|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-329 |
1.83e-14 |
|
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: 74.71 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 19 DLQGAQSEIEAKQEIQHLRKELIEAQELARASKQKCFEL---QALLEEERKAYRNQVEESSKQIQVLQAQLQRLHINIEN 95
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELrkeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 96 LREEkdseITSTRDELLSARDEILLLHQAAEKA---ASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF- 171
Cdd:TIGR02168 745 LEER----IAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAa 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 172 --QLRCQQCEDQQREEATRLQS----------ELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHNSQKQSLELT 239
Cdd:TIGR02168 821 nlRERLESLERRIAATERRLEDleeqieelseDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 240 SDLSILQMTRKQLENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQkeyektQTVLSELKLKFEMTEQEKQSITDELKQC 319
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330
....*....|
gi 1212200356 320 KDNLKLLREK 329
Cdd:TIGR02168 971 RRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-310 |
2.56e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 28 EAKQEIQHLRKELIEAQ-ELARASKQKCFELQALLEEERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREEkDSEITS 106
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-EYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 107 TRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSfqlrcqqcEDQQREEA 186
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE--------LAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 187 TRLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQHLRD 266
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1212200356 267 SADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 310
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-328 |
3.75e-11 |
|
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: 64.70 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 3 EQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARASKQKCfelqalLEEERKAYRNQVEESSKQIQVL 82
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 83 QAQLQRLHINIENLREEKD------------------SEITSTRDELLSARDEILLLHQAAEKAASER---DTDIASLQE 141
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEelnkkikdlgeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAEERLaklEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 142 ELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQ------REEATRLQSELEKLRKEWNVLETECHSLKKENV 215
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 216 LLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVL 295
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD-----------LSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350
....*....|....*....|....*....|...
gi 1212200356 296 SELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 328
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-279 |
2.80e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 5 DLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARASKQkcfELQALLEEERKAYRNQVEESSKQIQVLQA 84
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 85 QLQRLHINIENLREEkdseitstRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEI 164
Cdd:TIGR02168 310 RLANLERQLEELEAQ--------LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 165 TSLQNSFQLRCQQCEDQQ------REEATRLQSELEKLRKEWNVLETECHSLKKEnvLLSSELQRQEKELHNSQKQSLEL 238
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNneierlEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERL 459
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1212200356 239 TSDLSILQMTRKQLENQVGSLKEQHLRDSADLKTLLSKAEN 279
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-270 |
5.67e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 11 AKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARASKQKcfelQALLEEERKAYRNQVEESSKQIQVLQAQLQRL 89
Cdd:COG1196 274 LELEELELELEEAQAEEyELLAELARLEQDIARLEERRRELEER----LEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 90 HINIENLREEKdSEITSTRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN 169
Cdd:COG1196 350 EEELEEAEAEL-AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 170 SfqlrcqqcEDQQREEATRLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTR 249
Cdd:COG1196 429 A--------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
250 260
....*....|....*....|.
gi 1212200356 250 KQLENQVGSLKEQHLRDSADL 270
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-318 |
7.27e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 56 ELQALLEE-ERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREE---KDSEITSTRDELLSARDEIlllhQAAEKAASE 131
Cdd:COG1196 217 ELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAElaeLEAELEELRLELEELELEL----EEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 132 RDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQcEDQQREEATRLQSELEKLRKEWNVLETECHSLK 211
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 212 KENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKT 291
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260
....*....|....*....|....*..
