|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-366 |
5.04e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 61 LLEEEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKDSAvfsmRQETHAAQEEVQVLRRTMEKTAAEREHEV--- 137
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLEerr 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 138 SALKGNLATLTSELEKWQQAANKYERELESVQASHLQQNQQRDRATKQQAGELEKVQKDceslrrdcASLRSEREQLADK 217
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA--------EAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 218 QQKEKASLQNENSSLRSEKEQLQKKQQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNS 297
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517582 298 RIKELQKEYEEMQAELSGLRGkfENAEEEKRSVSLELQQSQERLRLMQDKDNHLSLLQPILAVAIGLVL 366
Cdd:COG1196 464 LLAELLEEAALLEAALAELLE--ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-352 |
4.31e-13 |
|
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: 70.86 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 66 KRANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKDSAVFSMR------QETHAAQEEVQVLRRTMEKTAAEREHEVSA 139
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEeltaelQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 140 LKGNLATLTSELEKWQQAANKYERELESVQASHLQQNQQRDRA---TKQQAGELEKVQKDCESLRRDCASLRSEREQLAD 216
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 217 KQQKEKASLQNENSSLRSEkeqlqkkqqqlekeldssKKQNTSLSNTVKSLEKTQADLEKRLSVLQEE------------ 284
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQL------------------ELQIASLNNEIERLEARLERLEDRRERLQQEieellkkleeae 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528517582 285 HQRDNGQLEQSNSRIKELQKEYEEMQAELSGLRGKFENAEEEKRSVSLELQQSQERLRLMQDKDNHLS 352
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-362 |
1.06e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 70 KQQAEEsAKQMKVLQTQLQKLQEEmenLRDQKDSAVFSMRQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATLTS 149
Cdd:COG1196 206 ERQAEK-AERYRELKEELKELEAE---LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 150 ELEKWQQAANKYERELESVQASHLQQNQQRDRATKQQA---GELEKVQKDCESLRRDCASLRSEREQLADKQQKEKASLQ 226
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEeleEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 227 NENSSLRSEKEQLQKKQQQLEKELD---SSKKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQ 303
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEellEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 528517582 304 KEYEEMQAELSGLRGKFENAEEEKRSVSLELQQSQERLRLMQDKDNHLSLLQPILAVAI 362
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
64-341 |
2.03e-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: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 64 EEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKDSAVFSMRQETHAAQEEVQVLRRTMEKTAAER---EHEVSAL 140
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIaqlSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 141 KGNLATLTSELEKWQQAANKYERELESVQAshlqqnqqrdratkqqagELEKVQKDCESLRRDCASLRSEREQLADKQQK 220
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEA------------------QIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 221 ekaslqnenssLRSEKEQLQKKQQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIK 300
Cdd:TIGR02168 822 -----------LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 528517582 301 ELQKEYEEMQAELSGLRGKFENAEEEKRSVSLELQQSQERL 341
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-333 |
3.30e-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: 58.54 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 11 NKVSLIKDELSRSTVEASESEKVIQRLNQELQEANEQPNSSKYKCVELqgllEEEKRANKQQAEESAKQMKVLQTQLQKL 90
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL----EQEIENVKSELKELEARIEELEEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 91 QEEMENLRDQKDSAVFsmrQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATLTSELEKWQQAANKYERELESVQA 170
Cdd:TIGR02169 778 EEALNDLEARLSHSRI---PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 171 ShLQQNQQRDRATKQQAGELEKVQKDCES----LRRDCASLRSEREQLADKQQKEKASLQNENSSLrSEKEQLQKKQQQL 246
Cdd:TIGR02169 855 E-IENLNGKKEELEEELEELEAALRDLESrlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRL-SELKAKLEALEEE 932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 247 EKELDSSKKQNTSLSNTVKSLEKTQADLEK---RLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSGLRGKFENA 323
Cdd:TIGR02169 933 LSEIEDPKGEDEEIPEEELSLEDVQAELQRveeEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
330
....*....|
gi 528517582 324 EEEKRSVSLE 333
Cdd:TIGR02169 1013 EKKKREVFME 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
61-342 |
7.28e-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: 57.77 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 61 LLEEEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKDSAVFSMRQETHAAQEEVQVLRRTMEKTAAEREHEVSAL 140
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 141 KGNLATLTSELEKWQQAANKYERELESVQASHlqqnQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLADKQQ- 219
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAe 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 220 --KEKASLQNENSSLRSEKEQLQKKQQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNS 297
Cdd:TIGR02169 383 trDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 528517582 298 RIKELQKEYEEMQAELSGLRGKFENAEEEKRSVSLELQQSQERLR 342
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-347 |
1.11e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 98 RDQKDSAVFSMRQETHAAQEEVQVlrrtMEKTAAEREHEVSALKGNLATLTSELEKWQQAANKYERELESVQAS---HLQ 174
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEE----LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 175 QNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLADKQQKEKASLQNENSSLRSEKEQLQKKQQQLEKELDSSk 254
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA- 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 255 kqnTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSGLRGKFENAEEEKRSVSLEL 334
Cdd:TIGR02168 820 ---ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250
....*....|...
