|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-338 |
6.44e-12 |
|
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: 70.09 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 107 DDNNLEKAEKERKY-EVEMAYND--GELERLKQLVKELEEREVKLEGELLEY-YGLKEQESDIVELQRQLKIKTVEIDML 182
Cdd:TIGR02168 270 EELRLEVSELEEEIeELQKELYAlaNEISRLEQQKQILRERLANLERQLEELeAQLEELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 183 NITINSLQAE----RKKLQEELSQNGIVRKELEVARNKIKELQRQIqldaNQTKGQLLLLKQHVSSLQMKEEEAMNKDTE 258
Cdd:TIGR02168 350 KEELESLEAEleelEAELEELESRLEELEEQLETLRSKVAQLELQI----ASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 259 VERKL--KAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNmtESDKVAKVREEVNNLKHNNEDLLKQVEG 336
Cdd:TIGR02168 426 LLKKLeeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ--ALDAAERELAQLQARLDSLERLQENLEG 503
|
..
gi 42565189 337 LQ 338
Cdd:TIGR02168 504 FS 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
116-340 |
8.30e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 116 KERKYEVE--MAYNDGELERLKQLVKELEEREVKLEGE---LLEYYGLKEQES---------DIVELQRQLKIKTVEIDM 181
Cdd:TIGR02168 171 KERRKETErkLERTRENLDRLEDILNELERQLKSLERQaekAERYKELKAELRelelallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 182 LNITINSLQAERKKLQEELSQN-----------GIVRKELEVARNKIKELQRQIQ--------LDANQTKGQLLLLKQHV 242
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELrlevseleeeiEELQKELYALANEISRLEQQKQilrerlanLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 243 SSLQMKEEEAMNKD------TEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNmtesdKVAKV 316
Cdd:TIGR02168 331 KLDELAEELAELEEkleelkEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-----EIERL 405
|
250 260
....*....|....*....|....
gi 42565189 317 REEVNNLKHNNEDLLKQVEGLQMN 340
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKK 429
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
127-319 |
9.33e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 9.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 127 NDGELERLKQLVKELEEREVKLEGELLEyygLKEQESDIVELQRQLKIKTVEIDMLNITIN--SLQAERKKLQEELSQng 204
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEE---LEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAE-- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 205 iVRKELEVARNKIKELQRQIQldanqtkgQLLLLKQHVSSLQMKEEEAMNKDTEVERklKAVQDLEVQVMELKRKNRELQ 284
Cdd:COG4717 144 -LPERLEELEERLEELRELEE--------ELEELEAELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELE 212
|
170 180 190
....*....|....*....|....*....|....*
gi 42565189 285 HEKRELSIKLDSAEARIATLSNMTESDKVAKVREE 319
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
86-349 |
4.44e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 86 DDILPEFEDLLSG--EIEYPLPDDDNNLEKAEKE-RKYEVEMAYNDGELERLKQLVKELEEREVKLEGELleyyglKEQE 162
Cdd:TIGR02168 708 EELEEELEQLRKEleELSRQISALRKDLARLEAEvEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL------AEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 163 SDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHV 242
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN---LRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 243 SSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnmteSDKVAKVREEVNN 322
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL-----REKLAQLELRLEG 933
|
250 260
....*....|....*....|....*..
gi 42565189 323 LKHNNEDLLKQVEGLQMNRFSEVEELV 349
Cdd:TIGR02168 934 LEVRIDNLQERLSEEYSLTLEEAEALE 960
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-304 |
7.00e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 128 DGELERLKQLVKELEEREVKLEGELLEYYG-LKEQESDIVELQRQL-----KIKTVEIDMLNITINSLQAERKKLQEELS 201
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSeLKELEARIEELEEDLhkleeALNDLEARLSHSRIPEIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 202 QNGIVRKELEVARNKiKELQRQIQLDANQTK-GQLLLLKQHVSSLQmKEEEAMNK-----DTEVERKLKAVQDLEVQVME 275
Cdd:TIGR02169 809 RIEARLREIEQKLNR-LTLEKEYLEKEIQELqEQRIDLKEQIKSIE-KEIENLNGkkeelEEELEELEAALRDLESRLGD 886
|
170 180
....*....|....*....|....*....
gi 42565189 276 LKRKNRELQHEKRELSIKLDSAEARIATL 304
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKK 915
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-352 |
1.08e-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: 59.30 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 130 ELERLKQLVKELEEREVKLEGELLEYYGLKEQ-ESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRK 208
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEElEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 209 ELEVarnKIKELQRQIqldaNQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDlevQVMELKRKNRELQHEKR 288
Cdd:TIGR02168 758 ELEA---EIEELEERL----EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42565189 289 ELSIKLDSAEARIATLSNMTE--SDKVAKVREEVNNLKHNNEDLLKQVEGLQMNRFSEVEELVYLR 352
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEelSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-350 |
4.06e-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: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 112 EKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYGLKEqesdivELQRQLKIKTVEIDMLNITINSLQA 191
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS------RLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 192 ErkkLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQ---TKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKA--- 265
Cdd:TIGR02168 324 Q---LEELESKLDELAEELAELEEKLEELKEELESLEAEleeLEAELEELESRLEELEEQLETLRSKVAQLELQIASlnn 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 266 -VQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARiatlsnmTESDKVAKVREEVNNLKHNNEDLLKQVEGLQmNRFSE 344
Cdd:TIGR02168 401 eIERLEARLERLEDRRERLQQEIEELLKKLEEAELK-------ELQAELEELEEELEELQEELERLEEALEELR-EELEE 472
|
....*.
gi 42565189 345 VEELVY 350
Cdd:TIGR02168 473 AEQALD 478
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-348 |
4.46e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 111 LEK-AEKERKYeveMAYNDgELERLKQ--LVKELEEREVKLEGELLEyygLKEQESDIVELQRQLKIKTVEIDMLNITIN 187
Cdd:COG1196 205 LERqAEKAERY---RELKE-ELKELEAelLLLKLRELEAELEELEAE---LEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 188 SLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAmnkDTEVERKLKAVQ 267
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL---EEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 268 DLEVQVMELKRKNRELQHEKRELSIKLDSAEARIAtlsnmTESDKVAKVREEVNNLKHNNEDLLKQVEGLQMNRFSEVEE 347
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
.
