|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
23-146 |
5.55e-41 |
|
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: 141.61 E-value: 5.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 23 VIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRcslnqtiqllitpdtgsiwhqVGWKTTREYYTFMWVtlPIDL 102
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFK---------------------VGWKSVNDYVTYVWA--KDDE 57
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 386869294 103 NNKSAKQQEVQFKAYYLPKDD-EYYQFCYVDEDGVVRGASIPFQF 146
Cdd:pfam17751 58 VEGSNSVRQVLFKASYLPKEPeGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
159-362 |
1.39e-12 |
|
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: 69.02 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQ 238
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE----ELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 239 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 318
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869294 319 KKQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:COG4942 195 AERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-368 |
9.43e-11 |
|
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: 64.31 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSEN 244
Cdd:TIGR02168 233 RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL----QKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 EKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 324
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869294 325 MDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
160-367 |
7.91e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQK 239
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 240 MSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 319
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386869294 320 KQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 367
Cdd:COG1196 408 AEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
165-412 |
1.15e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetellQLKEQNQKMSSEN 244
Cdd:COG3883 17 QIQAKQKEL----SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA-------EIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 EKMGIRVDQLQ------------------AQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQT 306
Cdd:COG3883 86 EELGERARALYrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 307 VEQMKQNETTAMKKQQELMDenfdlskRLSENEiicNALQRQKERLEGENDLLKRENSRLLSYmGLDFNSLPYQVPTSDE 386
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLA-------QLSAEE---AAAEAQLAELEAELAAAEAAAAAAAAA-AAAAAAAAAAAAAAAA 234
|
250 260
....*....|....*....|....*.
gi 386869294 387 GGARQNPGLAYGNPYSGIQESSSPSP 412
Cdd:COG3883 235 AAAAAAAAAASAAGAGAAGAAGAAAG 260
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-367 |
1.65e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQhnKELCKENQELKDSCISLQKQNSDMQAELQKKQEELE----TLQSINKKLELKVKEQKDYWETELLQLKE 235
Cdd:TIGR02169 217 LKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISelekRLEEIEQLLEELNKKIKDLGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 236 QNQKMSSEnekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEqtvEQMKQNET 315
Cdd:TIGR02169 295 KIGELEAE-------IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKE 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386869294 316 TAMKKQQELMDEnfdlSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 367
Cdd:TIGR02169 365 ELEDLRAELEEV----DKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
441-467 |
2.29e-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: 2.29e-09
10 20
....*....|....*....|....*..
gi 386869294 441 FNCPICDKIFPATEKQIFEDHVFCHSL 467
Cdd:cd21968 1 FECPICSKIFEATSKQEFEDHVFCHSL 27
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-368 |
2.53e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMS 241
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 242 SENEkmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 321
Cdd:COG1196 376 EAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 386869294 322 QELMDENFDLSKRLSENEiicNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:COG1196 452 AELEEEEEALLELLAELL---EEAALLEAALAELLEELAEAAARLLL 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
154-366 |
3.28e-09 |
|
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: 58.62 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 154 ILVVTTQGEVEEIEQHNKELckenqelkdscISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQL 233
Cdd:COG4942 10 LLALAAAAQADAAAEAEAEL-----------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL----ARRIRAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 234 KEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLV-----QGDQDKTE-------------QLEQLKKENDHLFLSLTE 295
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrLGRQPPLAlllspedfldavrRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869294 296 QRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-366 |
4.75e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILvvttQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET----LQSINKKLELKVKEQKD 224
Cdd:TIGR02169 687 KRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 225 YwETELLQLKEQNQKMSSENEKM-----GIRVDQLQAQLSTQEKE----------MEKLVQGDQDKTEQLEQLKKENDHL 289
Cdd:TIGR02169 763 L-EARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEvsriearlreIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 290 FLSLTEQRKDQKK----LEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 365
Cdd:TIGR02169 842 RIDLKEQIKSIEKeienLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
.
gi 386869294 366 L 366
Cdd:TIGR02169 922 L 922
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-366 |
5.11e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 195 QAELQKKQEELETLQSINKKLElkvkEQKDYWETELLQLkeQNQKMSSENEkmgIRVDQLQAQLSTQEKEMEKLVQGDQD 274
Cdd:COG4913 616 EAELAELEEELAEAEERLEALE----AELDALQERREAL--QRLAEYSWDE---IDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 275 ---KTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE-----NFDLSKRLsENEIICNALQ 346
Cdd:COG4913 687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEERF-AAALGDAVER 765
|
170 180
....*....|....*....|
gi 386869294 347 RQKERLEGENDLLKRENSRL 366
Cdd:COG4913 766 ELRENLEERIDALRARLNRA 785
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-366 |
6.39e-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: 58.53 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETL----QSINKKLELKVKEQKDYwETELLQLKE 235
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkQILRERLANLERQLEEL-EAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 236 QNQKMSSENEKMGIRVDQLQ-------AQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE 308
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294 309 QMKQNettamkkQQELMDENFDLSKRLSENEIicNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR02168 411 RLEDR-------RERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERL 459
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
162-337 |
8.47e-09 |
|
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: 57.72 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKvkEQKDYWETELLQLKEQNQKMS 241
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE--KEIDEKNKEIEELKQTQKSLK 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 242 SENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 321
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
170
....*....|....*.
gi 386869294 322 QELMDENFDLSKRLSE 337
Cdd:TIGR04523 662 PEIIKKIKESKTKIDD 677
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
164-366 |
1.54e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET-LQSINKKLELKVKEQKDYWET------ELLQLKEQ 236
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAeIASLERSIAEKERELEDAEERlakleaEIDKLLAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 237 NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT------------EQLEQLKKENDHLFLSLTEQRKDQKK 302
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAelEEVDKEfaetrdelkdyrEKLEKLKREINELKRELDRLQEELQR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386869294 303 LEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-368 |
1.83e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 171 KELcKENQELKDSCISLQKQNsDMQAELQKKQEELETLQSINKKLELKVKEqkdyWETELLQLKEQNQKMSSENEKMGIR 250
Cdd:COG1196 216 REL-KEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 251 VDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFD 330
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190
....*....|....*....|....*....|....*...
gi 386869294 331 LSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-360 |
2.40e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 150 NEEDILVVTTQGEVEEIEQHNKelcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET- 228
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETl 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 229 --ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQgdqdkteqlEQLKKENDHLFLSLTEQRKDQKKLEQT 306
Cdd:TIGR02168 385 rsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK---------KLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386869294 307 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 360
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
160-366 |
3.68e-08 |
|
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: 55.80 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLE----LKVKEQKDYWETELLQ--- 232
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqekeLLEKEIERLKETIIKNnse 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 233 ---LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKE-------MEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKK 302
Cdd:TIGR04523 442 ikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294 303 LEQTVEQM----KQNETTAMKKQQELMDENFDLSKRLSENEIicNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR04523 522 LKEKIEKLesekKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
160-362 |
3.78e-08 |
|
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: 55.80 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQ-----NSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLK 234
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE----QISQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 235 EQNQKMSSENEKmgirvdqLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 314
Cdd:TIGR04523 349 KELTNSESENSE-------KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 315 TTAMKKQQELMDENF-------DLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:TIGR04523 422 ELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-367 |
4.09e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN 244
Cdd:COG1196 233 KLRELEAELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 EKM---GIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 321
Cdd:COG1196 309 ERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 386869294 322 QELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 367
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-366 |
6.95e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELckenQELKDSCISLQKQnsdmQAELQKKQEELETLQSinkklelKVKEQKDYWETELLQLKEQNQKMSSEN 244
Cdd:TIGR02168 678 EIEELEEKI----EELEEKIAELEKA----LAELRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 EKMGIRVDQLQAQLSTQEKEMEklvqgdqdktEQLEQLKKENDHLflslTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 324
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIE----------ELEERLEEAEEEL----AEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 386869294 325 MDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
156-368 |
1.18e-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: 54.26 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 156 VVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSIN--KKLELK-VKEQKDYWETELLQ 232
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENqsYKQEIKnLESQINDLESKIQN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 233 LKEQNQKMSsenekmgIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE---- 308
Cdd:TIGR04523 403 QEKLNQQKD-------EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsr 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 309 QMKQNETTAMKKQQELMDENFDLSKrlseneiicnaLQRQKERLEGENDLLKRENSRLLS 368
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKK-----------LNEEKKELEEKVKDLTKKISSLKE 524
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
243-374 |
1.48e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.71 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 243 ENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQ 322
Cdd:COG2433 393 EEPEAEREKEHEERELTEEEEEIRRL-------EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 386869294 323 ELmdenfdlSKRlsENEIicNALQRQKERLEGENDLLKRENSRLLSYMGLDF 374
Cdd:COG2433 466 EI-------SRL--DREI--ERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
194-366 |
2.28e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 194 MQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQ 273
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 274 DKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLE 353
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170
....*....|...