gi 528517582 335 QQSQERLRLMQDK 347
Cdd:TIGR02168 897 EELSEELRELESK 909
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-347 |
4.99e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 3 EQKLKDPINKVSLIKDELSRSTVEASESEKVIQRLNQELQEANEQPNSSKYKCVELQGLLEEEKrankQQAEESAKQMKV 82
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 83 LQTQLQKLQEEMENLRDQKDSAvFSMRQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATLTSELEKWQQAANKYE 162
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEA-EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 163 RELESVQashlQQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLadkqQKEKASLQNENSSLRSEKEqlqkk 242
Cdd:TIGR02168 831 RRIAATE----RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL----LNERASLEEALALLRSELE----- 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 243 qqqlekeldsskkqntslsntvkSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSGL-RGKFE 321
Cdd:TIGR02168 898 -----------------------ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLE 954
|
330 340
....*....|....*....|....*.
gi 528517582 322 NAEEEKRSVSLELQQSQERLRLMQDK 347
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
63-341 |
1.13e-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: 53.92 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 63 EEEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKDSAVfsMRQETHAAQEEVQVLRRTMEKTAAEREHEvsALKG 142
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEKREYEGYELLKEKEALERQKE--AIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 143 NLATLTSELEKWQQAANKYERELESVQASHLQQNQQRDRATKQQA----GELEKVQKDCESLRRDCASLRSEREQLADKQ 218
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 219 QKEKA---SLQNENSSLRSEKEQLQKKQQQLEKELDSSKKQNTSLSNTVKSLEKT-------QADLEKRLSVLQEEHQRD 288
Cdd:TIGR02169 325 AKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetrdeLKDYREKLEKLKREINEL 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528517582 289 NGQLEQSNSRIKELQKEYEEMQAELSGLRGKFENAEEEKRSVSLELQQSQERL 341
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-361 |
1.58e-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: 53.53 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 86 QLQKLQEEMENLRDQKDSA---VFSMRQETHAAQEEVQVLRRTMEktaaEREHEVSALKGNLATLTSELEKWQQAANKYE 162
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLqseLRRIENRLDELSQELSDASRKIG----EIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 163 RELESVQAshlqqnqqrdratkqqagELEKVQKDCESLRRDCASLRSEREQLADKQQKEK-ASLQNENSSLRSEKEQLQK 241
Cdd:TIGR02169 751 QEIENVKS------------------ELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 242 KQQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSGLRGKFE 321
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 528517582 322 NAEEEKRSVSLELQQSQERLrlmQDKDNHLSLLQPILAVA 361
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQI---EKKRKRLSELKAKLEAL 929
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-318 |
4.89e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 26 EASESEKVIQRLNQELQEANEQPNSSKYKCVELQGLLEEEkraNKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKDSAV 105
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 106 FSMrQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATLTSELEKWQQAANKYERELESVQASHlqqnqqrdRATKQ 185
Cdd:TIGR02169 315 REL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF--------AETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 186 qagELEKVQKDCESLRRDCASLRSEREQLADKQQKEKASLQNENSSLRSEKEQLQKKQQQLEKELDSSKKQNTSLSNTVK 265
Cdd:TIGR02169 386 ---ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528517582 266 SLEK----------TQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSGLRG 318
Cdd:TIGR02169 463 DLSKyeqelydlkeEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHG 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-339 |
1.02e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 17 KDELSRSTVEASESEKVIQRLNQELQEANEQPNSSKYKCVELQGLLEEEKRANKQQAEESAKqmkvLQTQLQKLQEEMEN 96
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----LEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 97 LRDQKDSAvfSMRQETHAAQEEVQvlrrtmEKTAAEREHEVSALKGNLATLTSELEKWQQAANKYERELESVQASHLQQN 176
Cdd:TIGR02168 314 LERQLEEL--EAQLEELESKLDEL------AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 177 QQRDRATKQQAgelekvqkdceSLRRDCASLRSEREQLADKQQKEKASLQNENSSLrsekeqlqkkqqqlekeldsSKKQ 256
Cdd:TIGR02168 386 SKVAQLELQIA-----------SLNNEIERLEARLERLEDRRERLQQEIEELLKKL--------------------EEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 257 NTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSGLRGKFENAEEEKRSVSLELQQ 336
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
...
