|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
23-125 |
7.77e-46 |
|
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: 153.94 E-value: 7.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 23 VIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVtlPIDLNNKSAKQQEVQFKAYYLPKDD 102
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 5031937 103 -EYYQFCYVDEDGVVRGASIPFQF 125
Cdd:pfam17751 79 eGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
138-341 |
1.76e-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: 68.64 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 138 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQ 217
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE----ELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 218 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 297
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 5031937 298 KKQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRE 341
Cdd:COG4942 195 AERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-347 |
1.44e-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: 63.54 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 144 EIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSEN 223
Cdd:TIGR02168 233 RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL----QKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 224 EKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 303
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 5031937 304 MDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 347
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-346 |
1.11e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQK 218
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 219 MSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 298
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 5031937 299 KQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 346
Cdd:COG1196 408 AEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
144-391 |
1.70e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 144 EIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetellQLKEQNQKMSSEN 223
Cdd:COG3883 17 QIQAKQKEL----SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA-------EIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 224 EKMGIRVDQLQ------------------AQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQT 285
Cdd:COG3883 86 EELGERARALYrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 286 VEQMKQNETTAMKKQQELMDenfdlskRLSENEiicNALQRQKERLEGENDLLKRENSRLLSYmGLDFNSLPYQVPTSDE 365
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLA-------QLSAEE---AAAEAQLAELEAELAAAEAAAAAAAAA-AAAAAAAAAAAAAAAA 234
|
250 260
....*....|....*....|....*.
gi 5031937 366 GGARQNPGLAYGNPYSGIQESSSPSP 391
Cdd:COG3883 235 AAAAAAAAAASAAGAGAAGAAGAAAG 260
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
420-446 |
2.26e-09 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 2 (CALCOCO2) and similar proteins; CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. It acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. It may play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion. CALCOCO2 contains a C2H2-type zinc binding domain.
Pssm-ID: 412014 Cd Length: 27 Bit Score: 52.45 E-value: 2.26e-09
10 20
....*....|....*....|....*..
gi 5031937 420 FNCPICDKIFPATEKQIFEDHVFCHSL 446
Cdd:cd21968 1 FECPICSKIFEATSKQEFEDHVFCHSL 27
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-346 |
3.27e-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: 59.31 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQhnKELCKENQELKDSCISLQKQNSDMQAELQKKQEELE----TLQSINKKLELKVKEQKDYWETELLQLKE 214
Cdd:TIGR02169 217 LKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISelekRLEEIEQLLEELNKKIKDLGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 215 QNQKMSSEnekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEqtvEQMKQNET 294
Cdd:TIGR02169 295 KIGELEAE-------IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKE 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5031937 295 TAMKKQQELMDEnfdlSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 346
Cdd:TIGR02169 365 ELEDLRAELEEV----DKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-347 |
3.77e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 141 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMS 220
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 221 SENEkmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 300
Cdd:COG1196 376 EAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5031937 301 QELMDENFDLSKRLSENEiicNALQRQKERLEGENDLLKRENSRLLS 347
Cdd:COG1196 452 AELEEEEEALLELLAELL---EEAALLEAALAELLEELAEAAARLLL 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
133-345 |
4.31e-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: 57.85 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 133 ILVVTTQGEVEEIEQHNKELckenqelkdscISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQL 212
Cdd:COG4942 10 LLALAAAAQADAAAEAEAEL-----------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL----ARRIRAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 213 KEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLV-----QGDQDKTE-------------QLEQLKKENDHLFLSLTE 274
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrLGRQPPLAlllspedfldavrRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031937 275 QRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 345
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-345 |
7.54e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 174 QAELQKKQEELETLQSINKKLElkvkEQKDYWETELLQLkeQNQKMSSENEkmgIRVDQLQAQLSTQEKEMEKLVQGDQD 253
Cdd:COG4913 616 EAELAELEEELAEAEERLEALE----AELDALQERREAL--QRLAEYSWDE---IDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 254 ---KTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE-----NFDLSKRLsENEIICNALQ 325
Cdd:COG4913 687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEERF-AAALGDAVER 765
|
170 180
....*....|....*....|
gi 5031937 326 RQKERLEGENDLLKRENSRL 345
Cdd:COG4913 766 ELRENLEERIDALRARLNRA 785
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-345 |
1.05e-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: 57.76 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETL----QSINKKLELKVKEQKDYwETELLQLKE 214
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkQILRERLANLERQLEEL-EAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 215 QNQKMSSENEKMGIRVDQLQ-------AQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE 287
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5031937 288 QMKQNettamkkQQELMDENFDLSKRLSENEIicNALQRQKERLEGENDLLKRENSRL 345
Cdd:TIGR02168 411 RLEDR-------RERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERL 459
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-345 |
1.10e-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: 57.77 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 128 ENEEDILvvttQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET----LQSINKKLELKVKEQKD 203
Cdd:TIGR02169 687 KRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 204 YwETELLQLKEQNQKMSSENEKM-----GIRVDQLQAQLSTQEKE----------MEKLVQGDQDKTEQLEQLKKENDHL 268
Cdd:TIGR02169 763 L-EARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEvsriearlreIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 269 FLSLTEQRKDQKK----LEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 344
Cdd:TIGR02169 842 RIDLKEQIKSIEKeienLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
.
gi 5031937 345 L 345
Cdd:TIGR02169 922 L 922
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
141-316 |
1.35e-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: 56.95 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 141 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKvkEQKDYWETELLQLKEQNQKMS 220
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE--KEIDEKNKEIEELKQTQKSLK 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 221 SENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 300
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
170
....*....|....*.
gi 5031937 301 QELMDENFDLSKRLSE 316
Cdd:TIGR04523 662 PEIIKKIKESKTKIDD 677
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
172-347 |
2.78e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 172 DMQAELQKKQEELETLQSINKKLELKVKEqkdyWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGD 251
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 252 QDKTEQLEQLKKEndhlflsLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERL 331
Cdd:COG1196 312 RELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170
....*....|....*.
gi 5031937 332 EGENDLLKRENSRLLS 347
Cdd:COG1196 385 AEELLEALRAAAELAA 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-345 |
3.31e-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: 56.23 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 143 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET-LQSINKKLELKVKEQKDYWET------ELLQLKEQ 215
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAeIASLERSIAEKERELEDAEERlakleaEIDKLLAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 216 NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT------------EQLEQLKKENDHLFLSLTEQRKDQKK 281
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAelEEVDKEfaetrdelkdyrEKLEKLKREINELKRELDRLQEELQR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031937 282 LEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 345
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
129-339 |
3.75e-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: 55.83 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 129 NEEDILVVTTQGEVEEIEQHNKelcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET- 207
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETl 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 208 --ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQgdqdkteqlEQLKKENDHLFLSLTEQRKDQKKLEQT 285
Cdd:TIGR02168 385 rsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK---------KLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5031937 286 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 339
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
144-346 |
6.12e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 144 EIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN 223
Cdd:COG1196 233 KLRELEAELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 224 EKM---GIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 300
Cdd:COG1196 309 ERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5031937 301 QELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 346
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
139-345 |
6.99e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLE----LKVKEQKDYWETELLQ--- 211
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqekeLLEKEIERLKETIIKNnse 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 212 ---LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKE-------MEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKK 281
Cdd:TIGR04523 442 ikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031937 282 LEQTVEQM----KQNETTAMKKQQELMDENFDLSKRLSENEIicNALQRQKERLEGENDLLKRENSRL 345
Cdd:TIGR04523 522 LKEKIEKLesekKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
139-341 |
7.12e-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: 54.64 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQELKDSCISLQKQ-----NSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLK 213
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE----QISQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 214 EQNQKMSSENEKmgirvdqLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 293
Cdd:TIGR04523 349 KELTNSESENSE-------KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5031937 294 TTAMKKQQELMDENF-------DLSKRLSENEIICNALQRQKERLEGENDLLKRE 341
Cdd:TIGR04523 422 ELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-345 |
1.20e-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: 54.29 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 144 EIEQHNKELckenQELKDSCISLQKQnsdmQAELQKKQEELETLQSinkklelKVKEQKDYWETELLQLKEQNQKMSSEN 223
Cdd:TIGR02168 678 EIEELEEKI----EELEEKIAELEKA----LAELRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 224 EKMGIRVDQLQAQLSTQEKEMEklvqgdqdktEQLEQLKKENDHLflslTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 303
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIE----------ELEERLEEAEEEL----AEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 5031937 304 MDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 345
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
222-353 |
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 5031937 222 ENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQ 301
Cdd:COG2433 393 EEPEAEREKEHEERELTEEEEEIRRL-------EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 5031937 302 ELmdenfdlSKRlsENEIicNALQRQKERLEGENDLLKRENSRLLSYMGLDF 353
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 ... |
135-347 |
2.42e-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: 53.10 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 135 VVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSIN--KKLELK-VKEQKDYWETELLQ 211
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENqsYKQEIKnLESQINDLESKIQN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 212 LKEQNQKMSsenekmgIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE---- 287
Cdd:TIGR04523 403 QEKLNQQKD-------EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsr 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 288 QMKQNETTAMKKQQELMDENFDLSKrlseneiicnaLQRQKERLEGENDLLKRENSRLLS 347
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKK-----------LNEEKKELEEKVKDLTKKISSLKE 524
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-302 |
4.91e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 138 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQ----------KDYWE- 206
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 207 -------TELL-------QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL 272
Cdd:COG3883 108 llgsesfSDFLdrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190
....*....|....*....|....*....|.
