|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
23-149 |
1.39e-40 |
|
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: 140.84 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 23 VIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRafkcfqdkleqellkwrsqgqklqVGWKTTREYYTFMWVtlP 102
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFK------------------------VGWKSVNDYVTYVWA--K 54
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 386869290 103 IDLNNKSAKQQEVQFKAYYLPKDD-EYYQFCYVDEDGVVRGASIPFQF 149
Cdd:pfam17751 55 DDEVEGSNSVRQVLFKASYLPKEPeGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-365 |
3.66e-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: 67.48 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 162 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQ 241
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE----ELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 242 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 321
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869290 322 KKQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRE 365
Cdd:COG4942 195 AERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
168-371 |
2.13e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 168 EIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSEN 247
Cdd:TIGR02168 233 RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL----QKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 248 EKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 327
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869290 328 MDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 371
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-370 |
1.86e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQK 242
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 243 MSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 322
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386869290 323 KQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 370
Cdd:COG1196 408 AEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
444-470 |
2.67e-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: 52.06 E-value: 2.67e-09
10 20
....*....|....*....|....*..
gi 386869290 444 FNCPICDKIFPATEKQIFEDHVFCHSL 470
Cdd:cd21968 1 FECPICSKIFEATSKQEFEDHVFCHSL 27
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
168-415 |
3.11e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 168 EIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetellQLKEQNQKMSSEN 247
Cdd:COG3883 17 QIQAKQKEL----SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA-------EIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 248 EKMGIRVDQLQ------------------AQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQT 309
Cdd:COG3883 86 EELGERARALYrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 310 VEQMKQNETTAMKKQQELMDenfdlskRLSENEiicNALQRQKERLEGENDLLKRENSRLLSYmGLDFNSLPYQVPTSDE 389
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLA-------QLSAEE---AAAEAQLAELEAELAAAEAAAAAAAAA-AAAAAAAAAAAAAAAA 234
|
250 260
....*....|....*....|....*.
gi 386869290 390 GGARQNPGLAYGNPYSGIQESSSPSP 415
Cdd:COG3883 235 AAAAAAAAAASAAGAGAAGAAGAAAG 260
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-370 |
4.85e-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: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQhnKELCKENQELKDSCISLQKQNSDMQAELQKKQEELE----TLQSINKKLELKVKEQKDYWETELLQLKE 238
Cdd:TIGR02169 217 LKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISelekRLEEIEQLLEELNKKIKDLGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 239 QNQKMSSEnekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEqtvEQMKQNET 318
Cdd:TIGR02169 295 KIGELEAE-------IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKE 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386869290 319 TAMKKQQELMDEnfdlSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 370
Cdd:TIGR02169 365 ELEDLRAELEEV----DKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-371 |
5.04e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 165 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMS 244
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 245 SENEkmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 324
Cdd:COG1196 376 EAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 386869290 325 QELMDENFDLSKRLSENEiicNALQRQKERLEGENDLLKRENSRLLS 371
Cdd:COG1196 452 AELEEEEEALLELLAELL---EEAALLEAALAELLEELAEAAARLLL 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
157-369 |
8.98e-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: 57.08 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 157 ILVVTTQGEVEEIEQHNKELckenqelkdscISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQL 236
Cdd:COG4942 10 LLALAAAAQADAAAEAEAEL-----------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL----ARRIRAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 237 KEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLV-----QGDQDKTE-------------QLEQLKKENDHLFLSLTE 298
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrLGRQPPLAlllspedfldavrRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869290 299 QRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 369
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-369 |
1.14e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 198 QAELQKKQEELETLQSINKKLElkvkEQKDYWETELLQLkeQNQKMSSENEkmgIRVDQLQAQLSTQEKEMEKLVQGDQD 277
Cdd:COG4913 616 EAELAELEEELAEAEERLEALE----AELDALQERREAL--QRLAEYSWDE---IDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 278 ---KTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE-----NFDLSKRLsENEIICNALQ 349
Cdd:COG4913 687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEERF-AAALGDAVER 765
|
170 180
....*....|....*....|
gi 386869290 350 RQKERLEGENDLLKRENSRL 369
Cdd:COG4913 766 ELRENLEERIDALRARLNRA 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
152-369 |
1.62e-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: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 152 ENEEDILvvttQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET----LQSINKKLELKVKEQKD 227
Cdd:TIGR02169 687 KRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 228 YwETELLQLKEQNQKMSSENEKM-----GIRVDQLQAQLSTQEKE----------MEKLVQGDQDKTEQLEQLKKENDHL 292
Cdd:TIGR02169 763 L-EARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEvsriearlreIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 293 FLSLTEQRKDQKK----LEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 368
Cdd:TIGR02169 842 RIDLKEQIKSIEKeienLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
.
gi 386869290 369 L 369
Cdd:TIGR02169 922 L 922
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-369 |
1.65e-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: 57.37 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETL----QSINKKLELKVKEQKDYwETELLQLKE 238
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkQILRERLANLERQLEEL-EAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 239 QNQKMSSENEKMGIRVDQLQ-------AQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE 311
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386869290 312 QMKQNettamkkQQELMDENFDLSKRLSENEIicNALQRQKERLEGENDLLKRENSRL 369
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 ... |
165-340 |
2.17e-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: 56.57 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 165 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKvkEQKDYWETELLQLKEQNQKMS 244
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE--KEIDEKNKEIEELKQTQKSLK 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 245 SENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 324
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
170
....*....|....*.
gi 386869290 325 QELMDENFDLSKRLSE 340
Cdd:TIGR04523 662 PEIIKKIKESKTKIDD 677
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
196-371 |
3.96e-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: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 196 DMQAELQKKQEELETLQSINKKLELKVKEqkdyWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGD 275
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 276 QDKTEQLEQLKKEndhlflsLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERL 355
Cdd:COG1196 312 RELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170
....*....|....*.
gi 386869290 356 EGENDLLKRENSRLLS 371
Cdd:COG1196 385 AEELLEALRAAAELAA 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-369 |
4.33e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 167 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET-LQSINKKLELKVKEQKDYWET------ELLQLKEQ 239
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAeIASLERSIAEKERELEDAEERlakleaEIDKLLAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 240 NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT------------EQLEQLKKENDHLFLSLTEQRKDQKK 305
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAelEEVDKEfaetrdelkdyrEKLEKLKREINELKRELDRLQEELQR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386869290 306 LEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 369
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-363 |
5.53e-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: 55.45 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 153 NEEDILVVTTQGEVEEIEQHNKelcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET- 231
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETl 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 232 --ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQgdqdkteqlEQLKKENDHLFLSLTEQRKDQKKLEQT 309
Cdd:TIGR02168 385 rsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK---------KLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386869290 310 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 363
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
168-370 |
8.49e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 168 EIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN 247
Cdd:COG1196 233 KLRELEAELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 248 EKM---GIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 324
Cdd:COG1196 309 ERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 386869290 325 QELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 370
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
163-369 |
1.30e-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: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLE----LKVKEQKDYWETELLQ--- 235
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqekeLLEKEIERLKETIIKNnse 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 236 ---LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKE-------MEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKK 305
Cdd:TIGR04523 442 ikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869290 306 LEQTVEQM----KQNETTAMKKQQELMDENFDLSKRLSENEIicNALQRQKERLEGENDLLKRENSRL 369
Cdd:TIGR04523 522 LKEKIEKLesekKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
163-365 |
1.37e-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: 53.87 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQELKDSCISLQKQ-----NSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLK 237
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE----QISQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 238 EQNQKMSSENEKmgirvdqLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 317
Cdd:TIGR04523 349 KELTNSESENSE-------KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386869290 318 TTAMKKQQELMDENF-------DLSKRLSENEIICNALQRQKERLEGENDLLKRE 365
Cdd:TIGR04523 422 ELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-369 |
1.74e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 199 AELQKKQEELE-TLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQD 277
Cdd:TIGR02168 680 EELEEKIEELEeKIAELEKALA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 278 KTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEG 357
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170
....*....|..