gi 528517582 337 SQE 339
Cdd:TIGR02168 515 QSG 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-251 |
1.18e-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: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 2 EEQKLKDPINKVSLIKDELSRSTVEASESEKVIQRLNQELQEAN---EQPNSSKYKCVELQGLLEEEKRANKQQAEESAK 78
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLaelARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 79 QMKVLQTQLQKLQEEMENLRDQKDSAVFSMRQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATLTSELEKwQQAA 158
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-EEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 159 NKYERELESVQASHLQQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLADKQQKEKASLQNENSSLRSEKEQ 238
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250
....*....|...
gi 528517582 239 LQKKQQQLEKELD 251
Cdd:COG1196 490 AARLLLLLEAEAD 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
68-277 |
1.96e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 68 ANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKDSAVfSMRQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATL 147
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALL-KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 148 TSELEKWQQAANKYERELESVQ-----------------ASHLQQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSE 210
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528517582 211 REQLADKQQKEKASLQNENSSLRSEKEQLQKKQQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKR 277
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-308 |
4.83e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 21 SRSTVEASESEKViQRLNQELQEANEQPNSSKYKCVELQGLLEE---EKRANKQQAEESAKQMKVLQTQLQKLQEEMENL 97
Cdd:TIGR02169 664 GGILFSRSEPAEL-QRLRERLEGLKRELSSLQSELRRIENRLDElsqELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 98 RDQKDSavfsMRQETHAAQEEVQvlrrTMEKTAAEREHEVSALKGNLATLTSEL--EKWQQAANKYE--RELESVQASHL 173
Cdd:TIGR02169 743 EEDLSS----LEQEIENVKSELK----ELEARIEELEEDLHKLEEALNDLEARLshSRIPEIQAELSklEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 174 QQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLADKQQKEKASLQNENSSLRSEKEQLQKKQQQLEKELDSS 253
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 528517582 254 KKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEE 308
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
26-233 |
1.04e-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: 43.98 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 26 EASESEKVIQRLNQELQEANEQPNSSKYKcvelQGLLEEEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKDSav 105
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 106 fsMRQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATLTSELEKWQQAANKYERELESVQASHLQQNQQRDRATKQ 185
Cdd:COG4942 95 --LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528517582 186 QAgELEKVQKDCESLRRDCASLRSEREQLADKQQKEKASLQNENSSLR 233
Cdd:COG4942 173 RA-ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3-217 |
1.35e-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: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 3 EQKLKDPINKVSLIKDELSRSTVEASESEKVIQRLNQELQEANEQPNsskykcvELQGLLEEEKRANKQQAEESAKQMKV 82
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 83 LQTQLQklQEEMENLRDQKDSAVFSMRQETHAAQeeVQVLRRTMEKTAAEREhEVSALKGNLATLTSELEKWQQAANKYE 162
Cdd:COG4942 113 LYRLGR--QPPLALLLSPEDFLDAVRRLQYLKYL--APARREQAEELRADLA-ELAALRAELEAERAELEALLAELEEER 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 528517582 163 RELESVQASHLQQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLADK 217
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-283 |
2.31e-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: 43.51 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 18 DELSRSTVEASESEKVIQRLNQELQEANEQPNSSKYKCVELQGL---LEEEKRANKQQAEESAKQMKVLQTQLQKLQEEM 94
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 95 ENLRDQKDS--AVFSMRQETHAAQ----EEVQVLRRTMEKTAAEREHEVSALKGNLATLTSELEKWQQAANKYERELESV 168
Cdd:TIGR02168 333 DELAEELAEleEKLEELKEELESLeaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 169 QASH-LQQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLADKQQKEKASLqNENSSLRSEKEQLQKKQQQLE 247
Cdd:TIGR02168 413 EDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL-EEAEQALDAAERELAQLQARL 491
|
250 260 270
....*....|....*....|....*....|....*.
