|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
1-53 |
6.41e-16 |
|
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.
Pssm-ID: 465482 Cd Length: 102 Bit Score: 72.66 E-value: 6.41e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 386869312 1 MWVtlPIDLNNKSAKQQEVQFKAYYLPKDD-EYYQFCYVDEDGVVRGASIPFQF 53
Cdd:pfam17751 51 VWA--KDDEVEGSNSVRQVLFKASYLPKEPeGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
66-269 |
2.08e-11 |
|
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: 64.79 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 66 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQ 145
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE----ELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 146 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 225
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869312 226 KKQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRE 269
Cdd:COG4942 195 AERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-275 |
1.46e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 72 EIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSEN 151
Cdd:TIGR02168 233 RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL----QKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 152 EKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 231
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869312 232 MDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 275
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
348-374 |
2.05e-09 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 2 (CALCOCO2) and similar proteins; CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. It acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. It may play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion. CALCOCO2 contains a C2H2-type zinc binding domain.
Pssm-ID: 412014 Cd Length: 27 Bit Score: 52.45 E-value: 2.05e-09
10 20
....*....|....*....|....*..
gi 386869312 348 FNCPICDKIFPATEKQIFEDHVFCHSL 374
Cdd:cd21968 1 FECPICSKIFEATSKQEFEDHVFCHSL 27
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-274 |
7.06e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 67 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQK 146
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 147 MSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 226
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386869312 227 KQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 274
Cdd:COG1196 408 AEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-275 |
1.96e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 69 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMS 148
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 149 SENEkmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 228
Cdd:COG1196 376 EAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 386869312 229 QELMDENFDLSKRLSENEiicNALQRQKERLEGENDLLKRENSRLLS 275
Cdd:COG1196 452 AELEEEEEALLELLAELL---EEAALLEAALAELLEELAEAAARLLL 495
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-273 |
2.11e-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: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 102 QAELQKKQEELETLQSINKKLElkvkEQKDYWETELLQLkeQNQKMSSENEkmgIRVDQLQAQLSTQEKEMEKLVQGDQD 181
Cdd:COG4913 616 EAELAELEEELAEAEERLEALE----AELDALQERREAL--QRLAEYSWDE---IDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 182 ---KTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE-----NFDLSKRLsENEIICNALQ 253
Cdd:COG4913 687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEERF-AAALGDAVER 765
|
170 180
....*....|....*....|
gi 386869312 254 RQKERLEGENDLLKRENSRL 273
Cdd:COG4913 766 ELRENLEERIDALRARLNRA 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-274 |
4.76e-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: 55.07 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 67 QGEVEEIEQhnKELCKENQELKDSCISLQKQNSDMQAELQKKQEELE----TLQSINKKLELKVKEQKDYWETELLQLKE 142
Cdd:TIGR02169 217 LKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISelekRLEEIEQLLEELNKKIKDLGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 143 QNQKMSSEnekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNET 222
Cdd:TIGR02169 295 KIGELEAE-------IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386869312 223 TAMKKQQELMDENFDLSKRLSEneiicnaLQRQKERLEGENDLLKRENSRLL 274
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKD-------YREKLEKLKREINELKRELDRLQ 412
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
61-273 |
7.47e-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: 53.61 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 61 ILVVTTQGEVEEIEQHNKELckenqelkdscISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQL 140
Cdd:COG4942 10 LLALAAAAQADAAAEAEAEL-----------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL----ARRIRAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 141 KEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLV-----QGDQDKTE-------------QLEQLKKENDHLFLSLTE 202
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrLGRQPPLAlllspedfldavrRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869312 203 QRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 273
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
100-275 |
1.52e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 100 DMQAELQKKQEELETLQSINKKLELKVKEqkdyWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGD 179
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 180 QDKTEQLEQLKKEndhlflsLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERL 259
Cdd:COG1196 312 RELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170
....*....|....*.
gi 386869312 260 EGENDLLKRENSRLLS 275
Cdd:COG1196 385 AEELLEALRAAAELAA 400
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
71-321 |
1.52e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 71 EEIEQHNKELCKENQELKdsciSLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSE 150
Cdd:COG3883 23 KELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 151 NEKMGIRVDQLQAQLSTQEKE--------MEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNET 222
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 223 TAMKKQQELMDenfDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGARQNPGL 302
Cdd:COG3883 175 AQQAEQEALLA---QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250
....*....|....*....
gi 386869312 303 AYGNPYSGIQESSSPSPLS 321
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAG 270
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-273 |
1.71e-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: 53.14 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 67 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETL----QSINKKLELKVKEQKDYwETELLQLKE 142
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkQILRERLANLERQLEEL-EAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 143 QNQKMSSENEKMGIRVDQLQ-------AQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE 215
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386869312 216 QMKQNettamkkQQELMDENFDLSKRLSENEIicNALQRQKERLEGENDLLKRENSRL 273
Cdd:TIGR02168 411 RLEDR-------RERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERL 459
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
56-273 |
2.00e-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: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 56 ENEEDILvvttQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET----LQSINKKLELKVKEQKD 131
Cdd:TIGR02169 687 KRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 132 YwETELLQLKEQNQKMSSENEKM-----GIRVDQLQAQLSTQEKE----------MEKLVQGDQDKTEQLEQLKKENDHL 196
Cdd:TIGR02169 763 L-EARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEvsriearlreIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 197 FLSLTEQRKDQKK----LEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 272
Cdd:TIGR02169 842 RIDLKEQIKSIEKeienLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
.
