSRcknllhenklIINKKNTKLEKVDGNYSLLTKLSLEEENHLIQLK----- 445
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQER----------LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEnkike 983
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 197927450 446 -----------CENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREK 484
Cdd:TIGR02168 984 lgpvnlaaieeYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-510 |
3.71e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 166 EKESALKANRFSQSVKVVHDRLQ-LQIQKREVENERLKEHIQSLETQIAKWNLQVkmnkQEAVAVKEASRQKAEALKKAS 244
Cdd:COG1196 208 QAEKAERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 245 KVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAvsasndwksryekiAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNS 324
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRREL--------------EERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 325 CEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKN 404
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 405 LLHENKLIINKKNTKLEkvdgnyslLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREK 484
Cdd:COG1196 430 LAELEEEEEEEEEALEE--------AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340
....*....|....*....|....*.
gi 197927450 485 AAEcTALSRQLEAALEEGRQKVSEEV 510
Cdd:COG1196 502 DYE-GFLEGVKAALLLAGLRGLAGAV 526
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-531 |
1.90e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 248 RQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMEthgknscee 327
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE--------- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 328 ilRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKAlvEGYRTQVQKLEEAAAMVKSRCKNLLH 407
Cdd:TIGR02169 751 --QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL--SKLEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 408 ENKLIINKKNTKLEKVdgNYSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREkaae 487
Cdd:TIGR02169 827 EKEYLEKEIQELQEQR--IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE---- 900
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 197927450 488 ctalsrqleaaLEEGRQKVSEEVEKMSSRERALQMKISDLETEL 531
Cdd:TIGR02169 901 -----------LERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
180-538 |
1.49e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 180 VKVVHDRLQLQIQKREVENERL-KEHIQSLETQIAKWNLQVKMNKQEAVAVKEASRQKAEALKKASKVyRQRLRHFTGDI 258
Cdd:TIGR02169 182 VEENIERLDLIIDEKRQQLERLrREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASL-EEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 259 EQLTSQIRDQEAKLSEaVSASNDWKSRYEKIAIEKT--ELEVQIETMKKQISHLLEDLRKMETHGKNSCEEI---LRKLH 333
Cdd:TIGR02169 261 SELEKRLEEIEQLLEE-LNKKIKDLGEEEQLRVKEKigELEAEIASLERSIAEKERELEDAEERLAKLEAEIdklLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 334 SLEDENEALNIENVKLKSTLDALKDEVASVENELvelQEVEKRQKALVEGYRTQVQKLEEAaamvksrcknllhenkliI 413
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKLEKL------------------K 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 414 NKKNtklekvdgnyslltklSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSR 493
Cdd:TIGR02169 399 REIN----------------ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 197927450 494 QLEAALEEGRQKvSEEVEKMSSRERALQMKISDLETELRKKNEEQ 538
Cdd:TIGR02169 463 DLSKYEQELYDL-KEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-541 |
2.52e-07 |
|
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: 53.97 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 130 CLLKD-LSDSDSENRDLKKKVLEKETYIQELSCLFHNEKESALKANRFSQSVKVVHDRLQlqiqkreveNERLKEHIQSL 208
Cdd:pfam15921 159 CLKEDmLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSL---------GSAISKILREL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 209 ETQIAKWNLQVKMNKQEAVAVKEASRQKAEALkkaskvyrqrLRHFTGDIEQLTSQ----IRDQEAKLSEAVSASNDWKS 284
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALKSESQNKIELL----------LQQHQDRIEQLISEheveITGLTEKASSARSQANSIQS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 285 RYEKIAIEKTELEV----QIETMKKQISHLLEDLRKMETHGKNSCEEILRKL-------HSLEDENEALNIENVKLKSTL 353
Cdd:pfam15921 300 QLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 354 DALKDEVASVENELVELQEVEKRQ--------------KALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTK 419
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNES 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 420 LEKVDGNYSLL----------------TKLSLEEENHLIQLKCENLKEKLEQMDAENKELER-----KLADQE-EFLKHS 477
Cdd:pfam15921 460 LEKVSSLTAQLestkemlrkvveeltaKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvDLKLQElQHLKNE 539
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 478 DLELREKAAECTALSRQL---EAALEEGRQKVSEEVEKMSSRER---ALQMKISDLETELRKKNEEQNQL 541
Cdd:pfam15921 540 GDHLRNVQTECEALKLQMaekDKVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEF 609
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-553 |
2.72e-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: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 226 AVAVKEASRQKAEALKKASKVYRQRLrhftgdiEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKK 305
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEEL-------EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 306 QISHLLEdlrkmethgknsceeilrKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYR 385
Cdd:TIGR02168 303 QKQILRE------------------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 386 TQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKVDGNYSLLTKLSLEEENhliqLKCENLKEKLEQMDAENKELER 465
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 466 KLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgRQKVSEEVEKMSSRERALQmkisDLETELRKKNEEQNQLVGNM 545
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQA-LDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALLKNQ 515
|
....*...
