|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
140-349 |
1.26e-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: 61.62 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 140 CQKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKC-----NRVSMLAVEEY 214
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeealnDLEARLSHSRI 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 215 EELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQ-----------LEEERIQH 283
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKeienlngkkeeLEEELEEL 873
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166851844 284 QKKVKELEERLENeaLHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSE 349
Cdd:TIGR02169 874 EAALRDLESRLGD--LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-350 |
3.33e-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: 60.07 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 140 CQKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLAVEEYEELQV 219
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 220 NLELEKDLRKKAEsfaQEMFIEQNKLKRQSHLLLQSslpDQQLLKALDENAKLIQQLEEERIQ-HQKKVKELEERLENEA 298
Cdd:TIGR02168 380 QLETLRSKVAQLE---LQIASLNNEIERLEARLERL---EDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQ 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 166851844 299 LHKEihNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:TIGR02168 454 EELE--RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-350 |
2.93e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 141 QKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLAVEEYEELQVN 220
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 221 LELEKDLRKKAESFAQEMFieqNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQKKVKELEERLENE--A 298
Cdd:COG4942 113 LYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 166851844 299 LHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-416 |
2.33e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 141 QKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLAVEEYEELQVN 220
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 221 LELEKDLRKKAESFAQEMfIEQNKLKRQSHLLLQSSLpdQQLLKALDENAKLIQQLEEERIQHQKKVKELEERLEN---- 296
Cdd:COG1196 304 IARLEERRRELEERLEEL-EEELAELEEELEELEEEL--EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaeee 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 297 -EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMS 375
Cdd:COG1196 381 lEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 166851844 376 MIRKRSHPSGNSAKKEKTTQPETAEEVTDLKRQAVEEMMDR 416
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-335 |
2.54e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 6 EEKQLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQkishmvieevnfmQNHLEIEktcresaEA 85
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR-------------LELEELE-------LE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 86 LATKLNKENKTLKRISMLymaklgpdviTEEINIDDDDPATDTDAAAETcvsvqcQKQIKELRDQIVSVQEEKKVLAIEL 165
Cdd:COG1196 283 LEEAQAEEYELLAELARL----------EQDIARLEERRRELEERLEEL------EEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 166 ENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLA----VEEYEELQVNLELEKDLRKKAESFAQEMFIE 241
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAlraaAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 242 QNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQKKVKELEERLenEALHKEIHNLRQQLELLEDDKRELE 321
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL--AELLEELAEAAARLLLLLEAEADYE 504
|
330
....*....|....
gi 166851844 322 QKYQSSEEKARNLK 335
Cdd:COG1196 505 GFLEGVKAALLLAG 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-350 |
3.26e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 141 QKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLE---QRKVLEKCNRVSMLAVEEYEEL 217
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaEIEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 218 QVNLELE-KDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQKKVKELEERLEN 296
Cdd:TIGR02168 784 IEELEAQiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166851844 297 ------------EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:TIGR02168 864 leelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
136-350 |
1.21e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 136 VSVQCQKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRkvlekcnrvsmlavEEYE 215
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ--------------AEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 216 ELQVNLElekDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPD-----QQLLKALDENAKLIQQLEEERIQHQKKVKEL 290
Cdd:COG3883 76 EAEAEIE---ERREELGERARALYRSGGSVSYLDVLLGSESFSDfldrlSALSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 291 EERLEnealhkeihNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:COG3883 153 EAKLA---------ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
225-344 |
1.69e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 225 KDLRKKAESFAQEMFIEQNKLKRQshlllqsslpdqQLLKALDENAKLIQQLEEERIQHQKKVKELEERLEN--EALHKE 302
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKE------------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkeENLDRK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 166851844 303 IHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKR 344
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2-341 |
2.61e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 2 NSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEfqkISHMVIEEV-----NFMQNHLEIE 76
Cdd:PLN02939 72 NGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQ---LSDFQLEDLvgmiqNAEKNILLLN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 77 KTCRESAEALATKLNKENKTLKRISMLYM--AKLGPDVIT---EEINIDDDDPATDTDAAAETCVSVQCQKQIKELRDQI 151
Cdd:PLN02939 149 QARLQALEDLEKILTEKEALQGKINILEMrlSETDARIKLaaqEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKEL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 152 VSVQEEKKVLAIELENLKSKLGEVM---EEVNKVKQEKAVLNSEVLE-QRKVLEKCNRVSMLAVEEYEELQVNLELEKDL 227
Cdd:PLN02939 229 DVLKEENMLLKDDIQFLKAELIEVAeteERVFKLEKERSLLDASLRElESKFIVAQEDVSKLSPLQYDCWWEKVENLQDL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 228 RKKAESFAQE--MFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQleeeriqhqkKVKELEERLenEALHKEIHN 305
Cdd:PLN02939 309 LDRATNQVEKaaLVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELLQQ----------KLKLLEERL--QASDHEIHS 376
|
330 340 350
....*....|....*....|....*....|....*...