gi 42565189 348 L 348
Cdd:COG1196 430 L 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
91-348 |
4.76e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 91 EFEDLLSGEIEYPLPDDDNNLEKAEKERK-YEVEMAYNDGELERLK----QLVKELEEREVKLEGELLEYYGLKEQEsdI 165
Cdd:TIGR02169 212 RYQALLKEKREYEGYELLKEKEALERQKEaIERQLASLEEELEKLTeeisELEKRLEEIEQLLEELNKKIKDLGEEE--Q 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 166 VELQRQLKIKTVEIDMLNITINSLQAERKKLQEElsqngivRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSL 245
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEER-------LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 246 QMKEEEAMNKDTEVERKLKA----VQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNmtesdKVAKVREEVN 321
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAEtrdeLKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA-----AIAGIEAKIN 437
|
250 260
....*....|....*....|....*..
gi 42565189 322 NLKHNNEDLLKQVEGLQMNRFSEVEEL 348
Cdd:TIGR02169 438 ELEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
114-317 |
5.96e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 114 AEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELleyyglKEQESDIVELQRQLKIKTVEIDMLNITINSLQAER 193
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL------AALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 194 KKLQEELSQNGIVRKELEVA------------------------------------RNKIKELQRQIQLDANQTKGQLLL 237
Cdd:COG4942 93 AELRAELEAQKEELAELLRAlyrlgrqpplalllspedfldavrrlqylkylaparREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 238 LKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVR 317
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-338 |
9.82e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 112 EKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELleyyglKEQESDIVELQRQLKIKTVEIDmlnitinSLQA 191
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI------EELEELIEELESELEALLNERA-------SLEE 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 192 ERKKLQEELSQngiVRKELEVARNKIKELQRQIQldanqtkgqllLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEV 271
Cdd:TIGR02168 888 ALALLRSELEE---LSEELRELESKRSELRRELE-----------ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42565189 272 QVMELKRKNRELqhEKRELSIKLDSAEARIATLS--NMTESDKVAKVREEVNNLKHNNEDLLKQVEGLQ 338
Cdd:TIGR02168 954 EEAEALENKIED--DEEEARRRLKRLENKIKELGpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-337 |
1.61e-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: 55.45 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 120 YEVEMAYNDGELERLKQLVKELEEREVKLEGELLEY--------YGLKEQESDIVELQRQLKIKTVEIDMLNITINSLQA 191
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELeeeleqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 192 ERKKLQEELSQNgivRKELEVARNKIKELQRQI---QLDANQTKGQLLLLKQHVSSLQMK----EEEAMNKDTEVERKLK 264
Cdd:TIGR02168 755 ELTELEAEIEEL---EERLEEAEEELAEAEAEIeelEAQIEQLKEELKALREALDELRAEltllNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42565189 265 AVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTE--SDKVAKVREEVNNLKHNNEDLLKQVEGL 337
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEalLNERASLEEALALLRSELEELSEELREL 906
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
108-338 |
3.51e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 108 DNNLEKAEKE-RKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYG--------LKEQESDIVELQRQLKIKTVE 178
Cdd:COG1196 252 EAELEELEAElAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarleerRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 179 IDMLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAM----N 254
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEeaeeA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 255 KDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnmteSDKVAKVREEVNNLKHNNEDLLKQV 334
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL-----LELLAELLEEAALLEAALAELLEEL 486
|
....
gi 42565189 335 EGLQ 338
Cdd:COG1196 487 AEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
144-392 |
5.96e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 144 REVKLEGELLEYYG--------LKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQngiVRKELEVARN 215
Cdd:TIGR02169 640 RMVTLEGELFEKSGamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE---LSQELSDASR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 216 KIKELQRQIQL---DANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKL-----------KAVQDLEV-----QVMEL 276
Cdd:TIGR02169 717 KIGEIEKEIEQleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeeleedlhkleEALNDLEArlshsRIPEI 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 277 KRKNRELQHEKRELSIKLDSAEARIATLSNMTES----------------DKVAKVREEVNNLKHNNEDLLKQVEGLQMN 340
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYlekeiqelqeqridlkEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 42565189 341 RFSEVEELVYLRWVNACLRYELRNYQTPAGKISA-----RDLSKNLSPKSQAKAKRL 392
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAqiekkRKRLSELKAKLEALEEEL 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
104-300 |
7.76e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 104 LPDDDNNLEKAEKER-KYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYG-LKEQESDIVELQRQLKIKTVEIDM 181
Cdd:TIGR02169 317 LEDAEERLAKLEAEIdKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAeLEEVDKEFAETRDELKDYREKLEK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 182 LNITINSLQAERKKLQEELSQngiVRKELEVARNKIKELQRQIqldanqtkgqllllKQHVSSLQMKEEEAMNKDTEVER 261
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQR---LSEELADLNAAIAGIEAKI--------------NELEEEKEDKALEIKKQEWKLEQ 459
|
170 180 190
....*....|....*....|....*....|....*....