gi 197927450 546 STKAQHQD 553
Cdd:TIGR02168 516 SGLSGILG 523
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
86-542 |
3.59e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 86 SNLKKIFEQ-KDILSKELDTFNRVKLALEHliKQTDYEQTGPRPPCLLKDLSDSDSENRDLKKKVLEKETYIQELsclfh 164
Cdd:TIGR04523 221 SELKKQNNQlKDNIEKKQQEINEKTTEISN--TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL----- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 165 NEKESALKANRFSQSVKVVHDRL-QLQIQKREVENE--RLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASRQKAEALK 241
Cdd:TIGR04523 294 KSEISDLNNQKEQDWNKELKSELkNQEKKLEEIQNQisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 242 KASKVYRQRLRhftgDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHL---LEDLRKME 318
Cdd:TIGR04523 374 KLKKENQSYKQ----EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseIKDLTNQD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 319 THGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELqeveKRQKALVEGyrtQVQKLEEAAAMV 398
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL----NEEKKELEE---KVKDLTKKISSL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 399 KSRCKNLLHENKLIINKKNTKLEKVDGNYSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSD 478
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927450 479 LELREKAAECTALSRQLEAALEEGRqKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQLV 542
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII 665
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-528 |
4.30e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 88 LKKIFEQKDILSKELDTFNRVKLALEHLIKQTDYEQTGPRPPclLKDLSDSDSENRDLKKKVLEKETYIQELSCLFHNEK 167
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE--IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 168 ESALKANRFSQSVKVVHDRLQ-----------LQIQKREVEN--ERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASR 234
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKeleekeerleeLKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 235 QKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSA------------SNDWKSRYEKIAIEKTELEVQIET 302
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreltEEHRKELLEEYTAELKRIEKELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 303 MKKQISHLLEDLRKMETHGKNSCE-----EILRKLHSLEDENEALNIENV--------KLKSTLDALKDEVASVENELVE 369
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEEKLKKYNLEELekkaeeyeKLKEKLIKLKGEIKSLKKELEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 370 LQEVEKRQKALVEgyrtQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKVDGNYSLL--TKLSLEEENHLIQLKCE 447
Cdd:PRK03918 551 LEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELkdAEKELEREEKELKKLEE 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 448 NLKEKLEQMDAENKELERKLADQEEFLK-HSDLELREKAAECTALSRQLEAA------LEEGRQKVSEEVEKMSSRERAL 520
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKkYSEEEYEELREEYLELSRELAGLraeleeLEKRREEIKKTLEKLKEELEER 706
|
....*...
gi 197927450 521 QMKISDLE 528
Cdd:PRK03918 707 EKAKKELE 714
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
223-401 |
3.98e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 223 KQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIET 302
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 303 MKKQISHLLEDLRKMETHGK-------NSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEK 375
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180
....*....|....*....|....*.
gi 197927450 376 RQKALVEGYRTQVQKLEEAAAMVKSR 401
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKE 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-568 |
4.71e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 292 EKTELEVQIETMKKQISHLLEDLRKMEThgknsceeILRKLHSLEDENEALN--IENVKLKSTLDALKDEVASVENELvE 369
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALED--------AREQIELLEPIRELAEryAAARERLAELEYLRAALRLWFAQR-R 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 370 LQEVEKRQKALvegyRTQVQKLEEAAAMVKSRCKNLLhenkliinkkntklEKVDGNYSLLTKLSLEEEnhliqlkcENL 449
Cdd:COG4913 290 LELLEAELEEL----RAELARLEAELERLEARLDALR--------------EELDELEAQIRGNGGDRL--------EQL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 450 KEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgrqkVSEEVEKMSSRERALQMKISDLET 529
Cdd:COG4913 344 EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDLRR 419
|
250 260 270
....*....|....*....|....*....|....*....