gi 1212200356 292 QTVLSELKLKFEMTEQEKQSITDELKQ 318
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAA 478
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
18-228 |
1.78e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 18 DDLQGAQSEIE-AKQEIQHLRkELIEAQELARASKQKCFELQALLEeerkayRNQVEESSKQIQVLQAQLQRLHINIENL 96
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRA------ALRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 97 REEKDSeitsTRDELLSARDEILLLHQAAEKAASERdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQ-------- 168
Cdd:COG4913 308 EAELER----LEARLDALREELDELEAQIRGNGGDR---LEQLEREIERLERELEERERRRARLEALLAALGlplpasae 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1212200356 169 ---------NSFQLRCQQCEDQQREEATRLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKEL 228
Cdd:COG4913 381 efaalraeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-319 |
2.23e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 11 AKVSLLKDDLQGAQSEIEA-KQEIQHLRKELIEAQELARASKQKCFELQAlleeERKAYRNQVEESSKQIQVLQAQLQRL 89
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSDASRKIGEIEK----EIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 90 HINIENLREEKD---SEITSTRDELLSARDEIlllhqaAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEITS 166
Cdd:TIGR02169 750 EQEIENVKSELKeleARIEELEEDLHKLEEAL------NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 167 LQ----------NSFQLRCQQCEDQQREEATR----------LQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEK 226
Cdd:TIGR02169 824 LTlekeylekeiQELQEQRIDLKEQIKSIEKEienlngkkeeLEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 227 ELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQHLRDSADLKTLLS----KAENQAKDVQ------------KEYEK 290
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEE 983
|
330 340
....*....|....*....|....*....
gi 1212200356 291 TQTVLSELKLKFEMTEQEKQSITDELKQC 319
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
21-206 |
1.33e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 21 QGAQSEIEAK-QEIQHLRKELIEAQELARASKQKcfelQALLEEERKAYRNQVEESSKQIQVLQAQLQrlhinIENLREE 99
Cdd:COG4913 606 FDNRAKLAALeAELAELEEELAEAEERLEALEAE----LDALQERREALQRLAEYSWDEIDVASAERE-----IAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 100 KDsEITSTRDELLSARDEILLLHQAAEKAASERD---TDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF---QL 173
Cdd:COG4913 677 LE-RLDASSDDLAALEEQLEELEAELEELEEELDelkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleeRF 755
|
170 180 190
....*....|....*....|....*....|...
gi 1212200356 174 RCQQCEDQQREEATRLQSELEKLRKEWNVLETE 206
Cdd:COG4913 756 AAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
64-329 |
1.76e-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: 53.15 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 64 ERKAYRNQVEESSKqIQVLQAQLQRLHINIENLREEKDsEITSTRDELLSARDEILLLHQAAEKAASERDTDIASLQEEL 143
Cdd:TIGR02169 662 PRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELR-RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 144 KKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE----EATRLQSELEKLRKEWNVLETECHSLKKENVLLSS 219
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 220 ELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 299
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK----KEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260 270
....*....|....*....|....*....|
gi 1212200356 300 LKFEMTEQEKQSITDELKQCKDNLKLLREK 329
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
23-262 |
3.69e-07 |
|
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: 51.30 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 23 AQSEIEAKQEIQHLRKELIEAQELARASKQKcfelQALLEEERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREekds 102
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 103 EITSTRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcedQQ 182
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 183 REEATRLQSELEKLRKEWNVLETEchsLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQ 262
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-206 |
3.86e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 3 EQDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARASKQKCFELQALLEEERKAYRNQVEESSKQIQV 81
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELaELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 82 LQAQLQRlhiniENLREEKDSEITSTRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYE 161
Cdd:COG1196 381 LEELAEE-----LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1212200356 162 KEITSLQNSFQLRCQQCEDQQREEATRLQSELEKLRKEWNVLETE 206
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-199 |
2.18e-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: 49.67 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 2 DEQDLNEPLAKVSLLKDDLQGAQSEIEAkqeiqhLRKELIEAQELARASKQKCFELQALLEEERKAY---RNQVEESSKQ 78
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELES------LEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIASLNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 79 IQVLQAQLQRLHINIENLREEKDSeitstrdellsardeilLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAAS 158
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEE-----------------LLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1212200356 159 EYEKEITSLQNSFQLRCQQcEDQQREEATRLQSELEKLRKE 199
Cdd:TIGR02168 465 ELREELEEAEQALDAAERE-LAQLQARLDSLERLQENLEGF 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-321 |
2.22e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 8 EPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARAsKQKCFELQALLEEERKAYRNQVEESSKQIQVLQAQLQ 87
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 88 RLHINIENLREEKDSEITSTRDELLSARDEILLLHQAAE---KAASERDTDIASLQEELKKVRAE----LERWRKAASEY 160
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEeakKAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEEL 1625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 161 EKEITSLQNSFQLRCQQCEDQQREEATRLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHNSQKQSLELTS 240
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 241 DLSILQMTRKQLENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE---KTQTVLSELKLKFEMTEQEKQSITDELK 317
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
....