gi 42565189 262 KLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEAR 300
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
109-338 |
1.38e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 109 NNLEK----AEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEgelleyyglkEQESDIVELQRQLKIKTVEIDMLNI 184
Cdd:TIGR04523 357 ENSEKqrelEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ----------NQEKLNQQKDEQIKKLQQEKELLEK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 185 TINSLQAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLK 264
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKD---LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 265 AVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDK-----------VAKVREEVNNLKHNNEDLLKQ 333
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelkkenlekeIDEKNKEIEELKQTQKSLKKK 583
|
....*
gi 42565189 334 VEGLQ 338
Cdd:TIGR04523 584 QEEKQ 588
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
111-319 |
4.90e-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: 50.51 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 111 LEKAEKERKYEvEMAYNDGELERLKQLVKELEEREVKLEGELLEYyglKEQESDIVELQRQL-------------KIKTV 177
Cdd:pfam17380 293 FEKMEQERLRQ-EKEEKAREVERRRKLEEAEKARQAEMDRQAAIY---AEQERMAMERERELerirqeerkreleRIRQE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 178 EIDMLNITINSLQaerkKLQEELSQ-NGIVRKELEVARN-KIKELQRQIQLDANQTKGQLLLLKQHVS---SLQMKEEEA 252
Cdd:pfam17380 369 EIAMEISRMRELE----RLQMERQQkNERVRQELEAARKvKILEEERQRKIQQQKVEMEQIRAEQEEArqrEVRRLEEER 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42565189 253 MN-----KDTEVERKlKAVQDLEVQVMELKRKNRELQHEKRElsiKLDSAEARIATLSNMTESDKVAKVREE 319
Cdd:pfam17380 445 ARemervRLEEQERQ-QQVERLRQQEEERKRKKLELEKEKRD---RKRAEEQRRKILEKELEERKQAMIEEE 512
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
165-323 |
9.41e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 165 IVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSS 244
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQ---LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 245 LQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQH-------EKRELSIKLDSAEARIATLSNMTESDKVAKVR 317
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSeiaereeELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
....*.
gi 42565189 318 EEVNNL 323
Cdd:COG4372 183 QALDEL 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
158-338 |
1.54e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 158 LKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNgivRKELEVARNKIKELQRQI--QLDANQTKG-- 233
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---QAEIAEAEAEIEERREELgeRARALYRSGgs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 234 ----QLLLLKQHVSSLqMKEEEAMNKDTEVERKLkaVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnmte 309
Cdd:COG3883 102 vsylDVLLGSESFSDF-LDRLSALSKIADADADL--LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL----- 173
|
170 180
....*....|....*....|....*....
gi 42565189 310 SDKVAKVREEVNNLKHNNEDLLKQVEGLQ 338
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
130-326 |
1.72e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 130 ELERLKQLVKELEEREVKLEgELLEYYGLKEQESDIVELQRQLK------IKTVEIDMLNITINSLQAERKKLQEELSQn 203
Cdd:COG4913 236 DLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRaalrlwFAQRRLELLEAELEELRAELARLEAELER- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 204 giVRKELEVARNKIKELQRQIQLDANQTKGQlllLKQHVSSLQMKEEEAMNKDTEVERKLKAV--------QDLEVQVME 275
Cdd:COG4913 314 --LEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALglplpasaEEFAALRAE 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 42565189 276 LKRKNRELQHEKRELSIKLDSAEARIATLSNmtesdKVAKVREEVNNLKHN 326
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRR-----ELRELEAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
170-341 |
1.77e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 170 RQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQI-----QLDANQTKGQLLLLKQHVSS 244
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELeklekLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 245 LQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEK--------RELSIKLDSAEARIATLSNmtesdKVAKV 316
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslateeelQDLAEELEELQQRLAELEE-----ELEEA 218
|
170 180
....*....|....*....|....*
gi 42565189 317 REEVNNLKHNNEDLLKQVEGLQMNR 341
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEE 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
109-326 |
2.19e-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: 48.53 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 109 NNLEKAEKERKYEVEmaYNDGELERLKQLVKELEEREVKLEGELLEYYGLKEqesdivELQRQLKIKTVEIDMLNITINS 188
Cdd:TIGR02169 815 REIEQKLNRLTLEKE--YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE------ELEEELEELEAALRDLESRLGD 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 189 LQAERKKLQEELSQNGIVRKELEVARNKIKELQrqiqldaNQTKGQLLLLKQHVSSLQ--MKEEEAMNKDTEVERKLKA- 265
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRL-------SELKAKLEALEEELSEIEdpKGEDEEIPEEELSLEDVQAe 959
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42565189 266 VQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnMTESDKVAKVREEVNNLKHN 326
Cdd:TIGR02169 960 LQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL--EEERKAILERIEEYEKKKRE 1018
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
111-288 |
2.21e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 111 LEKAEKERKYEVEmAYND--GELERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVE---LQRQLKIKTVEIDMLNIT 185
Cdd:COG4717 76 LEEELKEAEEKEE-EYAElqEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleaLEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 186 InslqAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQTkgqlllLKQHVSSLQMKEEEAMNKDTEVERKLKA 265
Cdd:COG4717 155 L----EELRELEEELEE---LEAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180
....*....|....*....|...
gi 42565189 266 VQDLEVQVMELKRKNRELQHEKR 288
Cdd:COG4717 222 LEELEEELEQLENELEAAALEER 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
128-304 |
2.76e-05 |
|
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: 46.46 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 128 DGELERLKQLVKELEERevklegelleyygLKEQESDIVELQRQLKIKTVEIDmlnitinSLQAERKKLQEELSQngiVR 207
Cdd:COG1579 16 DSELDRLEHRLKELPAE-------------LAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEE---VE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 208 KELEVARNKIKELQRQIQLDANQtkGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDlevqvmELKRKNRELQHEK 287
Cdd:COG1579 73 ARIKKYEEQLGNVRNNKEYEALQ--KEIESLKRRISDLEDEILELMERIEELEEELAELEA------ELAELEAELEEKK 144
|
170
....*....|....*..
gi 42565189 288 RELSIKLDSAEARIATL 304
Cdd:COG1579 145 AELDEELAELEAELEEL 161
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-348 |
2.82e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 112 EKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELL---EYYGLKEQESDIVELQRQLKI--------KTVEID 180
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkesELIKLKELAEQLKELEEKLKKynleelekKAEEYE 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 181 MLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRqiqldanqtkgQLLLLKQHVSSLQMKEEEamnkdtEVE 260
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE-----------ELAELLKELEELGFESVE------ELE 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 261 RKLKAVQDLEVQVMELKRKNRELQHEKRELSI---KLDSAEARIATLSNMTEsdkvaKVREEVNNLKHN-NEDLLKQVEG 336
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKELEREEKELKKleeELDKAFEELAETEKRLE-----ELRKELEELEKKySEEEYEELRE 666
|
250
....*....|..