gi 197927450 530 ELRKKNEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSET 568
Cdd:COG4913 420 ELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
234-533 |
8.16e-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: 48.91 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 234 RQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAvsaSNDWKSRYEKIAIEKTELEvQIETMKKQISHLLED 313
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI---EKEIEQLEQEEEKLKERLE-ELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 314 LRKMETHGKNSCEEILRKLHSLEDENEALNIENV-----KLKSTLDALKDEVASVENEL----VELQEVEKRQKALVEGY 384
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLreieQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 385 RTQVQKLEEAAAMVKSRCKNLlHENKLIINKKNTKLEKVDGnysllTKLSLEEENHLIQLKCENLKEKLEQMdaenKELE 464
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEELEELEA-----ALRDLESRLGDLKKERDELEAQLREL----ERKI 905
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 197927450 465 RKLADQEEFLKHSDLELREKAAectALSRQLEAALEEGRQKVSEEVEKMSsrERALQMKISDLETELRK 533
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLE---ALEEELSEIEDPKGEDEEIPEEELS--LEDVQAELQRVEEEIRA 969
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-580 |
1.45e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 186 RLQLQIQKREVENERLKEHIQSLETQIAkwnlqvkmnkQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQI 265
Cdd:COG4913 278 RAALRLWFAQRRLELLEAELEELRAELA----------RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 266 RDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLrkmethgknscEEILRKLHSLEDENEAlniE 345
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL-----------EEELEALEEALAEAEA---A 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 346 NVKLKSTLDALKDEVASVEN-------------------------------ELVELQEVEKRQKALVEGY-RTQ------ 387
Cdd:COG4913 414 LRDLRRELRELEAEIASLERrksniparllalrdalaealgldeaelpfvgELIEVRPEEERWRGAIERVlGGFaltllv 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 388 -VQKLEEAAAMVKSR-CKNLLHENKLIINKKNTKLEKVDGNySLLTKLSLEE-------ENHLIQ----LKCENLKE--- 451
Cdd:COG4913 494 pPEHYAAALRWVNRLhLRGRLVYERVRTGLPDPERPRLDPD-SLAGKLDFKPhpfrawlEAELGRrfdyVCVDSPEElrr 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 452 --------------------------------------KLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSR 493
Cdd:COG4913 573 hpraitragqvkgngtrhekddrrrirsryvlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 494 ------------QLEAALEEGRQKVsEEVEKMSSRERALQMKISDLETELRKKNEEQNQLVGNMSTKAQHQDICLKEIQH 561
Cdd:COG4913 653 laeyswdeidvaSAEREIAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
490
....*....|....*....
gi 197927450 562 SLEKSETQNESIKNYLQFL 580
Cdd:COG4913 732 LQDRLEAAEDLARLELRAL 750
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-541 |
1.94e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 187 LQLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASRQKAE--ALKKASKVYRQRLRHFTGDIEQLTSQ 264
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 265 IRDQEAKLSEAvsasNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMEthgknsceeilrKLHSLEDENEALNI 344
Cdd:PRK03918 323 INGIEERIKEL----EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE------------ELERLKKRLTGLTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 345 EnvKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSrCKNLL--HENKLIINKKNTKLEK 422
Cdd:PRK03918 387 E--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPV-CGRELteEHRKELLEEYTAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 423 vdgnyslltklsleeenhlIQLKCENLKEKLEQMDAENKELERKLADQEEFLKhsdleLREKAAECTALSRQLEAALEEG 502
Cdd:PRK03918 464 -------------------IEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELEEKLKKYNLEE 519
|
330 340 350
....*....|....*....|....*....|....*....
gi 197927450 503 RQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQL 541
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
151-394 |
2.26e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 151 EKETYIQELSCLFHNEKESALKANRFSQsvkvvhdrlQLQIQKREVENERLKEHIQSLETQIAKwnLQVKMNKQEAVAVK 230
Cdd:COG3206 132 VKGSNVIEISYTSPDPELAAAVANALAE---------AYLEQNLELRREEARKALEFLEEQLPE--LRKELEEAEAALEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 231 EASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDW----------------KSRYEKIAIEKT 294
Cdd:COG3206 201 FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpellqspviqqlRAQLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 295 ELEV-------QIETMKKQISHLLEDLRkmethgknscEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENEL 367
Cdd:COG3206 281 ELSArytpnhpDVIALRAQIAALRAQLQ----------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
250 260
....*....|....*....|....*..