gi 386869312 273 L 273
Cdd:TIGR02169 922 L 922
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
150-281 |
2.99e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.17 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 150 ENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQ 229
Cdd:COG2433 393 EEPEAEREKEHEERELTEEEEEIRRL-------EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 386869312 230 ELmdenfdlSKRlsENEIicNALQRQKERLEGENDLLKRENSRLLSYMGLDF 281
Cdd:COG2433 466 EI-------SRL--DREI--ERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-274 |
3.06e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 72 EIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN 151
Cdd:COG1196 233 KLRELEAELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 152 EKM---GIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 228
Cdd:COG1196 309 ERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 386869312 229 QELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 274
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
71-273 |
3.80e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 71 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET-LQSINKKLELKVKEQKDYWET------ELLQLKEQ 143
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAeIASLERSIAEKERELEDAEERlakleaEIDKLLAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 144 NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT------------EQLEQLKKENDHLFLSLTEQRKDQKK 209
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAelEEVDKEfaetrdelkdyrEKLEKLKREINELKRELDRLQEELQR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386869312 210 LEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 273
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-267 |
3.80e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 57 NEEDILVVTTQGEVEEIEQHNKelcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET- 135
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETl 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 136 --ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQgdqdkteqlEQLKKENDHLFLSLTEQRKDQKKLEQT 213
Cdd:TIGR02168 385 rsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK---------KLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386869312 214 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 267
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
69-244 |
6.96e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 69 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKvkEQKDYWETELLQLKEQNQKMS 148
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE--KEIDEKNKEIEELKQTQKSLK 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 149 SENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 228
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
170
....*....|....*.
gi 386869312 229 QELMDENFDLSKRLSE 244
Cdd:TIGR04523 662 PEIIKKIKESKTKIDD 677
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-273 |
8.14e-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: 51.21 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 103 AELQKKQEELE-TLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQD 181
Cdd:TIGR02168 680 EELEEKIEELEeKIAELEKALA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 182 KTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEG 261
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170
....*....|..
gi 386869312 262 ENDLLKRENSRL 273
Cdd:TIGR02168 839 RLEDLEEQIEEL 850
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
66-267 |
1.87e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 66 TQGEVEEIEQ-HNKELCKENQELKDSCislqKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQ----- 139
Cdd:COG5022 887 LKIDVKSISSlKLVNLELESEIIELKK----SLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNklhev 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 140 ---LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG------DQDKTEQLEQLKKENDHLflslteqrkdqkkl 210
Cdd:COG5022 963 eskLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELskqygaLQESTKQLKELPVEVAEL-------------- 1028
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 386869312 211 eQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 267
Cdd:COG5022 1029 -QSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLY 1084
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-264 |
5.58e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 67 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLELKVKEQKDYWETELLQLKEQNQK 146
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA---ELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 147 MSsenekmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 226
Cdd:COG1196 399 AA--------QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 386869312 227 KQQELMDENFDLSKRLSENEIICNALQRQKERLEGEND 264
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
51-268 |
1.26e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 51 FQFRPENEEDILVVTtqgevEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkeqk 130
Cdd:PRK03918 174 IKRRIERLEKFIKRT-----ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 131 dywetellQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKENDhLFLSLTEQRKDQKKL 210
Cdd:PRK03918 242 --------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL----EEKVKELKELKEKAE-EYIKLSEFYEEYLDE 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386869312 211 EQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKR 268
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-269 |
1.56e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 67 QGEVEEIEQHNKELCKENQELKDSCISLQKQ-----NSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLK 141
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE----QISQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 142 EQNQKMSSENEKmgirvdqLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 221
Cdd:TIGR04523 349 KELTNSESENSE-------KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386869312 222 TTAMKKQQELMDENF-------DLSKRLSENEIICNALQRQKERLEGENDLLKRE 269
Cdd:TIGR04523 422 ELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-259 |
1.81e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 66 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkEQKDYWETELLQLKEQnq 145
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE----RRIAATERRLEDLEEQ-- 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 146 kmssenekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 225
Cdd:TIGR02168 847 ------------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
170 180 190
....*....|....*....|....*....|....
gi 386869312 226 KKQQELMDENFDLSKRLSENEiicNALQRQKERL 259
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLE---VRIDNLQERL 945
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
66-230 |
1.95e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 66 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQ----------KDYWE- 134
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 135 -------TELL-------QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL 200
Cdd:COG3883 108 llgsesfSDFLdrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190
....*....|....*....|....*....|
gi 386869312 201 TEQRKDQKKLEQTVEQMKQNETTAMKKQQE 230
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-273 |
2.11e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 67 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLE----LKVKEQKDYWETELLQ--- 139
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqekeLLEKEIERLKETIIKNnse 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 140 ---LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKE-------MEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKK 209
Cdd:TIGR04523 442 ikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869312 210 LEQTVEQM----KQNETTAMKKQQELMDENFDLSKRLSENEIicNALQRQKERLEGENDLLKRENSRL 273
Cdd:TIGR04523 522 LKEKIEKLesekKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
58-264 |
2.30e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 58 EEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQnsdmQAELQKKQEELETLQSIN--KKLELKVKEQKDYWET 135
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK----EAEEKKKAEELKKAEEENkiKAAEEAKKAEEDKKKA 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 136 ELLQLKEQNQKMSSENEKmgirvdqlqaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE 215
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALK----------KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386869312 216 QMKQNETTAMKKQQELMDENFDLSKRLSENE-IICNALQRQKERLEGEND 264
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEaVIEEELDEEDEKRRMEVD 1797
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
350-372 |
2.43e-05 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 40.63 E-value: 2.43e-05
10 20
....*....|....*....|....