gi 386869290 358 ENDLLKRENSRL 369
Cdd:TIGR02168 839 RLEDLEEQIEEL 850
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
246-377 |
2.19e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.32 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 246 ENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQ 325
Cdd:COG2433 393 EEPEAEREKEHEERELTEEEEEIRRL-------EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 386869290 326 ELmdenfdlSKRlsENEIicNALQRQKERLEGENDLLKRENSRLLSYMGLDF 377
Cdd:COG2433 466 EI-------SRL--DREI--ERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
159-371 |
4.41e-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: 52.33 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 159 VVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSIN--KKLELK-VKEQKDYWETELLQ 235
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENqsYKQEIKnLESQINDLESKIQN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 236 LKEQNQKMSsenekmgIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE---- 311
Cdd:TIGR04523 403 QEKLNQQKD-------EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsr 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 312 QMKQNETTAMKKQQELMDENFDLSKrlseneiicnaLQRQKERLEGENDLLKRENSRLLS 371
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKK-----------LNEEKKELEEKVKDLTKKISSLKE 524
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
162-363 |
6.23e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 52.00 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 162 TQGEVEEIEQ-HNKELCKENQELKDSCislqKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQ----- 235
Cdd:COG5022 887 LKIDVKSISSlKLVNLELESEIIELKK----SLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNklhev 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 236 ---LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG------DQDKTEQLEQLKKENDHLflslteqrkdqkkl 306
Cdd:COG5022 963 eskLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELskqygaLQESTKQLKELPVEVAEL-------------- 1028
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 386869290 307 eQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 363
Cdd:COG5022 1029 -QSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLY 1084
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
162-326 |
8.19e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 162 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQ----------KDYWE- 230
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 231 -------TELL-------QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL 296
Cdd:COG3883 108 llgsesfSDFLdrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190
....*....|....*....|....*....|.
gi 386869290 297 TEQRKD-QKKLEQTVEQMKQNETTAMKKQQE 326
Cdd:COG3883 188 SAEEAAaEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
147-364 |
1.08e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 147 FQFRPENEEDILVVTtqgevEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkeqk 226
Cdd:PRK03918 174 IKRRIERLEKFIKRT-----ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 227 dywetellQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKENDhLFLSLTEQRKDQKKL 306
Cdd:PRK03918 242 --------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL----EEKVKELKELKEKAE-EYIKLSEFYEEYLDE 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386869290 307 EQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKR 364
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
197-369 |
1.10e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 197 MQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQ 276
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 277 DKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLE 356
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170
....*....|...
gi 386869290 357 GENDLLKRENSRL 369
Cdd:COG4372 164 EELAALEQELQAL 176
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-360 |
1.59e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLELKVKEQKDYWETELLQLKEQNQK 242
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA---ELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 243 MSsenekmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 322
Cdd:COG1196 399 AA--------QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 386869290 323 KQQELMDENFDLSKRLSENEIICNALQRQKERLEGEND 360
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
161-382 |
1.73e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 161 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLE---LKVKEQKDYWETELLQLK 237
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeelESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 238 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 317
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869290 318 TTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPY 382
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
152-365 |
2.01e-06 |
|
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: 50.36 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 152 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK--EQKDYW 229
Cdd:pfam02463 807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEleEQKLKD 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 230 ETELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKLvqgdqdktEQLEQLKKENDHLFLSLtEQRKDQKKLEQT 309
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEES---QKLNLLEEKENEIEERIKE--------EAEILLKYEEEPEELLL-EEADEKEKEENN 954
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 386869290 310 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRE 365
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
163-371 |
2.10e-06 |
|
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: 49.89 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETellqLKEQNQK 242
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKT----LTQRVLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 243 MSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 322
Cdd:pfam07888 148 RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386869290 323 KQqelmdenfdlskrlSENEIICNALQRQKERL---EGENDLLKRENSRLLS 371
Cdd:pfam07888 228 KE--------------AENEALLEELRSLQERLnasERKVEGLGEELSSMAA 265
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-355 |
2.53e-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: 50.06 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 162 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkEQKDYWETELLQLKEQNQ 241
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE----RRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 242 KMSSENEKmgirvdqLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 321
Cdd:TIGR02168 849 ELSEDIES-------LAAEIEELEELIEEL-------ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
170 180 190
....*....|....*....|....*....|....
gi 386869290 322 KKQQELMDENFDLSKRLSENEiicNALQRQKERL 355
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLE---VRIDNLQERL 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
154-360 |
3.85e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 154 EEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQnsdmQAELQKKQEELETLQSIN--KKLELKVKEQKDYWET 231
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK----EAEEKKKAEELKKAEEENkiKAAEEAKKAEEDKKKA 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 232 ELLQLKEQNQKMSSENEKmgirvdqlqaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE 311
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALK----------KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386869290 312 QMKQNETTAMKKQQELMDENFDLSKRLSENE-IICNALQRQKERLEGEND 360
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEaVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
152-356 |
4.86e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 152 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET 231
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 232 ELLQLKEQNQKMSSENEKMG---IRVDQLQAQLSTQEKEMEKLVQgdqdkteQLEQLKKENDHLFLSLTEQRKDQKKLEQ 308
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAAnlrERLESLERRIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELES 873
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386869290 309 TVE-------QMKQNETTAMKKQQELMDENFDLSKRLSENEiicNALQRQKERLE 356
Cdd:TIGR02168 874 ELEallneraSLEEALALLRSELEELSEELRELESKRSELR---RELEELREKLA 925
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
161-360 |
7.58e-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: 48.63 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 161 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELK-VKEQKDY--WETELLQLK 237
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKnIKLSKDVssLESQLQDTQ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 238 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEqlkkendhlflSLTEQRKD-QKKLEQTVEQMKQN 316
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLS-----------TLQAQLSDmKKKLEEDAGTLEAL 543
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869290 317 ETTAMKKQQELMdenfDLSKRLSENEIICNALQRQKERLEGEND 360
Cdd:pfam01576 544 EEGKKRLQRELE----ALTQQLEEKAAAYDKLEKTKNRLQQELD 583
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
200-371 |
8.99e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 200 ELQKKQEELETLQSINKKLELKVKEQKDywETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKT 279
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEEL--EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 280 EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEiicNALQRQKERLEGEN 359
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAE 371
|
170
....*....|..
gi 386869290 360 DLLKRENSRLLS 371
Cdd:COG1196 372 AELAEAEEELEE 383
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
166-317 |
9.13e-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: 46.66 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 166 VEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSS 245
Cdd:pfam17078 68 LKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKL 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869290 246 ENEKmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 317
Cdd:pfam17078 148 ENEK---QLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKLDSLAQLLDLPSWLNLYPESR 216
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
152-378 |
1.08e-05 |
|
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: 48.12 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 152 ENEEDILVVTTQGEVEEIEQHNKELckenQELKDScisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKD---- 227
Cdd:TIGR00606 722 EKRRDEMLGLAPGRQSIIDLKEKEI----PELRNK---LQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtim 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 228 ---YWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG-------DQDKTEQLEQLKKENDHL---FL 294
Cdd:TIGR00606 795 erfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKielnrklIQDQQEQIQHLKSKTNELkseKL 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 295 SLTEQRKDQKKL-EQTVEQMKQ----NETTAMKKQQELMDENFdLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 369
Cdd:TIGR00606 875 QIGTNLQRRQQFeEQLVELSTEvqslIREIKDAKEQDSPLETF-LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI 953
|
....*....