gi 197927450 368 VELQEVEKRQKALVEGYRTQVQKLEEA 394
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQRLEEA 377
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-582 |
3.53e-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: 46.97 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 330 RKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHEN 409
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 410 KLIINKKNTKLEKVDGNYSLL-----TKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREK 484
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 485 AAECTALSRQLEaaleegrqKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQL----------VGNMSTKAQHQDI 554
Cdd:TIGR02168 837 ERRLEDLEEQIE--------ELSEDIESLAAEIEELEELIEELESELEALLNERASLeealallrseLEELSEELRELES 908
|
250 260
....*....|....*....|....*...
gi 197927450 555 CLKEIQHSLEKSETQNESIKNYLQFLQI 582
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEV 936
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
185-536 |
4.76e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 185 DRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEAS---RQKAEALKKASKVYRQRLRHFTGDIEQL 261
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeelREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 262 TSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMET---HGK--------------NS 324
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleAGKcpecgqpvegsphvET 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 325 CEEILRKLHSLEDENEALNIENVKLKSTLDALKD------------EVASVENELVELQEV---EKRQKAlvEGYRTQVQ 389
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedrierleERREDLEELIAERREtieEKRERA--EELRERAA 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 390 KLE-------EAAAMVKSRCKNLLHENKLIINKKNTKLEKVDGNYSLLTKLSLEEEnhlIQLKCENLKEKLEQMDAENKE 462
Cdd:PRK02224 548 ELEaeaeekrEAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD---AEDEIERLREKREALAELNDE 624
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197927450 463 LERKLADQEEflKHSDLELREKAAECTALSRQLEAAlEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNE 536
Cdd:PRK02224 625 RRERLAEKRE--RKRELEAEFDEARIEEAREDKERA-EEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
295-575 |
1.72e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.46 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 295 ELEVQIETMKKQISHLLEDLRKMETHGKNsceEILRKLHSLEDENEALNIENVKLKSTLDALKDEV--ASVENELVELQE 372
Cdd:PLN03229 433 ELEGEVEKLKEQILKAKESSSKPSELALN---EMIEKLKKEIDLEYTEAVIAMGLQERLENLREEFskANSQDQLMHPVL 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 373 VEKRQKALVE---------GYRTQVQKLEeaaaMVK--SRCKNLLHEN------KLIINKkntKLEKVDGNYSLLTKL-S 434
Cdd:PLN03229 510 MEKIEKLKDEfnkrlsrapNYLSLKYKLD----MLNefSRAKALSEKKskaeklKAEINK---KFKEVMDRPEIKEKMeA 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 435 LEEENHLIQLKC-----ENLKEKLEQMdaeNKELERKLAdqeEFLKHSDLEL-----REKAAECTALSRQLEAALEEGRQ 504
Cdd:PLN03229 583 LKAEVASSGASSgdeldDDLKEKVEKM---KKEIELELA---GVLKSMGLEVigvtkKNKDTAEQTPPPNLQEKIESLNE 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 505 KVSEEVEKM---------------------SSRERALQMKISDLETELRKKNEEqnqlVGNMSTKAQHQDICLKEIQHSL 563
Cdd:PLN03229 657 EINKKIERVirssdlkskiellklevakasKTPDVTEKEKIEALEQQIKQKIAE----ALNSSELKEKFEELEAELAAAR 732
|
330
....*....|..
gi 197927450 564 EKSETQNESIKN 575
Cdd:PLN03229 733 ETAAESNGSLKN 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
290-515 |
2.32e-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: 43.60 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 290 AIEKTELEVQIETMKKQISHLLEDLRKMethgKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVE 369
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 370 LQEVEKRQKALVEGYRTQVQKLEEA--AAMVKSRCKNLLHENKLIINKKNTKLEKVDGNYSLLTKLSLEEENHLIQLKCE 447
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197927450 448 NLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTAL---SRQLEAALEEGRQKVSEEVEKMSS 515
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
445-541 |
2.72e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 445 KCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREkaaectalsrqleaALEEGRQKVSEEvEKMSSRERalqmKI 524
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE--------------ARSEERREIRKD-REISRLDR----EI 474
|
90
....*....|....*..