gi 42565189 337 LQMNRFSEVEEL 348
Cdd:PRK03918 667 EYLELSRELAGL 678
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
112-304 |
3.26e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.37 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 112 EKAEKERKYEVEMAYNDgeleRLKQLVKELEEREVKLEGELLEYYG--------LKEQESDIVELQRQLKIKTVEIDMLN 183
Cdd:pfam19220 49 RLLELEALLAQERAAYG----KLRRELAGLTRRLSAAEGELEELVArlakleaaLREAEAAKEELRIELRDKTAQAEALE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 184 itiNSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIqldaNQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKL 263
Cdd:pfam19220 125 ---RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGEL----ATARERLALLEQENRRLQALSEEQAAELAELTRRL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42565189 264 K-----------AVQDLEVQVME-----------LKRKNRELQHEKRELSIKLDSAEARIATL 304
Cdd:pfam19220 198 AeletqldatraRLRALEGQLAAeqaereraeaqLEEAVEAHRAERASLRMKLEALTARAAAT 260
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-347 |
3.40e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 132 ERLKQLVKELEEREVKLEGELLEYYGLKEQesdIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELsqngivrKELE 211
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEEL---IKEKEKELEEVLREINEISSELPELREELEKLEKEV-------KELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 212 VARNKIKELQRQIQLdanqTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEvqvmELKRKNRELQHEKRELS 291
Cdd:PRK03918 235 ELKEEIEELEKELES----LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK----EKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 42565189 292 IKLDSAEARIATLSNMTESdkVAKVREEVNNLKHNNEDLLKQVEGLQmNRFSEVEE 347
Cdd:PRK03918 307 DELREIEKRLSRLEEEING--IEERIKELEEKEERLEELKKKLKELE-KRLEELEE 359
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
99-324 |
4.06e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 99 EIEYPLPDDDNNLEKAEKERK-----------YEVEMAYNDGELERLKQLVKELEER--EVKLEGELLE-----YYGLKE 160
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKeleelkeeieeLEKELESLEGSKRKLEEKIRELEERieELKKEIEELEekvkeLKELKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 161 QESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIqldaNQTKGQLLLLkq 240
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL----EELEERHELY-- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 241 hvsslqmkeEEAMNKDTEVERKLKAVQDLEVQvmELKRKNRELQHEKRELSIKLDSAEARIATLSNmtesdKVAKVREEV 320
Cdd:PRK03918 365 ---------EEAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKK-----EIKELKKAI 428
|
....
gi 42565189 321 NNLK 324
Cdd:PRK03918 429 EELK 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
161-338 |
4.59e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 161 QESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEEL------------------SQNGIVRKELEVARNKIKELQR 222
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLaalerriaalarriraleQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 223 QI---------QLDANQTKGQ----LLLLKQHvSSLQMKEEEAMNKDTEVERKlKAVQDLEVQVMELKRKNRELQHEKRE 289
Cdd:COG4942 98 ELeaqkeelaeLLRALYRLGRqpplALLLSPE-DFLDAVRRLQYLKYLAPARR-EQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 42565189 290 LSIKLDSAEARIATLSNMTES--DKVAKVREEVNNLKHNNEDLLKQVEGLQ 338
Cdd:COG4942 176 LEALLAELEEERAALEALKAErqKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-321 |
4.89e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 128 DGELERLKQLVKELEEREVKLEGElleyygLKEQESDIVELQRQLKiktvEIDmlNITINSLQAERKKLQEELsqngivr 207
Cdd:COG4913 294 EAELEELRAELARLEAELERLEAR------LDALREELDELEAQIR----GNG--GDRLEQLEREIERLEREL------- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 208 KELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEamnkdteverklkAVQDLEVQVMELKRKNRELQHEK 287
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE-------------ELEALEEALAEAEAALRDLRREL 421
|
170 180 190
....*....|....*....|....*....|....
gi 42565189 288 RELSIKLDSAEARIatlSNMTEsdKVAKVREEVN 321
Cdd:COG4913 422 RELEAEIASLERRK---SNIPA--RLLALRDALA 450
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
137-352 |
5.30e-05 |
|
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: 47.41 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 137 LVKELEEREVKLEgELL--EYYGLKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQngivRKELEVAR 214
Cdd:pfam05483 350 VVTEFEATTCSLE-ELLrtEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----DEKLLDEK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 215 NKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMkeeEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKl 294
Cdd:pfam05483 425 KQFEKIAEELKGKEQELIFLLQAREKEIHDLEI---QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE- 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 42565189 295 dsAEARIATLSNMTESDKvaKVREEVNNLKHNNEDLLKQVEGLQMNRFSEVEELVYLR 352
Cdd:pfam05483 501 --NKELTQEASDMTLELK--KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
132-345 |
6.92e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 132 ERLKQLVKELEEREVKLEgellEYyglkEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQngiVRKELE 211
Cdd:COG3206 182 EQLPELRKELEEAEAALE----EF----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA---LRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 212 VARNKIKEL----------QRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNR 281
Cdd:COG3206 251 SGPDALPELlqspviqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREA 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42565189 282 ELQHEKRELSIKLDSAEARIATLSNMTesdkvakvrEEVNNLKHNNEDLLKQVEGLQMNRFSEV 345
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELRRLE---------REVEVARELYESLLQRLEEARLAEALTV 385
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
107-245 |
9.90e-05 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 45.38 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 107 DDNNLEKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEyyglkeqesdiveLQRQLKIKTVEIDMLNITI 186