gi 386869294 354 GENDLLKRENSRL 366
Cdd:COG4372 164 EELAALEQELQAL 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-361 |
2.59e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 144 FQFRPENEEDILVVTtqgevEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkeqk 223
Cdd:PRK03918 174 IKRRIERLEKFIKRT-----ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 224 dywetellQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKENDhLFLSLTEQRKDQKKL 303
Cdd:PRK03918 242 --------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL----EEKVKELKELKEKAE-EYIKLSEFYEEYLDE 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294 304 EQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKR 361
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
158-379 |
2.84e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 158 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLE---LKVKEQKDYWETELLQLK 234
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeelESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 235 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 314
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 315 TTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPY 379
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
159-323 |
3.93e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQ----------KDYWE- 227
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 228 -------TELL-------QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL 293
Cdd:COG3883 108 llgsesfSDFLdrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190
....*....|....*....|....*....|.
gi 386869294 294 TEQRKD-QKKLEQTVEQMKQNETTAMKKQQE 323
Cdd:COG3883 188 SAEEAAaEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
149-362 |
4.28e-07 |
|
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: 52.67 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK--EQKDYW 226
Cdd:pfam02463 807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEleEQKLKD 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 227 ETELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKLvqgdqdktEQLEQLKKENDHLFLSLtEQRKDQKKLEQT 306
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEES---QKLNLLEEKENEIEERIKE--------EAEILLKYEEEPEELLL-EEADEKEKEENN 954
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 386869294 307 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
159-360 |
4.40e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 52.77 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQ-HNKELCKENQELKDSCislqKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQ----- 232
Cdd:COG5022 887 LKIDVKSISSlKLVNLELESEIIELKK----SLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNklhev 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 233 ---LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG------DQDKTEQLEQLKKENDHLflslteqrkdqkkl 303
Cdd:COG5022 963 eskLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELskqygaLQESTKQLKELPVEVAEL-------------- 1028
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 386869294 304 eQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 360
Cdd:COG5022 1029 -QSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLY 1084
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
160-368 |
7.42e-07 |
|
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: 51.43 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETellqLKEQNQK 239
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKT----LTQRVLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 240 MSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 319
Cdd:pfam07888 148 RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386869294 320 KQqelmdenfdlskrlSENEIICNALQRQKERL---EGENDLLKRENSRLLS 368
Cdd:pfam07888 228 KE--------------AENEALLEELRSLQERLnasERKVEGLGEELSSMAA 265
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
160-357 |
8.29e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLELKVKEQKDYWETELLQLKEQNQK 239
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA---ELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 240 MSsenekmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 319
Cdd:COG1196 399 AA--------QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 386869294 320 KQQELMDENFDLSKRLSENEIICNALQRQKERLEGEND 357
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
159-352 |
1.02e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkEQKDYWETELLQLKEQNQ 238
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE----RRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 239 KMSSENEKmgirvdqLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 318
Cdd:TIGR02168 849 ELSEDIES-------LAAEIEELEELIEEL-------ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
170 180 190
....*....|....*....|....*....|....
gi 386869294 319 KKQQELMDENFDLSKRLSENEiicNALQRQKERL 352
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLE---VRIDNLQERL 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
151-357 |
1.32e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 151 EEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQnsdmQAELQKKQEELETLQSIN--KKLELKVKEQKDYWET 228
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK----EAEEKKKAEELKKAEEENkiKAAEEAKKAEEDKKKA 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 229 ELLQLKEQNQKMSSENEKmgirvdqlqaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE 308
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALK----------KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386869294 309 QMKQNETTAMKKQQELMDENFDLSKRLSENE-IICNALQRQKERLEGEND 357
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEaVIEEELDEEDEKRRMEVD 1797
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
158-357 |
1.82e-06 |
|
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: 50.56 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 158 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELK-VKEQKDY--WETELLQLK 234
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKnIKLSKDVssLESQLQDTQ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 235 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEqlkkendhlflSLTEQRKD-QKKLEQTVEQMKQN 313
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLS-----------TLQAQLSDmKKKLEEDAGTLEAL 543
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869294 314 ETTAMKKQQELMdenfDLSKRLSENEIICNALQRQKERLEGEND 357
Cdd:pfam01576 544 EEGKKRLQRELE----ALTQQLEEKAAAYDKLEKTKNRLQQELD 583
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-353 |
2.21e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET 228
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 229 ELLQLKEQNQKMSSENEKMG---IRVDQLQAQLSTQEKEMEKLVQgdqdkteQLEQLKKENDHLFLSLTEQRKDQKKLEQ 305
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAAnlrERLESLERRIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELES 873
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 306 TVE-------QMKQNETTAMKKQQELMDENFDLSKRLSENEiicNALQRQKERLE 353
Cdd:TIGR02168 874 ELEallneraSLEEALALLRSELEELSEELRELESKRSELR---RELEELREKLA 925
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
149-375 |
3.29e-06 |
|
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: 49.66 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILVVTTQGEVEEIEQHNKELckenQELKDScisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKD---- 224
Cdd:TIGR00606 722 EKRRDEMLGLAPGRQSIIDLKEKEI----PELRNK---LQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtim 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 225 ---YWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG-------DQDKTEQLEQLKKENDHL---FL 291
Cdd:TIGR00606 795 erfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKielnrklIQDQQEQIQHLKSKTNELkseKL 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 292 SLTEQRKDQKKL-EQTVEQMKQ----NETTAMKKQQELMDENFdLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR00606 875 QIGTNLQRRQQFeEQLVELSTEvqslIREIKDAKEQDSPLETF-LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI 953
|
....*....
gi 386869294 367 LSYMGLDFN 375
Cdd:TIGR00606 954 HGYMKDIEN 962
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
144-370 |
4.00e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 144 FQFRPENEEDILVV--TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDM---QAELQKKQEEletLQSINKKLELK 218
Cdd:COG4372 16 FGLRPKTGILIAALseQLRKALFELDKLQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEE---LEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 219 VKEQKDYwETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRK 298
Cdd:COG4372 93 QAELAQA-QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294 299 DQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYM 370
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
163-314 |
5.76e-06 |
|
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: 47.43 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 163 VEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSS 242
Cdd:pfam17078 68 LKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKL 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294 243 ENEKmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 314
Cdd:pfam17078 148 ENEK---QLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKLDSLAQLLDLPSWLNLYPESR 216
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
131-357 |
5.80e-06 |
|
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: 48.97 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 131 VDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKElcKENQELKDSCISLQ----KQNSDMQAELQKKQEELE 206
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK--RELERIRQEEIAMEisrmRELERLQMERQQKNERVR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 207 TLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSENEKMgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEN 286
Cdd:pfam17380 396 QELEAARKVKILEEER----QRKIQQQKVEMEQIRAEQEEA--RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294 287 DHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLS-ENEIICNALQRQKERLEGEND 357
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEkEMEERQKAIYEEERRREAEEE 541
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
162-368 |
8.73e-06 |
|
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: 48.09 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELEtlqsiNKKLELKVKEQkdywetELLQLKEQNQKMS 241
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE-----QKQKELKSKEK------ELKKLNEEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 242 SENEKMgirvDQLQAQLSTQEKEMEKLVQGDQDKTEQLE-QLKKENDHLFLSLTEQRKDQKklEQTVEQMKQNETTAMKK 320
Cdd:TIGR04523 510 EKVKDL----TKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKKENLEKEIDEK--NKEIEELKQTQKSLKKK 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 321 Q-------QELMDENFDLSKRLSENEIicnalqrQKERLEGENDLLKRENSRLLS 368
Cdd:TIGR04523 584 QeekqeliDQKEKEKKDLIKEIEEKEK-------KISSLEKELEKAKKENEKLSS 631
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
140-353 |
1.00e-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: 48.04 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 140 ASIPFQFRPENEEDILVvttQGEVEEIEQHNKELCKENQELKdscislQKQNSDMQAELQKKQEELETLQSINKKLELKV 219
Cdd:pfam02463 148 AMMKPERRLEIEEEAAG---SRLKRKKKEALKKLIEETENLA------ELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 220 KEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKD 299
Cdd:pfam02463 219 LELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386869294 300 QKKLEQTveqmKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLE 353
Cdd:pfam02463 299 KSELLKL----ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
162-362 |
1.02e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQHNKELCKENQELK-------------DSCISLQKQNSDMQAELQKKQEElETLQSINKKLELKVKEQKDYWET 228
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRkaeeakkaeeariEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 229 ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDhlflsltEQRKdqkkleqtVE 308
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKK--------AE 1705
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386869294 309 QMKQNETTAMKKQQELMDENfdlskrlSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAE-------EENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
153-366 |
1.32e-05 |
|
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: 47.81 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 153 DILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQE-ELETLQSINKKLELKVKEQK----DYWE 227
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElEFEIQSQEQDSEIVKNSKSElariPELE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 228 TELLQLKEQNQKMSSENEKMGI---RVDQLQAQLSTQEKEMEKLVQGDQDKtEQLEQLKKENDHLFLSLTEQRKDQKKLE 304
Cdd:pfam05557 204 KELERLREHNKHLNENIENKLLlkeEVEDLKRKLEREEKYREEAATLELEK-EKLEQELQSWVKLAQDTGLNLRSPEDLS 282
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294 305 QTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-366 |
1.32e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 195 QAELQKKQEELETLQSINKKLELKVKEQK-DYWETELLQLKEqnqkmssENEKMGIRVDQLQAQLSTQEKEMEKL-VQGD 272
Cdd:COG4913 261 AERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRA-------ELARLEAELERLEARLDALREELDELeAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 273 QDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMK-------------QNETTAMK-----KQQELMDENFDLSKR 334
Cdd:COG4913 334 GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefaalRAEAAALLealeeELEALEEALAEAEAA 413
|
170 180 190
....*....|....*....|....*....|..