gi 386869290 370 LSYMGLDFN 378
Cdd:TIGR00606 954 HGYMKDIEN 962
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
134-360 |
1.39e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 134 VDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKElcKENQELKDSCISLQ----KQNSDMQAELQKKQEELE 209
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK--RELERIRQEEIAMEisrmRELERLQMERQQKNERVR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 210 TLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSENEKMgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEN 289
Cdd:pfam17380 396 QELEAARKVKILEEER----QRKIQQQKVEMEQIRAEQEEA--RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869290 290 DHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLS-ENEIICNALQRQKERLEGEND 360
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEkEMEERQKAIYEEERRREAEEE 541
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
446-468 |
2.37e-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: 2.37e-05
10 20
....*....|....*....|....
gi 386869290 446 CPICDKIFPATEKQ-IFEDHVFCH 468
Cdd:cd21965 1 CPICNKQFPPQVDQeAFEDHVESH 24
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-369 |
2.91e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 198 QAELQKKQEELETLQSINKKLELKVKEQK-DYWETELLQLKEqnqkmssENEKMGIRVDQLQAQLSTQEKEMEKL-VQGD 275
Cdd:COG4913 261 AERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRA-------ELARLEAELERLEARLDALREELDELeAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 276 QDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMK-------------QNETTAMK-----KQQELMDENFDLSKR 337
Cdd:COG4913 334 GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefaalRAEAAALLealeeELEALEEALAEAEAA 413
|
170 180 190
....*....|....*....|....*....|..
gi 386869290 338 LSEneiicnaLQRQKERLEGENDLLKRENSRL 369
Cdd:COG4913 414 LRD-------LRRELRELEAEIASLERRKSNI 438
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
163-373 |
2.93e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDM---QAELQKKQEEletLQSINKKLELKVKEQKDYwETELLQLKEQ 239
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEE---LEELNEQLQAAQAELAQA-QEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 240 NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT 319
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386869290 320 AMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYM 373
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
165-365 |
3.10e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 165 EVEEIEQHNKELCKENQELK-------------DSCISLQKQNSDMQAELQKKQEElETLQSINKKLELKVKEQKDYWET 231
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRkaeeakkaeeariEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 232 ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDhlflsltEQRKdqkkleqtVE 311
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKK--------AE 1705
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386869290 312 QMKQNETTAMKKQQELMDENfdlskrlSENEIICNALQRQKERLEGENDLLKRE 365
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAE-------EENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
165-371 |
3.49e-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: 46.17 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 165 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELEtlqsiNKKLELKVKEQkdywetELLQLKEQNQKMS 244
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE-----QKQKELKSKEK------ELKKLNEEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 245 SENEKMgirvDQLQAQLSTQEKEMEKLVQGDQDKTEQLE-QLKKENDHLFLSLTEQRKDQKklEQTVEQMKQNETTAMKK 323
Cdd:TIGR04523 510 EKVKDL----TKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKKENLEKEIDEK--NKEIEELKQTQKSLKKK 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 386869290 324 Q-------QELMDENFDLSKRLSENEIicnalqrQKERLEGENDLLKRENSRLLS 371
Cdd:TIGR04523 584 QeekqeliDQKEKEKKDLIKEIEEKEK-------KISSLEKELEKAKKENEKLSS 631
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
156-369 |
3.68e-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: 46.27 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 156 DILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQE-ELETLQSINKKLELKVKEQK----DYWE 230
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElEFEIQSQEQDSEIVKNSKSElariPELE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 231 TELLQLKEQNQKMSSENEKMGI---RVDQLQAQLSTQEKEMEKLVQGDQDKtEQLEQLKKENDHLFLSLTEQRKDQKKLE 307
Cdd:pfam05557 204 KELERLREHNKHLNENIENKLLlkeEVEDLKRKLEREEKYREEAATLELEK-EKLEQELQSWVKLAQDTGLNLRSPEDLS 282
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869290 308 QTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 369
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
143-356 |
3.75e-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: 46.50 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 143 ASIPFQFRPENEEDILVvttQGEVEEIEQHNKELCKENQELKdscislQKQNSDMQAELQKKQEELETLQSINKKLELKV 222
Cdd:pfam02463 148 AMMKPERRLEIEEEAAG---SRLKRKKKEALKKLIEETENLA------ELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 223 KEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKD 302
Cdd:pfam02463 219 LELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386869290 303 QKKLEQTveqmKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLE 356
Cdd:pfam02463 299 KSELLKL----ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
178-350 |
4.32e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 178 KENQELKDSCIS-----LQKQNSDMQAELQKKQEELetlqsinKKLELKVKEQKDYWETELlqlkEQNQKMSSENEKMGI 252
Cdd:PRK12704 49 KEAEAIKKEALLeakeeIHKLRNEFEKELRERRNEL-------QKLEKRLLQKEENLDRKL----ELLEKREEELEKKEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 253 RVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsltEQRKDQkkLEQTVEQMKQnETTAMKKQQElmDENF 332
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEIL--LEKVEEEARH-EAAVLIKEIE--EEAK 183
|
170
....*....|....*...
gi 386869290 333 DLSKRLSeNEIICNALQR 350
Cdd:PRK12704 184 EEADKKA-KEILAQAIQR 200
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-326 |
4.63e-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: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 162 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET----LQSINKKLElKVKEQKDYWETELLQLK 237
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdeLKDYREKLE-KLKREINELKRELDRLQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 238 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLK----KENDHLFLSLTEQRKDQKKLEQTVEQM 313
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlsKYEQELYDLKEEYDRVEKELSKLQREL 492
|
170
....*....|...
gi 386869290 314 KQNETTAMKKQQE 326
Cdd:TIGR02169 493 AEAEAQARASEER 505
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
167-320 |
5.10e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 167 EEIEQHNKELCKENQELKDSCISLQKQ-----------NSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQ 235
Cdd:COG3883 72 AEIAEAEAEIEERREELGERARALYRSggsvsyldvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 236 LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 315
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*
gi 386869290 316 NETTA 320
Cdd:COG3883 232 AAAAA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
167-344 |
5.55e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 167 EEIEQHNKELcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELL---------QLK 237
Cdd:COG4717 71 KELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeaelaelpeRLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 238 EQNQKMSSENEKMgIRVDQLQAQLSTQEKEMEKLVQGDQDKTE-QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN 316
Cdd:COG4717 150 ELEERLEELRELE-EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|....*...