gi 386869312 350 CPICDKIFPATEKQ-IFEDHVFCH 372
Cdd:cd21965 1 CPICNKQFPPQVDQeAFEDHVESH 24
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-275 |
2.80e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 104 ELQKKQEELETLQSINKKLELKVKEQKDywETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKT 183
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEEL--EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 184 EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEiicNALQRQKERLEGEN 263
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAE 371
|
170
....*....|..
gi 386869312 264 DLLKRENSRLLS 275
Cdd:COG1196 372 AELAEAEEELEE 383
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
67-260 |
3.07e-05 |
|
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: 45.66 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 67 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETellqLKEQNQK 146
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKT----LTQRVLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 147 MSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 226
Cdd:pfam07888 148 RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
170 180 190
....*....|....*....|....*....|....
gi 386869312 227 KQqelmdenfdlskrlSENEIICNALQRQKERLE 260
Cdd:pfam07888 228 KE--------------AENEALLEELRSLQERLN 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
56-260 |
3.48e-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: 45.82 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 56 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET 135
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 136 ELLQLKEQNQKMSSENEKMG---IRVDQLQAQLSTQEKEMEKLVQgdqdkteQLEQLKKENDHLFLSLTEQRKDQKKLEQ 212
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAAnlrERLESLERRIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELES 873
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386869312 213 TVE-------QMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLE 260
Cdd:TIGR02168 874 ELEallneraSLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-275 |
4.00e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 63 VVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLelkvKEQKDYWETELLQLKE 142
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY----KQEIKNLESQINDLES 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 143 QNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE----QMK 218
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrSIN 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 386869312 219 QNETTAMKKQQELMDENFDLSKrlseneiicnaLQRQKERLEGENDLLKRENSRLLS 275
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKK-----------LNEEKKELEEKVKDLTKKISSLKE 524
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-273 |
4.80e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 102 QAELQKKQEELETLQSINKKLELKVKEQK-DYWETELLQLKEqnqkmssENEKMGIRVDQLQAQLSTQEKEMEKL-VQGD 179
Cdd:COG4913 261 AERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRA-------ELARLEAELERLEARLDALREELDELeAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 180 QDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQM-----------KQNETTAMKKQQELMDENFDLSKRLSENEII 248
Cdd:COG4913 334 GNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
170 180
....*....|....*....|....*
gi 386869312 249 CNALQRQKERLEGENDLLKRENSRL 273
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRKSNI 438
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
38-264 |
7.00e-05 |
|
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: 44.73 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 38 VDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKElcKENQELKDSCISLQ----KQNSDMQAELQKKQEELE 113
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK--RELERIRQEEIAMEisrmRELERLQMERQQKNERVR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 114 TLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSENEKMgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEN 193
Cdd:pfam17380 396 QELEAARKVKILEEER----QRKIQQQKVEMEQIRAEQEEA--RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869312 194 DHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLS-ENEIICNALQRQKERLEGEND 264
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEkEMEERQKAIYEEERRREAEEE 541
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
70-221 |
8.79e-05 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 43.58 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 70 VEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSS 149
Cdd:pfam17078 68 LKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKL 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869312 150 ENEKmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 221
Cdd:pfam17078 148 ENEK---QLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKLDSLAQLLDLPSWLNLYPESR 216
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
101-273 |
9.55e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 101 MQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQ 180
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 181 DKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLE 260
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170
....*....|...
gi 386869312 261 GENDLLKRENSRL 273
Cdd:COG4372 164 EELAALEQELQAL 176
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
56-269 |
9.69e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 56 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK--EQKDYW 133
Cdd:pfam02463 807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEleEQKLKD 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 134 ETELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKlvqgdqdktEQLEQLKKENDHLFLSLTEQRKDQKKLEQT 213
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEES---QKLNLLEEKENEIEERIK---------EEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 386869312 214 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRE 269
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
85-239 |
1.24e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 44.21 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 85 QELKDScisLQKQNSDmqAELQKKQEELEtlQSINKKL-ELKvkEQKDYWETELLQLKEQNQKMssenekmgIRVDQLQA 163
Cdd:pfam13779 496 ERLSEA---LERGASD--EEIAKLMQELR--EALDDYMqALA--EQAQQNPQDLQQPDDPNAQE--------MTQQDLQR 558
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869312 164 QLstqeKEMEKLVQ-GDQDKTEQ-LEQLKKENDHLFLSLTEQRKDQKKlEQTVEQMKQNETTaMKKQQELMDENFDLS 239
Cdd:pfam13779 559 ML----DRIEELARsGRRAEAQQmLSQLQQMLENLQAGQPQQQQQQGQ-SEMQQAMDELGDL-LREQQQLLDETFRQL 630
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
82-254 |
1.32e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 82 KENQELKDSCIS-----LQKQNSDMQAELQKKQEELetlqsinKKLELKVKEQKDYWETELlqlkEQNQKMSSENEKMGI 156
Cdd:PRK12704 49 KEAEAIKKEALLeakeeIHKLRNEFEKELRERRNEL-------QKLEKRLLQKEENLDRKL----ELLEKREEELEKKEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 157 RVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsltEQRKDQkkLEQTVEQMKQnETTAMKKQQElmDENF 236
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEIL--LEKVEEEARH-EAAVLIKEIE--EEAK 183
|
170
....*....|....*...