gi 197927450 525 SDLETELRKKNEEQNQL 541
Cdd:COG2433 475 ERLERELEEERERIEEL 491
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
146-569 |
4.33e-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: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 146 KKKVLEK-ETYIQELSCLFHnEKESALKANrfSQSVKVVHDRLQLQIQK-REVENErlKEHIQSLETQIAKWNLQVKmnk 223
Cdd:pfam15921 487 KKMTLESsERTVSDLTASLQ-EKERAIEAT--NAEITKLRSRVDLKLQElQHLKNE--GDHLRNVQTECEALKLQMA--- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 224 qEAVAVKEASRQKAEALKKaskvyrqrlrhFTGDIEQLTSQIRDQEAKLSEAVsasNDWKSRYEKIAIEKTELEVQIETM 303
Cdd:pfam15921 559 -EKDKVIEILRQQIENMTQ-----------LVGQHGRTAGAMQVEKAQLEKEI---NDRRLELQEFKILKDKKDAKIREL 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 304 KKQISHLleDLRKMEThgKNSCEEILRKLHSLEDENealnienvklkstlDALKDEVASVENELVELQEvekRQKALVEG 383
Cdd:pfam15921 624 EARVSDL--ELEKVKL--VNAGSERLRAVKDIKQER--------------DQLLNEVKTSRNELNSLSE---DYEVLKRN 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 384 YRTQVQKLEEAAAMVKSRCKNLLHEnkliINKKNTKLEKVDGNYSLLTKLSLEEEnhliqlkcENLKEKLEQMDAenkeL 463
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSE----LEQTRNTLKSMEGSDGHAMKVAMGMQ--------KQITAKRGQIDA----L 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 464 ERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQLVG 543
Cdd:pfam15921 747 QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
410 420
....*....|....*....|....*.
gi 197927450 544 NMstKAQHQDICLKEIQHSLEKSETQ 569
Cdd:pfam15921 826 II--QRQEQESVRLKLQHTLDVKELQ 849
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
248-541 |
5.61e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 248 RQRLRHFTGDIEQLTSQIRDQEAKLSEAvsasndwKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEE 327
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADDLEERAEEL-------REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 328 ilrkLHSLEDENEAlnienvkLKSTLDALKDEVASVENELVELQE-VEKRQKALVEG--------------------YRT 386
Cdd:PRK02224 407 ----LGNAEDFLEE-------LREERDELREREAELEATLRTARErVEEAEALLEAGkcpecgqpvegsphvetieeDRE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 387 QVQKLEEAAAMVKSRCKNL--LHENKLIINKKNTKLEKVDGNYSLLTKLSLEEENHLiqlkcENLKEKLEQMDAENKELE 464
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVeeRLERAEDLVEAEDRIERLEERREDLEELIAERRETI-----EEKRERAEELRERAAELE 550
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 197927450 465 RKLADQEEflkhSDLELREKAAECtalsRQLEAALEEGRQKVSEEVEKMsSRERALQMKISDLETELRKKNEEQNQL 541
Cdd:PRK02224 551 AEAEEKRE----AAAEAEEEAEEA----REEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREAL 618
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
168-537 |
6.86e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 168 ESALKANRFSQSVKVVHDRLQLQIQKREVENERLKEHIQSLETQIAKWNLQ--VKMNKQEAVAVKEASRQKAEALKKASK 245
Cdd:PLN02939 81 RTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEdlVGMIQNAEKNILLLNQARLQALEDLEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 246 VYRQRlrhftgdiEQLTSQIRDQEAKLSEAVSASNdwKSRYEKIAIEKteLEVQIETMKKQISHLLEDLRKMEthgknsc 325
Cdd:PLN02939 161 ILTEK--------EALQGKINILEMRLSETDARIK--LAAQEKIHVEI--LEEQLEKLRNELLIRGATEGLCV------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 326 eeilrklHSLEDENEALNIENVKLKSTLDALKDevasvenELVELQEVEKRqkalvegyrtqVQKLEEAAAMVKSRCKNL 405
Cdd:PLN02939 222 -------HSLSKELDVLKEENMLLKDDIQFLKA-------ELIEVAETEER-----------VFKLEKERSLLDASLREL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 406 lhENKLIINKKN-TKL---------EKVDGNYSLLTKLSLEEENHLIQLKcenlkekleqmdaENKELERKLADQEEFLK 475
Cdd:PLN02939 277 --ESKFIVAQEDvSKLsplqydcwwEKVENLQDLLDRATNQVEKAALVLD-------------QNQDLRDKVDKLEASLK 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 197927450 476 HSDLElrEKAAECTALSRQLEAALEEGRQKVSEEvekMSSRERALQMKISDLETELRKKNEE 537
Cdd:PLN02939 342 EANVS--KFSSYKVELLQQKLKLLEERLQASDHE---IHSYIQLYQESIKEFQDTLSKLKEE 398
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
326-426 |
7.48e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 326 EEILRKLHSLEDENEALNIE-NVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKN 404
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKE 493
|
90 100
....*....|....*....|..