gi 386869294 335 LSEneiicnaLQRQKERLEGENDLLKRENSRL 366
Cdd:COG4913 414 LRD-------LRRELRELEAEIASLERRKSNI 438
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
164-341 |
1.80e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELL---------QLK 234
Cdd:COG4717 71 KELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeaelaelpeRLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 235 EQNQKMSSENEKMgIRVDQLQAQLSTQEKEMEKLVQGDQDKTE-QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN 313
Cdd:COG4717 150 ELEERLEELRELE-EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|....*...
gi 386869294 314 EttamkKQQELMDENFDLSKRLSENEII 341
Cdd:COG4717 229 L-----EQLENELEAAALEERLKEARLL 251
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
443-465 |
2.03e-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: 41.02 E-value: 2.03e-05
10 20
....*....|....*....|....
gi 386869294 443 CPICDKIFPATEKQ-IFEDHVFCH 465
Cdd:cd21965 1 CPICNKQFPPQVDQeAFEDHVESH 24
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
159-323 |
2.22e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET----LQSINKKLElKVKEQKDYWETELLQLK 234
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdeLKDYREKLE-KLKREINELKRELDRLQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 235 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLK----KENDHLFLSLTEQRKDQKKLEQTVEQM 310
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlsKYEQELYDLKEEYDRVEKELSKLQREL 492
|
170
....*....|...
gi 386869294 311 KQNETTAMKKQQE 323
Cdd:TIGR02169 493 AEAEAQARASEER 505
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
175-347 |
2.65e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 175 KENQELKDSCIS-----LQKQNSDMQAELQKKQEELetlqsinKKLELKVKEQKDYWETELlqlkEQNQKMSSENEKMGI 249
Cdd:PRK12704 49 KEAEAIKKEALLeakeeIHKLRNEFEKELRERRNEL-------QKLEKRLLQKEENLDRKL----ELLEKREEELEKKEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 250 RVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsltEQRKDQkkLEQTVEQMKQnETTAMKKQQElmDENF 329
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEIL--LEKVEEEARH-EAAVLIKEIE--EEAK 183
|
170
....*....|....*...
gi 386869294 330 DLSKRLSeNEIICNALQR 347
Cdd:PRK12704 184 EEADKKA-KEILAQAIQR 200
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
164-368 |
3.11e-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: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELCKENQELK---DSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKdyweTELLQLKEQ---- 236
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISntqTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK----SEISDLNNQkeqd 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 237 -NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNET 315
Cdd:TIGR04523 308 wNKELKSELKNQEKKLEEIQNQISQNNKIISQL-------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 386869294 316 TAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
164-317 |
3.11e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELCKENQELKDSCISLQKQ-----------NSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQ 232
Cdd:COG3883 72 AEIAEAEAEIEERREELGERARALYRSggsvsyldvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 233 LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 312
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*
gi 386869294 313 NETTA 317
Cdd:COG3883 232 AAAAA 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-285 |
3.76e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLEL---------KVKEQKDYWETEL 230
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQAELQRVEEEI 967
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 231 LQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKE 285
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI----LERIEEYEKKKRE 1018
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
155-312 |
3.96e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 155 LVVTTQGEVEEIEQHNKELCKENQELKDscISLQKQNSDMQAELQKKQEELETL---------QSINKKLEL-------- 217
Cdd:PRK04778 224 LQTELPDQLQELKAGYRELVEEGYHLDH--LDIEKEIQDLKEQIDENLALLEELdldeaeeknEEIQERIDQlydilere 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 218 -----KVKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT---- 276
Cdd:PRK04778 302 vkarkYVEKNSDTLPDFLEHAKEQNKELKEEidrvkqsytlNESELESVRQLEKQLESLEKQYDEITEriAEQEIAysel 381
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869294 277 --------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 312
Cdd:PRK04778 382 qeeleeilKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRN 425
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
162-362 |
4.40e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE-----TELLQLKE- 235
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADelkkaEELKKAEEk 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 236 ---QNQKMSSENEKMGIRVDQLQAQLSTQEKEmEKLVQGDQDKTEQLEQLKKENDHLFLSltEQRKDQKKLEQTVEQMKQ 312
Cdd:PTZ00121 1564 kkaEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKK 1640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386869294 313 NETTAMKKQQELMDENfdlskrlSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAE-------EENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
151-368 |
5.66e-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: 45.73 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 151 EEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEE-------LETLQSINKKLELKVKEQK 223
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekekklQEEELKLLAKEEEELKSEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 224 DYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLflsltEQRKDQKKL 303
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL-----EQLEEELLA 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 304 EQTVEQmKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:pfam02463 378 KKKLES-ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
160-312 |
6.01e-05 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 43.06 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQkkqeeletlqsinkKLELKVKEQKdywetellQLKEQNQK 239
Cdd:pfam12718 13 QERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVE--------------KLEEQLKEAK--------EKAEESEK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294 240 MSSENEKMGIRVDQLQAQLSTQEKE----MEKLVQGDQdKTEQLEQLKKendhlflSLTEQR-KDQKKLEQTVEQMKQ 312
Cdd:pfam12718 71 LKTNNENLTRKIQLLEEELEESDKRlketTEKLRETDV-KAEHLERKVQ-------ALEQERdEWEKKYEELEEKYKE 140
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
178-332 |
6.60e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 45.36 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 178 QELKDScisLQKQNSDmqAELQKKQEELEtlQSINKKL-ELKvkEQKDYWETELLQLKEQNQKMssenekmgIRVDQLQA 256
Cdd:pfam13779 496 ERLSEA---LERGASD--EEIAKLMQELR--EALDDYMqALA--EQAQQNPQDLQQPDDPNAQE--------MTQQDLQR 558
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294 257 QLstqeKEMEKLVQ-GDQDKTEQ-LEQLKKENDHLFLSLTEQRKDQKKlEQTVEQMKQNETTaMKKQQELMDENFDLS 332
Cdd:pfam13779 559 ML----DRIEELARsGRRAEAQQmLSQLQQMLENLQAGQPQQQQQQGQ-SEMQQAMDELGDL-LREQQQLLDETFRQL 630
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-353 |
7.05e-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: 45.43 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 158 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK---EQKDYWETELLQLK 234
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEEALALLR 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 235 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVqgdqdktEQLEQLKKENDHLFLSLTEQRKDqkkleqTVEQMKQNE 314
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLE-------LRLEGLEVRIDNLQERLSEEYSL------TLEEAEALE 960
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386869294 315 TTAMKKQQELMDENFDLSKRLSE----NEIICNALQRQKERLE 353
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYD 1003
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-364 |
7.75e-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: 45.43 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 241 SSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKK 320
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 386869294 321 QQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENS 364
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
196-364 |
8.48e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 196 AELQKKQEELETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMgirvdQLQAQLSTQEKEMEKLVQGDQDK 275
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 276 TEQLEQLKKEND---HLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ--------QELMDENFDLSKRLSENEIICNA 344
Cdd:COG4717 145 PERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEAQEELEE 224
|
170 180
....*....|....*....|
gi 386869294 345 LQRQKERLEGENDLLKRENS 364
Cdd:COG4717 225 LEEELEQLENELEAAALEER 244
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
162-339 |
1.00e-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: 45.04 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQHNKELCKENQELKDScisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYW----ETEL----LQL 233
Cdd:TIGR00606 910 QDSPLETFLEKDQQEKEELISS---KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYlkqkETELntvnAQL 986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 234 KEQNQKMSSENEKMGIRVDQLQAQlstqeKEMEKLVQGD------QDKTEQLEQLKKENDHLF--LSLTEQRKDQKKLEQ 305
Cdd:TIGR00606 987 EECEKHQEKINEDMRLMRQDIDTQ-----KIQERWLQDNltlrkrENELKEVEEELKQHLKEMgqMQVLQMKQEHQKLEE 1061
|
170 180 190
....*....|....*....|....*....|....
gi 386869294 306 TVEQMKQNETTAMKKQQELMDENFDLSKRLSENE 339
Cdd:TIGR00606 1062 NIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
145-364 |
1.16e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 145 QFRPENEEDILVVTT------QGEVEEIEQ--HNKELckENQELK------DSCISLQKQNSDMQAELQKKQEELETLQS 210
Cdd:pfam05483 369 QQRLEKNEDQLKIITmelqkkSSELEEMTKfkNNKEV--ELEELKkilaedEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 211 INKK----LELK--------------VKEQKDYWETELLQLKE----------QNQKMSSENEKMGIRVDQLQAQLSTQE 262
Cdd:pfam05483 447 AREKeihdLEIQltaiktseehylkeVEDLKTELEKEKLKNIEltahcdklllENKELTQEASDMTLELKKHQEDIINCK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 263 KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQK-KLEQTVEQMKQNETTAMKKQqelmdenfdlsKRLSENEII 341
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKE-----------KQMKILENK 595
|
250 260 270
....*....|....*....|....*....|
gi 386869294 342 CNALQRQK-------ERLEGENDLLKRENS 364
Cdd:pfam05483 596 CNNLKKQIenknkniEELHQENKALKKKGS 625
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
164-366 |
1.16e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQhnkelcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWEtELLQLKEQnqkmsse 243
Cdd:PRK02224 194 AQIEE------KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-ELETLEAE------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 244 nekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAmkkQQE 323
Cdd:PRK02224 260 -------IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL---RDR 329
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386869294 324 LMDENFDLSKRLSENEiicnALQRQKERLEGENDLLKRENSRL 366
Cdd:PRK02224 330 LEECRVAAQAHNEEAE----SLREDADDLEERAEELREEAAEL 368
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
164-354 |
1.33e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELCKENQELKdsciSLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWET---ELLQLKEQNQKM 240
Cdd:PRK03918 238 EEIEELEKELESLEGSKR----KLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKlseFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 241 SSENEKMGIRVDQLQAQLSTQE------KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLE-QTVEQMKQN 313
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKE 392
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 386869294 314 ETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEG 354
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
218-326 |
1.36e-04 |
|
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: 42.74 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 218 KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQ---AQLSTQEKEMEKLVQGDQDKT-EQLEQLKKENDHLFLSL 293
Cdd:pfam05010 12 KARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEktiAQMIEEKQKQKELEHAEIQKVlEEKDQALADLNSVEKSF 91
|
90 100 110
....*....|....*....|....*....|...