gi 5031937 273 TEQRKD-QKKLEQTVEQMKQNETTAMKKQQE 302
Cdd:COG3883 188 SAEEAAaEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
173-345 |
4.98e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 173 MQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQ 252
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 253 DKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLE 332
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170
....*....|...
gi 5031937 333 GENDLLKRENSRL 345
Cdd:COG4372 164 EELAALEQELQAL 176
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
138-339 |
5.42e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 52.39 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 138 TQGEVEEIEQ-HNKELCKENQELKDSCislqKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQ----- 211
Cdd:COG5022 887 LKIDVKSISSlKLVNLELESEIIELKK----SLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNklhev 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 212 ---LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG------DQDKTEQLEQLKKENDHLflslteqrkdqkkl 282
Cdd:COG5022 963 eskLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELskqygaLQESTKQLKELPVEVAEL-------------- 1028
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 5031937 283 eQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 339
Cdd:COG5022 1029 -QSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLY 1084
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
123-340 |
7.59e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 123 FQFRPENEEDILVVTtqgevEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkeqk 202
Cdd:PRK03918 174 IKRRIERLEKFIKRT-----ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 203 dywetellQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKENDhLFLSLTEQRKDQKKL 282
Cdd:PRK03918 242 --------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL----EEKVKELKELKEKAE-EYIKLSEFYEEYLDE 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5031937 283 EQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKR 340
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
137-358 |
7.62e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 137 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLE---LKVKEQKDYWETELLQLK 213
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeelESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 214 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 293
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031937 294 TTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPY 358
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 ... |
36-332 |
9.59e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.51 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 36 GDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTfmwvtlpidLNNKSAKQQEVQ--FKAYYLPKDDEYYQfcyVDED 113
Cdd:pfam02463 75 AEVEITFDNEDHELPIDKEEVSIRRRVYRGGDSEYY---------INGKNVTKKEVAelLESQGISPEAYNFL---VQGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 114 GVVRGASIPFQFRPENEEDILVvttQGEVEEIEQHNKELCKENQELKdscislQKQNSDMQAELQKKQEELETLQSINKK 193
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAG---SRLKRKKKEALKKLIEETENLA------ELIIDLEELKLQELKLKEQAKKALEYY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 194 LELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLT 273
Cdd:pfam02463 214 QLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 5031937 274 EQRKDQKKLEQTveqmKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLE 332
Cdd:pfam02463 294 EEEELKSELLKL----ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
128-341 |
1.08e-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: 51.13 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 128 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK--EQKDYW 205
Cdd:pfam02463 807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEleEQKLKD 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 206 ETELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKLvqgdqdktEQLEQLKKENDHLFLSLtEQRKDQKKLEQT 285
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEES---QKLNLLEEKENEIEERIKE--------EAEILLKYEEEPEELLL-EEADEKEKEENN 954
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5031937 286 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRE 341
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-336 |
1.17e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLELKVKEQKDYWETELLQLKEQNQK 218
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA---ELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 219 MSsenekmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 298
Cdd:COG1196 399 AA--------QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 5031937 299 KQQELMDENFDLSKRLSENEIICNALQRQKERLEGEND 336
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
139-347 |
1.20e-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: 50.66 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETellqLKEQNQK 218
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKT----LTQRVLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 219 MSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 298
Cdd:pfam07888 148 RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5031937 299 KQqelmdenfdlskrlSENEIICNALQRQKERL---EGENDLLKRENSRLLS 347
Cdd:pfam07888 228 KE--------------AENEALLEELRSLQERLnasERKVEGLGEELSSMAA 265
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-331 |
1.60e-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: 50.83 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 138 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkEQKDYWETELLQLKEQNQ 217
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE----RRIAATERRLEDLEEQIE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 218 KMSSENEKmgirvdqLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 297
Cdd:TIGR02168 849 ELSEDIES-------LAAEIEELEELIEEL-------ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
170 180 190
....*....|....*....|....*....|....
gi 5031937 298 KKQQELMDENFDLSKRLSENEiicNALQRQKERL 331
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLE---VRIDNLQERL 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
130-336 |
3.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 130 EEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQnsdmQAELQKKQEELETLQSIN--KKLELKVKEQKDYWET 207
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK----EAEEKKKAEELKKAEEENkiKAAEEAKKAEEDKKKA 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 208 ELLQLKEQNQKMSSENEKmgirvdqlqaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE 287
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALK----------KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5031937 288 QMKQNETTAMKKQQELMDENFDLSKRLSENE-IICNALQRQKERLEGEND 336
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEaVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
128-332 |
3.34e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 128 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET 207
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 208 ELLQLKEQNQKMSSENEKMG---IRVDQLQAQLSTQEKEMEKLVQgdqdkteQLEQLKKENDHLFLSLTEQRKDQKKLEQ 284
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAAnlrERLESLERRIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELES 873
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5031937 285 TVE-------QMKQNETTAMKKQQELMDENFDLSKRLSENEiicNALQRQKERLE 332
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 ... |
137-336 |
3.79e-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: 49.40 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 137 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELK-VKEQKDY--WETELLQLK 213
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKnIKLSKDVssLESQLQDTQ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 214 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEqlkkendhlflSLTEQRKD-QKKLEQTVEQMKQN 292
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLS-----------TLQAQLSDmKKKLEEDAGTLEAL 543
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 5031937 293 ETTAMKKQQELMdenfDLSKRLSENEIICNALQRQKERLEGEND 336
Cdd:pfam01576 544 EEGKKRLQRELE----ALTQQLEEKAAAYDKLEKTKNRLQQELD 583
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
128-354 |
6.37e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 128 ENEEDILVVTTQGEVEEIEQHNKELckenQELKDScisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKD---- 203
Cdd:TIGR00606 722 EKRRDEMLGLAPGRQSIIDLKEKEI----PELRNK---LQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtim 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 204 ---YWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG-------DQDKTEQLEQLKKENDHL---FL 270
Cdd:TIGR00606 795 erfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKielnrklIQDQQEQIQHLKSKTNELkseKL 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 271 SLTEQRKDQKKL-EQTVEQMKQ----NETTAMKKQQELMDENFdLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 345
Cdd:TIGR00606 875 QIGTNLQRRQQFeEQLVELSTEvqslIREIKDAKEQDSPLETF-LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI 953
|
....*....
gi 5031937 346 LSYMGLDFN 354
Cdd:TIGR00606 954 HGYMKDIEN 962
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-347 |
6.68e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 176 ELQKKQEELETLQSINKKLELKVKEQKDywETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKT 255
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEEL--EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 256 EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEiicNALQRQKERLEGEN 335
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAE 371
|
170
....*....|..