Cdd:pfam14932 45 EGAALDEALKTISAESPGLLNQQDVEALEESLEEIREATEDLEAELQE-------------LQKTKQLKINRLNKLQAQA 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 42565189 187 NSLQAERKKLQEELSQngivrkelevARNKIKELQRQIQLDANQTKGQLLLLKQHVSSL 245
Cdd:pfam14932 112 SSLSQGLRALVAEEEE----------AAKQLEELQEELAALNAKTNNVLQSLQSEVKEL 160
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
112-335 |
1.06e-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: 46.58 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 112 EKAEKERKYEVEMAYNDGELERLKQLVKELEEREvKLEGELLEYYGLKEQ-ESDIVELQRQLKIKTVEIDMLNITInSLQ 190
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEE-ESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDR-TVQ 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 191 AERKKLQEELSQNGIVRKELEVARNKIKELQRQIQL---DANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQ 267
Cdd:TIGR00606 826 QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHlksKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42565189 268 DLEVQVMELKRKNRELQHEKRELSIKLDSaeariatlSNMTESDKVAKVREEVNNLKHNNEDLLKQVE 335
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKET--------SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
130-264 |
1.06e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 44.12 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 130 ELERLKQLVKELEEREVKLEGELleyyglKEQESDIVELQRQLKiktveiDMLNITINSLQAERKKLQEELSQngiVRKE 209
Cdd:pfam15619 68 EVRVLRERLRRLQEKERDLERKL------KEKEAELLRLRDQLK------RLEKLSEDKNLAEREELQKKLEQ---LEAK 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 42565189 210 LEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLK 264
Cdd:pfam15619 133 LEDKDEKIQDLERKLELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
135-337 |
1.10e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 135 KQLVKELEEREVKLEGELLEYYGLKEQESDIVELQ----RQLKIKTVEIDMLNITINSLQAERKKLQEELSQ-------- 202
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQnkikKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlnnqkeqd 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 203 -NGIVRKELEVARNKIKELQRQIqldaNQTKGQLLLLKQHVSSLqmkEEEAMNKDTEVERKLKavqdlevqvmELKRKNR 281
Cdd:TIGR04523 308 wNKELKSELKNQEKKLEEIQNQI----SQNNKIISQLNEQISQL---KKELTNSESENSEKQR----------ELEEKQN 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42565189 282 ELQHEKRELSIKLDSA---EARIATL-SNMTESDKVAKVREE-VNNLKHNNEDLLKQVEGL 337
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIknlESQINDLeSKIQNQEKLNQQKDEqIKKLQQEKELLEKEIERL 431
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
112-347 |
1.11e-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: 46.19 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 112 EKAEKERKYEVEMAYNDgELERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLKIKTVEI-----DMLN--- 183
Cdd:TIGR00606 229 KEAQLESSREIVKSYEN-ELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtdEQLNdly 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 184 ----ITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEE-EAMNKDTE 258
Cdd:TIGR00606 308 hnhqRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLElDGFERGPF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 259 VERKLKAVQDLEVQVMELKRKN-----RELQHEKRELSIKLDSAEARIATLSNMTESDKVaKVREEVNNLKHNNEDlLKQ 333
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTaaqlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKE-ILEKKQEELKFVIKE-LQQ 465
|
250
....*....|....
gi 42565189 334 VEGlQMNRFSEVEE 347
Cdd:TIGR00606 466 LEG-SSDRILELDQ 478
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
113-317 |
1.31e-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: 46.26 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 113 KAEKERKY-EVEMAYNDGELERLKqLVKELEER-----EVKLEGELL--EYYGLKEQESDIVE----LQRQLKIKTVEID 180
Cdd:pfam15921 613 KDKKDAKIrELEARVSDLELEKVK-LVNAGSERlravkDIKQERDQLlnEVKTSRNELNSLSEdyevLKRNFRNKSEEME 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 181 MlniTINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKqhvSSLQMKEEEAMNKDTE-- 258
Cdd:pfam15921 692 T---TTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQ---SKIQFLEEAMTNANKEkh 765
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42565189 259 --VERKLKAVQDLEVQVME----------LKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVR 317
Cdd:pfam15921 766 flKEEKNKLSQELSTVATEknkmagelevLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-348 |
1.61e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 50 LNDKNLQEEEEEEEEEVKLINSVINQTRGSFSDyLDDDIlpefeDLLSGEIEyplpDDDNNLEKA-EKERKYEVEMAYND 128
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAE-LEAEL-----EELRLELE----ELELELEEAqAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 129 GELERLKQLVKELEEREVKLEGELLEYYG-LKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNgivR 207
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---E 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 208 KELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEK 287
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42565189 288 RELSIKLDSAEARIATLsnmteSDKVAKVREEVNNLKhNNEDLLKQVEGLQMNRFSEVEEL 348
Cdd:COG1196 459 EALLELLAELLEEAALL-----EAALAELLEELAEAA-ARLLLLLEAEADYEGFLEGVKAA 513
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-341 |
1.78e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 111 LEKAEKERKYEVEMAYNDGE-LERLKQLVKELEEREV-------KLEGELLEYYGLKEQESDIVELQRQLKIKTVEIdml 182
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEeKKKAEELKKAEEENKIkaaeeakKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA--- 1701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 183 nitiNSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTK------------GQLLLLKQHVSSLQMKEE 250
Cdd:PTZ00121 1702 ----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEeakkdeeekkkiAHLKKEEEKKAEEIRKEK 1777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 251 EAMNKD----------TEVERKLKAVQDLEVQVMELKRKNRELQHEKRELsikLDSAEARIATLSNMT--ESDKVAKVRE 318
Cdd:PTZ00121 1778 EAVIEEeldeedekrrMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM---EDSAIKEVADSKNMQleEADAFEKHKF 1854
|
250 260 270
....*....|....*....|....*....|....*..