gi 166851844 306 lrqQLELLEDDKRELEQKYQS--SEEKARNLKHSVDEL 341
Cdd:PLN02939 377 ---YIQLYQESIKEFQDTLSKlkEESKKRSLEHPADDM 411
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-349 |
3.47e-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: 50.44 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 141 QKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLAVEEYEELQVN 220
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 221 LElekDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQKKVKELEERLEN---- 296
Cdd:TIGR02168 756 LT---ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESlerr 832
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 166851844 297 -EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSE 349
Cdd:TIGR02168 833 iAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
211-409 |
4.76e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 211 VEEYeeLQVNLELEKDLRKKAESFAQEMFIE--------QNKLK--RQSHLLLQSSLPDQQLLKALDENAKLIQQLEEER 280
Cdd:COG3206 158 AEAY--LEQNLELRREEARKALEFLEEQLPElrkeleeaEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 281 IQHQKKVKELEERLENEAL-------HKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSENSVP 353
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDalpellqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 166851844 354 PPPPPPPPLPPPPPNPIRSLMSMIRKRShpsgnsakkekTTQPETAEEVTDLKRQA 409
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREV 360
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
142-350 |
1.05e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 142 KQIKELRDQIVSVQEEKKVLAiELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRkvlekcnrvsmlaVEEYEELQVNL 221
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRR-------------LELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 222 ELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSlpDQQLLKALdenAKLIQQLEEERIQHQKKVKELEERLEN----- 296
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQL---EREIERLERELEERERRRARLEALLAAlglpl 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 166851844 297 ----EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSEN 350
Cdd:COG4913 376 pasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
139-311 |
2.12e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 139 QCQKQIKELRDQIVSVQEEKKVLAI---ELENLKSKLGEVMEEVNKVKQEKavlnsEVLEQRKVLEKCNRVSMLAVEEYE 215
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 216 ELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPD-QQLLKALDENAKLIQQLEEERIQHQKKVKELEERL 294
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|....*..
gi 166851844 295 ENEALHKEIHNLRQQLE 311
Cdd:COG4717 230 EQLENELEAAALEERLK 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-352 |
1.25e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 8 KQLQLITSLKEQAIgEYEDLRAENQKTKEKcdKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHL-EIEKTCresaEAL 86
Cdd:TIGR02169 198 QQLERLRREREKAE-RYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEEELEKLTEEIsELEKRL----EEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 87 ATKLNKENKTLKRISMLYMAKLGPDVITEEINIDDDDPATDTDAAAETcvsvQCQKQIKELRDQIVSVQEEKKVLAIELE 166
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE----DAEERLAKLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 167 NLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLK 246
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 247 RQshlllqsslpdqqlLKALDENaklIQQLEEERIQHQKKVKELEERLEnealhkeihNLRQQLELLEDDKRELEQKYQS 326
Cdd:TIGR02169 427 AA--------------IAGIEAK---INELEEEKEDKALEIKKQEWKLE---------QLAADLSKYEQELYDLKEEYDR 480
|
330 340
....*....|....*....|....*.