gi 5031937 336 DLLKRENSRLLS 347
Cdd:COG1196 372 AELAEAEEELEE 383
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
142-293 |
7.06e-06 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 47.04 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 142 VEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSS 221
Cdd:pfam17078 68 LKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKL 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031937 222 ENEKmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 293
Cdd:pfam17078 148 ENEK---QLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKLDSLAQLLDLPSWLNLYPESR 216
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
110-336 |
8.95e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 110 VDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKElcKENQELKDSCISLQ----KQNSDMQAELQKKQEELE 185
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK--RELERIRQEEIAMEisrmRELERLQMERQQKNERVR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 186 TLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSENEKMgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEN 265
Cdd:pfam17380 396 QELEAARKVKILEEER----QRKIQQQKVEMEQIRAEQEEA--RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031937 266 DHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLS-ENEIICNALQRQKERLEGEND 336
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEkEMEERQKAIYEEERRREAEEE 541
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
139-349 |
1.12e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDM---QAELQKKQEEletLQSINKKLELKVKEQKDYwETELLQLKEQ 215
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEE---LEELNEQLQAAQAELAQA-QEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 216 NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT 295
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5031937 296 AMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYM 349
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-345 |
1.81e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 174 QAELQKKQEELETLQSINKKLELKVKEQK-DYWETELLQLKEqnqkmssENEKMGIRVDQLQAQLSTQEKEMEKL-VQGD 251
Cdd:COG4913 261 AERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRA-------ELARLEAELERLEARLDALREELDELeAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 252 QDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMK-------------QNETTAMK-----KQQELMDENFDLSKR 313
Cdd:COG4913 334 GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefaalRAEAAALLealeeELEALEEALAEAEAA 413
|
170 180 190
....*....|....*....|....*....|..
gi 5031937 314 LSEneiicnaLQRQKERLEGENDLLKRENSRL 345
Cdd:COG4913 414 LRD-------LRRELRELEAEIASLERRKSNI 438
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
141-347 |
1.81e-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: 47.32 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 141 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELEtlqsiNKKLELKVKEQkdywetELLQLKEQNQKMS 220
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE-----QKQKELKSKEK------ELKKLNEEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 221 SENEKMgirvDQLQAQLSTQEKEMEKLVQGDQDKTEQLE-QLKKENDHLFLSLTEQRKDQKklEQTVEQMKQNETTAMKK 299
Cdd:TIGR04523 510 EKVKDL----TKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKKENLEKEIDEK--NKEIEELKQTQKSLKKK 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5031937 300 Q-------QELMDENFDLSKRLSENEIicnalqrQKERLEGENDLLKRENSRLLS 347
Cdd:TIGR04523 584 QeekqeliDQKEKEKKDLIKEIEEKEK-------KISSLEKELEKAKKENEKLSS 631
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
422-444 |
2.21e-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: 2.21e-05
10 20
....*....|....*....|....
gi 5031937 422 CPICDKIFPATEKQ-IFEDHVFCH 444
Cdd:cd21965 1 CPICNKQFPPQVDQeAFEDHVESH 24
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
132-345 |
2.23e-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: 46.66 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 132 DILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQE-ELETLQSINKKLELKVKEQK----DYWE 206
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElEFEIQSQEQDSEIVKNSKSElariPELE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 207 TELLQLKEQNQKMSSENEKMGI---RVDQLQAQLSTQEKEMEKLVQGDQDKtEQLEQLKKENDHLFLSLTEQRKDQKKLE 283
Cdd:pfam05557 204 KELERLREHNKHLNENIENKLLlkeEVEDLKRKLEREEKYREEAATLELEK-EKLEQELQSWVKLAQDTGLNLRSPEDLS 282
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031937 284 QTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 345
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
143-320 |
2.55e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 143 EEIEQHNKELcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELL---------QLK 213
Cdd:COG4717 71 KELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeaelaelpeRLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 214 EQNQKMSSENEKMgIRVDQLQAQLSTQEKEMEKLVQGDQDKTE-QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN 292
Cdd:COG4717 150 ELEERLEELRELE-EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|....*...
gi 5031937 293 EttamkKQQELMDENFDLSKRLSENEII 320
Cdd:COG4717 229 L-----EQLENELEAAALEERLKEARLL 251
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-341 |
2.57e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 141 EVEEIEQHNKELCKENQELK-------------DSCISLQKQNSDMQAELQKKQEElETLQSINKKLELKVKEQKDYWET 207
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRkaeeakkaeeariEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 208 ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDhlflsltEQRKdqkkleqtVE 287
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKK--------AE 1705
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5031937 288 QMKQNETTAMKKQQELMDENfdlskrlSENEIICNALQRQKERLEGENDLLKRE 341
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAE-------EENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
143-296 |
3.40e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 143 EEIEQHNKELCKENQELKDSCISLQKQ-----------NSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQ 211
Cdd:COG3883 72 AEIAEAEAEIEERREELGERARALYRSggsvsyldvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 212 LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 291
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*
gi 5031937 292 NETTA 296
Cdd:COG3883 232 AAAAA 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
138-302 |
3.77e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 138 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET----LQSINKKLElKVKEQKDYWETELLQLK 213
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdeLKDYREKLE-KLKREINELKRELDRLQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 214 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLK----KENDHLFLSLTEQRKDQKKLEQTVEQM 289
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlsKYEQELYDLKEEYDRVEKELSKLQREL 492
|
170
....*....|...
gi 5031937 290 KQNETTAMKKQQE 302
Cdd:TIGR02169 493 AEAEAQARASEER 505
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
154-326 |
4.01e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 154 KENQELKDSCIS-----LQKQNSDMQAELQKKQEELetlqsinKKLELKVKEQKDYWETELlqlkEQNQKMSSENEKMGI 228
Cdd:PRK12704 49 KEAEAIKKEALLeakeeIHKLRNEFEKELRERRNEL-------QKLEKRLLQKEENLDRKL----ELLEKREEELEKKEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 229 RVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsltEQRKDQkkLEQTVEQMKQnETTAMKKQQElmDENF 308
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEIL--LEKVEEEARH-EAAVLIKEIE--EEAK 183
|
170
....*....|....*...
gi 5031937 309 DLSKRLSeNEIICNALQR 326
Cdd:PRK12704 184 EEADKKA-KEILAQAIQR 200
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
143-347 |
5.38e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 143 EEIEQHNKELCKENQEL---KDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKdyweTELLQLKEQ---- 215
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEIsntQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK----SEISDLNNQkeqd 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 216 -NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNET 294
Cdd:TIGR04523 308 wNKELKSELKNQEKKLEEIQNQISQNNKIISQL-------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5031937 295 TAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 347
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
185-344 |
5.88e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 185 ETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKE 264
Cdd:COG4372 31 EQLRKALFELD-KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 265 NDHLFLSLTEQRKDQKKLEQTVEQMKQnettamkKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 344
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEA-------QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
157-311 |
6.13e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 45.36 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 157 QELKDScisLQKQNSDmqAELQKKQEELEtlQSINKKL-ELKvkEQKDYWETELLQLKEQNQKMssenekmgIRVDQLQA 235
Cdd:pfam13779 496 ERLSEA---LERGASD--EEIAKLMQELR--EALDDYMqALA--EQAQQNPQDLQQPDDPNAQE--------MTQQDLQR 558
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031937 236 QLstqeKEMEKLVQ-GDQDKTEQ-LEQLKKENDHLFLSLTEQRKDQKKlEQTVEQMKQNETTaMKKQQELMDENFDLS 311
Cdd:pfam13779 559 ML----DRIEELARsGRRAEAQQmLSQLQQMLENLQAGQPQQQQQQGQ-SEMQQAMDELGDL-LREQQQLLDETFRQL 630
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-264 |
6.21e-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: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLEL---------KVKEQKDYWETEL 209
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQAELQRVEEEI 967
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 5031937 210 LQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKE 264
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI----LERIEEYEKKKRE 1018
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
134-291 |
6.47e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 134 LVVTTQGEVEEIEQHNKELCKENQELKDscISLQKQNSDMQAELQKKQEELETL---------QSINKKLEL-------- 196
Cdd:PRK04778 224 LQTELPDQLQELKAGYRELVEEGYHLDH--LDIEKEIQDLKEQIDENLALLEELdldeaeeknEEIQERIDQlydilere 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 197 -----KVKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT---- 255
Cdd:PRK04778 302 vkarkYVEKNSDTLPDFLEHAKEQNKELKEEidrvkqsytlNESELESVRQLEKQLESLEKQYDEITEriAEQEIAysel 381
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 5031937 256 --------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 291
Cdd:PRK04778 382 qeeleeilKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRN 425
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-341 |
8.92e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 141 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE-----TELLQLKE- 214
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADelkkaEELKKAEEk 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 215 ---QNQKMSSENEKMGIRVDQLQAQLSTQEKEmEKLVQGDQDKTEQLEQLKKENDHLFLSltEQRKDQKKLEQTVEQMKQ 291
Cdd:PTZ00121 1564 kkaEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKK 1640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5031937 292 NETTAMKKQQELMDENfdlskrlSENEIICNALQRQKERLEGENDLLKRE 341
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAE-------EENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-343 |
9.73e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 220 SSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKK 299
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 5031937 300 QQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENS 343
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-332 |
1.10e-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: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 137 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK---EQKDYWETELLQLK 213
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEEALALLR 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 214 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVqgdqdktEQLEQLKKENDHLFLSLTEQRKDqkkleqTVEQMKQNE 293
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLE-------LRLEGLEVRIDNLQERLSEEYSL------TLEEAEALE 960
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5031937 294 TTAMKKQQELMDENFDLSKRLSE----NEIICNALQRQKERLE 332
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYD 1003
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-343 |
1.27e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 175 AELQKKQEELETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMgirvdQLQAQLSTQEKEMEKLVQGDQDK 254
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 255 TEQLEQLKKEND---HLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ--------QELMDENFDLSKRLSENEIICNA 323
Cdd:COG4717 145 PERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEAQEELEE 224
|
170 180
....*....|....*....|
gi 5031937 324 LQRQKERLEGENDLLKRENS 343
Cdd:COG4717 225 LEEELEQLENELEAAALEER 244
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
130-347 |
1.29e-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: 44.58 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 130 EEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEE-------LETLQSINKKLELKVKEQK 202
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekekklQEEELKLLAKEEEELKSEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 203 DYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLflsltEQRKDQKKL 282
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL-----EQLEEELLA 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031937 283 EQTVEQmKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 347
Cdd:pfam02463 378 KKKLES-ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
141-318 |
1.80e-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: 44.27 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 141 EVEEIEQHNKELCKENQELKDScisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYW----ETEL----LQL 212
Cdd:TIGR00606 910 QDSPLETFLEKDQQEKEELISS---KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYlkqkETELntvnAQL 986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 213 KEQNQKMSSENEKMGIRVDQLQAQlstqeKEMEKLVQGD------QDKTEQLEQLKKENDHLF--LSLTEQRKDQKKLEQ 284
Cdd:TIGR00606 987 EECEKHQEKINEDMRLMRQDIDTQ-----KIQERWLQDNltlrkrENELKEVEEELKQHLKEMgqMQVLQMKQEHQKLEE 1061
|
170 180 190
....*....|....*....|....*....|....