gi 1212200356 318 QCKD 321
Cdd:PTZ00121 1786 DEED 1789
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
57-311 |
2.81e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 57 LQALLEEERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREEKDSEITSTRDELLSARdeilllhqaaekaASERDTDI 136
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQ-------------LSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 137 ASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQSELEKLRKEWnvleTECHSLKKEnvl 216
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ------QLRAQLAELEAELAELSARY----TPNHPDVIA--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 217 LSSELQRQEKELHNSQKQSL-ELTSDLSILQMTRKQLENQVGSLKEQHLRdsadlktlLSKAENQAKDVQKEYEKTQTVL 295
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELY 367
|
250
....*....|....*.
gi 1212200356 296 SELKLKFEMTEQEKQS 311
Cdd:COG3206 368 ESLLQRLEEARLAEAL 383
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-331 |
7.04e-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: 48.13 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 137 ASLQEELKKVRAELERWRKAAseYEKEITSLQNSFqlrcqqceDQQREEATRLQSELEKLRKEWNVLETECHSLKKENVL 216
Cdd:TIGR02168 209 AEKAERYKELKAELRELELAL--LVLRLEELREEL--------EELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 217 LSSELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQ---HLRDSADLKTLLSKAENQAKDVQKEYEKTQT 293
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQleeLESKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190
....*....|....*....|....*....|....*...
gi 1212200356 294 VLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGN 331
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-328 |
1.03e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 127 KAASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlrcqqcedQQREEATRLQSELEKLRKEWNVLETE 206
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 207 CHSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQHLRDSADLKTL---LSKAENQAKD 283
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAELTL 814
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1212200356 284 VQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 328
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-234 |
1.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 59 ALLEEERKAYRNQVEESSKQIQVLQAQLQRLHINIENLReeKDSEITSTRDELLSARDEILLLHQAAEkAASERDTDIAS 138
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQ--RLAEYSWDEIDVASAEREIAELEAELE-RLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 139 LQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQREEATRLQSELEKLRKEWNV-LETECHSLKKENVL- 216
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDAVEr 765
|
170 180
....*....|....*....|...
gi 1212200356 217 -----LSSELQRQEKELHNSQKQ 234
Cdd:COG4913 766 elrenLEERIDALRARLNRAEEE 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3-168 |
2.92e-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: 45.53 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 3 EQDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARASKQKCFELQALLEEERKAYRNQV--------- 72
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlgrq 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 73 ------------EESSKQIQVLQAQLQRLHINIENLREEKD------SEITSTRDELLSARDEILLLHQAAEKAASERDT 134
Cdd:COG4942 120 pplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAelaalrAELEAERAELEALLAELEEERAALEALKAERQK 199
|
170 180 190
....*....|....*....|....*....|....
gi 1212200356 135 DIASLQEELKKVRAELERWRKAASEYEKEITSLQ 168
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-163 |
7.80e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 12 KVSLLKDDLQGAQSEIE-AKQEIQHLRKELIEAQELARASKQKCFELQ----ALLEEERKAYRNQVEESSKQIQVLQAQL 86
Cdd:COG4913 289 RLELLEAELEELRAELArLEAELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1212200356 87 QRLHINIENLREEkdseITSTRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKE 163
Cdd:COG4913 369 AALGLPLPASAEE----FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
62-330 |
9.29e-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: 44.67 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 62 EEERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREEKDSEITStrDELLSARDEILLLHQAAEKAASERdtdiaslqe 141
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYELLKEKEALER--------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 142 ELKKVRAELERWRKAASEYEKEITSLqnsfQLRCQQCEDQQREEATRLQSELEklrKEWNVLETECHSLKKENVLLSSEL 221
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISEL----EKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 222 QRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSL---KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 298
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270
....*....|....*....|....*....|..