gi 528517582 248 KELDSSKKQNTSLSNTVKSLEKTQADLEKRLSVLQE 283
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
144-374 |
3.22e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 144 LATLTSELEKWQQAANKYERELESVQASHLQQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLadKQQKEKA 223
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL--REELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 224 SLQNENSSLRSEKEQLQKKQQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQsnsRIKELQ 303
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLA 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528517582 304 KEYEEMQAELSGLRGKFENAEEEKRSVSLELQQSQERLRLMQDKDNHLSLLQPILAVAIGLVLALLYWCLG 374
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLL 269
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
5-336 |
3.49e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 5 KLKDPINKVSLIKDELSRSTVEASESEKVIQRLNQELQEANEQPNSSKYKCVELQGLLEEEKR---ANKQQAEESAKQMK 81
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKqlsEKQKELEQNNKKIK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 82 VLQTQLQKLQEEMENLRDQKDSAVFSMRQETHAAQEEVqvlRRTMEKTAAEREHEVSALKGNLATLTSELEKWQQAANKY 161
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKK---LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 162 ERELEsvqashlQQNQQRDRATKQQAGELEKVQKdCESLRRDCASLRSEREQLADKQQKEKASLQNENSSLRSEKEQLQK 241
Cdd:TIGR04523 362 QRELE-------EKQNEIEKLKKENQSYKQEIKN-LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 242 KQQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSGLRGKFE 321
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
330
....*....|....*
gi 528517582 322 NAEEEKRSVSLELQQ 336
Cdd:TIGR04523 514 DLTKKISSLKEKIEK 528
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
83-319 |
3.88e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 83 LQTQLQKLQEEMENLRDqkdsavfsMRQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATLTSELEKWQQAANKYE 162
Cdd:COG4913 223 TFEAADALVEHFDDLER--------AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 163 RELESVQASHLQQNQQRDRATKQqageLEKVQKDCESLRRdcaslrsereQLADKQQKEKASLQNEnssLRSEKEQLQKK 242
Cdd:COG4913 295 AELEELRAELARLEAELERLEAR----LDALREELDELEA----------QIRGNGGDRLEQLERE---IERLERELEER 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528517582 243 QQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSGLRGK 319
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
57-355 |
5.74e-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: 42.03 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 57 ELQGLLEEEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKDSAVFSMRQethAAQEEVQVLRRTMEKTAAEREHE 136
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQ---AEMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 137 VSALKGNLATLTSELEKWQQAANKYE--RELESVQASHLQQNQ-----------------QRDRATKQQAGELEKVQKDC 197
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAMEISrmRELERLQMERQQKNErvrqeleaarkvkileeERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 198 ESLR-RDCASLRSEREQLADKQQKEKASLQNENSSLRSEKEQLQKKQQQLEKELDsskkqntslsntvkslEKTQADLEK 276
Cdd:pfam17380 430 EEARqREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR----------------DRKRAEEQR 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 277 RLSVLQEEHQRDNGQLEQSNSRiKELQKEYEEMQAELSGLRGKFENAEEEKRSVSL-ELQQSQERLRLMQDKDNHLSLLQ 355
Cdd:pfam17380 494 RKILEKELEERKQAMIEEERKR-KLLEKEMEERQKAIYEEERRREAEEERRKQQEMeERRRIQEQMRKATEERSRLEAME 572
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
63-166 |
9.71e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 63 EEEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQ---KDSAVFSMRQETHAAQEEvqvlrrtmEKTAAEREHEVSA 139
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEleeKDERIERLERELSEARSE--------ERREIRKDREISR 469
|
90 100
....*....|....*....|....*..