gi 386869312 237 DLSKRLSeNEIICNALQR 254
Cdd:PRK12704 184 EEADKKA-KEILAQAIQR 200
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
69-274 |
1.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 69 EVEEIEQHNKELCKENQELK-------------DSCISLQKQNSDMQAELQKKQEElETLQSINKKLELKVKEQKDYWET 135
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRkaeeakkaeeariEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 136 ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLfLSLTEQRKDQKKLEQTVE 215
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAE 1719
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869312 216 QMKQNETTAMKKQQELMDENFDLSKRLSE---NEIICNALQRQKERLEGENDLLKRENSRLL 274
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEakkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
65-264 |
2.31e-04 |
|
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: 43.24 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 65 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELK-VKEQKDY--WETELLQLK 141
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKnIKLSKDVssLESQLQDTQ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 142 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEqlkkendhlflSLTEQRKD-QKKLEQTVEQMKQN 220
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLS-----------TLQAQLSDmKKKLEEDAGTLEAL 543
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869312 221 ETTAMKKQQELMdenfDLSKRLSENEIICNALQRQKERLEGEND 264
Cdd:pfam01576 544 EEGKKRLQRELE----ALTQQLEEKAAAYDKLEKTKNRLQQELD 583
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-230 |
2.37e-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: 43.13 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 66 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET----LQSINKKLElKVKEQKDYWETELLQLK 141
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdeLKDYREKLE-KLKREINELKRELDRLQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 142 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLK----KENDHLFLSLTEQRKDQKKLEQTVEQM 217
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlsKYEQELYDLKEEYDRVEKELSKLQREL 492
|
170
....*....|...
gi 386869312 218 KQNETTAMKKQQE 230
Cdd:TIGR02169 493 AEAEAQARASEER 505
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
65-286 |
2.53e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 65 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLE---LKVKEQKDYWETELLQLK 141
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeelESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 142 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 221
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869312 222 TTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPY 286
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
69-275 |
2.63e-04 |
|
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: 43.04 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 69 EVEEIEQHNKELCKENQELKdsciSLQKQNSDMQAELQKKQEELETLQSINKKLELKV-KEQKDYWETELLQLKEQNQKM 147
Cdd:pfam02463 181 ETENLAELIIDLEELKLQEL----KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 148 SSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKK 227
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 386869312 228 QQELMDENFDLSKRLSENEII---CNALQRQKERLEGENDLLKRENSRLLS 275
Cdd:pfam02463 337 IEELEKELKELEIKREAEEEEeeeLEKLQEKLEQLEEELLAKKKLESERLS 387
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
56-282 |
2.67e-04 |
|
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: 43.11 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 56 ENEEDILVVTTQGEVEEIEQHNKELckenQELKDScisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKD---- 131
Cdd:TIGR00606 722 EKRRDEMLGLAPGRQSIIDLKEKEI----PELRNK---LQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtim 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 132 ---YWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG-------DQDKTEQLEQLKKENDHL---FL 198
Cdd:TIGR00606 795 erfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKielnrklIQDQQEQIQHLKSKTNELkseKL 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 199 SLTEQRKDQKKL-EQTVEQMKQ----NETTAMKKQQELMDENFdLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 273
Cdd:TIGR00606 875 QIGTNLQRRQQFeEQLVELSTEvqslIREIKDAKEQDSPLETF-LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI 953
|
....*....
gi 386869312 274 LSYMGLDFN 282
Cdd:TIGR00606 954 HGYMKDIEN 962
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-271 |
3.22e-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: 42.74 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 148 SSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKK 227
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 386869312 228 QQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENS 271
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-192 |
3.60e-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: 42.75 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 67 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLEL---------KVKEQKDYWETEL 137
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQAELQRVEEEI 967
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 386869312 138 LQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKE 192
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI----LERIEEYEKKKRE 1018
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
60-273 |
4.02e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 60 DILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQE-ELETLQSINKKLELKVKEQK----DYWE 134
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElEFEIQSQEQDSEIVKNSKSElariPELE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 135 TELLQLKEQNQKMSSENEKMGI---RVDQLQAQLSTQEKEMEKLVQGDQDKtEQLEQLKKENDHLFLSLTEQRKDQKKLE 211
Cdd:pfam05557 204 KELERLREHNKHLNENIENKLLlkeEVEDLKRKLEREEKYREEAATLELEK-EKLEQELQSWVKLAQDTGLNLRSPEDLS 282
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869312 212 QTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 273
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
71-248 |
4.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 71 EEIEQHNKELcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELL---------QLK 141
Cdd:COG4717 71 KELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeaelaelpeRLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 142 EQNQKMSSENEKMgIRVDQLQAQLSTQEKEMEKLVQGDQDKTE-QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN 220
Cdd:COG4717 150 ELEERLEELRELE-EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|....*...