gi 5031937 285 TVEQMKQNETTAMKKQQELMDENFDLSKRLSENE 318
Cdd:TIGR00606 1062 NIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
139-291 |
1.81e-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: 41.52 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQkkqeeletlqsinkKLELKVKEQKdywetellQLKEQNQK 218
Cdd:pfam12718 13 QERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVE--------------KLEEQLKEAK--------EKAEESEK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031937 219 MSSENEKMGIRVDQLQAQLSTQEKE----MEKLVQGDQdKTEQLEQLKKendhlflSLTEQR-KDQKKLEQTVEQMKQ 291
Cdd:pfam12718 71 LKTNNENLTRKIQLLEEELEESDKRlketTEKLRETDV-KAEHLERKVQ-------ALEQERdEWEKKYEELEEKYKE 140
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
166-345 |
1.90e-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: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 166 LQKQNSDMQAELQKKQEELETLQSINKKLELkvKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEME 245
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 246 KLVQGD--QDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNettamkKQQElmdenfdLSKRLSENEIICNA 323
Cdd:COG3206 258 ELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------LQQE-------AQRILASLEAELEA 324
|
170 180
....*....|....*....|..
gi 5031937 324 LQRQKERLEGENDLLKRENSRL 345
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAEL 346
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
169-352 |
1.95e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 169 QNSDMQAELQKKQEELETLQSinkKLELKVKEQKDywetellQLKEQNQKMSSENEkmgiRVDQLQAQLSTQEKEMEKL- 247
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERT---RAREQLRQAQA-------QLAQYNQVLASLKS----SYDAKRQMLQELKQELQDLg 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 248 VQGDQDKTEQLEQLKKENDHLfLSLTEQRKDQKKLEQTVEQMkqnETTAMKKQQELMDENFDLSKRLSENE--IICNALq 325
Cdd:PRK04863 1048 VPADSGAEERARARRDELHAR-LSANRSRRNQLEKQLTFCEA---EMDNLTKKLRKLERDYHEMREQVVNAkaGWCAVL- 1122
|
170 180
....*....|....*....|....*..
gi 5031937 326 rqkeRLEGENDLLKRENSRLLSYMGLD 352
Cdd:PRK04863 1123 ----RLVKDNGVERRLHRRELAYLSAD 1145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-338 |
2.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 150 KELCKENQELKDScislQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDyweteLLQLKEQNQKMSSENEKMGIR 229
Cdd:COG4717 74 KELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 230 VDQLQaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQ-KKLEQTVEQMKQNETTAMKKQQELMDENF 308
Cdd:COG4717 145 PERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190
....*....|....*....|....*....|
gi 5031937 309 DLSKRLSENEIICNALQRQKERLEGENDLL 338
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
143-345 |
2.04e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 143 EEIEQhnkelcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWEtELLQLKEQnqkmsse 222
Cdd:PRK02224 194 AQIEE------KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-ELETLEAE------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 223 nekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAmkkQQE 302
Cdd:PRK02224 260 -------IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL---RDR 329
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5031937 303 LMDENFDLSKRLSENEiicnALQRQKERLEGENDLLKRENSRL 345
Cdd:PRK02224 330 LEECRVAAQAHNEEAE----SLREDADDLEERAEELREEAAEL 368
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
197-305 |
2.15e-04 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 42.36 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 197 KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQ---AQLSTQEKEMEKLVQGDQDKT-EQLEQLKKENDHLFLSL 272
Cdd:pfam05010 12 KARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEktiAQMIEEKQKQKELEHAEIQKVlEEKDQALADLNSVEKSF 91
|
90 100 110
....*....|....*....|....*....|...
gi 5031937 273 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMD 305
Cdd:pfam05010 92 SDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA 124
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-365 |
2.22e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 166 LQKQNSDMQAELQKKQEELETLQSinkklELKVKEQKdywETELLQLKEQNQkmssenekmGIRVDQLQAQLSTQEKEME 245
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEA-----RLDALREE---LDELEAQIRGNG---------GDRLEQLEREIERLERELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 246 KLVQgdqdkteQLEQLKKENDHLFLSLTEQRKD----QKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSE--NEI 319
Cdd:COG4913 356 ERER-------RRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleAEI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5031937 320 icNALQRQKERLEGENDLLKREnsrLLSYMGLDFNSLPY-----QVPTSDE 365
Cdd:COG4913 429 --ASLERRKSNIPARLLALRDA---LAEALGLDEAELPFvgeliEVRPEEE 474
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
139-263 |
2.42e-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: 42.77 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEEL-------ETLQSINKkLELKVKEQKDYWETELLQ 211
Cdd:pfam15294 132 HMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQgakkdvkSNLKEISD-LEEKMAALKSDLEKTLNA 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031937 212 LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGD----------QDKTEQLEQLKK 263
Cdd:pfam15294 211 STALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTaayrnmkemlTKKNEQIKELRK 272
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
128-300 |
2.51e-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: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 128 ENEEDILVVTTQGEVEE-IEQHNKELCKenqeLKDSCISLQKQNSDMQAELQKKQEE-----------LETLQSINKKLE 195
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQlISEHEVEITG----LTEKASSARSQANSIQSQLEIIQEQarnqnsmymrqLSDLESTVSQLR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 196 LKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEN---------- 265
Cdd:pfam15921 331 SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNkrlwdrdtgn 410
|
170 180 190
....*....|....*....|....*....|....*....