gi 166851844 327 SEEKARNLKHSVDELQKRVNQSENSV 352
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERV 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-341 |
1.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 9 QLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKTCRESAEALAT 88
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 89 KLNKENKTLKRISMLymaklgpdviTEEINIDDDDPATDTDAAAETCVSVQCQKQIKELRDQIVSVQEEKKVLAIE---- 164
Cdd:PRK03918 322 EINGIEERIKELEEK----------EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEklek 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 165 -LENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEK----------CNRvsMLAVEEYEEL--QVNLELEKDLRKKA 231
Cdd:PRK03918 392 eLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvCGR--ELTEEHRKELleEYTAELKRIEKELK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 232 ESFAQEMFIEQNKLKRQSHLLLQSSLpdQQLLKALDENAKLIQQLEEERIQHQKKVKELEERLENEA--LHKEIHNLRQQ 309
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESEL--IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLikLKGEIKSLKKE 547
|
330 340 350
....*....|....*....|....*....|....*
gi 166851844 310 LE---LLEDDKRELEQKYQSSEEKARNLKHSVDEL 341
Cdd:PRK03918 548 LEkleELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
260-343 |
1.82e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 260 QQLLKALDENAKLIQQLEEERIQHQKKVKELEERLENEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVD 339
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
....
gi 166851844 340 ELQK 343
Cdd:COG4717 171 ELAE 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
164-326 |
2.27e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 164 ELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVlEKCNRVSMLAVEEYEELQVNLELEKDLRKKAESfAQEMFIEQN 243
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQELKEELEE-LEEQLEELL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 244 KLKRQshllLQSSLPDQQLLKALDENAKLIQQLEEERIQHQKKVKELEERLENEALHKEIHNLRQQLELLEDDKRELEQK 323
Cdd:COG4717 416 GELEE----LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
...
gi 166851844 324 YQS 326
Cdd:COG4717 492 WAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
260-515 |
3.21e-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: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 260 QQLLKALDENAKLIQQLEEERIQHQKKVKELEERLenEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKhsvD 339
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRI--AALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---E 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 340 ELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMirkrshpsgnsakkeKTTQPETAEEVTDLKRQAVEemMDRIKK 419
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL---------------KYLAPARREQAEELRADLAE--LAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 420 GVHLRPVNQTARPKAKPDSLKGSESAVDELKGILGTLNKSTSSRSLKSLGPENSETELERILRR-RKLTAEADSSSPTGI 498
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARlEAEAAAAAERTPAAG 247
|
250
....*....|....*...
gi 166851844 499 LATSESK-SMPVLGSVSS 515
Cdd:COG4942 248 FAALKGKlPWPVSGRVVR 265
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-292 |
3.30e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 4 SDEEKQLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEiektcRESA 83
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS-----HSRI 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 84 EALATKLNKENKTLKRIsmlymaklgpDVITEEINIDDDDPATDTDAAAETcvSVQCQKQIKELRDQIVSVQEEKKVLAI 163
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRI----------EARLREIEQKLNRLTLEKEYLEKE--IQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 164 ELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLAVEEYEELQVNL---------------ELEKDLR 228
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLselkaklealeeelsEIEDPKG 941
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166851844 229 KKAESFAQEMFIEQNKLKRQSHLLLQSSLPD---------QQLLKALDENAKLIQQLEEERIQHQKKVKELEE 292
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEEIRALEPvnmlaiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
141-313 |
3.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 141 QKQIKELRDQIVSVQEEKKVLAIELENLKsKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKcnrvsmlaVEEYEELQVN 220
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEELEER--------LEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 221 LElekDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPD-QQLLKALDENAKLIQQLEEERIQHQKKVKELEERLENEAL 299
Cdd:COG4717 165 LE---ELEAELAELQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
170
....*....|....
gi 166851844 300 HKEIHNLRQQLELL 313
Cdd:COG4717 242 EERLKEARLLLLIA 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-350 |
3.73e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 260 QQLLKALDENAKLIQQLEEERIQHQKKVKELEERLENEALHKEIHNLRQQLELLE---DDKRELEQKYQSSEEKARNLKH 336
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDassDDLAALEEQLEELEAELEELEE 706
|
90
....*....|....