gi 197927450 405 LLHENKLIINKKNTKLEKVDGN 426
Cdd:COG0542 494 LAELEEELAELAPLLREEVTEE 515
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
188-576 |
7.70e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 188 QLQIQKREVENERLKEHIQSLETQIAKWNLQVK-MNKQEAVAVkeASRQKAEALKKASKVYRQRLRHFTGDIEQLTS--- 263
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIErYEEQREQAR--ETRDEADEVLEEHEERREELETLEAEIEDLREtia 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 264 -----------QIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHL---LEDLRKMETHGKNSCEEIL 329
Cdd:PRK02224 269 eterereelaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELrdrLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 330 RKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHEN 409
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 410 KLIINKKNTKLEKVDGNYSLLTK-------LSLEEENHLIQLkcENLKEKLEQMDAENKELERKLADQEEFLKHSDlELR 482
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETI--EEDRERVEELEAELEDLEEEVEEVEERLERAE-DLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 483 EKAAECTALSRQLEAA---LEEGRQKVSEEVEKMSS-RERAlqmkiSDLETELRKKNEEQNQLVGNMSTKAQHQDIC--- 555
Cdd:PRK02224 506 EAEDRIERLEERREDLeelIAERRETIEEKRERAEElRERA-----AELEAEAEEKREAAAEAEEEAEEAREEVAELnsk 580
|
410 420
....*....|....*....|....
gi 197927450 556 ---LKEIQHSLEKSETQNESIKNY 576
Cdd:PRK02224 581 laeLKERIESLERIRTLLAAIADA 604
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
284-575 |
9.06e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 284 SRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMEtHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASV 363
Cdd:TIGR04523 159 NKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK-NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 364 ENELVELQEVEKRQKalvEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNtKLEKVDGNYSLLTKLSLEEENHLIQ 443
Cdd:TIGR04523 238 QQEINEKTTEISNTQ---TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-QLNQLKSEISDLNNQKEQDWNKELK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 444 LKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERaLQMK 523
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN-LESQ 392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 197927450 524 ISDLETELRKKNEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIKN 575
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
370-523 |
1.05e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 370 LQEVEKRQKALVEGYRTQVQKL-EEAAAMVKSRCKNLLHENKLIINKKNTKLEKVdgnyslltklsleeENHLIQlKCEN 448
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNELQKL--------------EKRLLQ-KEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 449 LKEKLEQMDAENKELErklaDQEEFLKHSDLELREKAAECTALSRQLEAALE--------EGRQKVSEEVEKMSSRERAL 520
Cdd:PRK12704 98 LDRKLELLEKREEELE----KKEKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEKVEEEARHEAAV 173
|
...