gi 5031937 266 ----DHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 300
Cdd:pfam15921 411 sitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQ 449
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
144-291 |
3.00e-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: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 144 EIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETELLQlkeqnQKMSSEN 223
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE-STKEMLRKVVEELTA-----KKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 224 EKMgiRVDQLQAQLSTQEK-------EMEKLVQGDQDKTEQLEQLKKENDHLF----------LSLTEQRKDQKKLEQTV 286
Cdd:pfam15921 494 SER--TVSDLTASLQEKERaieatnaEITKLRSRVDLKLQELQHLKNEGDHLRnvqtecealkLQMAEKDKVIEILRQQI 571
|
....*
gi 5031937 287 EQMKQ 291
Cdd:pfam15921 572 ENMTQ 576
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-333 |
3.43e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 143 EEIEQHNKELCKENQELKdsciSLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWET---ELLQLKEQNQKM 219
Cdd:PRK03918 238 EEIEELEKELESLEGSKR----KLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKlseFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 220 SSENEKMGIRVDQLQAQLSTQE------KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLE-QTVEQMKQN 292
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKE 392
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 5031937 293 ETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEG 333
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
124-345 |
3.54e-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: 43.17 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 124 QFRPENEEDILVVTT------QGEVEEIEQ--HNKELckENQELK------DSCISLQKQNSDMQAELQKKQEELETLQS 189
Cdd:pfam05483 369 QQRLEKNEDQLKIITmelqkkSSELEEMTKfkNNKEV--ELEELKkilaedEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 190 INKK----LELK--------------VKEQKDYWETELLQLKE----------QNQKMSSENEKMGIRVDQLQAQLSTQE 241
Cdd:pfam05483 447 AREKeihdLEIQltaiktseehylkeVEDLKTELEKEKLKNIEltahcdklllENKELTQEASDMTLELKKHQEDIINCK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 242 KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQK-KLEQTVEQMKQNETTAMKKQqelmdenfdlsKRLSENEII 320
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKE-----------KQMKILENK 595
|
250 260
....*....|....*....|....*
gi 5031937 321 CNALQRQKERLEGENDLLKRENSRL 345
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKAL 620
|
|
| CCDC14 |
pfam15254 |
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ... |
146-243 |
3.57e-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: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 146 EQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLeLKVKE-QKDY----------WETELLQLKE 214
Cdd:pfam15254 412 EQEKTEKTSGSGDCNLELFSLQSLNMSLQNQLQESLKSQELLQSKNEEL-LKVIEnQKEEnkkltkifkeKEQTLLENKQ 490
|
90 100 110
....*....|....*....|....*....|...
gi 5031937 215 Q----NQKMSSENEKMGIRVDQLQAQLSTQEKE 243
Cdd:pfam15254 491 QfdieTTRVKIELEEALVNMKSFQFKLEAAEKE 523
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
134-312 |
3.63e-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: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 134 LVVTTQGEVEEIEQHNKELCK----------ENQELKDSCISLQKQNSDMQA---ELQKKQEELETL-QSINKKLEL--- 196
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKlrsrvdlklqELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILrQQIENMTQLvgq 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 197 ------KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFL 270
Cdd:pfam15921 581 hgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN 660
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5031937 271 SLTEQRKDQKKLEQTVEQMKQN--------ETTAMKKQQELMDENFDLSK 312
Cdd:pfam15921 661 EVKTSRNELNSLSEDYEVLKRNfrnkseemETTTNKLKMQLKSAQSELEQ 710
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-334 |
3.66e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 143 EEIEQHNKEL--CKENQELKDSCISLQKQNSDmqaELQKKQEELETLQSINKKLElkvkeqkDYWETELLQLKEQNQKms 220
Cdd:TIGR02169 170 RKKEKALEELeeVEENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKR-------EYEGYELLKEKEALER-- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 221 senekmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLF-----LSLTEQRKDQKKLEQTVEQMKQNETT 295
Cdd:TIGR02169 238 --------QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdLGEEEQLRVKEKIGELEAEIASLERS 309
|
170 180 190
....*....|....*....|....*....|....*....
gi 5031937 296 AMKKQQELMdenfDLSKRLSENEIICNALQRQKERLEGE 334
Cdd:TIGR02169 310 IAEKERELE----DAEERLAKLEAEIDKLLAEIEELERE 344
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
174-306 |
4.39e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 174 QAELQKKQEELEtLQSINKKLELKVKEqkdywetELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKlvqgdqd 253
Cdd:PRK12704 39 EAKRILEEAKKE-AEAIKKEALLEAKE-------EIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDR------- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 5031937 254 KTEQLEQLKKEndhlflsLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE 306
Cdd:PRK12704 101 KLELLEKREEE-------LEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
172-291 |
4.50e-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: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 172 DMQAELQKKQEELETLQSI-NKKLELK--VKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLS 238
Cdd:pfam06160 260 EAEEALEEIEERIDQLYDLlEKEVDAKkyVEKNLPEIEDYLEHAEEQNKELKEElervqqsytlNENELERVRGLEKQLE 339
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031937 239 TQEKEMEKLVQGDQDKT--------------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 291
Cdd:pfam06160 340 ELEKRYDEIVERLEEKEvayselqeeleeilEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKL 406
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
138-304 |
5.09e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 138 TQGEVEEIEQHNKELCKENQELKDSCISLQKQN-SDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET--------- 207
Cdd:pfam10174 85 AQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENfRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGArdesikkll 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 208 ELLQLKEQNQKMSSENEKMGIR-------VDQLQAQLSTQEKEMEKL---------VQGDQDKTEQLEQLKKENDHLFLS 271
Cdd:pfam10174 165 EMLQSKGLPKKSGEEDWERTRRiaeaemqLGHLEVLLDQKEKENIHLreelhrrnqLQPDPAKTKALQTVIEMKDTKISS 244
|
170 180 190
....*....|....*....|....*....|...
gi 5031937 272 LTEQRKDqkkLEQTVEQMKQNETTAMKKQQELM 304
Cdd:pfam10174 245 LERNIRD---LEDEVQMLKTNGLLHTEDREEEI 274
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
126-319 |
6.06e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 126 RPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEEletlQSINKKLELKvKEQKDYW 205
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE----ERKRKKLELE-KEKRDRK 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 206 ETELL-------QLKEQNQKMSSENEKMGIrvdqlqaqlstQEKEME---KLVQGDQDKTEQLEQLKKENDhlflsLTEQ 275
Cdd:pfam17380 488 RAEEQrrkilekELEERKQAMIEEERKRKL-----------LEKEMEerqKAIYEEERRREAEEERRKQQE-----MEER 551
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 5031937 276 RKDQKKLEQTVEQMKQNEttAMKKQQELMDENFDLSKRLSENEI 319
Cdd:pfam17380 552 RRIQEQMRKATEERSRLE--AMEREREMMRQIVESEKARAEYEA 593
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
144-329 |
6.13e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 144 EIEQHNKELCKENQELkdsCISLQKQNSDMQAE---LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMS 220
Cdd:TIGR00618 708 ELETHIEEYDREFNEI---ENASSSLGSDLAARedaLNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 221 SENEKMGIRVDQLQAQLSTQEKEM-EKLVQGDQDKTEQLEQLKKENDHLflsLTEQRKDQKKLEQTVEQMKQNETTaMKK 299
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQF---LSRLEEKSATLGEITHQLLKYEEC-SKQ 860
|
170 180 190
....*....|....*....|....*....|
gi 5031937 300 QQELMDENFDLSKRLSENEIIcNALQRQKE 329
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 ... |
141-291 |
7.10e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 141 EVEEIEQhnkELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLEL-------KVKEQkdywETELLQLK 213
Cdd:pfam01576 72 ELEEILH---ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLekvtteaKIKKL----EEDILLLE 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031937 214 EQNQKMSSENEKMGIRVDQLQAQLSTQEkemeklvqgdqDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 291
Cdd:pfam01576 145 DQNSKLSKERKLLEERISEFTSNLAEEE-----------EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR 211
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
182-304 |
7.15e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 182 EELETLQSINKKLELKVKEQKDYWETELLQLKEQNQK----MSSENEKMGIRVDQLQAQLstqeKEMEKLVQGDQDKTEQ 257
Cdd:pfam05622 282 EKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRrkneLETQNRLANQRILELQQQV----EELQKALQEQGSKAED 357
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 5031937 258 LEQLKKENDHLFLSLTE-QRKDQKKLEQTVEQMKQNETTAMKKQQELM 304
Cdd:pfam05622 358 SSLLKQKLEEHLEKLHEaQSELQKKKEQIEELEPKQDSNLAQKIDELQ 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
144-303 |
7.40e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 144 EIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetelLQLKEQNQKMSSEN 223
Cdd:COG1579 18 ELDRLEHRLKELPAELAE----LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA------RIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 224 EKMgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKD----QKKLEQTVEQMKQNETTAMKK 299
Cdd:COG1579 88 NKE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEELEAE 164
|
....