gi 166851844 337 SVDELQKRVNQSEN 350
Cdd:COG4913 707 ELDELKGEIGRLEK 720
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-352 |
3.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 141 QKQIKELRDQIVSVQEEKKVLAIELENLKSKLgevmeevnkvkqekavlnsEVLEQRKVLEKcnrvsmlAVEEYEELQVN 220
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAEL-------------------DALQERREALQ-------RLAEYSWDEID 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 221 L-ELEKDLRKKaesfaqemfieQNKLKRqshllLQSSLPD-QQLLKALDENAKLIQQLEEERIQHQKKVKELEERLenEA 298
Cdd:COG4913 663 VaSAEREIAEL-----------EAELER-----LDASSDDlAALEEQLEELEAELEELEEELDELKGEIGRLEKEL--EQ 724
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166851844 299 LHKEIHNLRQQLELLEDDKR-----ELEQKYQ------SSEEKARNLKHSVDELQKRVNQSENSV 352
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARlelraLLEERFAaalgdaVERELRENLEERIDALRARLNRAEEEL 789
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
215-349 |
3.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 215 EELQVNLE-LEKDlRKKAESFAQemfIEQNKLKRQSHLLLQSslpDQQLLKALDENAKLIQQLEEERIQHQKKVKELEER 293
Cdd:COG1196 196 GELERQLEpLERQ-AEKAERYRE---LKEELKELEAELLLLK---LRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166851844 294 LEN-----EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSE 349
Cdd:COG1196 269 LEElrlelEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
168-344 |
4.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 168 LKSKLGEVMEEVNKVKQEKAVLNsevLEQRKVLEKCNRVSMLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKR 247
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELN---LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 248 QSHLL--------LQSSLPD-QQLLKALDENAKLIQQLEEERIQHQKKVKELEERLENE------ALHKEIHNLRQQLEL 312
Cdd:COG4717 124 LLQLLplyqeleaLEAELAElPERLEELEERLEELRELEEELEELEAELAELQEELEELleqlslATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|..
gi 166851844 313 LEDDKRELEQKYQSSEEKARNLKHSVDELQKR 344
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-347 |
5.91e-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: 43.12 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 23 EYEDLRAENQKTKEKCDKIRQERDEAVKKLEE-------FQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENK 95
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEEleeeleqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 96 TLKRISMLYMAKLgpdviteEINIDDDDPATDTDAAAETCVSVQcQKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEV 175
Cdd:TIGR02168 758 ELEAEIEELEERL-------EEAEEELAEAEAEIEELEAQIEQL-KEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 176 MEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQshlLLQS 255
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE---LREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 256 SLPDQQLLKALDENAKLIQQLEEERIQHQKKVKELEERLenealhkeihnlrqqLELLEDDKRELEQKYQSSEEKARNLK 335
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL---------------SEEYSLTLEEAEALENKIEDDEEEAR 971
|
330
....*....|..
gi 166851844 336 HSVDELQKRVNQ 347
Cdd:TIGR02168 972 RRLKRLENKIKE 983
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
142-323 |
7.44e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 142 KQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKcNRVSMLAV---EEYEELQ 218
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVrnnKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 219 VNLELEKDLRKKAESFAQEmfieqnklkrqshlllqsslpdqqLLKALDENAKLIQQLEEERIQHQKKVKELEERLEnea 298
Cdd:COG1579 96 KEIESLKRRISDLEDEILE------------------------LMERIEELEEELAELEAELAELEAELEEKKAELD--- 148
|
170 180
....*....|....*....|....*
gi 166851844 299 lhKEIHNLRQQLELLEDDKRELEQK 323
Cdd:COG1579 149 --EELAELEAELEELEAEREELAAK 171
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
39-321 |
7.93e-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: 42.42 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 39 DKIRQERDEAVKKLEEFQKIShmviEEVNFMQNHLEIEKTCRESAEALATKLNKEnktLKRISMLYMAKLGPDVITEEIN 118
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLE----EAEKARQAEMDRQAAIYAEQERMAMERERE---LERIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 119 IDDDDPATDTDAAAEtcvsvqcQKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRK 198
Cdd:pfam17380 372 MEISRMRELERLQME-------RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 199 V----------LEKCNRVSMLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDE 268
Cdd:pfam17380 445 AremervrleeQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166851844 269 NAKLIQQLEEERIQHQKKVKELE----------------ERLENEALHKEIHNLRQQLElLEDDKRELE 321
Cdd:pfam17380 525 RQKAIYEEERRREAEEERRKQQEmeerrriqeqmrkateERSRLEAMEREREMMRQIVE-SEKARAEYE 592
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
169-332 |
1.02e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 169 KSKLGEVMEEVNKVKQEkAVLNSEVLEQRKVLEkcnrvsmlAVEEYEELQvnLELEKDLR-KKAESFAQEMFIEQNK--L 245
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE-AKKEAEAIKKEALLE--------AKEEIHKLR--NEFEKELReRRNELQKLEKRLLQKEenL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 246 KRQSHLLLQSslpDQQLLKALDENAKLIQQLEEERIQHQKKVKELEERLEN-------EAlhKEIhnLRQQLEllEDDKR 318
Cdd:PRK12704 99 DRKLELLEKR---EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeEA--KEI--LLEKVE--EEARH 169
|
170
....*....|....