gi 528517582 140 LKGNLATLTSELEKWQQAANKYERELE 166
Cdd:COG2433 470 LDREIERLERELEEERERIEELKRKLE 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
76-333 |
1.03e-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: 40.90 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 76 SAKQMKVLQTQLQKLQEEMENLRDQkdsavfsmRQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATLTSELEKWQ 155
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKE--------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 156 QAANKYERELESVQASHLQQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRsereQLADKQQKEKASLQNEnsslrse 235
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEELRAD------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 236 keqlqkkQQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSG 315
Cdd:COG4942 159 -------LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|....*...
gi 528517582 316 LRGKFENAEEEKRSVSLE 333
Cdd:COG4942 232 LEAEAAAAAERTPAAGFA 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-299 |
1.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 72 QAEESAKQMKVLQTQLQKLQEEMENLRDQKD--SAVFSMRQETHAAQEEVQVLRRTMEKTAAEREHEVSALkgnlatLTS 149
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL------LEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 150 ELEKWQQAANKYERELESVQASHLQQNQQRDRATKQQAG----ELEKVQKDCESLRRDCASLRSEREQLADKQQKEKASL 225
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528517582 226 QNENSSLRSEKEQLQKKQQQLEKELDSskkqntsLSNTVKSLEKTQADLEKRLSVLQEEHQRdngqLEQSNSRI 299
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEA-------LEEALAEAEAALRDLRRELRELEAEIAS----LERRKSNI 438
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
11-326 |
2.17e-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: 40.00 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 11 NKVSLIKDELSRSTVEASESEKVIQRLNQELQEANEQPNSSKYKCVELQ---GLLEEEKRANKQQAEESAKQMKVLQTQL 87
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLEsqiNDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 88 QKLQEEMENLRDQKDSAvfsmRQETHAAQEEVQVLRRTMEKTAAEREH---EVSALKGNLATLTSELEKWQQAANKYERE 164
Cdd:TIGR04523 422 ELLEKEIERLKETIIKN----NSEIKDLTNQDSVKELIIKNLDNTRESletQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 165 LESVQASHLQQNQQRDRATKQQAGELEKVQK-DCESLRRDCASLRSEREQLADKQ-------QKEKASLQNENSSLRSEK 236
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKlESEKKEKESKISDLEDELNKDDFelkkenlEKEIDEKNKEIEELKQTQ 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 237 EQLQKKQQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSGL 316
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
330
....*....|
gi 528517582 317 RGKFENAEEE 326
Cdd:TIGR04523 658 RNKWPEIIKK 667
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
61-223 |
2.85e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 61 LLEEEKRANK--QQAEESAKQMKvlQTQLQKLQEEMENLRDQKDSAVFSMRQEthAAQEEVQVLRRtmEKTAAEREHEVS 138
Cdd:PRK12704 33 IKEAEEEAKRilEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNE--LQKLEKRLLQK--EENLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 139 ALKGNLATLTSELEKWQQAANKYERELESVQASHLQQNQQRDRATKQQAGE--LEKVQkdcESLRRDCASLRSEREQLAD 216
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVE---EEARHEAAVLIKEIEEEAK 183
|
....*..
gi 528517582 217 KQQKEKA 223
Cdd:PRK12704 184 EEADKKA 190
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
20-343 |
3.79e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 20 LSRSTVEASESEKVIQRLNQELQEANEQPNSSKYKCVELQGLLEEEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLRD 99
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 100 QKDSAVFSMRQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATLTSelekwqqAANKYERELESVQASHLQQNQQR 179
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA-------AKKKLELDLKELEAQIDAANKGR 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 180 DRATKQqageLEKVQKDCESLRRDCASLRSEREQL---ADKQQKEKASLQNENSSLRSEKEQLQKKQQQLEKELDSSKKQ 256
Cdd:pfam01576 794 EEAVKQ----LKKLQAQMKDLQRELEEARASRDEIlaqSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 257 NTSLSNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKEYEEMQAELSGLRGKFENAEEEKRsvSLELQQ 336
Cdd:pfam01576 870 IASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQ--QLERQN 947
|
....*..