gi 386869294 294 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMD 326
Cdd:pfam05010 92 SDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA 124
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
171-359 |
1.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 171 KELCKENQELKDScislQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDyweteLLQLKEQNQKMSSENEKMGIR 250
Cdd:COG4717 74 KELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 251 VDQLQaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQ-KKLEQTVEQMKQNETTAMKKQQELMDENF 329
Cdd:COG4717 145 PERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190
....*....|....*....|....*....|
gi 386869294 330 DLSKRLSENEIICNALQRQKERLEGENDLL 359
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
190-373 |
1.54e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 190 QNSDMQAELQKKQEELETLQSinkKLELKVKEQKDywetellQLKEQNQKMSSENEkmgiRVDQLQAQLSTQEKEMEKL- 268
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERT---RAREQLRQAQA-------QLAQYNQVLASLKS----SYDAKRQMLQELKQELQDLg 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 269 VQGDQDKTEQLEQLKKENDHLfLSLTEQRKDQKKLEQTVEQMkqnETTAMKKQQELMDENFDLSKRLSENE--IICNALq 346
Cdd:PRK04863 1048 VPADSGAEERARARRDELHAR-LSANRSRRNQLEKQLTFCEA---EMDNLTKKLRKLERDYHEMREQVVNAkaGWCAVL- 1122
|
170 180
....*....|....*....|....*..
gi 386869294 347 rqkeRLEGENDLLKRENSRLLSYMGLD 373
Cdd:PRK04863 1123 ----RLVKDNGVERRLHRRELAYLSAD 1145
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
160-284 |
1.58e-04 |
|
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: 43.54 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEEL-------ETLQSINKkLELKVKEQKDYWETELLQ 232
Cdd:pfam15294 132 HMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQgakkdvkSNLKEISD-LEEKMAALKSDLEKTLNA 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294 233 LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGD----------QDKTEQLEQLKK 284
Cdd:pfam15294 211 STALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTaayrnmkemlTKKNEQIKELRK 272
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
187-386 |
1.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 187 LQKQNSDMQAELQKKQEELETLQSinkklELKVKEQKdywETELLQLKEQNQkmssenekmGIRVDQLQAQLSTQEKEME 266
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEA-----RLDALREE---LDELEAQIRGNG---------GDRLEQLEREIERLERELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 267 KLVQgdqdkteQLEQLKKENDHLFLSLTEQRKD----QKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSE--NEI 340
Cdd:COG4913 356 ERER-------RRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleAEI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 386869294 341 icNALQRQKERLEGENDLLKREnsrLLSYMGLDFNSLPY-----QVPTSDE 386
Cdd:COG4913 429 --ASLERRKSNIPARLLALRDA---LAEALGLDEAELPFvgeliEVRPEEE 474
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-321 |
1.65e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILVVTTQGEVEE-IEQHNKELCKenqeLKDSCISLQKQNSDMQAELQKKQEE-----------LETLQSINKKLE 216
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQlISEHEVEITG----LTEKASSARSQANSIQSQLEIIQEQarnqnsmymrqLSDLESTVSQLR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 217 LKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVqGDQDKTEQLEQLKKEN---------- 286
Cdd:pfam15921 331 SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL-ADLHKREKELSLEKEQnkrlwdrdtg 409
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 386869294 287 -----DHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 321
Cdd:pfam15921 410 nsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQ 449
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
164-355 |
1.89e-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: 44.29 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKEL--CKENQELKDSCISLQKQNSDmqaELQKKQEELETLQSINKKLElkvkeqkDYWETELLqlkeqNQKMS 241
Cdd:TIGR02169 170 RKKEKALEELeeVEENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKR-------EYEGYELL-----KEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 242 SENEKmgirvDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLF-----LSLTEQRKDQKKLEQTVEQMKQNETT 316
Cdd:TIGR02169 235 LERQK-----EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdLGEEEQLRVKEKIGELEAEIASLERS 309
|
170 180 190
....*....|....*....|....*....|....*....
gi 386869294 317 AMKKQQELMdenfDLSKRLSENEIICNALQRQKERLEGE 355
Cdd:TIGR02169 310 IAEKERELE----DAEERLAKLEAEIDKLLAEIEELERE 344
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
165-312 |
2.01e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETELLQlkeqnQKMSSEN 244
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE-STKEMLRKVVEELTA-----KKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 EKMgiRVDQLQAQLSTQEK-------EMEKLVQGDQDKTEQLEQLKKENDHLF----------LSLTEQRKDQKKLEQTV 307
Cdd:pfam15921 494 SER--TVSDLTASLQEKERaieatnaEITKLRSRVDLKLQELQHLKNEGDHLRnvqtecealkLQMAEKDKVIEILRQQI 571
|
....*
gi 386869294 308 EQMKQ 312
Cdd:pfam15921 572 ENMTQ 576
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
187-366 |
2.04e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 187 LQKQNSDMQAELQKKQEELETLQSINKKLELkvKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEME 266
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 267 KLVQGD--QDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNettamkKQQElmdenfdLSKRLSENEIICNA 344
Cdd:COG3206 258 ELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------LQQE-------AQRILASLEAELEA 324
|
170 180
....*....|....*....|..
gi 386869294 345 LQRQKERLEGENDLLKRENSRL 366
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAEL 346
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
155-333 |
2.25e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 155 LVVTTQGEVEEIEQHNKELCK----------ENQELKDSCISLQKQNSDMQA---ELQKKQEELETL-QSINKKLEL--- 217
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKlrsrvdlklqELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILrQQIENMTQLvgq 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 218 ------KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFL 291
Cdd:pfam15921 581 hgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN 660
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386869294 292 SLTEQRKDQKKLEQTVEQMKQN--------ETTAMKKQQELMDENFDLSK 333
Cdd:pfam15921 661 EVKTSRNELNSLSEDYEVLKRNfrnkseemETTTNKLKMQLKSAQSELEQ 710
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
193-312 |
2.72e-04 |
|
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: 43.30 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 193 DMQAELQKKQEELETLQSI-NKKLELK--VKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLS 259
Cdd:pfam06160 260 EAEEALEEIEERIDQLYDLlEKEVDAKkyVEKNLPEIEDYLEHAEEQNKELKEElervqqsytlNENELERVRGLEKQLE 339
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869294 260 TQEKEMEKLVQGDQDKT--------------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 312
Cdd:pfam06160 340 ELEKRYDEIVERLEEKEvayselqeeleeilEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKL 406
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
195-327 |
3.36e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 195 QAELQKKQEELEtLQSINKKLELKVKEqkdywetELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKlvqgdqd 274
Cdd:PRK12704 39 EAKRILEEAKKE-AEAIKKEALLEAKE-------EIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDR------- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 386869294 275 KTEQLEQLKKEndhlflsLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE 327
Cdd:PRK12704 101 KLELLEKREEE-------LEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
147-340 |
3.37e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 147 RPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEEletlQSINKKLELKvKEQKDYW 226
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE----ERKRKKLELE-KEKRDRK 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 227 ETELL-------QLKEQNQKMSSENEKMGIrvdqlqaqlstQEKEME---KLVQGDQDKTEQLEQLKKENDhlflsLTEQ 296
Cdd:pfam17380 488 RAEEQrrkilekELEERKQAMIEEERKRKL-----------LEKEMEerqKAIYEEERRREAEEERRKQQE-----MEER 551
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869294 297 RKDQKKLEQTVEQMKQNEttAMKKQQELMDENFDLSKRLSENEI 340
Cdd:pfam17380 552 RRIQEQMRKATEERSRLE--AMEREREMMRQIVESEKARAEYEA 593
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
159-325 |
3.58e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQN-SDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET--------- 228
Cdd:pfam10174 85 AQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENfRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGArdesikkll 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 229 ELLQLKEQNQKMSSENEKMGIR-------VDQLQAQLSTQEKEMEKL---------VQGDQDKTEQLEQLKKENDHLFLS 292
Cdd:pfam10174 165 EMLQSKGLPKKSGEEDWERTRRiaeaemqLGHLEVLLDQKEKENIHLreelhrrnqLQPDPAKTKALQTVIEMKDTKISS 244
|
170 180 190
....*....|....*....|....*....|...