gi 386869290 317 EttamkKQQELMDENFDLSKRLSENEII 344
Cdd:COG4717 229 L-----EQLENELEAAALEERLKEARLL 251
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
181-335 |
6.67e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 45.36 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 181 QELKDScisLQKQNSDmqAELQKKQEELEtlQSINKKL-ELKvkEQKDYWETELLQLKEQNQKMssenekmgIRVDQLQA 259
Cdd:pfam13779 496 ERLSEA---LERGASD--EEIAKLMQELR--EALDDYMqALA--EQAQQNPQDLQQPDDPNAQE--------MTQQDLQR 558
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869290 260 QLstqeKEMEKLVQ-GDQDKTEQ-LEQLKKENDHLFLSLTEQRKDQKKlEQTVEQMKQNETTaMKKQQELMDENFDLS 335
Cdd:pfam13779 559 ML----DRIEELARsGRRAEAQQmLSQLQQMLENLQAGQPQQQQQQGQ-SEMQQAMDELGDL-LREQQQLLDETFRQL 630
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-288 |
8.16e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLEL---------KVKEQKDYWETEL 233
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQAELQRVEEEI 967
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 386869290 234 LQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKE 288
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI----LERIEEYEKKKRE 1018
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
158-315 |
8.43e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 158 LVVTTQGEVEEIEQHNKELCKENQELKDscISLQKQNSDMQAELQKKQEELETL---------QSINKKLEL-------- 220
Cdd:PRK04778 224 LQTELPDQLQELKAGYRELVEEGYHLDH--LDIEKEIQDLKEQIDENLALLEELdldeaeeknEEIQERIDQlydilere 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 221 -----KVKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT---- 279
Cdd:PRK04778 302 vkarkYVEKNSDTLPDFLEHAKEQNKELKEEidrvkqsytlNESELESVRQLEKQLESLEKQYDEITEriAEQEIAysel 381
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869290 280 --------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 315
Cdd:PRK04778 382 qeeleeilKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRN 425
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
167-371 |
9.26e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 167 EEIEQHNKELCKENQELK---DSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKdyweTELLQLKEQ---- 239
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISntqTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK----SEISDLNNQkeqd 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 240 -NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNET 318
Cdd:TIGR04523 308 wNKELKSELKNQEKKLEEIQNQISQNNKIISQL-------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 386869290 319 TAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 371
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
165-365 |
1.07e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 165 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE-----TELLQLKE- 238
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADelkkaEELKKAEEk 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 239 ---QNQKMSSENEKMGIRVDQLQAQLSTQEKEmEKLVQGDQDKTEQLEQLKKENDHLFLSltEQRKDQKKLEQTVEQMKQ 315
Cdd:PTZ00121 1564 kkaEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKK 1640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386869290 316 NETTAMKKQQELMDENfdlskrlSENEIICNALQRQKERLEGENDLLKRE 365
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAE-------EENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-367 |
1.28e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 244 SSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKK 323
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 386869290 324 QQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENS 367
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
209-368 |
1.42e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 209 ETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKE 288
Cdd:COG4372 31 EQLRKALFELD-KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 289 NDHLFLSLTEQRKDQKKLEQTVEQMKQnettamkKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 368
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEA-------QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-356 |
1.51e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 161 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK---EQKDYWETELLQLK 237
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEEALALLR 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 238 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVqgdqdktEQLEQLKKENDHLFLSLTEQRKDqkkleqTVEQMKQNE 317
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLE-------LRLEGLEVRIDNLQERLSEEYSL------TLEEAEALE 960
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386869290 318 TTAMKKQQELMDENFDLSKRLSE----NEIICNALQRQKERLE 356
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYD 1003
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
190-369 |
2.06e-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: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 190 LQKQNSDMQAELQKKQEELETLQSINKKLELkvKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEME 269
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 270 KLVQGD--QDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNettamkKQQElmdenfdLSKRLSENEIICNA 347
Cdd:COG3206 258 ELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------LQQE-------AQRILASLEAELEA 324
|
170 180
....*....|....*....|..
gi 386869290 348 LQRQKERLEGENDLLKRENSRL 369
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAEL 346
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
154-371 |
2.10e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 154 EEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEE-------LETLQSINKKLELKVKEQK 226
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekekklQEEELKLLAKEEEELKSEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 227 DYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKL 306
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869290 307 EQtveqmkQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 371
Cdd:pfam02463 383 SE------RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
167-369 |
2.25e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 167 EEIEQhnkelcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWEtELLQLKEQnqkmsse 246
Cdd:PRK02224 194 AQIEE------KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-ELETLEAE------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 247 nekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAmkkQQE 326
Cdd:PRK02224 260 -------IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL---RDR 329
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386869290 327 LMDENFDLSKRLSENEiicnALQRQKERLEGENDLLKRENSRL 369
Cdd:PRK02224 330 LEECRVAAQAHNEEAE----SLREDADDLEERAEELREEAAEL 368
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
199-367 |
2.48e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 199 AELQKKQEELETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMgirvdQLQAQLSTQEKEMEKLVQGDQDK 278
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 279 TEQLEQLKKEND---HLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ--------QELMDENFDLSKRLSENEIICNA 347
Cdd:COG4717 145 PERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEAQEELEE 224
|
170 180
....*....|....*....|
gi 386869290 348 LQRQKERLEGENDLLKRENS 367
Cdd:COG4717 225 LEEELEQLENELEAAALEER 244
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
165-342 |
2.81e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 165 EVEEIEQHNKELCKENQELKDScisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYW----ETEL----LQL 236
Cdd:TIGR00606 910 QDSPLETFLEKDQQEKEELISS---KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYlkqkETELntvnAQL 986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 237 KEQNQKMSSENEKMGIRVDQLQAQlstqeKEMEKLVQGD------QDKTEQLEQLKKENDHLF--LSLTEQRKDQKKLEQ 308
Cdd:TIGR00606 987 EECEKHQEKINEDMRLMRQDIDTQ-----KIQERWLQDNltlrkrENELKEVEEELKQHLKEMgqMQVLQMKQEHQKLEE 1061
|
170 180 190
....*....|....*....|....*....|....
gi 386869290 309 TVEQMKQNETTAMKKQQELMDENFDLSKRLSENE 342
Cdd:TIGR00606 1062 NIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
193-376 |
2.86e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 193 QNSDMQAELQKKQEELETLQSinkKLELKVKEQKDywetellQLKEQNQKMSSENEkmgiRVDQLQAQLSTQEKEMEKL- 271
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERT---RAREQLRQAQA-------QLAQYNQVLASLKS----SYDAKRQMLQELKQELQDLg 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 272 VQGDQDKTEQLEQLKKENDHLfLSLTEQRKDQKKLEQTVEQMkqnETTAMKKQQELMDENFDLSKRLSENE--IICNALq 349
Cdd:PRK04863 1048 VPADSGAEERARARRDELHAR-LSANRSRRNQLEKQLTFCEA---EMDNLTKKLRKLERDYHEMREQVVNAkaGWCAVL- 1122
|
170 180
....*....|....*....|....*..
gi 386869290 350 rqkeRLEGENDLLKRENSRLLSYMGLD 376
Cdd:PRK04863 1123 ----RLVKDNGVERRLHRRELAYLSAD 1145
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
152-324 |
2.91e-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: 43.57 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 152 ENEEDILVVTTQGEVEE-IEQHNKELCKenqeLKDSCISLQKQNSDMQAELQKKQEE-----------LETLQSINKKLE 219
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQlISEHEVEITG----LTEKASSARSQANSIQSQLEIIQEQarnqnsmymrqLSDLESTVSQLR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 220 LKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVqGDQDKTEQLEQLKKEN---------- 289
Cdd:pfam15921 331 SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL-ADLHKREKELSLEKEQnkrlwdrdtg 409
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 386869290 290 -----DHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 324
Cdd:pfam15921 410 nsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQ 449
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
163-287 |
3.39e-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: 42.38 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEEL-------ETLQSINKkLELKVKEQKDYWETELLQ 235
Cdd:pfam15294 132 HMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQgakkdvkSNLKEISD-LEEKMAALKSDLEKTLNA 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869290 236 LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGD----------QDKTEQLEQLKK 287
Cdd:pfam15294 211 STALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTaayrnmkemlTKKNEQIKELRK 272
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
163-315 |
3.52e-04 |
|
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: 40.75 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQkkqeeletlqsinkKLELKVKEQKdywetellQLKEQNQK 242
Cdd:pfam12718 13 QERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVE--------------KLEEQLKEAK--------EKAEESEK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869290 243 MSSENEKMGIRVDQLQAQLSTQEKE----MEKLVQGDQdKTEQLEQLKKendhlflSLTEQR-KDQKKLEQTVEQMKQ 315
Cdd:pfam12718 71 LKTNNENLTRKIQLLEEELEESDKRlketTEKLRETDV-KAEHLERKVQ-------ALEQERdEWEKKYEELEEKYKE 140
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
221-329 |
3.53e-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: 41.59 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 221 KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQ---AQLSTQEKEMEKLVQGDQDKT-EQLEQLKKENDHLFLSL 296
Cdd:pfam05010 12 KARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEktiAQMIEEKQKQKELEHAEIQKVlEEKDQALADLNSVEKSF 91
|
90 100 110
....*....|....*....|....*....|...