gi 528517582 337 SQERLRL 343
Cdd:pfam01576 948 KELKAKL 954
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-347 |
3.86e-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: 3.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528517582 272 ADLEKRLSVLQEEHQRdngqLEQSNSRIKELQKEYEEMQAELSGLRGKFENAEEEKRSVSLELQQSQERLRLMQDK 347
Cdd:COG4913 664 ASAEREIAELEAELER----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-333 |
4.49e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 18 DELSRSTVEASESEKVIQRLNQ--ELQEANEQPNSSKYKCVELQGLLEEEKRANK-QQAEESAKQMKVLQTQLQKLQEEM 94
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEA 1539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 95 ENLRDQKDSAVFSMRQETHAAQEEVQVL-------RRTMEKTAAEREHEVSALKGNLATLTSELEKWQQAANKYERELES 167
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEeakkaeeDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 168 VQASHLQQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLADKQQKEK----------------ASLQNENSS 231
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeeakkaeedekkaAEALKKEAE 1699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 232 LRSEKEQLQKKQQQLEKELDSSKKQNTSLSNTVKSLEKTQADLEKRlsvlQEEHQRDNGQLEQSNSRIKELQKEYEEMQA 311
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
330 340
....*....|....*....|..
gi 528517582 312 ELSGLRGKFENAEEEKRSVSLE 333
Cdd:PTZ00121 1776 EKEAVIEEELDEEDEKRRMEVD 1797
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
8-203 |
4.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 8 DPINKVSLIKDELSRSTVEASESEKVIQRLNQELQEANEQPNSSK------YKCVELQGLLEE--EKRANKQQAEESAKQ 79
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeysWDEIDVASAEREiaELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 80 MKVLQTQLQKLQEEMENLRDQKDsavfsmrqethaaqeEVQVLRRTMEKTAAEREHEVSALKGNLATLTSELEKWQ--QA 157
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELD---------------ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELraLL 751
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 528517582 158 ANKYERELESVQASHLQQNQQRDRatKQQAGELEKVQKDCESLRRD 203
Cdd:COG4913 752 EERFAAALGDAVERELRENLEERI--DALRARLNRAEEELERAMRA 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
73-325 |
5.46e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 73 AEESAKQMKVLQTQLQKLQEEMENLRDQKDSAVFSMRQETHAAQ-----EEVQVLRRTMEKTAAEREHEVSALKGNLATL 147
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERleerrEDLEELIAERRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 148 TSELEKWQQAANKYERELESVQ--ASHLQQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLADKQQKEKASL 225
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAReeVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERL 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 226 QNENSSLRSEKEQLQkkqqqlekeldsskkqntslsntvkslektqadlEKRLSVLQEEHQRDNGQLEQSNSRIKELQKE 305
Cdd:PRK02224 630 AEKRERKRELEAEFD----------------------------------EARIEEAREDKERAEEYLEQVEEKLDELREE 675
|
250 260
....*....|....*....|
gi 528517582 306 YEEMQAELSGLRGKFENAEE 325
Cdd:PRK02224 676 RDDLQAEIGAVENELEELEE 695
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-170 |
5.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 11 NKVSLIKDELSRSTVEASESEKVIQRLNQELQEANEQPNSSKYKCVElqgLLEEEKRANKQQAEESAKQMKVLQTQLQKL 90
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE---QLEREIERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 91 QEEMENLRDqkdsAVFSMRQETHAAQEEVQVLRRTMEKTAAEREHEVSALKGNLATLTSELEKWQQAANKYERELESVQA 170
Cdd:COG4913 372 GLPLPASAE----EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
34-342 |
5.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.78 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 34 IQRLNQELQEANEQPNSSKyKCVELQGLLEEEKRANKQQAEESAKQmkvLQTQLQKLQEEMEnlrdqkdsavfsmRQETH 113
Cdd:PRK04863 350 IERYQADLEELEERLEEQN-EVVEEADEQQEENEARAEAAEEEVDE---LKSQLADYQQALD-------------VQQTR 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 114 AAQ--EEVQVLRRTMEKTAAErEHEVSALKGNLATLTSELEKWQQAANKYERELESVQAsHLQQNQQRDRATKQQAGELE 191
Cdd:PRK04863 413 AIQyqQAVQALERAKQLCGLP-DLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQA-AHSQFEQAYQLVRKIAGEVS 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 192 KVQKDcESLRRDCASLRSEREQLADKQQkekasLQNENSSLRsekeQLQKKQQQLEKELDSSKKQNTSLSNTVKSLEKTQ 271
Cdd:PRK04863 491 RSEAW-DVARELLRRLREQRHLAEQLQQ-----LRMRLSELE----QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQ 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 272 ADLEKRLSVLQEEhQRDNG--------QLEQSNSRIKELQK---EYEEMQAELSGLRGKFENAEEEKRSVSLELQQSQER 340
Cdd:PRK04863 561 EELEARLESLSES-VSEARerrmalrqQLEQLQARIQRLAArapAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLER 639
|
..