gi 386869294 293 LTEQRKDqkkLEQTVEQMKQNETTAMKKQQELM 325
Cdd:pfam10174 245 LERNIRD---LEDEVQMLKTNGLLHTEDREEEI 274
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-312 |
3.73e-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: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQhnkELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLEL-------KVKEQkdywETELLQLK 234
Cdd:pfam01576 72 ELEEILH---ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLekvtteaKIKKL----EEDILLLE 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294 235 EQNQKMSSENEKMGIRVDQLQAQLSTQEkemeklvqgdqDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 312
Cdd:pfam01576 145 DQNSKLSKERKLLEERISEFTSNLAEEE-----------EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR 211
|
|
| CCDC14 |
pfam15254 |
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ... |
167-264 |
3.77e-04 |
|
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: 43.25 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 167 EQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLeLKVKE-QKDY----------WETELLQLKE 235
Cdd:pfam15254 412 EQEKTEKTSGSGDCNLELFSLQSLNMSLQNQLQESLKSQELLQSKNEEL-LKVIEnQKEEnkkltkifkeKEQTLLENKQ 490
|
90 100 110
....*....|....*....|....*....|...
gi 386869294 236 Q----NQKMSSENEKMGIRVDQLQAQLSTQEKE 264
Cdd:pfam15254 491 QfdieTTRVKIELEEALVNMKSFQFKLEAAEKE 523
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
159-366 |
3.93e-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: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQHNKELCKENQELKDSC---ISLQKQNSDMQAELQKKQEELEtlqSINKKLELKVKEQkdywetellqlKE 235
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLAARKQELE---EILHELESRLEEE-----------EE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 236 QNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvQGDQDKTEQleQLKKENDHLfLSLTEQR----KDQKKLEQTVEQMK 311
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL-QLEKVTTEA--KIKKLEEDI-LLLEDQNsklsKERKLLEERISEFT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386869294 312 QNET---------TAMKKQQELMDEnfDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:pfam01576 166 SNLAeeeekakslSKLKNKHEAMIS--DLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
162-356 |
4.14e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQHNKELCKENQELKDSCiSLQKQNSDMQAELQKKQE------------------------ELETLQSINKKLEL 217
Cdd:pfam05483 135 KLEEEIQENKDLIKENNATRHLC-NLLKETCARSAEKTKKYEyereetrqvymdlnnniekmilafEELRVQAENARLEM 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 218 KVKEQKDYweTELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKL---VQGDQDKTEQLEQLKKENDHlflSLT 294
Cdd:pfam05483 214 HFKLKEDH--EKIQHLEEEYKKEINDKEK---QVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDE---NLK 285
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294 295 EQRKDQKKLEQTVEQMKQNETTAMKKQQELmDENFDLSKRlseneIICNALQRQKERLEGEN 356
Cdd:pfam05483 286 ELIEKKDHLTKELEDIKMSLQRSMSTQKAL-EEDLQIATK-----TICQLTEEKEAQMEELN 341
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
165-324 |
4.29e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetelLQLKEQNQKMSSEN 244
Cdd:COG1579 18 ELDRLEHRLKELPAELAE----LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA------RIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 EKMgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKD----QKKLEQTVEQMKQNETTAMKK 320
Cdd:COG1579 88 NKE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEELEAE 164
|
....
gi 386869294 321 QQEL 324
Cdd:COG1579 165 REEL 168
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
165-350 |
4.31e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELCKENQELkdsCISLQKQNSDMQAE---LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMS 241
Cdd:TIGR00618 708 ELETHIEEYDREFNEI---ENASSSLGSDLAARedaLNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 242 SENEKMGIRVDQLQAQLSTQEKEM-EKLVQGDQDKTEQLEQLKKENDHLflsLTEQRKDQKKLEQTVEQMKQNETTaMKK 320
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQF---LSRLEEKSATLGEITHQLLKYEEC-SKQ 860
|
170 180 190
....*....|....*....|....*....|
gi 386869294 321 QQELMDENFDLSKRLSENEIIcNALQRQKE 350
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKLNGI-NQIKIQFD 889
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
194-325 |
5.32e-04 |
|
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: 42.37 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 194 MQAELQKKQ--EELETLQSINKKLELKVKEQKDYWETELLQLKEQNQK----MSSENEKMGIRVDQLQAQLstqeKEMEK 267
Cdd:pfam05622 271 LAAEIMPAEirEKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRrkneLETQNRLANQRILELQQQV----EELQK 346
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 386869294 268 LVQGDQDKTEQLEQLKKENDHLFLSLTE-QRKDQKKLEQTVEQMKQNETTAMKKQQELM 325
Cdd:pfam05622 347 ALQEQGSKAEDSSLLKQKLEEHLEKLHEaQSELQKKKEQIEELEPKQDSNLAQKIDELQ 405
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
130-284 |
5.58e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 130 YVDED----GVVRGASI----------------PFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDscislqk 189
Cdd:COG2433 362 DVDRDevkaRVIRGLSIeealeeliekelpeeePEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 190 qnsdmqaELQKKQEELEtlqsinkKLELKVKEQKdywetellqlKEQNQKMSSENE--KMGIRVDQLQAQLSTQEKEMEK 267
Cdd:COG2433 435 -------ELEEKDERIE-------RLERELSEAR----------SEERREIRKDREisRLDREIERLERELEEERERIEE 490
|
170
....*....|....*..
gi 386869294 268 LvqgdQDKTEQLEQLKK 284
Cdd:COG2433 491 L----KRKLERLKELWK 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
178-368 |
5.89e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 178 QELKDSCISLQKQNSDMQAELQKKQEELETLQsinKKLELKvkeqkdywETELLQLKEQNQKMSSENEKMGIRVDQLQAQ 257
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALE---ARLEAA--------KTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 258 LSTQ--EKEMEKLvqgdqdkTEQLEQLKKENDHLflslteqRKDQKKLEQTVEQMKQNETTAMKKQQELMDEnfdLSKRL 335
Cdd:COG1579 82 LGNVrnNKEYEAL-------QKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAE---LEEKK 144
|
170 180 190
....*....|....*....|....*....|....
gi 386869294 336 SENEIICNALQRQKERLEGE-NDLLKRENSRLLS 368
Cdd:COG1579 145 AELDEELAELEAELEELEAErEELAAKIPPELLA 178
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
188-362 |
6.17e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 188 QKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE---------------------TELLQLKEQNQKMSSEN-- 244
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEedknmalrkaeeakkaeeariEEVMKLYEEEKKMKAEEak 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 --EKMGIRVDQLQAQlSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQ 322
Cdd:PTZ00121 1614 kaEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 386869294 323 ELMDENFD------LSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:PTZ00121 1693 ALKKEAEEakkaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
194-361 |
6.40e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 194 MQAELQKKQEELETLQS---INKKLELKVKEQKDYWeTELLQLK-----EQNQKMSSENekmgirvDQLQAQLStqekem 265
Cdd:PRK04863 926 IVSVLQSDPEQFEQLKQdyqQAQQTQRDAKQQAFAL-TEVVQRRahfsyEDAAEMLAKN-------SDLNEKLR------ 991
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 266 EKLVQGDQDKTEQLEQLKK------ENDHLFLSLTE--QRKDQ--KKLEQTVEQMKQNETTAMKKQQELMDEnfDLSKRL 335
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQaqaqlaQYNQVLASLKSsyDAKRQmlQELKQELQDLGVPADSGAEERARARRD--ELHARL 1069
|
170 180
....*....|....*....|....*..
gi 386869294 336 SENEIICNALQRQKERLEGE-NDLLKR 361
Cdd:PRK04863 1070 SANRSRRNQLEKQLTFCEAEmDNLTKK 1096
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-362 |
6.81e-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: 42.47 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLElkvkeqkdywetellqlKEQNQKMSSE 243
Cdd:pfam01576 204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLE-----------------EETAQKNNAL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 244 NekmgiRVDQLQAQLSTQEKEME-------KLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMK---QN 313
Cdd:pfam01576 264 K-----KIRELEAQISELQEDLEseraarnKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkalEE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 314 ETTAMKKQ-QEL----------MDENFDLSKRLSENeiicnaLQRQKERLEGENDLLKRE 362
Cdd:pfam01576 339 ETRSHEAQlQEMrqkhtqaleeLTEQLEQAKRNKAN------LEKAKQALESENAELQAE 392
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
164-311 |
7.46e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELK---VKEQKDY--WETELLQLKEQNQ 238
Cdd:COG1579 31 AELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnVRNNKEYeaLQKEIESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386869294 239 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDhlfLSLTEQRKDQKKLEQTVEQMK 311
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAEL-------EAELEEKKAELD---EELAELEAELEELEAEREELA 169
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
164-376 |
8.19e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQsinKKLElKVKEQKDYWETELLQLKEQNQKMSSE 243
Cdd:pfam10174 355 EEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ---KKIE-NLQEQLRDKDKQLAGLKERVKSLQTD 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 244 NEKMGIRVDQLQAQLSTQEKEMEKLVQ----GDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT--- 316
Cdd:pfam10174 431 SSNTDTALTTLEEALSEKERIIERLKEqrerEDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlas 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869294 317 -AMKKQQELMDENFDLSKRLSEneiiCNALQRQkerlegendLLKRENSRLLSYMGLDFNS 376
Cdd:pfam10174 511 sGLKKDSKLKSLEIAVEQKKEE----CSKLENQ---------LKKAHNAEEAVRTNPEIND 558
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
152-366 |
9.39e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 152 EDILVVTTQGEVEEIeqhNKELCKE-NQELKDscISLQKQNSDMQAELQKK-QEELETLQSIN-KKLELKVkeqkdyweT 228
Cdd:PHA02562 157 EDLLDISVLSEMDKL---NKDKIRElNQQIQT--LDMKIDHIQQQIKTYNKnIEEQRKKNGENiARKQNKY--------D 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 229 ELLQlKEQNQKMSsenekmgirVDQLQAQLSTQEKEME-------KLVQGDQDKTEQLEQLKKEndHLFL-------SLT 294
Cdd:PHA02562 224 ELVE-EAKTIKAE---------IEELTDELLNLVMDIEdpsaalnKLNTAAAKIKSKIEQFQKV--IKMYekggvcpTCT 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386869294 295 EQRKDQ-KKLEQTVEQMKQNET------TAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:PHA02562 292 QQISEGpDRITKIKDKLKELQHslekldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
198-362 |
1.03e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 198 LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN---EKMGI--RVDQLQAQLSTQEKEMEKLvqgD 272
Cdd:PRK04778 200 LDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGyhlDHLDIekEIQDLKEQIDENLALLEEL---D 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 273 QDKTE-QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE--NFDLSKRLSENEI-ICNALQRQ 348
Cdd:PRK04778 277 LDEAEeKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEidRVKQSYTLNESELeSVRQLEKQ 356
|
170
....*....|....