gi 166851844 319 ELEQKYQSSEEKAR 332
Cdd:PRK12704 170 EAAVLIKEIEEEAK 183
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
144-333 |
1.18e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 144 IKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSML--AVEEYEElqvnl 221
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLlaAIADAED----- 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 222 ELEKdLRKKAESFAQEMFIEQNKL--KRQSHLLLQSSLPD----------QQLLKALDENAKLIQQLEEERIQHQKKVKE 289
Cdd:PRK02224 607 EIER-LREKREALAELNDERRERLaeKRERKRELEAEFDEarieearedkERAEEYLEQVEEKLDELREERDDLQAEIGA 685
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 166851844 290 LEERLEN-EAL---HKEIHNLRQQLELLEDDKRELEQKYQS--SEEKARN 333
Cdd:PRK02224 686 VENELEElEELrerREALENRVEALEALYDEAEELESMYGDlrAELRQRN 735
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
216-349 |
1.24e-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: 42.08 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 216 ELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQ-----------QLLKALDENAKLI-QQLEEERIQH 283
Cdd:pfam01576 275 ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQelrskreqevtELKKALEEETRSHeAQLQEMRQKH 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 166851844 284 QKKVKELEERLEN-----EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSE 349
Cdd:pfam01576 355 TQALEELTEQLEQakrnkANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESE 425
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
164-350 |
1.36e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 164 ELENLKSKLGEVMEEVNKVKQEKAVLNSEvlEQRKVLekcnrvsmlaVEEYEELQVNLELEKDLRKKAESFAQEMfieqN 243
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDLS--EEAKLL----------LQQLSELESQLAEARAELAEAEARLAAL----R 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 244 KLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEER----------IQHQKKVKELEERLENEA------LHKEIHNLR 307
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAqrilasLEAELEALQ 326
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 166851844 308 QQLELLEDDKRELEQKYQSSEEKARNLKhsvdELQKRVNQSEN 350
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARE 365
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-320 |
1.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 141 QKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVK-QEKAVLNSEVLEQRKVLEKCNRvsmlAVEEYEELQV 219
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERER----RRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 220 NLELEKDLrkKAESFAqemfieqnKLKRQSHLLLQSSLPDQQLL-KALDENAKLIQQLEEERIQHQKKVKELEERLENea 298
Cdd:COG4913 370 ALGLPLPA--SAEEFA--------ALRAEAAALLEALEEELEALeEALAEAEAALRDLRRELRELEAEIASLERRKSN-- 437
|
170 180
....*....|....*....|...
gi 166851844 299 LHKEIHNLRQQL-ELLEDDKREL 320
Cdd:COG4913 438 IPARLLALRDALaEALGLDEAEL 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-347 |
1.53e-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: 41.29 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 251 LLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQKKVKELEErlENEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEK 330
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKK--EEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90
....*....|....*..
gi 166851844 331 ARNLKHSVDELQKRVNQ 347
Cdd:COG4942 85 LAELEKEIAELRAELEA 101
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
139-314 |
1.76e-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: 41.42 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 139 QCQKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLAVEEYEELQ 218
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 219 VNLELEKDLRKKAESFAQEMFIE----QNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQKKVKELEER- 293
Cdd:pfam07888 150 TELERMKERAKKAGAQRKEEEAErkqlQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKe 229
|
170 180
....*....|....*....|.