gi 1212200356 299 KLKFEMTEQEKQSITDELKQCKDNLKLLREKG 330
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
109-318 |
1.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 109 DELLSARDEILLLHQAAEKAASERDT--DIASLQEELKKVRAELERWR--KAASEYEKEITSLQnSFQLRCQQCEDQQR- 183
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEylRAALRLWFAQRRLE-LLEAELEELRAELAr 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 184 --EEATRLQSELEKLRKEWNVLETECHSLKKENV-LLSSELQRQEKELHNsqkqsleltsdlsiLQMTRKQLENQVGSLK 260
Cdd:COG4913 307 leAELERLEARLDALREELDELEAQIRGNGGDRLeQLEREIERLERELEE--------------RERRRARLEALLAALG 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1212200356 261 EQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 318
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-234 |
1.40e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 42 EAQELARASKQKCFELQALLEEERKAyRNQVEESSKQIQVLQAQLQRLHINIENLREEkdseITSTRDELLSARDEILLL 121
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEE-LKEAEEKEEEYAELQEELEELEEELEELEAE----LEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 122 HQAAEKAASERDtdIASLQEELKKVRAELERWRKAASEY---EKEITSLQNSFQLRCQQCEDQQREEATRLQSELEKLRK 198
Cdd:COG4717 129 PLYQELEALEAE--LAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*.
gi 1212200356 199 EWNVLETECHSLKKENVLLSSELQRQEKELHNSQKQ 234
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11-234 |
1.71e-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: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 11 AKVSLLKDDLQGAQSEIEAKQEiqhlrkeliEAQELARASKQKCFELQAlLEEERKAYRNQVEESSKQIQVLQAQLQRLH 90
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRA---------ELTLLNEEAANLRERLES-LERRIAATERRLEDLEEQIEELSEDIESLA 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 91 INIENLREEKDsEITSTRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNs 170
Cdd:TIGR02168 859 AEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV- 936
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1212200356 171 fqlrcqqcedqqreeatRLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHNSQKQ 234
Cdd:TIGR02168 937 -----------------RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
80-331 |
2.57e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 80 QVLQAqLQRLHI-NIENLREEKDSE-ITSTRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELErwrKAA 157
Cdd:PRK05771 20 EVLEA-LHELGVvHIEDLKEELSNErLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVE---EEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 158 SEYEKEITSLQnsfqlrcqqcedqqrEEATRLQSELEKLRKEWNVLEtechSLKKENVLLsSELQRQEK------ELHNS 231
Cdd:PRK05771 96 EKIEKEIKELE---------------EEISELENEIKELEQEIERLE----PWGNFDLDL-SLLLGFKYvsvfvgTVPED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 232 QKQSLELTSDLS-------------ILQMTRKQLENQVGSL------KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQ 292
Cdd:PRK05771 156 KLEELKLESDVEnveyistdkgyvyVVVVVLKELSDEVEEElkklgfERLELEEEGTPSELIREIKEELEEIEKERESLL 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 1212200356 293 TVLSELKLKFEmteqekqsitDELKQCKDNLKLLREKGN 331
Cdd:PRK05771 236 EELKELAKKYL----------EELLALYEYLEIELERAE 264
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
61-220 |
2.62e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 61 LEEERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREEKDSeitstrdellsardeilLLHQAAEKaaserDTDIASLQ 140
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEE-----------------LEAELEEK-----DERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 141 EELKKVRAElerwRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQSELEKLRKEWNVLETECHSLKKENVLLSSE 220
Cdd:COG2433 448 RELSEARSE----ERREIRKDREISRLDR---------------EIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3-321 |
3.09e-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: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 3 EQDLNEPLAKVSLLKDDLQGAQSEIEAKQEiqHLRKELIEAQELARASKQKCFELQAL------LEEERKAYRNQVEESS 76
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQR--ELEEKQNEIEKLKKENQSYKQEIKNLesqindLESKIQNQEKLNQQKD 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 77 KQIQVLQAQLQRLHINIENLREEKDSEiTSTRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKA 156
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKN-NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 157 ASEYEKEITSLQNSFQLRCQQCEDQQREEATrLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQ--EKELHNSQKQ 234
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISS-LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 235 SLELTSDLSILQMTRKQLENQVGSLKEQHL---RDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 311