gi 386869294 349 KERLEGENDLLKRE 362
Cdd:PRK04778 357 LESLEKQYDEITER 370
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
189-350 |
1.16e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 189 KQNSDMQAELQKKQEELET---LQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKmgirVDQLQAQLSTQEKEM 265
Cdd:PRK12705 39 LQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK----LDNLENQLEEREKAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 266 EklvqgdqDKTEQLEQLKKENDHLFLSLTEQRKDQ------KKLEQTVEQMKQNETTAMKkqqelmdENFDLSKRLSENE 339
Cdd:PRK12705 115 S-------ARELELEELEKQLDNELYRVAGLTPEQarklllKLLDAELEEEKAQRVKKIE-------EEADLEAERKAQN 180
|
170
....*....|.
gi 386869294 340 IICNALQRQKE 350
Cdd:PRK12705 181 ILAQAMQRIAS 191
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
163-362 |
1.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 163 VEEIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETELLQLkeqnqKMSS 242
Cdd:PRK03918 517 LEELEKKAEEY----EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD-ELEEELAELLKELEEL-----GFES 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 243 ENEkmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHL---FLSLTEQRKDQKKLEQTVEQMKQNETTamK 319
Cdd:PRK03918 587 VEE-----LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELdkaFEELAETEKRLEELRKELEELEKKYSE--E 659
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386869294 320 KQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| FtsL2 |
COG4839 |
Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning]; |
184-225 |
1.49e-03 |
|
Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443867 Cd Length: 123 Bit Score: 38.40 E-value: 1.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 386869294 184 CISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDY 225
Cdd:COG4839 57 LLSLQASIYELNREIQSLESKISEQQKENEDLEQEVSELSSP 98
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
163-366 |
1.52e-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: 41.19 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 163 VEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKE----------QKDYWETELLQ 232
Cdd:TIGR00606 669 ITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglapgrqsIIDLKEKEIPE 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 233 LKEQNQKMSSENEKMGIRVDQLQAQLST--QEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQrKDQKKLEQTVEQM 310
Cdd:TIGR00606 749 LRNKLQKVNRDIQRLKNDIEEQETLLGTimPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK-LQGSDLDRTVQQV 827
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 386869294 311 KQnettamkKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR00606 828 NQ-------EKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
158-258 |
1.52e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.82 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 158 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkeqkdywetELLQLKEqn 237
Cdd:pfam10473 49 NSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESLNSSLE------------NLLEEKE-- 114
|
90 100
....*....|....*....|.
gi 386869294 238 QKMSSENEKMGIRVDQLQAQL 258
Cdd:pfam10473 115 QEKVQMKEESKTAVEMLQTQL 135
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-324 |
1.68e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 186 SLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywETELLQLKEQNQKMSSENEKMGIR-------VDQLQAQL 258
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQI 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869294 259 STQEKEMEKLVQGDQDKTE--------QLEQLKKENDHL---FLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 324
Cdd:COG3206 301 AALRAQLQQEAQRILASLEaelealqaREASLQAQLAQLearLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
198-360 |
1.68e-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: 40.61 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 198 LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN---EKMGI--RVDQLQAQLstqEKEMEKLVQGD 272
Cdd:pfam06160 181 LEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGyalEHLNVdkEIQQLEEQL---EENLALLENLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 273 QDKTEQ-LEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE--NFDLSKRLSENEI-ICNALQRQ 348
Cdd:pfam06160 258 LDEAEEaLEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEEleRVQQSYTLNENELeRVRGLEKQ 337
|
170
....*....|..
gi 386869294 349 KERLEGENDLLK 360
Cdd:pfam06160 338 LEELEKRYDEIV 349
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
158-341 |
1.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 158 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQ- 236
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQa 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 237 --NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 314
Cdd:COG4372 185 ldELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
170 180
....*....|....*....|....*..
gi 386869294 315 TTAMKKQQELMDENFDLSKRLSENEII 341
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEA 291
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
163-366 |
1.78e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 163 VEEIEQHNKELCKENQELKDSCIslqkqnsdmQAELQKKQEELET--LQSINKK-------LELKVKEQKDYWET--ELL 231
Cdd:pfam02841 102 VELLEAKKDDFLKQNEEASSKYC---------SALLQDLSEPLEEkiSQGTFSKpggyklfLEERDKLEAKYNQVprKGV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 232 QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKlvqgDQDKTEQLEQLKKEndhlflslteQRKDQKKLEQTVEQMK 311
Cdd:pfam02841 173 KAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEA----ERAKAEAAEAEQEL----------LREKQKEEEQMMEAQE 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 312 QNETTAMKKQQELMDEnfDLSKRLSENE-IICNALQRQKERL-EG---ENDLLKRENSRL 366
Cdd:pfam02841 239 RSYQEHVKQLIEKMEA--EREQLLAEQErMLEHKLQEQEELLkEGfktEAESLQKEIQDL 296
|
|
| Mod_r |
pfam07200 |
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ... |
157-285 |
1.88e-03 |
|
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region approximately 150 residues long within a number of eukaryotic proteins that show homology with Drosophila melanogaster Modifier of rudimentary (Mod(r)) proteins. The N-terminal half of Mod(r) proteins is acidic, whereas the C-terminal half is basic, and both of these regions are represented in this family. Members of this family include the Vps37 subunit of the endosomal sorting complex ESCRT-I, a complex involved in recruiting transport machinery for protein sorting at the multivesicular body (MVB). The yeast ESCRT-I complex consists of three proteins (Vps23, Vps28 and Vps37). The mammalian homolog of Vps37 interacts with Tsg101 (Pfam: PF05743) through its mod(r) domain and its function is essential for lysosomal sorting of EGF receptors.
Pssm-ID: 462117 [Multi-domain] Cd Length: 146 Bit Score: 38.75 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 157 VTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkklelkvkeqkdYWETELLQLKEQ 236
Cdd:pfam07200 22 VHSLPQVKALQAEKEELLAENESLAEENLSLEPELEELRSQLQELLEELKALKS--------------EYEEKEQELDEL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 386869294 237 NQKMSSENEKMgirvdQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKE 285
Cdd:pfam07200 88 LSKFSPDALLA-----RLQAAAAEAEEESEALAESFLEGEIDLDEFLKQ 131
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
150-365 |
2.23e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 150 NEEDILVV----TTQGEVEEIEQHNKELckenqelkdscISLQKQNSDMQAELQKKQEELETLQSINK--------KLEL 217
Cdd:PRK11281 55 EAEDKLVQqdleQTLALLDKIDRQKEET-----------EQLKQQLAQAPAKLRQAQAELEALKDDNDeetretlsTLSL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 218 KVKEQKdyWETELLQLK--------------------EQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKLVqgdqdkTE 277
Cdd:PRK11281 124 RQLESR--LAQTLDQLQnaqndlaeynsqlvslqtqpERAQAALYANSQ---RLQQIRNLLKGGKVGGKALR------PS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 278 QLEQLKKENDHLFLSLTEQRKDqkkLE-----QTVEQMKQNETTAmkKQQELMDENFDL-----SKRLSENEIICNALQR 347
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQRKS---LEgntqlQDLLQKQRDYLTA--RIQRLEHQLQLLqeainSKRLTLSEKTVQEAQS 267
|
250
....*....|....*....