gi 166851844 294 LENEALHKEIHNLRQQLELLE 314
Cdd:pfam07888 230 AENEALLEELRSLQERLNASE 250
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
13-236 |
2.17e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 13 ITSLKEQAIGEY-EDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQN--HLEIEKTCRESAEALATK 89
Cdd:PRK05771 33 IEDLKEELSNERlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEeeLEKIEKEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 90 LNKENKTLKRISML-YMAKLGPDVI----TEEINIDDDDPATDTDAAAETCVSVQCQKQIKELRDQ-----IVSVQEEKK 159
Cdd:PRK05771 113 ENEIKELEQEIERLePWGNFDLDLSlllgFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvVVLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 160 VLAI----ELENLK-SKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKcnrvsmLAVEEYEELQVNLELEKDLRKKAESF 234
Cdd:PRK05771 193 VEEElkklGFERLElEEEGTPSELIREIKEELEEIEKERESLLEELKE------LAKKYLEELLALYEYLEIELERAEAL 266
|
..
gi 166851844 235 AQ 236
Cdd:PRK05771 267 SK 268
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
6-344 |
2.75e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 6 EEKQLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEktcresaEA 85
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL-------QE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 86 LATKLNKENKTLKRISMLYMAKLgpdviteeINIDDDDPATDTDAAAETCVSVQCQKQIKELRDQIVSVQEEKKVLAIEL 165
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKL--------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 166 ENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRvsmlAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKL 245
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE----EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 246 KRQSHLLLQSSLPDQQLLKALDENAKLIqqLEEERIQHQKKVKELEERLENEALHKEIHNLRQQLELLEDDKRELEQKYQ 325
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDL--LKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330
....*....|....*....
gi 166851844 326 SSEEKARNLKHSVDELQKR 344
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELL 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
160-351 |
3.01e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 160 VLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSmlaVEEYEELQVNLELEKDLRKKAESFAQEMF 239
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS---PEELLELLDRIEELQELLREAEELEEELQ 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 240 IEQNKLKRQSHLLLQSSLPDQQLLKALDEnakliqqlEEERIQHQKKVKELEERLENEALHKEIHNLRQQLELLEDDKRE 319
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQ--------AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE 436
|
170 180 190
....*....|....*....|....*....|..
gi 166851844 320 LEQKYQSSEEKARNLKHSVDELQKRVNQSENS 351
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-419 |
3.05e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 142 KQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKcnrvsmlAVEEYEELQVNL 221
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-------LEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 222 ELEKDLRKKAESFAQEMFIEQNKLKRqshllLQSSLPDQQL-LKALDENAKLIQQLEEERIQHQKKVKELEERLENEA-L 299
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRE-----LEERIEELKKeIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELReI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 300 HKEIHNLRQQLELLEDDKRELEQKyqssEEKARNLKHSVDELQKRVNQSENSVppppppppplppPPPNPIRSLMSMIRK 379
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERH------------ELYEEAKAKKEELER 376
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 166851844 380 RShpsgnsaKKEKTTQPETAEEVTDLKRQAVEEMMDRIKK 419
Cdd:PRK03918 377 LK-------KRLTGLTPEKLEKELEELEKAKEEIEEEISK 409
|
|
| Rod_C |
pfam10493 |
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic ... |
215-306 |
3.11e-03 |
|
Rough deal protein C-terminal region; Rod, the Rough deal protein, displays a dynamic intracellular staining pattern, localising first to kinetochores in pro-metaphase, but moving to kinetochore microtubules at metaphase. Early in anaphase the protein is once again restricted to the kinetochores, where it persists until the end of telophase. This behaviour is in all respects similar to that described for ZW10, and indeed the two proteins function together, localization of each depending upon the other. These two proteins are found at the kinetochore in complex with a third, Zwilch, in both flies and humans. The C-terminus is the most conserved part of the protein. During pro-metaphase, the ZW10-Rod complex, dynein/dynactin, and Mad2 all accumulate on unattached kinetochores; microtubule capture leads to Mad2 depletion as it is carried off by dynein/dynactin; ZW10-Rod complex accumulation continues, replenishing kinetochore dynein. The continuing recruitment of the ZW10-Rod complex during metaphase may serve to maintain adequate dynein/dynactin complex on kinetochores for assisting chromatid movement during anaphase. The ZW10-Rod complex acts as a bridge whose association with Zwint-1 links Mad1 and Mad2, components that are directly responsible for generating the diffusible 'wait anaphase' signal, to a structural, inner kinetochore complex containing Mis12 and KNL-1AF15q14, the last of which has been proved to be essential for kinetochore assembly in C. elegans. Removal of ZW10 or Rod inactivates the mitotic checkpoint.