gi 386869312 221 EttamkKQQELMDENFDLSKRLSENEII 248
Cdd:COG4717 229 L-----EQLENELEAAALEERLKEARLL 251
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
94-273 |
7.36e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 94 LQKQNSDMQAELQKKQEELETLQSINKKLELkvKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEME 173
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 174 KLVQGD--QDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNettamkKQQElmdenfdLSKRLSENEIICNA 251
Cdd:COG3206 258 ELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------LQQE-------AQRILASLEAELEA 324
|
170 180
....*....|....*....|..
gi 386869312 252 LQRQKERLEGENDLLKRENSRL 273
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAEL 346
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
62-219 |
8.14e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 62 LVVTTQGEVEEIEQHNKELCKENQELKDscISLQKQNSDMQAELQKKQEELETL---------QSINKKLEL-------- 124
Cdd:PRK04778 224 LQTELPDQLQELKAGYRELVEEGYHLDH--LDIEKEIQDLKEQIDENLALLEELdldeaeeknEEIQERIDQlydilere 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 125 -----KVKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT---- 183
Cdd:PRK04778 302 vkarkYVEKNSDTLPDFLEHAKEQNKELKEEidrvkqsytlNESELESVRQLEKQLESLEKQYDEITEriAEQEIAysel 381
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869312 184 --------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 219
Cdd:PRK04778 382 qeeleeilKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRN 425
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
69-269 |
8.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 69 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE-----TELLQLKE- 142
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADelkkaEELKKAEEk 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 143 ---QNQKMSSENEKMGIRVDQLQAQLSTQEKEmEKLVQGDQDKTEQLEQLKKENDHLFLSltEQRKDQKKLEQTVEQMKQ 219
Cdd:PTZ00121 1564 kkaEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKK 1640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386869312 220 NETTAMKKQQELMDENfdlskrlSENEIICNALQRQKERLEGENDLLKRE 269
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAE-------EENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
94-293 |
8.57e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 94 LQKQNSDMQAELQKKQEELETLQSinkklELKVKEQKdywETELLQLKEQNQkmssenekmGIRVDQLQAQLSTQEKEME 173
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEA-----RLDALREE---LDELEAQIRGNG---------GDRLEQLEREIERLERELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 174 KLVQgdqdkteQLEQLKKENDHLFLSLTEQRKD----QKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSE--NEI 247
Cdd:COG4913 356 ERER-------RRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleAEI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 386869312 248 icNALQRQKERLEGENDLLKREnsrLLSYMGLDFNSLPY-----QVPTSDE 293
Cdd:COG4913 429 --ASLERRKSNIPARLLALRDA---LAEALGLDEAELPFvgeliEVRPEEE 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-260 |
1.04e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 65 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK---EQKDYWETELLQLK 141
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEEALALLR 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 142 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVqgdqdktEQLEQLKKENDHLFLSLTEQRKDqkkleqTVEQMKQNE 221
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLE-------LRLEGLEVRIDNLQERLSEEYSL------TLEEAEALE 960
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386869312 222 TTAMKKQQELMDENFDLSKRLSE----NEIICNALQRQKERLE 260
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYD 1003
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
102-234 |
1.07e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 102 QAELQKKQEELEtLQSINKKLELKVKEqkdywetELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKlvqgdqd 181
Cdd:PRK12704 39 EAKRILEEAKKE-AEAIKKEALLEAKE-------EIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDR------- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 386869312 182 KTEQLEQLKKEndhlflsLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE 234
Cdd:PRK12704 101 KLELLEKREEE-------LEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
97-280 |
1.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 97 QNSDMQAELQKKQEELETLQSinkKLELKVKEQKDywetellQLKEQNQKMSSENEkmgiRVDQLQAQLSTQEKEMEKL- 175
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERT---RAREQLRQAQA-------QLAQYNQVLASLKS----SYDAKRQMLQELKQELQDLg 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 176 VQGDQDKTEQLEQLKKENDHLfLSLTEQRKDQKKLEQTVEQMkqnETTAMKKQQELMDENFDLSKRLSENE--IICNALq 253
Cdd:PRK04863 1048 VPADSGAEERARARRDELHAR-LSANRSRRNQLEKQLTFCEA---EMDNLTKKLRKLERDYHEMREQVVNAkaGWCAVL- 1122
|
170 180
....*....|....*....|....*..
gi 386869312 254 rqkeRLEGENDLLKRENSRLLSYMGLD 280
Cdd:PRK04863 1123 ----RLVKDNGVERRLHRRELAYLSAD 1145
|
|
| CCDC14 |
pfam15254 |
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ... |
74-171 |
1.38e-03 |
|
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing protein 14 (CCDC14) is a domain of unknown function. This family of proteins is found in eukaryotes. Proteins in this family are typically between 301 and 912 amino acids in length.