gi 386869290 297 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMD 329
Cdd:pfam05010 92 SDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA 124
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
168-315 |
3.68e-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: 43.18 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 168 EIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETELLQlkeqnQKMSSEN 247
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE-STKEMLRKVVEELTA-----KKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 248 EKMgiRVDQLQAQLSTQEK-------EMEKLVQGDQDKTEQLEQLKKENDHLF----------LSLTEQRKDQKKLEQTV 310
Cdd:pfam15921 494 SER--TVSDLTASLQEKERaieatnaEITKLRSRVDLKLQELQHLKNEGDHLRnvqtecealkLQMAEKDKVIEILRQQI 571
|
....*
gi 386869290 311 EQMKQ 315
Cdd:pfam15921 572 ENMTQ 576
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
174-362 |
3.79e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 174 KELCKENQELKDScislQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDyweteLLQLKEQNQKMSSENEKMGIR 253
Cdd:COG4717 74 KELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 254 VDQLQaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQ-KKLEQTVEQMKQNETTAMKKQQELMDENF 332
Cdd:COG4717 145 PERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190
....*....|....*....|....*....|
gi 386869290 333 DLSKRLSENEIICNALQRQKERLEGENDLL 362
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
190-389 |
3.94e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 190 LQKQNSDMQAELQKKQEELETLQSinkklELKVKEQKdywETELLQLKEQNQkmssenekmGIRVDQLQAQLSTQEKEME 269
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEA-----RLDALREE---LDELEAQIRGNG---------GDRLEQLEREIERLERELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 270 KLVQgdqdkteQLEQLKKENDHLFLSLTEQRKD----QKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSE--NEI 343
Cdd:COG4913 356 ERER-------RRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleAEI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 386869290 344 icNALQRQKERLEGENDLLKREnsrLLSYMGLDFNSLPY-----QVPTSDE 389
Cdd:COG4913 429 --ASLERRKSNIPARLLALRDA---LAEALGLDEAELPFvgeliEVRPEEE 474
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
158-336 |
4.25e-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: 43.18 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 158 LVVTTQGEVEEIEQHNKELCK----------ENQELKDSCISLQKQNSDMQA---ELQKKQEELETL-QSINKKLEL--- 220
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKlrsrvdlklqELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILrQQIENMTQLvgq 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 221 ------KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFL 294
Cdd:pfam15921 581 hgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN 660
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386869290 295 SLTEQRKDQKKLEQTVEQMKQN--------ETTAMKKQQELMDENFDLSK 336
Cdd:pfam15921 661 EVKTSRNELNSLSEDYEVLKRNfrnkseemETTTNKLKMQLKSAQSELEQ 710
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
167-357 |
4.38e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 167 EEIEQHNKELCKENQELKdsciSLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWET---ELLQLKEQNQKM 243
Cdd:PRK03918 238 EEIEELEKELESLEGSKR----KLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKlseFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 244 SSENEKMGIRVDQLQAQLSTQE------KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLE-QTVEQMKQN 316
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKE 392
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 386869290 317 ETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEG 357
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| CCDC14 |
pfam15254 |
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ... |
170-267 |
4.48e-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: 42.86 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 170 EQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLeLKVKE-QKDY----------WETELLQLKE 238
Cdd:pfam15254 412 EQEKTEKTSGSGDCNLELFSLQSLNMSLQNQLQESLKSQELLQSKNEEL-LKVIEnQKEEnkkltkifkeKEQTLLENKQ 490
|
90 100 110
....*....|....*....|....*....|...
gi 386869290 239 Q----NQKMSSENEKMGIRVDQLQAQLSTQEKE 267
Cdd:pfam15254 491 QfdieTTRVKIELEEALVNMKSFQFKLEAAEKE 523
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
198-330 |
4.71e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 198 QAELQKKQEELEtLQSINKKLELKVKEqkdywetELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKlvqgdqd 277
Cdd:PRK12704 39 EAKRILEEAKKE-AEAIKKEALLEAKE-------EIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDR------- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 386869290 278 KTEQLEQLKKEndhlflsLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE 330
Cdd:PRK12704 101 KLELLEKREEE-------LEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-358 |
5.27e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 167 EEIEQHNKEL--CKENQELKDSCISLQKQNSDmqaELQKKQEELETLQSINKKLElkvkeqkDYWETELLQLKEQNQKms 244
Cdd:TIGR02169 170 RKKEKALEELeeVEENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKR-------EYEGYELLKEKEALER-- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 245 senekmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLF-----LSLTEQRKDQKKLEQTVEQMKQNETT 319
Cdd:TIGR02169 238 --------QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdLGEEEQLRVKEKIGELEAEIASLERS 309
|
170 180 190
....*....|....*....|....*....|....*....
gi 386869290 320 AMKKQQELMdenfDLSKRLSENEIICNALQRQKERLEGE 358
Cdd:TIGR02169 310 IAEKERELE----DAEERLAKLEAEIDKLLAEIEELERE 344
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
196-315 |
5.50e-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: 42.53 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 196 DMQAELQKKQEELETLQSI-NKKLELK--VKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLS 262
Cdd:pfam06160 260 EAEEALEEIEERIDQLYDLlEKEVDAKkyVEKNLPEIEDYLEHAEEQNKELKEElervqqsytlNENELERVRGLEKQLE 339
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869290 263 TQEKEMEKLVQGDQDKT--------------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 315
Cdd:pfam06160 340 ELEKRYDEIVERLEEKEvayselqeeleeilEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKL 406
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
148-369 |
6.43e-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: 42.40 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 148 QFRPENEEDILVVTT------QGEVEEIEQ--HNKELckENQELK------DSCISLQKQNSDMQAELQKKQEELETLQS 213
Cdd:pfam05483 369 QQRLEKNEDQLKIITmelqkkSSELEEMTKfkNNKEV--ELEELKkilaedEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 214 INKK----LELK--------------VKEQKDYWETELLQLKE----------QNQKMSSENEKMGIRVDQLQAQLSTQE 265
Cdd:pfam05483 447 AREKeihdLEIQltaiktseehylkeVEDLKTELEKEKLKNIEltahcdklllENKELTQEASDMTLELKKHQEDIINCK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 266 KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQK-KLEQTVEQMKQNETTAMKKQqelmdenfdlsKRLSENEII 344
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKE-----------KQMKILENK 595
|
250 260
....*....|....*....|....*
gi 386869290 345 CNALQRQKERLEGENDLLKRENSRL 369
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKAL 620
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
133-287 |
8.46e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 133 YVDED----GVVRGASI----------------PFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDscislqk 192
Cdd:COG2433 362 DVDRDevkaRVIRGLSIeealeeliekelpeeePEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 193 qnsdmqaELQKKQEELEtlqsinkKLELKVKEQKdywetellqlKEQNQKMSSENE--KMGIRVDQLQAQLSTQEKEMEK 270
Cdd:COG2433 435 -------ELEEKDERIE-------RLERELSEAR----------SEERREIRKDREisRLDREIERLERELEEERERIEE 490
|
170
....*....|....*..