gi 386869294 348 QKERLE-GENDLLKRENSR 365
Cdd:PRK11281 268 QDEAARiQANPLVAQELEI 286
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
220-366 |
2.40e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 220 KEQKDYWETELLQLKEQNQKMSSENE------KMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL 293
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386869294 294 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSK---RLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtLLAAIADAEDEIERLREKREALAELNDERRERL 629
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
162-365 |
2.64e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE-----TELLQLKEQ 236
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakkkAEEKKKADE 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 237 NQKMSSENEKMGIRVDQLQAQLSTQE---KEMEKLVQGDQDKTEQLEqlKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN 313
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADeakKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386869294 314 EttaMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 365
Cdd:PTZ00121 1474 E---AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
205-309 |
2.81e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 39.14 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 205 LETLQSINKkLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKK 284
Cdd:pfam11932 19 LDLAEKAVA-AAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASL----ERQIEEIERTER 93
|
90 100
....*....|....*....|....*
gi 386869294 285 ENDHLFLSLTEQrkdqkkLEQTVEQ 309
Cdd:pfam11932 94 ELVPLMLKMLDR------LEQFVAL 112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
227-364 |
2.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 227 ETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHL----------------- 289
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeaeieerreelgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 290 ----------------------FLS---------------LTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLS 332
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdFLDrlsalskiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190
....*....|....*....|....*....|..
gi 386869294 333 KRLSENEIICNALQRQKERLEGENDLLKRENS 364
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
165-326 |
3.19e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELCKEN----QELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKlELKVKEQKDYWETELLQLKEQNQ-- 238
Cdd:pfam05483 489 ELTAHCDKLLLENkeltQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK-EMNLRDELESVREEFIQKGDEVKck 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 239 -KMSSENEK-MGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT 316
Cdd:pfam05483 568 lDKSEENARsIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
170
....*....|
gi 386869294 317 AMKKQQELMD 326
Cdd:pfam05483 648 AKQKFEEIID 657
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
166-353 |
3.37e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 166 IEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKlelkvkeqkdywetELLQLKEQNQKMSSENE 245
Cdd:pfam13851 3 MKNHEKAF----NEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEK--------------LMSEIQQENKRLTEPLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 246 KMGIRVDQLQAQLSTQEK---EMEKLVQGDQDKTEQLEQLKKENDHLFLSLT--EQRKDQ--KKLEQTVEQMKQ---NET 315
Cdd:pfam13851 65 KAQEEVEELRKQLENYEKdkqSLKNLKARLKVLEKELKDLKWEHEVLEQRFEkvERERDElyDKFEAAIQDVQQktgLKN 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386869294 316 TAMKKQQELMDENFD-----LSKRLSENEIICNALQRQKERLE 353
Cdd:pfam13851 145 LLLEKKLQALGETLEkkeaqLNEVLAAANLDPDALQAVTEKLE 187
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
145-368 |
3.78e-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: 39.95 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 145 QFRPENEEDILVvTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKD 224
Cdd:pfam02463 257 KQEIEKEEEKLA-QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 225 YWETELLQLKEQNQKMSSENEKM---------------------GIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLK 283
Cdd:pfam02463 336 EIEELEKELKELEIKREAEEEEEeeleklqekleqleeellakkKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 284 KENDHL-------FLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGEN 356
Cdd:pfam02463 416 QLEDLLkeekkeeLEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
250
....*....|..
gi 386869294 357 DLLKRENSRLLS 368
Cdd:pfam02463 496 EERSQKESKARS 507
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-363 |
4.03e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQA----ELQKKQEELEtlqsinKKLELKVKEQKDYwETELLQLKEQN 237
Cdd:pfam01576 693 QVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAqferDLQARDEQGE------EKRRQLVKQVREL-EAELEDERKQR 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 238 QKMSSENEKMGIRVDQLQAQLSTQE-------KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQM 310
Cdd:pfam01576 766 AQAVAAKKKLELDLKELEAQIDAANkgreeavKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQL 845
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 386869294 311 KQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKREN 363
Cdd:pfam01576 846 QEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEEL 898
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
149-341 |
4.05e-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: 39.95 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELEtlqsINKKLELKVKEQKDYWET 228
Cdd:pfam02463 341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE----LKSEEEKEAQLLLELARQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 229 ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlfLSLTEQRKDQKKLEQTVE 308
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL-----LKETQLVKLQEQLELLLS 491
|
170 180 190
....*....|....*....|....*....|....
gi 386869294 309 QMKQNETTAM-KKQQELMDENFDLSKRLSENEII 341
Cdd:pfam02463 492 RQKLEERSQKeSKARSGLKVLLALIKDGVGGRII 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-368 |
4.07e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILVVTTQgEVEEIEQHNKELCKENQELKDSCISLQKQNSDmQAELQKKQEELETLQSINKKLEL----------- 217
Cdd:PRK03918 448 EHRKELLEEYTA-ELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKynleelekkae 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 218 ---KVKEQKDYWETELLQLKEQNQK---MSSENEKMGIRVDQLQAQLSTQEKEMEKL----VQGDQDKTEQLEQLKKEnd 287
Cdd:PRK03918 526 eyeKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPFYNE-- 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 288 hlFLSLteqRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFD---LSKRLSENEIICNalQRQKERLEGENDLLKRENS 364
Cdd:PRK03918 604 --YLEL---KDAEKELEREEKELKKLEEELDKAFEELAETEKRleeLRKELEELEKKYS--EEEYEELREEYLELSRELA 676
|
....
gi 386869294 365 RLLS 368
Cdd:PRK03918 677 GLRA 680
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
189-333 |
4.17e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 189 KQNSDMQA---ELQKKQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQ---KMSSENEKMGIRVDQLQAQLSTQE 262
Cdd:pfam01576 2 RQEEEMQAkeeELQKVKERQQKAESELKELEKKHQQLCE----EKNALQEQLQaetELCAEAEEMRARLAARKQELEEIL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 263 KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQE----LMDENFDLSK 333
Cdd:pfam01576 78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdillLEDQNSKLSK 152
|
|
| CENP-K |
pfam11802 |
Centromere-associated protein K; CENP-K is one of seven new CENP-A-nucleosome distal (CAD) ... |
160-315 |
5.07e-03 |
|
Centromere-associated protein K; CENP-K is one of seven new CENP-A-nucleosome distal (CAD) centromere components (the others being CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S) that are identified as assembling on the CENP-A nucleosome associated complex, NAC. The CENP-A NAC is essential, as disruption of the complex causes errors of chromosome alignment and segregation that preclude cell survival despite continued centromere-derived mitotic checkpoint signalling. CENP-K is centromere-associated through its interaction with one or more components of the CENP-A NAC.
Pssm-ID: 463355 [Multi-domain] Cd Length: 263 Bit Score: 38.51 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQElkdSCISLQKQnsdmqaELQKKQEELETLQSInkkLELKVKEQKDYWETELLQLKEQNQK 239
Cdd:pfam11802 59 TAELEQWQKRTPEIISLNPE---VLLTLGKE------ELQKLRHQLEMVLST---IQSKNKKLKEDLEREQQWLDEQQQI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 240 MSSENEKMGIRVDQlQAQLSTQEK--EMEKLVQGDQDKTEQLEQLKKE--NDHLFLSLTEQRKDQKKLEQTVEQMKQNET 315
Cdd:pfam11802 127 LESLNEKHKELKNQ-VVTFSEKRKfqELKTKIRKIKEYKEKLLTTLGEflDEHFPLPEENGNSVKKKRKNSQEPTINLIT 205
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
193-357 |
5.18e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 38.27 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 193 DMQAELQKKQEELETLQSINKKLELKVKEQKDY---WETELLQLKEQN----------QKMSSENEkmgirVDQLQAQLS 259
Cdd:COG1842 34 DMEEDLVEARQALAQVIANQKRLERQLEELEAEaekWEEKARLALEKGredlarealeRKAELEAQ-----AEALEAQLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 260 TQEKEMEKLVQGDQDKTEQLEQLKKENDhLFLSLTEQRKDQKKLEQTVEQMKQNETTA----MKKQQELMDENFDLSKRL 335
Cdd:COG1842 109 QLEEQVEKLKEALRQLESKLEELKAKKD-TLKARAKAAKAQEKVNEALSGIDSDDATSalerMEEKIEEMEARAEAAAEL 187
|
170 180
....*....|....*....|..
gi 386869294 336 SENeiicNALQRQKERLEGEND 357
Cdd:COG1842 188 AAG----DSLDDELAELEADSE 205
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
155-368 |
5.18e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 155 LVVTTQGEVEEIEQHN--KELCKENQELK---DSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEqkdywETE 229
Cdd:PRK04863 481 LVRKIAGEVSRSEAWDvaRELLRRLREQRhlaEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-----EDE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 230 LLQLKEQnqkmssenekmgirvdqLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQ 309
Cdd:PRK04863 556 LEQLQEE-----------------LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQ 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 386869294 310 MKQNETTAmkkqQELMdenfDLSKRLSENEiicNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:PRK04863 619 SGEEFEDS----QDVT----EYMQQLLERE---RELTVERDELAARKQALDEEIERLSQ 666
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
255-391 |
5.35e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 255 QAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsLTEQRKD----QKKLEQTVEQMKQNETTAMKKQQELMDENFD 330
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKE-------LRERRNElqklEKRLLQKEENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869294 331 LSKRLSEneiicnaLQRQKERLEgenDLLKRENSRLLSYMGLdfnslpyqvpTSDEggARQ 391
Cdd:PRK12704 119 LEQKQQE-------LEKKEEELE---ELIEEQLQELERISGL----------TAEE--AKE 157
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
149-243 |
6.06e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 38.56 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILVVttQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET 228
Cdd:COG4026 132 ELREELLEL--KEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLL 209
|
90
....*....|....*
gi 386869294 229 ELLQLKEQNQKMSSE 243
Cdd:COG4026 210 EVFSLEELWKELFPE 224
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
185-348 |
6.29e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 185 ISLQKQNSDMQAELQKKQEELetlQSINKKL-------ELKVKEQKDYWETELLQLKEQN--QKMSSENEkmgirvDQLQ 255
Cdd:PRK11281 152 VSLQTQPERAQAALYANSQRL---QQIRNLLkggkvggKALRPSQRVLLQAEQALLNAQNdlQRKSLEGN------TQLQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 256 AQLSTQEKEMeklvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKklEQTVEQMKQNETTAMKK-----QQELmDENFD 330
Cdd:PRK11281 223 DLLQKQRDYL----------TARIQRLEHQLQLLQEAINSKRLTLS--EKTVQEAQSQDEAARIQanplvAQEL-EINLQ 289
|
170
....*....|....*...