gi 5031937 300 QQEL 303
Cdd:COG1579 165 REEL 168
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
173-340 |
8.40e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 173 MQAELQKKQEELETLQS---INKKLELKVKEQKDYWeTELLQLK-----EQNQKMSSENekmgirvDQLQAQLStqekem 244
Cdd:PRK04863 926 IVSVLQSDPEQFEQLKQdyqQAQQTQRDAKQQAFAL-TEVVQRRahfsyEDAAEMLAKN-------SDLNEKLR------ 991
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 245 EKLVQGDQDKTEQLEQLKK------ENDHLFLSLTE--QRKDQ--KKLEQTVEQMKQNETTAMKKQQELMDEnfDLSKRL 314
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQaqaqlaQYNQVLASLKSsyDAKRQmlQELKQELQDLGVPADSGAEERARARRD--ELHARL 1069
|
170 180
....*....|....*....|....*..
gi 5031937 315 SENEIICNALQRQKERLEGE-NDLLKR 340
Cdd:PRK04863 1070 SANRSRRNQLEKQLTFCEAEmDNLTKK 1096
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
109-263 |
8.90e-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: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 109 YVDED----GVVRGASI----------------PFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDscislqk 168
Cdd:COG2433 362 DVDRDevkaRVIRGLSIeealeeliekelpeeePEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 169 qnsdmqaELQKKQEELEtlqsinkKLELKVKEQKdywetellqlKEQNQKMSSENE--KMGIRVDQLQAQLSTQEKEMEK 246
Cdd:COG2433 435 -------ELEEKDERIE-------RLERELSEAR----------SEERREIRKDREisRLDREIERLERELEEERERIEE 490
|
170
....*....|....*..
gi 5031937 247 LvqgdQDKTEQLEQLKK 263
Cdd:COG2433 491 L----KRKLERLKELWK 503
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
138-345 |
9.60e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 138 TQGEVEEIEQHNKELCKENQELKDSC---ISLQKQNSDMQAELQKKQEELEtlqSINKKLELKVKEQkdywetellqlKE 214
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLAARKQELE---EILHELESRLEEE-----------EE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 215 QNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvQGDQDKTEQleQLKKENDHLfLSLTEQR----KDQKKLEQTVEQMK 290
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL-QLEKVTTEA--KIKKLEEDI-LLLEDQNsklsKERKLLEERISEFT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031937 291 QNET---------TAMKKQQELMDEnfDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 345
Cdd:pfam01576 166 SNLAeeeekakslSKLKNKHEAMIS--DLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
167-341 |
1.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 167 QKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEK 246
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 247 LVQGDQDKTEQL---EQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNA 323
Cdd:PTZ00121 1614 KAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
|
170
....*....|....*...
gi 5031937 324 LQRQKERLEGENDLLKRE 341
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKE 1711
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
141-335 |
1.11e-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: 41.63 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 141 EVEEIEQHNKELCKENQELKDSCiSLQKQNSDMQAELQKKQE------------------------ELETLQSINKKLEL 196
Cdd:pfam05483 135 KLEEEIQENKDLIKENNATRHLC-NLLKETCARSAEKTKKYEyereetrqvymdlnnniekmilafEELRVQAENARLEM 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 197 KVKEQKDYweTELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKL---VQGDQDKTEQLEQLKKENDHlflSLT 273
Cdd:pfam05483 214 HFKLKEDH--EKIQHLEEEYKKEINDKEK---QVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDE---NLK 285
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031937 274 EQRKDQKKLEQTVEQMKQNETTAMKKQQELmDENFDLSKRlseneIICNALQRQKERLEGEN 335
Cdd:pfam05483 286 ELIEKKDHLTKELEDIKMSLQRSMSTQKAL-EEDLQIATK-----TICQLTEEKEAQMEELN 341
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
157-347 |
1.23e-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: 40.29 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 157 QELKDSCISLQKQNSDMQAELQKKQEELETLQsinKKLELKvkeqkdywETELLQLKEQNQKMSSENEKMGIRVDQLQAQ 236
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALE---ARLEAA--------KTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 237 LSTQ--EKEMEKLvqgdqdkTEQLEQLKKENDHLflslteqRKDQKKLEQTVEQMKQNETTAMKKQQELMDEnfdLSKRL 314
Cdd:COG1579 82 LGNVrnNKEYEAL-------QKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAE---LEEKK 144
|
170 180 190
....*....|....*....|....*....|....
gi 5031937 315 SENEIICNALQRQKERLEGE-NDLLKRENSRLLS 347
Cdd:COG1579 145 AELDEELAELEAELEELEAErEELAAKIPPELLA 178
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
131-345 |
1.25e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 131 EDILVVTTQGEVEEIeqhNKELCKE-NQELKDscISLQKQNSDMQAELQKK-QEELETLQSIN-KKLELKVkeqkdyweT 207
Cdd:PHA02562 157 EDLLDISVLSEMDKL---NKDKIRElNQQIQT--LDMKIDHIQQQIKTYNKnIEEQRKKNGENiARKQNKY--------D 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 208 ELLQlKEQNQKMSsenekmgirVDQLQAQLSTQEKEME-------KLVQGDQDKTEQLEQLKKEndHLFL-------SLT 273
Cdd:PHA02562 224 ELVE-EAKTIKAE---------IEELTDELLNLVMDIEdpsaalnKLNTAAAKIKSKIEQFQKV--IKMYekggvcpTCT 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5031937 274 EQRKDQ-KKLEQTVEQMKQNET------TAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 345
Cdd:PHA02562 292 QQISEGpDRITKIKDKLKELQHslekldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
143-355 |
1.44e-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: 40.96 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 143 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQsinKKLElKVKEQKDYWETELLQLKEQNQKMSSE 222
Cdd:pfam10174 355 EEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ---KKIE-NLQEQLRDKDKQLAGLKERVKSLQTD 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 223 NEKMGIRVDQLQAQLSTQEKEMEKLVQ----GDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT--- 295
Cdd:pfam10174 431 SSNTDTALTTLEEALSEKERIIERLKEqrerEDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlas 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031937 296 -AMKKQQELMDENFDLSKRLSEneiiCNALQRQkerlegendLLKRENSRLLSYMGLDFNS 355
Cdd:pfam10174 511 sGLKKDSKLKSLEIAVEQKKEE----CSKLENQ---------LKKAHNAEEAVRTNPEIND 558
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
143-290 |
1.46e-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: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 143 EEIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELK---VKEQKDY--WETELLQLKEQNQ 217
Cdd:COG1579 31 AELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnVRNNKEYeaLQKEIESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031937 218 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDhlfLSLTEQRKDQKKLEQTVEQMK 290
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAEL-------EAELEEKKAELD---EELAELEAELEELEAEREELA 169
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
168-329 |
1.49e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 168 KQNSDMQAELQKKQEELET---LQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKmgirVDQLQAQLSTQEKEM 244
Cdd:PRK12705 39 LQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK----LDNLENQLEEREKAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 245 EklvqgdqDKTEQLEQLKKENDHLFLSLTEQRKDQ------KKLEQTVEQMKQNETTAMKkqqelmdENFDLSKRLSENE 318
Cdd:PRK12705 115 S-------ARELELEELEKQLDNELYRVAGLTPEQarklllKLLDAELEEEKAQRVKKIE-------EEADLEAERKAQN 180
|
170
....*....|.
gi 5031937 319 IICNALQRQKE 329
Cdd:PRK12705 181 ILAQAMQRIAS 191
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
177-341 |
1.51e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 177 LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN---EKMGI--RVDQLQAQLSTQEKEMEKLvqgD 251
Cdd:PRK04778 200 LDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGyhlDHLDIekEIQDLKEQIDENLALLEEL---D 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 252 QDKTE-QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE--NFDLSKRLSENEI-ICNALQRQ 327
Cdd:PRK04778 277 LDEAEeKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEidRVKQSYTLNESELeSVRQLEKQ 356
|
170
....*....|....
gi 5031937 328 KERLEGENDLLKRE 341
Cdd:PRK04778 357 LESLEKQYDEITER 370
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
165-303 |
1.57e-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: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 165 SLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywETELLQLKEQNQKMSSENEKMGIR-------VDQLQAQL 237
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQI 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031937 238 STQEKEMEKLVQGDQDKTE--------QLEQLKKENDHL---FLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 303
Cdd:COG3206 301 AALRAQLQQEAQRILASLEaelealqaREASLQAQLAQLearLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
129-344 |
1.59e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 129 NEEDILVV----TTQGEVEEIEQHNKELckenqelkdscISLQKQNSDMQAELQKKQEELETLQSINK--------KLEL 196
Cdd:PRK11281 55 EAEDKLVQqdleQTLALLDKIDRQKEET-----------EQLKQQLAQAPAKLRQAQAELEALKDDNDeetretlsTLSL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 197 KVKEQKdyWETELLQLK--------------------EQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKLVqgdqdkTE 256
Cdd:PRK11281 124 RQLESR--LAQTLDQLQnaqndlaeynsqlvslqtqpERAQAALYANSQ---RLQQIRNLLKGGKVGGKALR------PS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 257 QLEQLKKENDHLFLSLTEQRKDqkkLE-----QTVEQMKQNETTAmkKQQELMDENFDL-----SKRLSENEIICNALQR 326
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDLQRKS---LEgntqlQDLLQKQRDYLTA--RIQRLEHQLQLLqeainSKRLTLSEKTVQEAQS 267
|
250
....*....|....*....