Pssm-ID: 464594 Cd Length: 857 Bit Score: 40.94 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 74 EQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLeLKVKE-QKDY----------WETELLQLKE 142
Cdd:pfam15254 412 EQEKTEKTSGSGDCNLELFSLQSLNMSLQNQLQESLKSQELLQSKNEEL-LKVIEnQKEEnkkltkifkeKEQTLLENKQ 490
|
90 100 110
....*....|....*....|....*....|...
gi 386869312 143 Q----NQKMSSENEKMGIRVDQLQAQLSTQEKE 171
Cdd:pfam15254 491 QfdieTTRVKIELEEALVNMKSFQFKLEAAEKE 523
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
37-191 |
1.42e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 37 YVDED----GVVRGASI----------------PFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDscislqk 96
Cdd:COG2433 362 DVDRDevkaRVIRGLSIeealeeliekelpeeePEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 97 qnsdmqaELQKKQEELEtlqsinkKLELKVKEQKdywetellqlKEQNQKMSSENE--KMGIRVDQLQAQLSTQEKEMEK 174
Cdd:COG2433 435 -------ELEEKDERIE-------RLERELSEAR----------SEERREIRKDREisRLDREIERLERELEEERERIEE 490
|
170
....*....|....*..
gi 386869312 175 LvqgdQDKTEQLEQLKK 191
Cdd:COG2433 491 L----KRKLERLKELWK 503
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
71-273 |
1.47e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 71 EEIEQhnkelcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWEtELLQLKEQnqkmsse 150
Cdd:PRK02224 194 AQIEE------KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-ELETLEAE------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 151 nekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAmkkQQE 230
Cdd:PRK02224 260 -------IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL---RDR 329
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386869312 231 LMDENFDLSKRLSENEiicnALQRQKERLEGENDLLKRENSRL 273
Cdd:PRK02224 330 LEECRVAAQAHNEEAE----SLREDADDLEERAEELREEAAEL 368
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-271 |
1.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 103 AELQKKQEELETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMgirvdQLQAQLSTQEKEMEKLVQGDQDK 182
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 183 TEQLEQLKKEND---HLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ--------QELMDENFDLSKRLSENEIICNA 251
Cdd:COG4717 145 PERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEAQEELEE 224
|
170 180
....*....|....*....|
gi 386869312 252 LQRQKERLEGENDLLKRENS 271
Cdd:COG4717 225 LEEELEQLENELEAAALEER 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
78-266 |
2.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 78 KELCKENQELKDScislQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDyweteLLQLKEQNQKMSSENEKMGIR 157
Cdd:COG4717 74 KELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 158 VDQLQaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQ-KKLEQTVEQMKQNETTAMKKQQELMDENF 236
Cdd:COG4717 145 PERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190
....*....|....*....|....*....|
gi 386869312 237 DLSKRLSENEIICNALQRQKERLEGENDLL 266
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
67-191 |
2.12e-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: 39.30 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 67 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQ------SINKKLELKVKEQKDYWETELLQL 140
Cdd:pfam15294 132 HMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKdvksnlKEISDLEEKMAALKSDLEKTLNAS 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869312 141 KEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGD----------QDKTEQLEQLKK 191
Cdd:pfam15294 212 TALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTaayrnmkemlTKKNEQIKELRK 272
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
125-233 |
2.73e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 38.50 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 125 KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQ---AQLSTQEKEMEKLVQGDQDKT-EQLEQLKKENDHLFLSL 200
Cdd:pfam05010 12 KARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEktiAQMIEEKQKQKELEHAEIQKVlEEKDQALADLNSVEKSF 91
|
90 100 110
....*....|....*....|....*....|...
gi 386869312 201 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMD 233
Cdd:pfam05010 92 SDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA 124
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
69-275 |
2.83e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 69 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELEtlqsiNKKLELKVKEQkdywetELLQLKEQNQKMS 148
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE-----QKQKELKSKEK------ELKKLNEEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 149 SENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQK--KLEQTVEQMKQNETTAMK 226
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieELKQTQKSLKKKQEEKQE 589
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 386869312 227 KQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 275
Cdd:TIGR04523 590 LIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
56-228 |
3.07e-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: 39.72 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 56 ENEEDILVVTTQGEVEE-IEQHNKELCKenqeLKDSCISLQKQNSDMQAELQKKQEE-----------LETLQSINKKLE 123
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQlISEHEVEITG----LTEKASSARSQANSIQSQLEIIQEQarnqnsmymrqLSDLESTVSQLR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 124 LKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEN---------- 193
Cdd:pfam15921 331 SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNkrlwdrdtgn 410
|
170 180 190
....*....|....*....|....*....|....*....
gi 386869312 194 ----DHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 228
Cdd:pfam15921 411 sitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQ 449
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
71-261 |
3.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 71 EEIEQHNKELCKENQELKdsciSLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELL--QLKEQNQKMS 148
Cdd:PRK03918 238 EEIEELEKELESLEGSKR----KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFyeEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 149 SENEKMGIRVDQLQAQLSTQE------KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLE-QTVEQMKQNE 221
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKEL 393
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 386869312 222 TTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEG 261
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
95-269 |
3.57e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 95 QKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEK 174
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 175 LVQGDQDKTEQL---EQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNA 251
Cdd:PTZ00121 1614 KAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
|
170
....*....|....*...
gi 386869312 252 LQRQKERLEGENDLLKRE 269
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKE 1711
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
69-246 |
3.72e-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: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 69 EVEEIEQHNKELCKENQELKDScisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYW----ETEL----LQL 140
Cdd:TIGR00606 910 QDSPLETFLEKDQQEKEELISS---KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYlkqkETELntvnAQL 986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 141 KEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLV-QGDQDKTEQLEQLKKENDHLF--LSLTEQRKDQKKLEQTVEQM 217
Cdd:TIGR00606 987 EECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTlRKRENELKEVEEELKQHLKEMgqMQVLQMKQEHQKLEENIDLI 1066
|
170 180
....*....|....*....|....*....