gi 42565189 319 EVNNL--------------KHNNEDLLKQVEGLQMNR 341
Cdd:PTZ00121 1855 NKNNEngedgnkeadfnkeKDLKEDDEEEIEEADEIE 1891
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
128-301 |
3.74e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 128 DGELERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLkIKTVEIDMLNITINSLQAERKKLQEELSQNGIVR 207
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQSPVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 208 KELevaRNKIKELQRQIQldaNQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRK---NREL- 283
Cdd:COG3206 294 IAL---RAQIAALRAQLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREvevARELy 367
|
170 180
....*....|....*....|...
gi 42565189 284 -----QHEKRELSIKLDSAEARI 301
Cdd:COG3206 368 esllqRLEEARLAEALTVGNVRV 390
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
93-229 |
5.48e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 93 EDLLSGEIEYPLPDDDNNLEKAEKE-----RKYEVEMAYNDGELERLKQLVKEL----EEREVKLEGELLEYYGLKEQES 163
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHeerelTEEEEEIRRLEEQVERLEAEVEELeaelEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42565189 164 DIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEEL-----------SQNGIVRKELE-VARNKIKELQRQIQLDAN 229
Cdd:COG2433 459 REIRKDREISRLDREIERLERELEEERERIEELKRKLerlkelwklehSGELVPVKVVEkFTKEAIRRLEEEYGLKEG 536
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
112-366 |
6.85e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 112 EKAEKERKYEVEMAyndgELERLKQLVKELEEREVKLEGELL-EYYGLKEQESDIVELQRQlkiktvEIDMLNITINSLQ 190
Cdd:pfam05557 17 EKKQMELEHKRARI----ELEKKASALKRQLDRESDRNQELQkRIRLLEKREAEAEEALRE------QAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 191 AERKKLQEELSQNGIVRKELEVARNKIKELQRQIQldanQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKlkaVQDLE 270
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELSELRRQIQ----RAELELQSTNSELEELQERLDLLKAKASEAEQL---RQNLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 271 VQVMELKRKNRELQHEKRELSIKLDSAE------ARIATLSNMTEsdKVAKVREE---VNNLKHNNEDLLKQVEGLQ--M 339
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDSEivknskSELARIPELEK--ELERLREHnkhLNENIENKLLLKEEVEDLKrkL 237
|
250 260
....*....|....*....|....*...
gi 42565189 340 NRFSEV-EELVYLRWVNACLRYELRNYQ 366
Cdd:pfam05557 238 EREEKYrEEAATLELEKEKLEQELQSWV 265
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
115-335 |
7.11e-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: 43.56 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 115 EKERKYEVEMAYNDGELE-RLKQLVKELEEREVKLegelleyyglKEQESDIVELQRQLKIKTVEIDMLNITINSLQAER 193
Cdd:pfam05483 481 EKEKLKNIELTAHCDKLLlENKELTQEASDMTLEL----------KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 194 KKLQEELSQNgivRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQmkeeeamnkdTEVERKLKAVQDLEVQV 273
Cdd:pfam05483 551 ESVREEFIQK---GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK----------KQIENKNKNIEELHQEN 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42565189 274 MELKRKNRELQHEKRELSIKLDSAEARIATLSNMTEsDKVAKVREEVNNLKHNNEDLLKQVE 335
Cdd:pfam05483 618 KALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE-EIIDNYQKEIEDKKISEEKLLEEVE 678
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-319 |
8.35e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 111 LEKAEKERKYEVEMAYNDGELERLKQLVKELEER----EVKLEGELLEYY-GLKEQESDIVELQRQLKIKTVEIDMLNIT 185
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaeELKKAEEEKKKVeQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 186 INSLQAERKKLQEELsqngivRKELEVARNKIKELQRQIQldanqtkgqlllLKQHVSSLQMKEEEAMNKDTEVErklKA 265
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEA------KKAEEDEKKAAEALKKEAE------------EAKKAEELKKKEAEEKKKAEELK---KA 1724
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 42565189 266 VQDLEVQVMELKRKNRELQHEKRELsiKLDSAEARIATLSNMTESDKVAKVREE 319
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
111-280 |
9.29e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 111 LEKAEKERKYEVEMAYNDG-ELER-LKQLVKELEEREVKLEgelleyyglkEQESDIVELQRQLKIKTVEIDMLNITINS 188
Cdd:TIGR00606 799 MELKDVERKIAQQAAKLQGsDLDRtVQQVNQEKQEKQHELD----------TVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 189 LQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQldanQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKlkavQD 268
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK----DAKEQDSPLETFLEKDQQEKEELISSKETSNKK----AQ 940
|
170
....*....|..
gi 42565189 269 LEVQVMELKRKN 280
Cdd:TIGR00606 941 DKVNDIKEKVKN 952
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
115-350 |
1.37e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 115 EKERKYEVEMAYNDGELERLK-QLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLKIKTVEIDMlnitinslqaER 193
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK----------AF 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 194 KKLQEelsqngiVRKELEVARNKIKELQRqiqldanqtkgqllllKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQV 273
Cdd:PRK03918 633 EELAE-------TEKRLEELRKELEELEK----------------KYSEEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42565189 274 MELKRKNRELQHEKRElsikLDSAEARIATLSNMTEsdKVAKVREEVNNLKHN-NEDLLKQVEGLQMNRFSEVEELVY 350
Cdd:PRK03918 690 EEIKKTLEKLKEELEE----REKAKKELEKLEKALE--RVEELREKVKKYKALlKERALSKVGEIASEIFEELTEGKY 761
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
115-293 |
1.66e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 115 EKERKYEVEMAYNDGELERLKQLVKELEEREVKLegelleyygLKEQESDIVElqrqlkiktveidmlnitiNSLQAERK 194
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRKR---------AEEQRRKILE-------------------KELEERKQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 195 KLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVsslqmkeEEAMNKDTEVERKLKAVQ---DLEV 271
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRI-------QEQMRKATEERSRLEAMErerEMMR 579
|
170 180
....*....|....*....|..