gi 5031937 327 QKERLE-GENDLLKRENSR 344
Cdd:PRK11281 268 QDEAARiQANPLVAQELEI 286
|
|
| FtsL2 |
COG4839 |
Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning]; |
163-204 |
1.72e-03 |
|
Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443867 Cd Length: 123 Bit Score: 38.40 E-value: 1.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 5031937 163 CISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDY 204
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 ... |
143-341 |
1.93e-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: 40.93 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 143 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLElkvkeqkdywetellqlKEQNQKMSSE 222
Cdd:pfam01576 204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLE-----------------EETAQKNNAL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 223 NekmgiRVDQLQAQLSTQEKEME-------KLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMK---QN 292
Cdd:pfam01576 264 K-----KIRELEAQISELQEDLEseraarnKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkalEE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 293 ETTAMKKQ-QEL----------MDENFDLSKRLSENeiicnaLQRQKERLEGENDLLKRE 341
Cdd:pfam01576 339 ETRSHEAQlQEMrqkhtqaleeLTEQLEQAKRNKAN------LEKAKQALESENAELQAE 392
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
142-345 |
2.22e-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: 40.42 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 142 VEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKE----------QKDYWETELLQ 211
Cdd:TIGR00606 669 ITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglapgrqsIIDLKEKEIPE 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 212 LKEQNQKMSSENEKMGIRVDQLQAQLST--QEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQrKDQKKLEQTVEQM 289
Cdd:TIGR00606 749 LRNKLQKVNRDIQRLKNDIEEQETLLGTimPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK-LQGSDLDRTVQQV 827
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5031937 290 KQnettamkKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 345
Cdd:TIGR00606 828 NQ-------EKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
177-339 |
2.65e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.22 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 177 LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN---EKMGI--RVDQLQAQLstqEKEMEKLVQGD 251
Cdd:pfam06160 181 LEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGyalEHLNVdkEIQQLEEQL---EENLALLENLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 252 QDKTEQ-LEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE--NFDLSKRLSENEI-ICNALQRQ 327
Cdd:pfam06160 258 LDEAEEaLEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEEleRVQQSYTLNENELeRVRGLEKQ 337
|
170
....*....|..
gi 5031937 328 KERLEGENDLLK 339
Cdd:pfam06160 338 LEELEKRYDEIV 349
|
|
| Mod_r |
pfam07200 |
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ... |
136-264 |
2.68e-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: 37.98 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 136 VTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkklelkvkeqkdYWETELLQLKEQ 215
Cdd:pfam07200 22 VHSLPQVKALQAEKEELLAENESLAEENLSLEPELEELRSQLQELLEELKALKS--------------EYEEKEQELDEL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 5031937 216 NQKMSSENEKMgirvdQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKE 264
Cdd:pfam07200 88 LSKFSPDALLA-----RLQAAAAEAEEESEALAESFLEGEIDLDEFLKQ 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-341 |
2.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 142 VEEIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETELLQLkeqnqKMSS 221
Cdd:PRK03918 517 LEELEKKAEEY----EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD-ELEEELAELLKELEEL-----GFES 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 222 ENEkmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHL---FLSLTEQRKDQKKLEQTVEQMKQNETTamK 298
Cdd:PRK03918 587 VEE-----LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELdkaFEELAETEKRLEELRKELEELEKKYSE--E 659
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5031937 299 KQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRE 341
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
184-288 |
2.84e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 39.14 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 184 LETLQSINKkLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKK 263
Cdd:pfam11932 19 LDLAEKAVA-AAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASL----ERQIEEIERTER 93
|
90 100
....*....|....*....|....*
gi 5031937 264 ENDHLFLSLTEQrkdqkkLEQTVEQ 288
Cdd:pfam11932 94 ELVPLMLKMLDR------LEQFVAL 112
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
137-237 |
2.89e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.05 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 137 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkeqkdywetELLQLKEqn 216
Cdd:pfam10473 49 NSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESLNSSLE------------NLLEEKE-- 114
|
90 100
....*....|....*....|.
gi 5031937 217 QKMSSENEKMGIRVDQLQAQL 237
Cdd:pfam10473 115 QEKVQMKEESKTAVEMLQTQL 135
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
199-345 |
3.37e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 199 KEQKDYWETELLQLKEQNQKMSSENE------KMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL 272
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031937 273 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSK---RLSENEIICNALQRQKERLEGENDLLKRENSRL 345
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtLLAAIADAEDEIERLREKREALAELNDERRERL 629
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
137-320 |
3.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 137 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQ- 215
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQa 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 216 --NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 293
Cdd:COG4372 185 ldELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
170 180
....*....|....*....|....*..
gi 5031937 294 TTAMKKQQELMDENFDLSKRLSENEII 320
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEA 291
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
206-343 |
3.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 206 ETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHL----------------- 268
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeaeieerreelgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 269 ----------------------FLS---------------LTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLS 311
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdFLDrlsalskiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190
....*....|....*....|....*....|..
gi 5031937 312 KRLSENEIICNALQRQKERLEGENDLLKRENS 343
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
142-345 |
4.06e-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: 39.19 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 142 VEEIEQHNKELCKENQELKDSCIslqkqnsdmQAELQKKQEELET--LQSINKK-------LELKVKEQKDYWET--ELL 210
Cdd:pfam02841 102 VELLEAKKDDFLKQNEEASSKYC---------SALLQDLSEPLEEkiSQGTFSKpggyklfLEERDKLEAKYNQVprKGV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 211 QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKlvqgDQDKTEQLEQLKKEndhlflslteQRKDQKKLEQTVEQMK 290
Cdd:pfam02841 173 KAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEA----ERAKAEAAEAEQEL----------LREKQKEEEQMMEAQE 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 291 QNETTAMKKQQELMDEnfDLSKRLSENE-IICNALQRQKERL-EG---ENDLLKRENSRL 345
Cdd:pfam02841 239 RSYQEHVKQLIEKMEA--EREQLLAEQErMLEHKLQEQEELLkEGfktEAESLQKEIQDL 296
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-344 |
4.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 141 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE-----TELLQLKEQ 215
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakkkAEEKKKADE 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 216 NQKMSSENEKMGIRVDQLQAQLSTQE---KEMEKLVQGDQDKTEQLEqlKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN 292
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADeakKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5031937 293 EttaMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 344
Cdd:PTZ00121 1474 E---AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
164-327 |
4.83e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 164 ISLQKQNSDMQAELQKKQEELetlQSINKKL-------ELKVKEQKDYWETELLQLKEQN--QKMSSENEkmgirvDQLQ 234
Cdd:PRK11281 152 VSLQTQPERAQAALYANSQRL---QQIRNLLkggkvggKALRPSQRVLLQAEQALLNAQNdlQRKSLEGN------TQLQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 235 AQLSTQEKEMeklvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKklEQTVEQMKQNETTAMKK-----QQELmDENFD 309
Cdd:PRK11281 223 DLLQKQRDYL----------TARIQRLEHQLQLLQEAINSKRLTLS--EKTVQEAQSQDEAARIQanplvAQEL-EINLQ 289
|
170
....*....|....*...