gi 386869312 218 KQNETTAMKKQQELMDENFDLSKRLSENE 246
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
58-275 |
3.86e-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: 39.57 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 58 EEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEE-------LETLQSINKKLELKVKEQK 130
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekekklQEEELKLLAKEEEELKSEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 131 DYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKL 210
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869312 211 EQtveqmkQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 275
Cdd:pfam02463 383 SE------RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
100-219 |
3.94e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.07 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 100 DMQAELQKKQEELETLQSI-NKKLELK--VKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLS 166
Cdd:pfam06160 260 EAEEALEEIEERIDQLYDLlEKEVDAKkyVEKNLPEIEDYLEHAEEQNKELKEElervqqsytlNENELERVRGLEKQLE 339
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869312 167 TQEKEMEKLVQGDQDKT--------------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 219
Cdd:pfam06160 340 ELEKRYDEIVERLEEKEvayselqeeleeilEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKL 406
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
96-257 |
4.13e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 38.92 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 96 KQNSDMQAELQKKQEELET---LQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKmgirVDQLQAQLSTQEKEM 172
Cdd:PRK12705 39 LQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK----LDNLENQLEEREKAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 173 EklvqgdqDKTEQLEQLKKENDHLFLSLTEQRKDQ------KKLEQTVEQMKQNETTAMKkqqelmdENFDLSKRLSENE 246
Cdd:PRK12705 115 S-------ARELELEELEKQLDNELYRVAGLTPEQarklllKLLDAELEEEKAQRVKKIE-------EEADLEAERKAQN 180
|
170
....*....|.
gi 386869312 247 IICNALQRQKE 257
Cdd:PRK12705 181 ILAQAMQRIAS 191
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
75-240 |
4.20e-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: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 75 QHNKELCKENQELKDSC--ISLQKQNSDMQAELQKKQ-EELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN 151
Cdd:pfam15921 534 QHLKNEGDHLRNVQTECeaLKLQMAEKDKVIEILRQQiENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILK 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 152 EKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN--------ETT 223
Cdd:pfam15921 614 DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNfrnkseemETT 693
|
170
....*....|....*..
gi 386869312 224 AMKKQQELMDENFDLSK 240
Cdd:pfam15921 694 TNKLKMQLKSAQSELEQ 710
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
72-219 |
4.20e-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: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 72 EIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETELLQlkeqnQKMSSEN 151
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE-STKEMLRKVVEELTA-----KKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 152 EKMgiRVDQLQAQLSTQEK-------EMEKLVQGDQDKTEQLEQLKKENDHLF----------LSLTEQRKDQKKLEQTV 214
Cdd:pfam15921 494 SER--TVSDLTASLQEKERaieatnaEITKLRSRVDLKLQELQHLKNEGDHLRnvqtecealkLQMAEKDKVIEILRQQI 571
|
....*
gi 386869312 215 EQMKQ 219
Cdd:pfam15921 572 ENMTQ 576
|
|
| FtsL2 |
COG4839 |
Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning]; |
91-132 |
4.34e-03 |
|
Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443867 Cd Length: 123 Bit Score: 36.86 E-value: 4.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 386869312 91 CISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDY 132
Cdd:COG4839 57 LLSLQASIYELNREIQSLESKISEQQKENEDLEQEVSELSSP 98
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
71-262 |
4.60e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 71 EEIEQHNKEL--CKENQELKDSCISLQKQNSDmqaELQKKQEELETLQSINKKLElkvkeqkDYWETELLQLKEQNQKms 148
Cdd:TIGR02169 170 RKKEKALEELeeVEENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKR-------EYEGYELLKEKEALER-- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 149 senekmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLF-----LSLTEQRKDQKKLEQTVEQMKQNETT 223
Cdd:TIGR02169 238 --------QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdLGEEEQLRVKEKIGELEAEIASLERS 309
|
170 180 190
....*....|....*....|....*....|....*....
gi 386869312 224 AMKKQQELMdenfDLSKRLSENEIICNALQRQKERLEGE 262
Cdd:TIGR02169 310 IAEKERELE----DAEERLAKLEAEIDKLLAEIEELERE 344
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
57-272 |
5.18e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 57 NEEDILVV----TTQGEVEEIEQHNKELckenqelkdscISLQKQNSDMQAELQKKQEELETLQSINK--------KLEL 124
Cdd:PRK11281 55 EAEDKLVQqdleQTLALLDKIDRQKEET-----------EQLKQQLAQAPAKLRQAQAELEALKDDNDeetretlsTLSL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 125 KVKEQKdyWETELLQLK--------------------EQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKLVqgdqdkTE 184
Cdd:PRK11281 124 RQLESR--LAQTLDQLQnaqndlaeynsqlvslqtqpERAQAALYANSQ---RLQQIRNLLKGGKVGGKALR------PS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 185 QLEQLKKENDHLFLSLTEQRKDqkkLE-----QTVEQMKQNETTAmkKQQELMDENFDL-----SKRLSENEIICNALQR 254
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQRKS---LEgntqlQDLLQKQRDYLTA--RIQRLEHQLQLLqeainSKRLTLSEKTVQEAQS 267
|
250
....*....|....*....