gi 42565189 272 QVMELKRKNRELQHEKRELSIK 293
Cdd:pfam17380 580 QIVESEKARAEYEATTPITTIK 601
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
106-338 |
1.79e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 106 DDDNNLEKAEKERKYEVEMAYNDGElERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLkikTVEIDMLNIT 185
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELK-EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDEL---NEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 186 INSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIqldanqtkgQLLLLKQHVSSLQMKEE-EAMNKDTEVERKLK 264
Cdd:COG1340 80 RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI---------ERLEWRQQTEVLSPEEEkELVEKIKELEKELE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42565189 265 AVQDLEvqvmELKRKNRELQHEKRELSIKLDSAEARIATLSNMTES--DKVAKVREEVNNLKHNNEDLLKQVEGLQ 338
Cdd:COG1340 151 KAKKAL----EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQElhEEMIELYKEADELRKEADELHKEIVEAQ 222
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
110-331 |
2.12e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 110 NLEKAEKerKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYG-LKEQESDIVELQRQLKIKTVEIDMLNITINS 188
Cdd:pfam01576 374 NLEKAKQ--ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQArLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 189 LQAERKKLQEELSQngiVRKELEVARNKIKELQRQiqldANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKlkaVQD 268
Cdd:pfam01576 452 AEGKNIKLSKDVSS---LESQLQDTQELLQEETRQ----KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQ---LST 521
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 269 LEVQVMELKRKNRE-------LQHEKRELSIKLDSAEARIAtlSNMTESDKVAKVReevNNLKHNNEDLL 331
Cdd:pfam01576 522 LQAQLSDMKKKLEEdagtleaLEEGKKRLQRELEALTQQLE--EKAAAYDKLEKTK---NRLQQELDDLL 586
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
131-335 |
2.27e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.51 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 131 LERLKQLVKELEEREVKLEGElleyyglkEQESDIVELQRQL-KIKTVEIDMLNI--TINSLQAERKKLQEELSQN-GIV 206
Cdd:cd00176 6 LRDADELEAWLSEKEELLSST--------DYGDDLESVEALLkKHEALEAELAAHeeRVEALNELGEQLIEEGHPDaEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 207 RKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMkeEEAMNKDTEVERKLKAVQDLEvQVMELKRKNRELQHE 286
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL--EQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 42565189 287 KRELSIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNNEDLLKQVE 335
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAE 203
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
109-350 |
2.80e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 109 NNLEKAEKERKYEVEMAYNDGELERLKQLVKEL---EEREVKLEGELLEYygLKEQESDIVELQRQLKIKTVEIDMLNIT 185
Cdd:TIGR00618 449 CTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIhlqETRKKAVVLARLLE--LQEEPCPLCGSCIHPNPARQDIDNPGPL 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 186 INSLQA---ERKKLQEELSQngiVRKELEVARNKIKELQRQIQLdANQTKGQLLLLKQHVSSLQ---MKEEEAMNKDTEV 259
Cdd:TIGR00618 527 TRRMQRgeqTYAQLETSEED---VYHQLTSERKQRASLKEQMQE-IQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEK 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 260 ERKLKAVQDLEVQVMELK--------RKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNNEDLL 331
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKlqpeqdlqDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLAL 682
|
250
....*....|....*....
gi 42565189 332 KQVEGLQMNRFSEVEELVY 350
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQ 701
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
133-395 |
2.89e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 133 RLKQLVKELEEREVKLEGELLEYYGLKEQESD---------------IVELQRQLKIKTVEIDMLNITINSL-QAERKKL 196
Cdd:PRK10929 99 PPNMSTDALEQEILQVSSQLLEKSRQAQQEQDrareisdslsqlpqqQTEARRQLNEIERRLQTLGTPNTPLaQAQLTAL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 197 QEELSQNGIVRKELEVAR---NKIKELQR-QIQL---DANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEverkLKAVQ-- 267
Cdd:PRK10929 179 QAESAALKALVDELELAQlsaNNRQELARlRSELakkRSQQLDAYLQALRNQLNSQRQREAERALESTE----LLAEQsg 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 268 DLEVQVMELKRKNREL-----QHEKRelsIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNN---EDLLKQVEGL-Q 338
Cdd:PRK10929 255 DLPKSIVAQFKINRELsqalnQQAQR---MDLIASQQRQAASQTLQVRQALNTLREQSQWLGVSNalgEALRAQVARLpE 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42565189 339 MNRFSEVE-ELVYLRwVNAcLRYELRNYQTPAGKISARDLSKNLSPK------SQAKAKRLMLE 395
Cdd:PRK10929 332 MPKPQQLDtEMAQLR-VQR-LRYEDLLNKQPQLRQIRQADGQPLTAEqnrildAQLRTQRELLN 393
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
83-202 |
2.90e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.19 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 83 YLDDDILPEFEDLLSGEIEYPLPDDDNNLEKA-EKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYyglkeq 161
Cdd:pfam06785 64 KFEKSFLEEKEAKLTELDAEGFKILEETLEELqSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEF------ 137
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 42565189 162 esdIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQ 202
Cdd:pfam06785 138 ---RLESEEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIEN 175
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
93-351 |
3.25e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 93 EDLLSGEIEYPLPDDDNNLEKAEKERKYEVEMAYNDGELERLKQlvkELEEREVKLEGELLEyygLKEQESDIVELQRQL 172
Cdd:COG5185 300 EYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTA---EIEQGQESLTENLEA---IKEEIENIVGEVELS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 173 KiKTVEIDMLNITINSL--------QAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSS 244
Cdd:COG5185 374 K-SSEELDSFKDTIESTkesldeipQNQRGYAQEILAT---LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 245 LQMKEEEAMNKDTeverklkavqdlEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnmteSDKVAKVREEVNNLK 324
Cdd:COG5185 450 LNKVMREADEESQ------------SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTL-----KATLEKLRAKLERQL 512
|
250 260
....*....|....*....|....*..