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEKQELIDQKEKEKKdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
330
....*....|
gi 1212200356 312 ITDELKQCKD 321
Cdd:TIGR04523 650 IKETIKEIRN 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
77-288 |
3.46e-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: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 77 KQIQVLQAQLQRLHINIENLREEKDseitsTRDELLSARDEILLLHQAAEKAaSERDTDIASLQEELKKVRAELERWRKA 156
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLE-----ALEAELDALQERREALQRLAEY-SWDEIDVASAEREIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 157 ASEYEkeitslqnsfqlrcqqcedqqreeatRLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHNSQKQSL 236
Cdd:COG4913 684 SDDLA--------------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1212200356 237 ELTSDLSILQMTR--KQLENQVGSLKEQHLRDS-----ADLKTLLSKAENQAKDVQKEY 288
Cdd:COG4913 738 AAEDLARLELRALleERFAAALGDAVERELRENleeriDALRARLNRAEEELERAMRAF 796
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
75-287 |
3.61e-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: 42.06 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 75 SSKQIQVLQAQLQRLHINIENLREEKD---SEITSTRDELLSARDEILLLH---QAAEKAASERDTDIASLQEELKKVRA 148
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAalkKEEKALLKQLAALERRIAALArriRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 149 ELERWRKAASEYEKEITSLQN----SFQLRCQQCEDQQREeATRLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQ 224
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1212200356 225 EKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQ---HLRDSADLKTLLSKAENQAKDVQKE 287
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAElaeLQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-333 |
4.01e-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: 42.35 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 190 QSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQHLRDSAD 269
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1212200356 270 LKTLLSKAENQAKDVQKEYEKTQTVLSE---LKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNNK 333
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
30-205 |
4.20e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 30 KQEIQHLRKELIEAQELARASKQKcfELQALLEEERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREE---------- 99
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQlgsgpdalpe 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 100 --KDSEITSTRDELLSARDEILLL-------HQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS 170
Cdd:COG3206 259 llQSPVIQQLRAQLAELEAELAELsarytpnHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
170 180 190
....*....|....*....|....*....|....*
gi 1212200356 171 FQlrcqqcedQQREEATRLQSELEKLRKEWNVLET 205
Cdd:COG3206 339 LE--------ARLAELPELEAELRRLEREVEVARE 365
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-201 |
5.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 2 DEQDLNEPLAKVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARASKQKCFELQALlEEERKAYRNQVEESSKQIQ 80
Cdd:COG4913 645 ERREALQRLAEYSWDEIDVASAEREIAELEaELERLDASSDDLAALEEQLEELEAELEEL-EEELDELKGEIGRLEKELE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 81 VLQAQLQRLHINIENLREEKDSEITSTRDELLSARDEILLLHQAAEKAASERD---TDIASLQEELKKVRAE-LERWRKA 156
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDalrARLNRAEEELERAMRAfNREWPAE 803
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1212200356 157 ASEYEKEITSLqNSFQlrcQQCEDQQREEATRLQSELEKLRKEWN 201
Cdd:COG4913 804 TADLDADLESL-PEYL---ALLDRLEEDGLPEYEERFKELLNENS 844
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
4-317 |
7.08e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 4 QDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQhlrkelIEAQELARASKQKCFELQALLEEERKAYRNQVEESSKQIQVLQ 83
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMERQ------MAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 84 AQlQRLHINIENLREEKDSEITSTRDELLSARDEILLLHQAAEKAASERDtdiaslqeELKKVRAELERWRKAASEYEKE 163
Cdd:pfam15921 493 SS-ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD--------HLRNVQTECEALKLQMAEKDKV 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 164 ITSLQNSFQlRCQQCEDQQREEATRLQSELEKLRKEWNVLETECHSLK----------KENVLLSSELQRQEKELHNSQK 233
Cdd:pfam15921 564 IEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdakiRELEARVSDLELEKVKLVNAGS 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 234 QSLELTSDLsilQMTRKQLENQVGSLKEqhlrdsaDLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSIT 313
Cdd:pfam15921 643 ERLRAVKDI---KQERDQLLNEVKTSRN-------ELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
....