gi 197927450 521 QMK 523
Cdd:PRK12704 174 LIK 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
185-396 |
1.09e-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: 41.67 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 185 DRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKmnkqeavavkeASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQ 264
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-----------ALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 265 IRDQEAKLSEAVSASndwksrYEKIAIEKTELEVQIETMkKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNI 344
Cdd:COG4942 99 LEAQKEELAELLRAL------YRLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 197927450 345 ENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAA 396
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
256-533 |
1.57e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 256 GDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEI------- 328
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeleekv 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 329 --LRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAaamvkSRCKNLL 406
Cdd:PRK03918 283 keLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL-----EKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 407 HENKLIINKKNTKLEKVDGNYSLLTKLSLEEENHLIQlKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAA 486
Cdd:PRK03918 358 EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE-ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 197927450 487 ECTALSRQL-EAALEEGRQKVSEEVEKMSSRERALQMKISDLETELRK 533
Cdd:PRK03918 437 KCPVCGRELtEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
272-475 |
2.70e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 272 LSEAVSASNDWKSRYEKIAiEKTELEVQIETMKkqiSHLLEDLrkmethgknSCEEILRKLhsledENEALNIENvklks 351
Cdd:COG2433 338 LAAALKAYDAYKNKFERVE-KKVPPDVDRDEVK---ARVIRGL---------SIEEALEEL-----IEKELPEEE----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 352 tlDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEeaaamvksrckNLLHENKLIINKKNTKLEKVDGNYsllt 431
Cdd:COG2433 395 --PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-----------AELEEKDERIERLERELSEARSEE---- 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 197927450 432 KLSLEEENHLIQLKCEN--LKEKLEQMDAENKELERKLADQEEFLK 475
Cdd:COG2433 458 RREIRKDREISRLDREIerLERELEEERERIEELKRKLERLKELWK 503
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
79-574 |
2.94e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 79 EHANLSASNLKKIFEQKDILSKELDTFnRVKLALEHLIKQTDYE--QTGPRPPCLLKDLSDSDSENRDLKKK-----VLE 151
Cdd:pfam05483 275 EKTKLQDENLKELIEKKDHLTKELEDI-KMSLQRSMSTQKALEEdlQIATKTICQLTEEKEAQMEELNKAKAahsfvVTE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 152 KETYIQELSCLFHNEKEsalKANRFSQSVKVVHDRLQLQIQK----------REVENERLKEHIQSLET------QIAKW 215
Cdd:pfam05483 354 FEATTCSLEELLRTEQQ---RLEKNEDQLKIITMELQKKSSEleemtkfknnKEVELEELKKILAEDEKlldekkQFEKI 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 216 NLQVKMNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTE 295
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 296 LEVQIETMKKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEK 375
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 376 RQKALVEGYRTQVQKleeaaamvKSRCKNLLHENKLIINKKNTKLEKVDGNYslltklslEEENHLIQLKCENLKEKLEQ 455
Cdd:pfam05483 591 ILENKCNNLKKQIEN--------KNKNIEELHQENKALKKKGSAENKQLNAY--------EIKVNKLELELASAKQKFEE 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 456 M-DAENKELERKLADQEEFLKHSDlELREKAAECTALSRQLEAALEegrQKVSEEVEKMSSRERALQMKISDLETEL--- 531
Cdd:pfam05483 655 IiDNYQKEIEDKKISEEKLLEEVE-KAKAIADEAVKLQKEIDKRCQ---HKIAEMVALMEKHKHQYDKIIEERDSELgly 730
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 197927450 532 RKKNEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIK 574
Cdd:pfam05483 731 KNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLK 773
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
329-510 |
3.45e-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: 39.52 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 329 LRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVekrqkalVEGYRTQVQKLEEAAAMVKSRcknllhe 408
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-------LEDLEKEIKRLELEIEEVEAR------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 409 nkliINKKNTKLEKVDGN--YSLLTK--LSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREK 484
Cdd:COG1579 75 ----IKKYEEQLGNVRNNkeYEALQKeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|....*.
gi 197927450 485 AAECTALSRQLEAALEEGRQKVSEEV 510
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
132-535 |
4.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 132 LKDLSDSDSENRDLKKKVLEKETYIQELSclfhnEKESALKANRFSQSVKVVHDRLQLQIQKREVENERLKEHIQSLETQ 211
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELE-----AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 212 IAKW-NLQVKMNKQEAvAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRyekia 290
Cdd:COG4717 155 LEELrELEEELEELEA-ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 291 IEKTELEVQIETMKKQISHLLEDLR----------------------------------KMETHGKNSCEEILRKLHSLE 336
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 337 DENEALNIENVKLKSTLDAL-------KDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNL--LH 407
Cdd:COG4717 309 ALPALEELEEEELEELLAALglppdlsPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeeLR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 408 ENKLIINKKNTKLEKVDGNYSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEflKHSDLELREKAAE 487
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE--ELAELEAELEQLE 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 197927450 488 CTALSRQLEAALEEGRQKVSEEVEKMSSReRALQMKISDLETELRKKN 535
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
430-541 |
4.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 430 LTKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKhsdlELREKAAECTALSRQLEAALEEGRQKVSEE 509
Cdd:COG4717 118 LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEE 193
|
90 100 110
....*....|....*....|....*....|..