gi 386869290 271 LvqgdQDKTEQLEQLKK 287
Cdd:COG2433 491 L----KRKLERLKELWK 503
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
150-343 |
8.71e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 150 RPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEEletlQSINKKLELKvKEQKDYW 229
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE----ERKRKKLELE-KEKRDRK 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 230 ETELL-------QLKEQNQKMSSENEKMGIrvdqlqaqlstQEKEME---KLVQGDQDKTEQLEQLKKENDhlflsLTEQ 299
Cdd:pfam17380 488 RAEEQrrkilekELEERKQAMIEEERKRKL-----------LEKEMEerqKAIYEEERRREAEEERRKQQE-----MEER 551
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386869290 300 RKDQKKLEQTVEQMKQNEttAMKKQQELMDENFDLSKRLSENEI 343
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 ... |
162-328 |
9.41e-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: 41.73 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 162 TQGEVEEIEQHNKELCKENQELKDSCISLQKQN-SDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET--------- 231
Cdd:pfam10174 85 AQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENfRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGArdesikkll 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 232 ELLQLKEQNQKMSSENEKMGIR-------VDQLQAQLSTQEKEMEKL---------VQGDQDKTEQLEQLKKENDHLFLS 295
Cdd:pfam10174 165 EMLQSKGLPKKSGEEDWERTRRiaeaemqLGHLEVLLDQKEKENIHLreelhrrnqLQPDPAKTKALQTVIEMKDTKISS 244
|
170 180 190
....*....|....*....|....*....|...
gi 386869290 296 LTEQRKDqkkLEQTVEQMKQNETTAMKKQQELM 328
Cdd:pfam10174 245 LERNIRD---LEDEVQMLKTNGLLHTEDREEEI 274
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
168-327 |
1.07e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 168 EIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetelLQLKEQNQKMSSEN 247
Cdd:COG1579 18 ELDRLEHRLKELPAELAE----LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA------RIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 248 EKMgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKD----QKKLEQTVEQMKQNETTAMKK 323
Cdd:COG1579 88 NKE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEELEAE 164
|
....
gi 386869290 324 QQEL 327
Cdd:COG1579 165 REEL 168
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
206-328 |
1.15e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 206 EELETLQSINKKLELKVKEQKDYWETELLQLKEQNQK----MSSENEKMGIRVDQLQAQLstqeKEMEKLVQGDQDKTEQ 281
Cdd:pfam05622 282 EKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRrkneLETQNRLANQRILELQQQV----EELQKALQEQGSKAED 357
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 386869290 282 LEQLKKENDHLFLSLTE-QRKDQKKLEQTVEQMKQNETTAMKKQQELM 328
Cdd:pfam05622 358 SSLLKQKLEEHLEKLHEaQSELQKKKEQIEELEPKQDSNLAQKIDELQ 405
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
191-365 |
1.24e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 191 QKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEK 270
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 271 LVQGDQDKTEQL---EQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNA 347
Cdd:PTZ00121 1614 KAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
|
170
....*....|....*...
gi 386869290 348 LQRQKERLEGENDLLKRE 365
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKE 1711
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
168-353 |
1.24e-03 |
|
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: 41.49 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 168 EIEQHNKELCKENQELkdsCISLQKQNSDMQAE---LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMS 244
Cdd:TIGR00618 708 ELETHIEEYDREFNEI---ENASSSLGSDLAARedaLNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 245 SENEKMGIRVDQLQAQLSTQEKEM-EKLVQGDQDKTEQLEQLKKENDHLflsLTEQRKDQKKLEQTVEQMKQNETTaMKK 323
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQF---LSRLEEKSATLGEITHQLLKYEEC-SKQ 860
|
170 180 190
....*....|....*....|....*....|
gi 386869290 324 QQELMDENFDLSKRLSENEIIcNALQRQKE 353
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKLNGI-NQIKIQFD 889
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
165-315 |
1.29e-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: 41.31 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 165 EVEEIEQhnkELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLEL-------KVKEQkdywETELLQLK 237
Cdd:pfam01576 72 ELEEILH---ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLekvtteaKIKKL----EEDILLLE 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869290 238 EQNQKMSSENEKMGIRVDQLQAQLSTQEkemeklvqgdqDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 315
Cdd:pfam01576 145 DQNSKLSKERKLLEERISEFTSNLAEEE-----------EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR 211
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
197-364 |
1.35e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 197 MQAELQKKQEELETLQS---INKKLELKVKEQKDYWeTELLQLK-----EQNQKMSSENekmgirvDQLQAQLStqekem 268
Cdd:PRK04863 926 IVSVLQSDPEQFEQLKQdyqQAQQTQRDAKQQAFAL-TEVVQRRahfsyEDAAEMLAKN-------SDLNEKLR------ 991
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 269 EKLVQGDQDKTEQLEQLKK------ENDHLFLSLTE--QRKDQ--KKLEQTVEQMKQNETTAMKKQQELMDEnfDLSKRL 338
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQaqaqlaQYNQVLASLKSsyDAKRQmlQELKQELQDLGVPADSGAEERARARRD--ELHARL 1069
|
170 180
....*....|....*....|....*..
gi 386869290 339 SENEIICNALQRQKERLEGE-NDLLKR 364
Cdd:PRK04863 1070 SANRSRRNQLEKQLTFCEAEmDNLTKK 1096
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
155-369 |
1.57e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 155 EDILVVTTQGEVEEIeqhNKELCKE-NQELKDscISLQKQNSDMQAELQKK-QEELETLQSIN-KKLELKVkeqkdyweT 231
Cdd:PHA02562 157 EDLLDISVLSEMDKL---NKDKIRElNQQIQT--LDMKIDHIQQQIKTYNKnIEEQRKKNGENiARKQNKY--------D 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 232 ELLQlKEQNQKMSsenekmgirVDQLQAQLSTQEKEME-------KLVQGDQDKTEQLEQLKKEndHLFL-------SLT 297
Cdd:PHA02562 224 ELVE-EAKTIKAE---------IEELTDELLNLVMDIEdpsaalnKLNTAAAKIKSKIEQFQKV--IKMYekggvcpTCT 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386869290 298 EQRKDQ-KKLEQTVEQMKQNET------TAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 369
Cdd:PHA02562 292 QQISEGpDRITKIKDKLKELQHslekldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-327 |
1.69e-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: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 189 SLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywETELLQLKEQNQKMSSENEKMGIR-------VDQLQAQL 261
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQI 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869290 262 STQEKEMEKLVQGDQDKTE--------QLEQLKKENDHL---FLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 327
Cdd:COG3206 301 AALRAQLQQEAQRILASLEaelealqaREASLQAQLAQLearLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
192-353 |
1.73e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 192 KQNSDMQAELQKKQEELET---LQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKmgirVDQLQAQLSTQEKEM 268
Cdd:PRK12705 39 LQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK----LDNLENQLEEREKAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 269 EklvqgdqDKTEQLEQLKKENDHLFLSLTEQRKDQ------KKLEQTVEQMKQNETTAMKkqqelmdENFDLSKRLSENE 342
Cdd:PRK12705 115 S-------ARELELEELEKQLDNELYRVAGLTPEQarklllKLLDAELEEEKAQRVKKIE-------EEADLEAERKAQN 180
|
170
....*....|.
gi 386869290 343 IICNALQRQKE 353
Cdd:PRK12705 181 ILAQAMQRIAS 191
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
165-359 |
1.78e-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: 40.86 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 165 EVEEIEQHNKELCKENQELKDSCiSLQKQNSDMQAELQKKQE------------------------ELETLQSINKKLEL 220
Cdd:pfam05483 135 KLEEEIQENKDLIKENNATRHLC-NLLKETCARSAEKTKKYEyereetrqvymdlnnniekmilafEELRVQAENARLEM 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 221 KVKEQKDYweTELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKL---VQGDQDKTEQLEQLKKENDHlflSLT 297
Cdd:pfam05483 214 HFKLKEDH--EKIQHLEEEYKKEINDKEK---QVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDE---NLK 285
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869290 298 EQRKDQKKLEQTVEQMKQNETTAMKKQQELmDENFDLSKRlseneIICNALQRQKERLEGEN 359
Cdd:pfam05483 286 ELIEKKDHLTKELEDIKMSLQRSMSTQKAL-EEDLQIATK-----TICQLTEEKEAQMEELN 341
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
201-365 |
1.83e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 201 LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN---EKMGI--RVDQLQAQLSTQEKEMEKLvqgD 275
Cdd:PRK04778 200 LDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGyhlDHLDIekEIQDLKEQIDENLALLEEL---D 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 276 QDKTE-QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE--NFDLSKRLSENEI-ICNALQRQ 351
Cdd:PRK04778 277 LDEAEeKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEidRVKQSYTLNESELeSVRQLEKQ 356
|
170
....*....|....