gi 5031937 310 LSKRLSENEIICNALQRQ 327
Cdd:PRK11281 290 LSQRLLKATEKLNTLTQQ 307
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
144-305 |
5.75e-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: 39.32 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 144 EIEQHNKELCKEN----QELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKlELKVKEQKDYWETELLQLKEQNQ-- 217
Cdd:pfam05483 489 ELTAHCDKLLLENkeltQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK-EMNLRDELESVREEFIQKGDEVKck 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 218 -KMSSENEK-MGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT 295
Cdd:pfam05483 568 lDKSEENARsIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
170
....*....|
gi 5031937 296 AMKKQQELMD 305
Cdd:pfam05483 648 AKQKFEEIID 657
|
|
| CENP-K |
pfam11802 |
Centromere-associated protein K; CENP-K is one of seven new CENP-A-nucleosome distal (CAD) ... |
139-294 |
6.58e-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: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 139 QGEVEEIEQHNKELCKENQElkdSCISLQKQnsdmqaELQKKQEELETLQSInkkLELKVKEQKDYWETELLQLKEQNQK 218
Cdd:pfam11802 59 TAELEQWQKRTPEIISLNPE---VLLTLGKE------ELQKLRHQLEMVLST---IQSKNKKLKEDLEREQQWLDEQQQI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 219 MSSENEKMGIRVDQlQAQLSTQEK--EMEKLVQGDQDKTEQLEQLKKE--NDHLFLSLTEQRKDQKKLEQTVEQMKQNET 294
Cdd:pfam11802 127 LESLNEKHKELKNQ-VVTFSEKRKfqELKTKIRKIKEYKEKLLTTLGEflDEHFPLPEENGNSVKKKRKNSQEPTINLIT 205
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
134-347 |
6.60e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 134 LVVTTQGEVEEIEQHN--KELCKENQELK---DSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEqkdywETE 208
Cdd:PRK04863 481 LVRKIAGEVSRSEAWDvaRELLRRLREQRhlaEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-----EDE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 209 LLQLKEQnqkmssenekmgirvdqLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQ 288
Cdd:PRK04863 556 LEQLQEE-----------------LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQ 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5031937 289 MKQNETTAmkkqQELMdenfDLSKRLSENEiicNALQRQKERLEGENDLLKRENSRLLS 347
Cdd:PRK04863 619 SGEEFEDS----QDVT----EYMQQLLERE---RELTVERDELAARKQALDEEIERLSQ 666
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
145-332 |
6.82e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 37.58 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 145 IEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKlelkvkeqkdywetELLQLKEQNQKMSSENE 224
Cdd:pfam13851 3 MKNHEKAF----NEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEK--------------LMSEIQQENKRLTEPLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 225 KMGIRVDQLQAQLSTQEK---EMEKLVQGDQDKTEQLEQLKKENDHLFLSLT--EQRKDQ--KKLEQTVEQMKQ---NET 294
Cdd:pfam13851 65 KAQEEVEELRKQLENYEKdkqSLKNLKARLKVLEKELKDLKWEHEVLEQRFEkvERERDElyDKFEAAIQDVQQktgLKN 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5031937 295 TAMKKQQELMDENFD-----LSKRLSENEIICNALQRQKERLE 332
Cdd:pfam13851 145 LLLEKKLQALGETLEkkeaqLNEVLAAANLDPDALQAVTEKLE 187
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
74-281 |
6.89e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.76 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 74 WVTLPIDLnnKSAKQQE-VQFKAYYLPKDdeyyqfcYVDEDGVVRGASIPFQFRPENEEDILVVTTqgEVEEIEQHNKEL 152
Cdd:PRK05771 129 WGNFDLDL--SLLLGFKyVSVFVGTVPED-------KLEELKLESDVENVEYISTDKGYVYVVVVV--LKELSDEVEEEL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 153 CK---ENQELKDSCISLQkqnsdmqaELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEqnqKMSSENEKmgir 229
Cdd:PRK05771 198 KKlgfERLELEEEGTPSE--------LIREIKEELEEIEKERESLLEELKELAKKYLEELLALYE---YLEIELER---- 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5031937 230 vdqlqAQLSTQEKEMEKL--VQG--DQDKTEQLEQL--KKENDHLFLSLTEQRKDQKK 281
Cdd:PRK05771 263 -----AEALSKFLKTDKTfaIEGwvPEDRVKKLKELidKATGGSAYVEFVEPDEEEEE 315
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
168-312 |
7.00e-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: 39.00 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 168 KQNSDMQA---ELQKKQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQ---KMSSENEKMGIRVDQLQAQLSTQE 241
Cdd:pfam01576 2 RQEEEMQAkeeELQKVKERQQKAESELKELEKKHQQLCE----EKNALQEQLQaetELCAEAEEMRARLAARKQELEEIL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031937 242 KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQE----LMDENFDLSK 312
Cdd:pfam01576 78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdillLEDQNSKLSK 152
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
234-370 |
7.02e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 234 QAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsLTEQRKD----QKKLEQTVEQMKQNETTAMKKQQELMDENFD 309
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKE-------LRERRNElqklEKRLLQKEENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031937 310 LSKRLSEneiicnaLQRQKERLEgenDLLKRENSRLLSYMGLdfnslpyqvpTSDEggARQ 370
Cdd:PRK12704 119 LEQKQQE-------LEKKEEELE---ELIEEQLQELERISGL----------TAEE--AKE 157
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
141-342 |
7.18e-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: 39.00 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 141 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQA----ELQKKQEELEtlqsinKKLELKVKEQKDYwETELLQLKEQN 216
Cdd:pfam01576 693 QVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAqferDLQARDEQGE------EKRRQLVKQVREL-EAELEDERKQR 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 217 QKMSSENEKMGIRVDQLQAQLSTQE-------KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQM 289
Cdd:pfam01576 766 AQAVAAKKKLELDLKELEAQIDAANkgreeavKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQL 845
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5031937 290 KQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKREN 342
Cdd:pfam01576 846 QEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEEL 898
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
128-222 |
7.56e-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: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 128 ENEEDILVVttQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET 207
Cdd:COG4026 132 ELREELLEL--KEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLL 209
|
90
....*....|....*
gi 5031937 208 ELLQLKEQNQKMSSE 222
Cdd:COG4026 210 EVFSLEELWKELFPE 224
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
128-329 |
7.60e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.80 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 128 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELEtlqsINKKLELKVKEQKDYWET 207
Cdd:pfam02463 341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE----LKSEEEKEAQLLLELARQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 208 ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlfLSLTEQRKDQKKLEQTVE 287
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL-----LKETQLVKLQEQLELLLS 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 5031937 288 QMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKE 329
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
422-444 |
8.48e-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: 8.48e-03
10 20
....*....|....*....|....
gi 5031937 422 CPICDKIFPA-TEKQIFEDHVFCH 444
Cdd:pfam18112 3 CPLCGEMFSPnIDQSEFEEHVESH 26
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
124-347 |
8.79e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.80 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 124 QFRPENEEDILVvTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKD 203
Cdd:pfam02463 257 KQEIEKEEEKLA-QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 204 YWETELLQLKEQNQKMSSENEKM---------------------GIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLK 262
Cdd:pfam02463 336 EIEELEKELKELEIKREAEEEEEeeleklqekleqleeellakkKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 263 KENDHL-------FLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGEN 335
Cdd:pfam02463 416 QLEDLLkeekkeeLEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
250
....*....|..
gi 5031937 336 DLLKRENSRLLS 347
Cdd:pfam02463 496 EERSQKESKARS 507
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
172-336 |
9.23e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 37.50 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 172 DMQAELQKKQEELETLQSINKKLELKVKEQKDY---WETELLQLKEQN----------QKMSSENEkmgirVDQLQAQLS 238
Cdd:COG1842 34 DMEEDLVEARQALAQVIANQKRLERQLEELEAEaekWEEKARLALEKGredlarealeRKAELEAQ-----AEALEAQLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 239 TQEKEMEKLVQGDQDKTEQLEQLKKENDhLFLSLTEQRKDQKKLEQTVEQMKQNETTA----MKKQQELMDENFDLSKRL 314
Cdd:COG1842 109 QLEEQVEKLKEALRQLESKLEELKAKKD-TLKARAKAAKAQEKVNEALSGIDSDDATSalerMEEKIEEMEARAEAAAEL 187
|
170 180
....*....|....*....|..
gi 5031937 315 SENeiicNALQRQKERLEGEND 336
Cdd:COG1842 188 AAG----DSLDDELAELEADSE 205
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
142-291 |
9.94e-03 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 38.01 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031937 142 VEEIEQHNKELCKEnqeLKDSCISLQKqnsdMQAELQKKQEELETL-QSINKKLElkvkeqkdyweTELLQLKEQNQKMS 220
Cdd:pfam10498 224 LEQMKQHKKSIEES---LPDTKSQLDK----LHTDISKTLEKIESReKYINSQLE-----------PLIQEYREAQDELS 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5031937 221 SENEKMgirvDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQkKLEQTVEQMKQ 291
Cdd:pfam10498 286 EVQEKY----KQLSEGVTERTRELAEI-------TEELEKVKQEMEERGSSMTDGSPLV-KIKQALTKLKE 344
|
|
| |