gi 197927450 510 VEKMSSRERALQMKISDLETELRKKNEEQNQL 541
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
265-536 |
5.71e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 265 IRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKN---SCEEILRKLHSLEDENEA 341
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKElsaSSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 342 LNIENVKLKSTLDALKDEVASVENELVELQEVEKR---QKALVEGYRTQVQ-KLEEAAAMVKSRCKNLLHENKLIINKKN 417
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKagaQRKEEEAERKQLQaKLQQTEEELRSLSKEFQELRNSLAQRDT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 418 TKLEKVDGNYSLLTKLSL----EEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLEL---REKAAECTA 490
Cdd:pfam07888 207 QVLQLQDTITTLTQKLTTahrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELhqaRLQAAQLTL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 197927450 491 LSRQLEAALEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNE 536
Cdd:pfam07888 287 QLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
46-274 |
6.68e-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: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 46 TELEAALREAELASCSVELLLPLlkntvegiglehanlsasnlKKIFEQKDILSKELDTFNRVKLALEHLIKQTDYEQtg 125
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPI--------------------RELAERYAAARERLAELEYLRAALRLWFAQRRLEL-- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 126 prppcLLKDLSDSDSENRDLKKKVLEKETYIQELsclfhNEKESALKANRFSQSVKVVhDRLQLQIQKREVENERLKEHI 205
Cdd:COG4913 293 -----LEAELEELRAELARLEAELERLEARLDAL-----REELDELEAQIRGNGGDRL-EQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 197927450 206 QSLETQIAKWNLQVKMNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSE 274
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
200-578 |
7.21e-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: 39.64 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 200 RLKEHIQSLETQIAKWNLQVKMNKQEAVAV-KEASRQKAEALKKASKVYRQ-RLRHFTGDIEQLTSQIRDQEAKLSEAVS 277
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHInNELESKEEQLSSYEDKLFDVcGSQDEESDLERLKEEIEKSSKQRAMLAG 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 278 ASNDWKSRYEKIAIEKTE---LEVQIETMKKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLD 354
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 355 ALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLeeaaaMVKSRCKNLLHENKLIINKKNTKLEKVDGNY----SLL 430
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTI-----MPEEESAKVCLTDVTIMERFQMELKDVERKIaqqaAKL 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 431 TKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLE--AALEEGRQKVSE 508
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQrrQQFEEQLVELST 895
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 509 EVEKMSSRERALQMKISDLETELRKKNEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIKNYLQ 578
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
131-541 |
9.32e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 131 LLKDLSDSDSENRDLKKKVLEKETYIQELSCLFHNEKESALKANRFSQSVKVVHDRLQlQIQKREVENERLKEHIQSLET 210
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYN-NLKSALNELSSLEDMKNRYES 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 211 QIAKWNLQVKMNKQEAVAVKEASRQKAEALKKASKVYRQRLRHF------TGDIEQLTSQIRDQEAKLSEAVSASNDWKS 284
Cdd:PRK01156 257 EIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYfkykndIENKKQILSNIDAEINKYHAIIKKLSVLQK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 285 RYEKIAIEKTELevqiETMKKQISHLLEDLRKMETHgKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVE 364
Cdd:PRK01156 337 DYNDYIKKKSRY----DDLNNQILELEGYEMDYNSY-LKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKEL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 365 NEL-VELQEVEKRQKALVEGYRTQVQKLEEA---AAMVKSR-----CKNLLHENKL--IINKKNTKL----EKVDGNYSL 429
Cdd:PRK01156 412 NEInVKLQDISSKVSSLNQRIRALRENLDELsrnMEMLNGQsvcpvCGTTLGEEKSnhIINHYNEKKsrleEKIREIEIE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197927450 430 LTKLSlEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFlKHSDLELREKAAECTALSRQLEAA-LEEGRQKVSE 508
Cdd:PRK01156 492 VKDID-EKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDI-KIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTS 569
|
410 420 430
....*....|....*....|....*....|...
gi 197927450 509 EVEKMSsreralQMKISDLETELRKKNEEQNQL 541
Cdd:PRK01156 570 WLNALA------VISLIDIETNRSRSNEIKKQL 596
|
|
| |