gi 42565189 325 HNNEDLLKQVEGLQMNRFSEVEELVYL 351
Cdd:COG5185 513 EGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
131-309 |
3.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 131 LERLKQLVKELEEREVKLEGELLEyyglKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQ----NGIV 206
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldasSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 207 R---KELEVARNKIKELQRQIQlDANQTKGQLLL----LKQHVSSLQMKEEEAMNKDTEVERklkavQDLEVQVMELKRK 279
Cdd:COG4913 688 AaleEQLEELEAELEELEEELD-ELKGEIGRLEKeleqAEEELDELQDRLEAAEDLARLELR-----ALLEERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|
gi 42565189 280 NRElQHEKRELSIKLDSAEARIATLSNMTE 309
Cdd:COG4913 762 AVE-RELRENLEERIDALRARLNRAEEELE 790
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
190-335 |
3.41e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 190 QAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLlllKQHVSSLQMKEEEAMNKDTEVERKlkaVQDL 269
Cdd:PRK12704 39 EAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNEL---QKLEKRLLQKEENLDRKLELLEKR---EEEL 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42565189 270 EVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVREEV-NNLKHNNEDLLKQVE 335
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVeEEARHEAAVLIKEIE 179
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-230 |
3.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 109 NNLEKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEyygLKEQESDIVELQRQLKIKTV-EIDMLNITIN 187
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE---LAELQEELEELLEQLSLATEeELQDLAEELE 202
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 42565189 188 SLQAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQ 230
Cdd:COG4717 203 ELQQRLAELEEELEE---AQEELEELEEELEQLENELEAAALE 242
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
179-325 |
3.76e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 179 IDMLNITINSLQAERKKLQEELsqngivrkelevarNKIKELQRQIQLDANQTKGQLLLLKQHvsslqmkEEEAMNKDTE 258
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMKEL--------------ELLNSIKPKLRDRKDALEEELRQLKQL-------EDELEDCDPT 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 259 VERKLK-AVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATL-------------SNMTESDKVAKVREEVNNLK 324
Cdd:smart00787 205 ELDRAKeKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELnteiaeaekkleqCRGFTFKEIEKLKEQLKLLQ 284
|
.
gi 42565189 325 H 325
Cdd:smart00787 285 S 285
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-311 |
4.72e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 169 QRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKELEVARN------KIKELQRQIQlDANQTKGQLLLLKQHV 242
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIA-ELEAELERLDASSDDL 687
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42565189 243 SSLQMKEEEAmnkdteverkLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESD 311
Cdd:COG4913 688 AALEEQLEEL----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
112-298 |
4.98e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 112 EKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLeyygLKEQESDIVELQRQLKIKTVEIDMLNITINSLQA 191
Cdd:COG1340 89 ELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVL----SPEEEKELVEKIKELEKELEKAKKALEKNEKLKE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 192 ERKKLQEelsqngiVRKELEVARNKIKELQRQIQldanQTKGQLLLLKQHVSSLqMKEEEAMNKdtEVERKLKAVQDLEV 271
Cdd:COG1340 165 LRAELKE-------LRKEAEEIHKKIKELAEEAQ----ELHEEMIELYKEADEL-RKEADELHK--EIVEAQEKADELHE 230
|
170 180
....*....|....*....|....*..
gi 42565189 272 QVMELKRKNRELQHEKRELSIKLDSAE 298
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALK 257
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
134-348 |
6.20e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.44 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 134 LKQLVKELEEREVKLEGELlEYYGLK--EQESDIVELQ-------------RQLKIktvEIDML-------NITINSLQA 191
Cdd:pfam05622 64 LQKQLEQLQEENFRLETAR-DDYRIKceELEKEVLELQhrneeltslaeeaQALKD---EMDILressdkvKKLEATVET 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 192 ERKKLqEELSQngiVRKELEVARNKIKE-LQRQIQLD-----ANQTKGQLLLLKQHVSSLQMKEEEAMNK-------DTE 258
Cdd:pfam05622 140 YKKKL-EDLGD---LRRQVKLLEERNAEyMQRTLQLEeelkkANALRGQLETYKRQVQELHGKLSEESKKadklefeYKK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 259 VERKLKAVQD----LEVQVMELKRKNREL---QHEKRELSIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNNEDLL 331
Cdd:pfam05622 216 LEEKLEALQKekerLIIERDTLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
250
....*....|....*..
gi 42565189 332 KQVEGLQMNRFSEVEEL 348
Cdd:pfam05622 296 LGQEGSYRERLTELQQL 312
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
130-339 |
8.39e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.12 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 130 ELERLKQLVKELeeREVKLEGELleyyglkeqesdivelqrQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKE 209
Cdd:pfam07111 74 ELRRLEEEVRLL--RETSLQQKM------------------RLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 210 LEVARNK-IKELQRqiqldanqtkgqllLLKQHVSSLQMKEEEAMNKDTEVERKL-KAVQDLEV----QVMELKRKNREL 283
Cdd:pfam07111 134 LEEGSQReLEEIQR--------------LHQEQLSSLTQAHEEALSSLTSKAEGLeKSLNSLETkragEAKQLAEAQKEA 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42565189 284 QHEKRELSIKLDSAEARIATLSNMTE--SDKV-------------AKVREEVNNLKHNNEDLLKQVEGLQM 339
Cdd:pfam07111 200 ELLRKQLSKTQEELEAQVTLVESLRKyvGEQVppevhsqtwelerQELLDTMQHLQEDRADLQATVELLQV 270
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
48-232 |
8.58e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 48 YNLNDKNLQEEEEEEEEEVKLINSVINQTRGSFS--DYLDDDI--LPEFEDLLSGEI---EYPLPDDDNNLEKAEKERKY 120
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEkvKDLTKKIssLKEKIEKLESEKkekESKISDLEDELNKDDFELKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565189 121 ---EVEMAYNDGELERLKQLVKELEEREVKLEGELleyyglKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQ 197
Cdd:TIGR04523 557 enlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI------DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
170 180 190
....*....|....*....|....*....|....*
gi 42565189 198 EELsqngivrKELEVARNKIKELQRQIQLDANQTK 232
Cdd:TIGR04523 631 SII-------KNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| |