gi 1212200356 314 DELK 317
Cdd:pfam15921 713 NTLK 716
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-152 |
8.56e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 20 LQGAQSEIEAKQEIQHLRKELIEAQELARASKQKCFELQALLEEERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREE 99
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1212200356 100 KDSEitstRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELER 152
Cdd:COG1196 730 LEAE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
13-150 |
1.08e-03 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 39.60 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 13 VSLLKDDLQGAQSEIEAK-QEIQHLRKELIEAQELARASKQKCFELQAlleeerkayrnQVEESSKQIQVLQAQLQRLHI 91
Cdd:pfam06818 12 ISLLKQQLKDSQAEVTQKlNEIVALRAQLRELRAKLEEKEEQIQELED-----------SLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1212200356 92 NIENLRE---EKDSEITSTRDEL--LSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAEL 150
Cdd:pfam06818 81 EAELLREkvgKLEEEVSGLREALsdVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAEL 144
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
12-206 |
1.85e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.04 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 12 KVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARASKQKC--------FELQALLEE-------------------- 63
Cdd:pfam13166 216 KAEILIQKVIGKSSAIEELIKNPDLADWVEQGLELHKAHLDTCpfcgqplpAERKAALEAhfddeftefqnrlqkliekv 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 64 -------------------ERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREE--KDSEITSTRDELLSARDEILLLH 122
Cdd:pfam13166 296 esaissllaqlpavsdlasLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfKSIELDSVDAKIESINDLVASIN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 123 QAAEKaASERDTDIASLQEELKKvraelERWRKAASEYEKEITSLQNSFQLRCQQCEDQQrEEATRLQSELEKLRKEWNV 202
Cdd:pfam13166 376 ELIAK-HNEITDNFEEEKNKAKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSLE-KEIKNLEAEIKKLREEIKE 448
|
....
gi 1212200356 203 LETE 206
Cdd:pfam13166 449 LEAQ 452
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
28-310 |
2.43e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 28 EAKQEIQHLRKELIEAQELARASKQKCFELQALLEEERKAYRNQVEESSKQIQVLQaqlqrlhiNIENLREEKDSEITST 107
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK--------DIKQERDQLLNEVKTS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 108 RDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEiTSLQNSFQLRCQQCEDQQREEAT 187
Cdd:pfam15921 666 RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS-DGHAMKVAMGMQKQITAKRGQID 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 188 RLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHnsqkqslELTSDLSILQMTRKQLENQVgslkeqhlrds 267
Cdd:pfam15921 745 ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN-------KMAGELEVLRSQERRLKEKV----------- 806
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1212200356 268 ADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 310
Cdd:pfam15921 807 ANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
70-328 |
2.58e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 70 NQVEESSKQIQVLQAQLQRLHINIENLREEKDSEITSTRDELLSArdeilllhqaaeKAASERDTDIASLQEELKKVRAE 149
Cdd:TIGR00606 587 NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDV------------CGSQDEESDLERLKEEIEKSSKQ 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 150 LERWRKAASEYEKEITSLQNSFQLRCQQC------EDQQREEATRLQSELEKLRKEWNVLETECHSLKKENVLL------ 217
Cdd:TIGR00606 655 RAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapg 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 218 -SSELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSL--KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTV 294
Cdd:TIGR00606 735 rQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
250 260 270
....*....|....*....|....*....|....*.
gi 1212200356 295 L--SELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 328
Cdd:TIGR00606 815 LqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
31-270 |
2.61e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 31 QEIQHLRKELIEAQElarASKQKCFELQALLEEERKAYRNQVEESSKQIQVLQAQLQRLHINIENLrEEKDSEITSTRDE 110
Cdd:pfam07888 37 EECLQERAELLQAQE---AANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-EEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 111 LLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWR---KAASEYEKEITSLQNSFQLRCQQCEdqqrEEAT 187
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKeraKKAGAQRKEEEAERKQLQAKLQQTE----EELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 188 RLQSELEKLRKEWNVLETECHSLKKENVLLSSEL---QRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQHL 264
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttaHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
....*.