gi 386869294 331 LSKRLSENEIICNALQRQ 348
Cdd:PRK11281 290 LSQRLLKATEKLNTLTQQ 307
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
150-366 |
6.58e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.35 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 150 NEEDILVVTTQGEVEEIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETE 229
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKE----LKEERDELNEKLNELREELDELRKELAELN-KAGGSIDKLRKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 230 LLQL--KEQNQKMSSENEKMGI-RVDQLQAQLSTQEKEMEKLVQGDQDKTEqLEQLKKENDHLFLSLTEQRKDQKKLEQT 306
Cdd:COG1340 118 IERLewRQQTEVLSPEEEKELVeKIKELEKELEKAKKALEKNEKLKELRAE-LKELRKEAEEIHKKIKELAEEAQELHEE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294 307 VEQMKQNETTAMKKQQELMDENFDLSKRLSE--NEIIcnALQRQKERLEGENDLLKRENSRL 366
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADElhEEII--ELQKELRELRKELKKLRKKQRAL 256
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
171-353 |
6.87e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 171 KELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLqsinkklelkvKEQKDYWETELLQLKEQNQKMSSENEKMGIR 250
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL-----------RERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 251 VDQLQAQLSTQEKEMEKL--VQGDQDK-----------TEQLEQLKKENDHLFLSLTEQRKDQKKLEQT-----VEQMKQ 312
Cdd:PRK02224 574 VAELNSKLAELKERIESLerIRTLLAAiadaedeierlREKREALAELNDERRERLAEKRERKRELEAEfdearIEEARE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386869294 313 NETTAMK-------KQQELMDENFDLSKRLS--ENEIicNALQRQKERLE 353
Cdd:PRK02224 654 DKERAEEyleqveeKLDELREERDDLQAEIGavENEL--EELEELRERRE 701
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
95-302 |
7.36e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.76 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 95 WVTLPIDLnnKSAKQQE-VQFKAYYLPKDdeyyqfcYVDEDGVVRGASIPFQFRPENEEDILVVTTqgEVEEIEQHNKEL 173
Cdd:PRK05771 129 WGNFDLDL--SLLLGFKyVSVFVGTVPED-------KLEELKLESDVENVEYISTDKGYVYVVVVV--LKELSDEVEEEL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 174 CK---ENQELKDSCISLQkqnsdmqaELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEqnqKMSSENEKmgir 250
Cdd:PRK05771 198 KKlgfERLELEEEGTPSE--------LIREIKEELEEIEKERESLLEELKELAKKYLEELLALYE---YLEIELER---- 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294 251 vdqlqAQLSTQEKEMEKL--VQG--DQDKTEQLEQL--KKENDHLFLSLTEQRKDQKK 302
Cdd:PRK05771 263 -----AEALSKFLKTDKTfaIEGwvPEDRVKKLKELidKATGGSAYVEFVEPDEEEEE 315
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
149-366 |
7.51e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.03 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILVVTTQGEVEeIEQHNKELcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLELKVKEQKDYWE- 227
Cdd:pfam10174 251 DLEDEVQMLKTNGLLH-TEDREEEI-KQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQT---KLETLTNQNSDCKQh 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 228 ----TELLQLKEQNQK-MSSEnekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL-TEQRKD-- 299
Cdd:pfam10174 326 ievlKESLTAKEQRAAiLQTE-------VDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLdVKERKInv 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 300 -QKKLEQTVEQMKQNETTAMKKQQELMDENFD----------LSKRLSENEIICNALQRQKERLE----GENDLLKRENS 364
Cdd:pfam10174 399 lQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttLEEALSEKERIIERLKEQREREDrerlEELESLKKENK 478
|
..
gi 386869294 365 RL 366
Cdd:pfam10174 479 DL 480
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
443-465 |
7.58e-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: 7.58e-03
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
160-310 |
7.59e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQK 239
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869294 240 MSSENEKMGIRVDQLQAQLSTQEKEMEKL--VqgDQDKTEQLEQLKKENDHlflsLTEQRKD----QKKLEQTVEQM 310
Cdd:COG1196 751 EALEELPEPPDLEELERELERLEREIEALgpV--NLLAIEEYEELEERYDF----LSEQREDleeaRETLEEAIEEI 821
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
188-355 |
7.71e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 38.96 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 188 QKQNSDMQAELQKKQEELETLQSINKKLELKVKEQ------KDYWETE-------LLQLKEQNQKMSSENEKMGIRVDQL 254
Cdd:pfam07111 196 QKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQvppevhSQTWELErqelldtMQHLQEDRADLQATVELLQVRVQSL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 255 QAQLSTQEKEMEKLVQG----DQDKTEQLEQLKKENDHLFLSLTEQRKDQkKLEQTvEQMKQNETTAMKKQQELMDENfd 330
Cdd:pfam07111 276 THMLALQEEELTRKIQPsdslEPEFPKKCRSLLNRWREKVFALMVQLKAQ-DLEHR-DSVKQLRGQVAELQEQVTSQS-- 351
|
170 180
....*....|....*....|....*
gi 386869294 331 lskrlSENEIICNALQRQKERLEGE 355
Cdd:pfam07111 352 -----QEQAILQRALQDKAAEVEVE 371
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
163-366 |
7.72e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 38.33 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 163 VEEIEQHNKELCKENQElkdscISLQKqnsdMQAELQKKQEELEtlQSINKKLELKVKEQKDYwetellqLKEQNQKMSS 242
Cdd:cd16269 96 MEQLEEKKEEFCKQNEE-----ASSKR----CQALLQELSAPLE--EKISQGSYSVPGGYQLY-------LEDREKLVEK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 243 ENEKM--GIRVDQ-LQAQLSTQEKEMEKLVQGDQDKTE---QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT 316
Cdd:cd16269 158 YRQVPrkGVKAEEvLQEFLQSKEAEAEAILQADQALTEkekEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEE 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 317 AMKKQQELMDEnfDLSKRLSENEIICNALQRQKERL-----EGENDLLKRENSRL 366
Cdd:cd16269 238 HLRQLKEKMEE--ERENLLKEQERALESKLKEQEALleegfKEQAELLQEEIRSL 290
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
163-310 |
7.80e-03 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 38.39 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 163 VEEIEQHNKELCKEnqeLKDSCISLQKqnsdMQAELQKKQEELETL-QSINKKLElkvkeqkdyweTELLQLKEQNQKMS 241
Cdd:pfam10498 224 LEQMKQHKKSIEES---LPDTKSQLDK----LHTDISKTLEKIESReKYINSQLE-----------PLIQEYREAQDELS 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 242 SENEKMgirvDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLT------EQRKDQKKLEQTVEQM 310
Cdd:pfam10498 286 EVQEKY----KQLSEGVTERTRELAEI-------TEELEKVKQEMEERGSSMTdgsplvKIKQALTKLKEEIKQM 349
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
165-358 |
8.06e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.05 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN 244
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 -----EKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKeNDHLFLSLTEQR-----KDQKKLEQTVEQMKQNE 314
Cdd:pfam12128 713 rtekqAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYK-RDLASLGVDPDViaklkREIRTLERKIERIAVRR 791
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386869294 315 TTAMK----KQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDL 358
Cdd:pfam12128 792 QEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKL 839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
108-326 |
8.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 108 KQQEVQFKAYYLPKDDEYYQFCYVDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHN-KELCKENQELKDSCIS 186
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEA 1693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 187 LQKQnsdmqAELQKKQEELETLQS--INKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKE 264
Cdd:PTZ00121 1694 LKKE-----AEEAKKAEELKKKEAeeKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294 265 MEKLVQGDQDKTEQlEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMD 326
Cdd:PTZ00121 1769 KAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMED 1829
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
166-304 |
9.65e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 38.65 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 166 IEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENE 245
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAK 583
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 386869294 246 KmgiRVDQLQAQLSTQEKeMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLE 304
Cdd:PRK00409 584 K---EADEIIKELRQLQK-GGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
172-289 |
9.73e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 37.22 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 172 ELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSENekmgirv 251
Cdd:pfam08614 68 ELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDR----EEELREKRKLNQDLQDEL------- 136
|
90 100 110
....*....|....*....|....*....|....*...
gi 386869294 252 DQLQAQLSTQEkemeklvqgdqdktEQLEQLKKENDHL 289
Cdd:pfam08614 137 VALQLQLNMAE--------------EKLRKLEKENREL 160
|
|
| |