gi 386869312 255 QKERLE-GENDLLKRENSR 272
Cdd:PRK11281 268 QDEAARiQANPLVAQELEI 286
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
2-209 |
5.26e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.76 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 2 WVTLPIDLnnKSAKQQE-VQFKAYYLPKDdeyyqfcYVDEDGVVRGASIPFQFRPENEEDILVVTTqgEVEEIEQHNKEL 80
Cdd:PRK05771 129 WGNFDLDL--SLLLGFKyVSVFVGTVPED-------KLEELKLESDVENVEYISTDKGYVYVVVVV--LKELSDEVEEEL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 81 CK---ENQELKDSCISLQkqnsdmqaELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEqnqKMSSENEKmgir 157
Cdd:PRK05771 198 KKlgfERLELEEEGTPSE--------LIREIKEELEEIEKERESLLEELKELAKKYLEELLALYE---YLEIELER---- 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386869312 158 vdqlqAQLSTQEKEMEKL--VQG--DQDKTEQLEQL--KKENDHLFLSLTEQRKDQKK 209
Cdd:PRK05771 263 -----AEALSKFLKTDKTfaIEGwvPEDRVKKLKELidKATGGSAYVEFVEPDEEEEE 315
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
71-275 |
5.29e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 38.85 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 71 EEIEQHNKELCKENQELK---DSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKdyweTELLQLKEQ---- 143
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISntqTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK----SEISDLNNQkeqd 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 144 -NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNET 222
Cdd:TIGR04523 308 wNKELKSELKNQEKKLEEIQNQISQNNKIISQL-------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 386869312 223 TAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 275
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
93-231 |
5.45e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 93 SLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywETELLQLKEQNQKMSSENEKMGIR-------VDQLQAQL 165
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQI 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869312 166 STQEKEMEKLVQGDQDKTE--------QLEQLKKENDHL---FLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 231
Cdd:COG3206 301 AALRAQLQQEAQRILASLEaelealqaREASLQAQLAQLearLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
59-273 |
6.08e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.46 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 59 EDILVVTTQGEVEEIeqhNKELCKE-NQELK--DSCISLQKQNSDMQAELQKKQEEL--ETLQSINKKLELKVKEQKDYw 133
Cdd:PHA02562 157 EDLLDISVLSEMDKL---NKDKIRElNQQIQtlDMKIDHIQQQIKTYNKNIEEQRKKngENIARKQNKYDELVEEAKTI- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 134 ETELLQLKEQNQKMSSENEKmgirvdqlqaqlstQEKEMEKLVQGDQDKTEQLEQLKKEndHLFL-------SLTEQRKD 206
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIED--------------PSAALNKLNTAAAKIKSKIEQFQKV--IKMYekggvcpTCTQQISE 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386869312 207 Q-KKLEQTVEQMKQNET------TAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 273
Cdd:PHA02562 297 GpDRITKIKDKLKELQHslekldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
350-372 |
6.34e-03 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 33.77 E-value: 6.34e-03
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
110-232 |
6.46e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 38.52 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 110 EELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQL 189
Cdd:pfam05622 282 EKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLL 361
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 386869312 190 KKENDHLFLSLTE-QRKDQKKLEQTVEQMKQNETTAMKKQQELM 232
Cdd:pfam05622 362 KQKLEEHLEKLHEaQSELQKKKEQIEELEPKQDSNLAQKIDELQ 405
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
101-268 |
6.67e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.78 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 101 MQAELQKKQEELETLQS---INKKLELKVKEQKDYWeTELLQLK-----EQNQKMSSENekmgirvDQLQAQLStqekem 172
Cdd:PRK04863 926 IVSVLQSDPEQFEQLKQdyqQAQQTQRDAKQQAFAL-TEVVQRRahfsyEDAAEMLAKN-------SDLNEKLR------ 991
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 173 EKLVQGDQDKTEQLEQLKK------ENDHLFLSLTE--QRKDQ--KKLEQTVEQMKQNETTAMKKQQELMDEnfDLSKRL 242
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQaqaqlaQYNQVLASLKSsyDAKRQmlQELKQELQDLGVPADSGAEERARARRD--ELHARL 1069
|
170 180
....*....|....*....|....*..
gi 386869312 243 SENEIICNALQRQKERLEGE-NDLLKR 268
Cdd:PRK04863 1070 SANRSRRNQLEKQLTFCEAEmDNLTKK 1096
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
54-247 |
6.87e-03 |
|
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: 38.57 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 54 RPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEEletlQSINKKLELKvKEQKDYW 133
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE----ERKRKKLELE-KEKRDRK 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 134 ETELL-------QLKEQNQKMSSENEKMGIrvdqlqaqlstQEKEME---KLVQGDQDKTEQLEQLKKENDhlflsLTEQ 203
Cdd:pfam17380 488 RAEEQrrkilekELEERKQAMIEEERKRKL-----------LEKEMEerqKAIYEEERRREAEEERRKQQE-----MEER 551
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869312 204 RKDQKKLEQTVEQMKQNEttAMKKQQELMDENFDLSKRLSENEI 247
Cdd:pfam17380 552 RRIQEQMRKATEERSRLE--AMEREREMMRQIVESEKARAEYEA 593
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
67-277 |
8.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.96 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 67 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDM---QAELQKKQEEletLQSINKKLELKVKEQKDYwETELLQLKEQ 143
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEE---LEELNEQLQAAQAELAQA-QEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869312 144 NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT 223
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386869312 224 AMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYM 277
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
|
| |