gi 1212200356 265 RDSADL 270
Cdd:pfam07888 269 RTQAEL 274
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
27-290 |
2.91e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 27 IEAKQEIQHLRKELIEAQELARASKQKCFELQALLEEERKAYRN----QVEESSKQIQVLQAQLQRLHIniENLREEKDS 102
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHlkskTNELKSEKLQIGTNLQRRQQF--EEQLVELST 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 103 EITSTRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQ 182
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 183 REEATRLQSELEKLRKEWNVLETECHSLKKenvllSSELQRQEKELHNSQKQSLELTSDLSILQMTRKQL-----ENQVG 257
Cdd:TIGR00606 976 ETELNTVNAQLEECEKHQEKINEDMRLMRQ-----DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHlkemgQMQVL 1050
|
250 260 270
....*....|....*....|....*....|...
gi 1212200356 258 SLKEQHLRDSADLKtLLSKAENQAKDVQKEYEK 290
Cdd:TIGR00606 1051 QMKQEHQKLEENID-LIKRNHVLALGRQKGYEK 1082
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
63-265 |
3.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 63 EERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREEKDSEITSTRDELLSARDEILLLhQAAEKAASERDTDIASLQEE 142
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEE 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 143 LKKVRAELERWRKAASEYEKEITSLQNSFQlrcQQCEDQQREEATRLQSELEKLRKEWNVLEtechSLKKENVLLSSELQ 222
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYS---EEEYEELREEYLELSRELAGLRAELEELE----KRREEIKKTLEKLK 700
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1212200356 223 RQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQHLR 265
Cdd:PRK03918 701 EELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALS 743
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-328 |
3.94e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.33 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 1 MDEQDLNEPLAKVSLLKDDLQGAQSEIEAKqeIQHLRKELIEAQ-EL--ARASKQKCFELQALLEEERKAYRNQVEESSK 77
Cdd:pfam15921 314 MYMRQLSDLESTVSQLRSELREAKRMYEDK--IEELEKQLVLANsELteARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 78 QIQVLQAQLQRL-------HINIENLREEKDS---EITSTRDELLSARDEI---LLLHQAAEKAASERDTDIASL----- 139
Cdd:pfam15921 392 ELSLEKEQNKRLwdrdtgnSITIDHLRRELDDrnmEVQRLEALLKAMKSECqgqMERQMAAIQGKNESLEKVSSLtaqle 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 140 --QEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcQQCEDQQREEATRLQS-------ELEKLRKEWNVL---ETEC 207
Cdd:pfam15921 472 stKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-ERAIEATNAEITKLRSrvdlklqELQHLKNEGDHLrnvQTEC 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 208 HSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVG----SLKE-QHLRDSADLKtlLSKAENQAK 282
Cdd:pfam15921 551 EALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdrrlELQEfKILKDKKDAK--IRELEARVS 628
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1212200356 283 DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 328
Cdd:pfam15921 629 DLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
44-298 |
4.24e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 44 QELARASKQKcfelqaLLEEERKAYRNQVEESSKQIQVLQAQLQRLhinienlrEEKDSEITSTRDELLSARDEILLLHQ 123
Cdd:PRK11281 43 AQLDALNKQK------LLEAEDKLVQQDLEQTLALLDKIDRQKEET--------EQLKQQLAQAPAKLRQAQAELEALKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 124 AAEKAASER--DTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN----------SFQLRCQQCEDQ----QREEAT 187
Cdd:PRK11281 109 DNDEETRETlsTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTqperaqaalyANSQRLQQIRNLlkggKVGGKA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 188 RLQSELEKLRKEWNVLEtechslkkenvlLSSELQRQEKElHNSQKQSL-ELTSDLSILQMTRKQLENQvgslkeqhlrd 266
Cdd:PRK11281 189 LRPSQRVLLQAEQALLN------------AQNDLQRKSLE-GNTQLQDLlQKQRDYLTARIQRLEHQLQ----------- 244
|
250 260 270
....*....|....*....|....*....|....*..