gi 528517582 341 LR 342
Cdd:PRK04863 640 ER 641
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
64-234 |
7.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 64 EEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKDSAvfsmrqETHAAQEEVQVLRRTMEKTAAEREHEVSALKGN 143
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL------REELEKLEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 144 LATLTSELEKWQQAANKYERELESVQASHLQQNQQRDRATKQQAGELEKVQKDCESLRRDCASLRSEREQLADKQQKEKA 223
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|.
gi 528517582 224 SLQNENSSLRS 234
Cdd:COG4717 228 ELEQLENELEA 238
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
86-341 |
7.65e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 86 QLQKLQEEMENLRDQKdSAVFSMRQETHAAQEEVQvlRRTMEKTAAEREHEVSALKGNLATLTSELEKWQ---QAANKYE 162
Cdd:PRK02224 160 QLGKLEEYRERASDAR-LGVERVLSDQRGSLDQLK--AQIEEKEEKDLHERLNGLESELAELDEEIERYEeqrEQARETR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 163 RELESVQASHLQQNQqrdratkqqagELEKVQKDCESLRRDCASLRSEREQLADK---QQKEKASLQNENSSLRSEKEQL 239
Cdd:PRK02224 237 DEADEVLEEHEERRE-----------ELETLEAEIEDLRETIAETEREREELAEEvrdLRERLEELEEERDDLLAEAGLD 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 240 QKKQQQLEKELDSSKKQNTSL--------------SNTVKSLEKTQADLEKRLSVLQEEHQRDNGQLEQSNSRIKELQKE 305
Cdd:PRK02224 306 DADAEAVEARREELEDRDEELrdrleecrvaaqahNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
250 260 270
....*....|....*....|....*....|....*.
gi 528517582 306 YEEMQAELSGLRGKFENAEEEKRSVSLELQQSQERL 341
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-225 |
7.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 34 IQRLNQELQEANEQpnsskykcvelqgllEEEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLRDQKdsAVFSMRQETH 113
Cdd:COG4717 73 LKELEEELKEAEEK---------------EEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 114 AAQEEVQVLRRTMEKtAAEREHEVSALKGNLATLTSELEKWQQAANKYERELESVQASHLQQNQQRDRATKQQA----GE 189
Cdd:COG4717 136 ALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLaeleEE 214
|
170 180 190
....*....|....*....|....*....|....*.
gi 528517582 190 LEKVQKDCESLRRDCASLRSEREQLADKQQKEKASL 225
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-223 |
8.10e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.51 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 19 ELSRSTVEASESEkvIQRLNQELQEANEQPNSSKYKCVELQGLLEEEKRANKQQAEESAKQMKVLQTQLQKLQEEMENLR 98
Cdd:TIGR02169 304 ASLERSIAEKERE--LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517582 99 DQKDsAVFSMRQETHAAQEEVQVLRRTMEKTA----------AEREHEVSALKGNLATLTSELEKWQQAANKYERELESV 168
Cdd:TIGR02169 382 ETRD-ELKDYREKLEKLKREINELKRELDRLQeelqrlseelADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 528517582 169 QAShLQQNQQRDRATKQqagELEKVQKDCESLRRDCASLRSEREQLADKQQKEKA 223
Cdd:TIGR02169 461 AAD-LSKYEQELYDLKE---EYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
|