gi 386869290 352 KERLEGENDLLKRE 365
Cdd:PRK04778 357 LESLEKQYDEITER 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
181-371 |
1.97e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 181 QELKDSCISLQKQNSDMQAELQKKQEELETLQsinKKLELKvkeqkdywETELLQLKEQNQKMSSENEKMGIRVDQLQAQ 260
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALE---ARLEAA--------KTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 261 LSTQ--EKEMEKLvqgdqdkTEQLEQLKKENDHLflslteqRKDQKKLEQTVEQMKQNETTAMKKQQELMDEnfdLSKRL 338
Cdd:COG1579 82 LGNVrnNKEYEAL-------QKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAE---LEEKK 144
|
170 180 190
....*....|....*....|....*....|....
gi 386869290 339 SENEIICNALQRQKERLEGE-NDLLKRENSRLLS 371
Cdd:COG1579 145 AELDEELAELEAELEELEAErEELAAKIPPELLA 178
|
|
| FtsL2 |
COG4839 |
Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning]; |
187-228 |
2.07e-03 |
|
Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443867 Cd Length: 123 Bit Score: 38.01 E-value: 2.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 386869290 187 CISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDY 228
Cdd:COG4839 57 LLSLQASIYELNREIQSLESKISEQQKENEDLEQEVSELSSP 98
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-369 |
2.12e-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: 40.54 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 162 TQGEVEEIEQHNKELCKENQELKDSC---ISLQKQNSDMQAELQKKQEELEtlqSINKKLELKVKEQkdywetellqlKE 238
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLAARKQELE---EILHELESRLEEE-----------EE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 239 QNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvQGDQDKTEQleQLKKENDHLfLSLTEQR----KDQKKLEQTVEQMK 314
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL-QLEKVTTEA--KIKKLEEDI-LLLEDQNsklsKERKLLEERISEFT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386869290 315 QNET---------TAMKKQQELMDEnfDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 369
Cdd:pfam01576 166 SNLAeeeekakslSKLKNKHEAMIS--DLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
167-379 |
2.27e-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: 40.58 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 167 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQsinKKLElKVKEQKDYWETELLQLKEQNQKMSSE 246
Cdd:pfam10174 355 EEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ---KKIE-NLQEQLRDKDKQLAGLKERVKSLQTD 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 247 NEKMGIRVDQLQAQLSTQEKEMEKLVQ----GDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT--- 319
Cdd:pfam10174 431 SSNTDTALTTLEEALSEKERIIERLKEqrerEDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlas 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869290 320 -AMKKQQELMDENFDLSKRLSEneiiCNALQRQkerlegendLLKRENSRLLSYMGLDFNS 379
Cdd:pfam10174 511 sGLKKDSKLKSLEIAVEQKKEE----CSKLENQ---------LKKAHNAEEAVRTNPEIND 558
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
167-314 |
2.34e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 167 EEIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELK---VKEQKDY--WETELLQLKEQNQ 241
Cdd:COG1579 31 AELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnVRNNKEYeaLQKEIESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386869290 242 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDhlfLSLTEQRKDQKKLEQTVEQMK 314
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAEL-------EAELEEKKAELD---EELAELEAELEELEAEREELA 169
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
153-368 |
2.60e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 153 NEEDILVV----TTQGEVEEIEQHNKELckenqelkdscISLQKQNSDMQAELQKKQEELETLQSINK--------KLEL 220
Cdd:PRK11281 55 EAEDKLVQqdleQTLALLDKIDRQKEET-----------EQLKQQLAQAPAKLRQAQAELEALKDDNDeetretlsTLSL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 221 KVKEQKdyWETELLQLK--------------------EQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKLVqgdqdkTE 280
Cdd:PRK11281 124 RQLESR--LAQTLDQLQnaqndlaeynsqlvslqtqpERAQAALYANSQ---RLQQIRNLLKGGKVGGKALR------PS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 281 QLEQLKKENDHLFLSLTEQRKDqkkLE-----QTVEQMKQNETTAmkKQQELMDENFDL-----SKRLSENEIICNALQR 350
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQRKS---LEgntqlQDLLQKQRDYLTA--RIQRLEHQLQLLqeainSKRLTLSEKTVQEAQS 267
|
250
....*....|....*....
gi 386869290 351 QKERLE-GENDLLKRENSR 368
Cdd:PRK11281 268 QDEAARiQANPLVAQELEI 286
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
166-369 |
3.38e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 166 VEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKE----------QKDYWETELLQ 235
Cdd:TIGR00606 669 ITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglapgrqsIIDLKEKEIPE 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 236 LKEQNQKMSSENEKMGIRVDQLQAQLST--QEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQrKDQKKLEQTVEQM 313
Cdd:TIGR00606 749 LRNKLQKVNRDIQRLKNDIEEQETLLGTimPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK-LQGSDLDRTVQQV 827
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 386869290 314 KQnettamkKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 369
Cdd:TIGR00606 828 NQ-------EKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
201-363 |
3.49e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 201 LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN---EKMGI--RVDQLQAQLstqEKEMEKLVQGD 275
Cdd:pfam06160 181 LEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGyalEHLNVdkEIQQLEEQL---EENLALLENLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 276 QDKTEQ-LEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE--NFDLSKRLSENEI-ICNALQRQ 351
Cdd:pfam06160 258 LDEAEEaLEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEEleRVQQSYTLNENELeRVRGLEKQ 337
|
170
....*....|..
gi 386869290 352 KERLEGENDLLK 363
Cdd:pfam06160 338 LEELEKRYDEIV 349
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
223-369 |
3.76e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 223 KEQKDYWETELLQLKEQNQKMSSENE------KMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL 296
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386869290 297 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSK---RLSENEIICNALQRQKERLEGENDLLKRENSRL 369
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtLLAAIADAEDEIERLREKREALAELNDERRERL 629
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
166-365 |
3.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 166 VEEIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETELLQLkeqnqKMSS 245
Cdd:PRK03918 517 LEELEKKAEEY----EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD-ELEEELAELLKELEEL-----GFES 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 246 ENEkmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHL---FLSLTEQRKDQKKLEQTVEQMKQNETTamK 322
Cdd:PRK03918 587 VEE-----LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELdkaFEELAETEKRLEELRKELEELEKKYSE--E 659
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 386869290 323 KQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRE 365
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
208-312 |
4.10e-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: 38.75 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 208 LETLQSINKkLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKK 287
Cdd:pfam11932 19 LDLAEKAVA-AAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASL----ERQIEEIERTER 93
|
90 100
....*....|....*....|....*
gi 386869290 288 ENDHLFLSLTEQrkdqkkLEQTVEQ 312
Cdd:pfam11932 94 ELVPLMLKMLDR------LEQFVAL 112
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
167-365 |
4.11e-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: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 167 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLElkvkeqkdywetellqlKEQNQKMSSE 246
Cdd:pfam01576 204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLE-----------------EETAQKNNAL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 247 NekmgiRVDQLQAQLSTQEKEME-------KLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMK---QN 316
Cdd:pfam01576 264 K-----KIRELEAQISELQEDLEseraarnKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkalEE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 317 ETTAMKKQ-QEL----------MDENFDLSKRLSENeiicnaLQRQKERLEGENDLLKRE 365
Cdd:pfam01576 339 ETRSHEAQlQEMrqkhtqaleeLTEQLEQAKRNKAN------LEKAKQALESENAELQAE 392
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
161-261 |
4.60e-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: 37.28 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 161 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkeqkdywetELLQLKEqn 240
Cdd:pfam10473 49 NSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESLNSSLE------------NLLEEKE-- 114
|
90 100
....*....|....*....|.