gi 1212200356 267 saDLKTL-----LSKAENQAKDVQKEYEKTQTVLSEL 298
Cdd:PRK11281 245 --LLQEAinskrLTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
185-308 |
6.42e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 37.76 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 185 EATRLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmtrkQLENQVGSLKeqhl 264
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1212200356 265 rdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 308
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
71-329 |
6.58e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.46 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 71 QVEESSKQIQVLQAQL----QRLHI---NIENLREEKDSEITSTRDELLSARDEILLLHQaaekaaserdtDIASLQEEL 143
Cdd:PHA02562 175 KIRELNQQIQTLDMKIdhiqQQIKTynkNIEEQRKKNGENIARKQNKYDELVEEAKTIKA-----------EIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 144 KKVRAELErwrkaasEYEKEITSLqnsfqlrcqqcedqqREEATRLQSELEKLRKEWNVLE--TEC----HSLKKENVLL 217
Cdd:PHA02562 244 LNLVMDIE-------DPSAALNKL---------------NTAAAKIKSKIEQFQKVIKMYEkgGVCptctQQISEGPDRI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 218 SS------ELQRQEKELHNSQKQSLELTSDLSILQMTRKQLENQVGSLKEQhlrdsadlktlLSKAENQAKDVQKEYEKT 291
Cdd:PHA02562 302 TKikdklkELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQS-----------LITLVDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|....*...
gi 1212200356 292 QTvlselklkfemteqEKQSITDELKQCKDNLKLLREK 329
Cdd:PHA02562 371 QA--------------EFVDNAEELAKLQDELDKIVKT 394
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
31-303 |
6.80e-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: 38.62 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 31 QEIQHLRKELIEAQELARASKQKCFELQALLEEERKAYRNQVEESSKQIQVLQAQLQRLHINIENLREEKDSEITSTRDE 110
Cdd:pfam01576 267 RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 111 LLSAR-------DEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYE---KEITSLQNSFQLRCQQCED 180
Cdd:pfam01576 347 LQEMRqkhtqalEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEhkrKKLEGQLQELQARLSESER 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 181 QQREEA---TRLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLsilqmtrKQLENQVG 257
Cdd:pfam01576 427 QRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-------RQLEDERN 499
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1212200356 258 SLKEQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 303
Cdd:pfam01576 500 SLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
118-337 |
7.93e-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: 37.82 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 118 ILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQcEDQQREEATRLQSELEKLR 197
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 198 KEWNVLETECHSLKKE-----------------NVLLSSE--------LQRQEKELHNSQKQSLELTSDLSILQMTRKQL 252
Cdd:COG4942 90 KEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 253 ENQVGSLKE---QHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 329
Cdd:COG4942 170 EAERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*...
gi 1212200356 330 GNNKPWPW 337
Cdd:COG4942 250 ALKGKLPW 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-286 |
8.75e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.10 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 13 VSLLKDDLQGAQSEIEAKQEiqhlRKELIEAQELARASKQKCFELQALLEEERKAYRNQVEESSKQIQVLQAQLQRLHiN 92
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIE----EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-E 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 93 IENLREEKDsEITSTRDELLSARDEILLLHQAAEKAASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQ 172
Cdd:PRK02224 253 LETLEAEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 173 lrcqqcedQQREEATRLQSELEKLRKEWNVLETECHSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQ------ 246
Cdd:PRK02224 332 --------ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRerfgda 403
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1212200356 247 -MTRKQLENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQK 286
Cdd:PRK02224 404 pVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE 444
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
31-146 |
9.83e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 37.84 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1212200356 31 QEIQHLRKELI-EAQELARASKQKCfELQAllEEERKAYRNQVE-ESSKQIQVLQAQLQRLHINIENLrEEKDSEITSTR 108
Cdd:PRK12704 34 KEAEEEAKRILeEAKKEAEAIKKEA-LLEA--KEEIHKLRNEFEkELRERRNELQKLEKRLLQKEENL-DRKLELLEKRE 109
|
90 100 110
....*....|....*....|....*....|....*...
gi 1212200356 109 DELLSARDEILLLHQAAEKAASERDTDIASLQEELKKV 146
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| |