Pssm-ID: 463114 Cd Length: 551 Bit Score: 40.43 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 215 EELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQsHLLLQSSLPDQQLLKALDENAKLIQQL-EEERIQHQKKVKELEER 293
Cdd:pfam10493 135 EKWLKNLAPDDEAREKAEALLKKLKRQYQRSKTE-NLLIAHGLNDEELLKLVGKPAELIVSLyEHSSIEQRYKNPGGRDY 213
|
90
....*....|....*.
gi 166851844 294 LENEALHKEI---HNL 306
Cdd:pfam10493 214 PDIHAAVKEIaeiNEL 229
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
212-409 |
3.15e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 212 EEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHL----LLQSSLpDQQLLKALDENAKLIQQLEEERiQHQKKV 287
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEaelaELEAEL-EELRLELEELELELEEAQAEEY-ELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 288 KELEERLenEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPP 367
Cdd:COG1196 298 ARLEQDI--ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 166851844 368 NPIRSLMSMIRKRSHPSGNSAKKEKTTQPETAEEVTDLKRQA 409
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
261-352 |
3.22e-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: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 261 QLLKALDENAKLIQQLEEERIQHQKKVKELEERLEN-------EALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARN 333
Cdd:COG1579 49 AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAE 128
|
90
....*....|....*....
gi 166851844 334 LKHSVDELQKRVNQSENSV 352
Cdd:COG1579 129 LEAELAELEAELEEKKAEL 147
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
191-348 |
3.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 191 SEVLEQRKVLEKCNRvsmlAVEEYEELqvnleleKDLRKKAEsfaqemfieqnKLKRQshlllqsslpdQQLLKALDENA 270
Cdd:COG4913 215 EYMLEEPDTFEAADA----LVEHFDDL-------ERAHEALE-----------DAREQ-----------IELLEPIRELA 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166851844 271 KLIQQLEEERIQHQkkvkELEERLENEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQS 348
Cdd:COG4913 262 ERYAAARERLAELE----YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
222-351 |
4.23e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 222 ELEKDLRK-KAESFAQEMFIEQNKLKRQSHLLLqSSLPDQQLLKALDENAKLIQQLEEERIQHQKKVKELEE-----RLE 295
Cdd:TIGR02168 197 ELERQLKSlERQAEKAERYKELKAELRELELAL-LVLRLEELREELEELQEELKEAEEELEELTAELQELEEkleelRLE 275
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 166851844 296 NEALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQSENS 351
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-323 |
7.44e-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: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 141 QKQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEvleqrkvlekcnrvsmlAVEEYEELQVN 220
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD-----------------RLEQLEREIER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 221 LELEKDLRkkaesfaqemfieQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEEriqhqkkVKELEERLENEA-- 298
Cdd:COG4913 350 LERELEER-------------ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA-------LEEELEALEEALae 409
|
170 180
....*....|....*....|....*
gi 166851844 299 LHKEIHNLRQQLELLEDDKRELEQK 323
Cdd:COG4913 410 AEAALRDLRRELRELEAEIASLERR 434
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
142-347 |
8.23e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 142 KQIKELRDQIVSVQEEKKVLAIELENLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSMLAVEEYEELQVNL 221
Cdd:COG1340 22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 222 ELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQsslpDQQLLKALDENAKLIQQLEEERIQHQKKVKELEE----RLENE 297
Cdd:COG1340 102 AELNKAGGSIDKLRKEIERLEWRQQTEVLSPEE----EKELVEKIKELEKELEKAKKALEKNEKLKELRAElkelRKEAE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 166851844 298 ALHKEIHNLRQQLELLEDDKRELEQKYQSSEEKARNLKHSVDELQKRVNQ 347
Cdd:COG1340 178 EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
210-321 |
8.76e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 38.88 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851844 210 AVEEYEELQVNLELEKDLRKKAESFAQ---EMFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQKK 286
Cdd:COG1566 95 AEAQLARLEAELGAEAEIAAAEAQLAAaqaQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQA 174
|
90 100 110
....*....|....*....|....*....|....*
gi 166851844 287 VKELEERLENEALHKEIHNLRQQLELLEDDKRELE 321
Cdd:COG1566 175 QAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| |