gi 386869290 241 QKMSSENEKMGIRVDQLQAQL 261
Cdd:pfam10473 115 QEKVQMKEESKTAVEMLQTQL 135
|
|
| Mod_r |
pfam07200 |
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ... |
160-288 |
4.90e-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: 37.60 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 160 VTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkklelkvkeqkdYWETELLQLKEQ 239
Cdd:pfam07200 22 VHSLPQVKALQAEKEELLAENESLAEENLSLEPELEELRSQLQELLEELKALKS--------------EYEEKEQELDEL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 386869290 240 NQKMSSENEKMgirvdQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKE 288
Cdd:pfam07200 88 LSKFSPDALLA-----RLQAAAAEAEEESEALAESFLEGEIDLDEFLKQ 131
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
165-368 |
5.29e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 165 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE-----TELLQLKEQ 239
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakkkAEEKKKADE 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 240 NQKMSSENEKMGIRVDQLQAQLSTQE---KEMEKLVQGDQDKTEQLEqlKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN 316
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADeakKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386869290 317 EttaMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 368
Cdd:PTZ00121 1474 E---AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
230-367 |
5.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 230 ETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHL----------------- 292
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeaeieerreelgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 293 ----------------------FLS---------------LTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLS 335
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdFLDrlsalskiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190
....*....|....*....|....*....|..
gi 386869290 336 KRLSENEIICNALQRQKERLEGENDLLKRENS 367
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
161-344 |
6.77e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 161 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQ- 239
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQa 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 240 --NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 317
Cdd:COG4372 185 ldELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
170 180
....*....|....*....|....*..
gi 386869290 318 TTAMKKQQELMDENFDLSKRLSENEII 344
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEA 291
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
188-351 |
6.86e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 188 ISLQKQNSDMQAELQKKQEELetlQSINKKL-------ELKVKEQKDYWETELLQLKEQN--QKMSSENEkmgirvDQLQ 258
Cdd:PRK11281 152 VSLQTQPERAQAALYANSQRL---QQIRNLLkggkvggKALRPSQRVLLQAEQALLNAQNdlQRKSLEGN------TQLQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 259 AQLSTQEKEMeklvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKklEQTVEQMKQNETTAMKK-----QQELmDENFD 333
Cdd:PRK11281 223 DLLQKQRDYL----------TARIQRLEHQLQLLQEAINSKRLTLS--EKTVQEAQSQDEAARIQanplvAQEL-EINLQ 289
|
170
....*....|....*...
gi 386869290 334 LSKRLSENEIICNALQRQ 351
Cdd:PRK11281 290 LSQRLLKATEKLNTLTQQ 307
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
166-369 |
7.36e-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: 38.42 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 166 VEEIEQHNKELCKENQELKDSCIslqkqnsdmQAELQKKQEELET--LQSINKK-------LELKVKEQKDYWET--ELL 234
Cdd:pfam02841 102 VELLEAKKDDFLKQNEEASSKYC---------SALLQDLSEPLEEkiSQGTFSKpggyklfLEERDKLEAKYNQVprKGV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 235 QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKlvqgDQDKTEQLEQLKKEndhlflslteQRKDQKKLEQTVEQMK 314
Cdd:pfam02841 173 KAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEA----ERAKAEAAEAEQEL----------LREKQKEEEQMMEAQE 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 386869290 315 QNETTAMKKQQELMDENFDLSKRLSENeIICNALQRQKERL-EG---ENDLLKRENSRL 369
Cdd:pfam02841 239 RSYQEHVKQLIEKMEAEREQLLAEQER-MLEHKLQEQEELLkEGfktEAESLQKEIQDL 296
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
98-305 |
7.43e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.76 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 98 WVTLPIDLnnKSAKQQE-VQFKAYYLPKDdeyyqfcYVDEDGVVRGASIPFQFRPENEEDILVVTTqgEVEEIEQHNKEL 176
Cdd:PRK05771 129 WGNFDLDL--SLLLGFKyVSVFVGTVPED-------KLEELKLESDVENVEYISTDKGYVYVVVVV--LKELSDEVEEEL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 177 CK---ENQELKDSCISLQkqnsdmqaELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEqnqKMSSENEKmgir 253
Cdd:PRK05771 198 KKlgfERLELEEEGTPSE--------LIREIKEELEEIEKERESLLEELKELAKKYLEELLALYE---YLEIELER---- 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386869290 254 vdqlqAQLSTQEKEMEKL--VQG--DQDKTEQLEQL--KKENDHLFLSLTEQRKDQKK 305
Cdd:PRK05771 263 -----AEALSKFLKTDKTfaIEGwvPEDRVKKLKELidKATGGSAYVEFVEPDEEEEE 315
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
258-394 |
7.57e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 258 QAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsLTEQRKD----QKKLEQTVEQMKQNETTAMKKQQELMDENFD 333
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKE-------LRERRNElqklEKRLLQKEENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869290 334 LSKRLSEneiicnaLQRQKERLEgenDLLKRENSRLLSYMGLdfnslpyqvpTSDEggARQ 394
Cdd:PRK12704 119 LEQKQQE-------LEKKEEELE---ELIEEQLQELERISGL----------TAEE--AKE 157
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
168-329 |
7.62e-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: 38.93 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 168 EIEQHNKELCKEN----QELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKlELKVKEQKDYWETELLQLKEQNQ-- 241
Cdd:pfam05483 489 ELTAHCDKLLLENkeltQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK-EMNLRDELESVREEFIQKGDEVKck 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 242 -KMSSENEK-MGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT 319
Cdd:pfam05483 568 lDKSEENARsIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
170
....*....|
gi 386869290 320 AMKKQQELMD 329
Cdd:pfam05483 648 AKQKFEEIID 657
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
152-246 |
7.64e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 38.17 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 152 ENEEDILVVttQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET 231
Cdd:COG4026 132 ELREELLEL--KEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLL 209
|
90
....*....|....*
gi 386869290 232 ELLQLKEQNQKMSSE 246
Cdd:COG4026 210 EVFSLEELWKELFPE 224
|
|
| CENP-K |
pfam11802 |
Centromere-associated protein K; CENP-K is one of seven new CENP-A-nucleosome distal (CAD) ... |
163-318 |
8.75e-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: 38.13 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 163 QGEVEEIEQHNKELCKENQElkdSCISLQKQnsdmqaELQKKQEELETLQSInkkLELKVKEQKDYWETELLQLKEQNQK 242
Cdd:pfam11802 59 TAELEQWQKRTPEIISLNPE---VLLTLGKE------ELQKLRHQLEMVLST---IQSKNKKLKEDLEREQQWLDEQQQI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869290 243 MSSENEKMGIRVDQlQAQLSTQEK--EMEKLVQGDQDKTEQLEQLKKE--NDHLFLSLTEQRKDQKKLEQTVEQMKQNET 318
Cdd:pfam11802 127 LESLNEKHKELKNQ-VVTFSEKRKfqELKTKIRKIKEYKEKLLTTLGEflDEHFPLPEENGNSVKKKRKNSQEPTINLIT 205
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
446-468 |
9.10e-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: 9.10e-03
|
| |
