|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
109-340 |
5.54e-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: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 109 DDNNLEKAEKERKY-EVEMAYND--GELERLKQLVKELEEREVKLEGELLEY-YGLKEQESDIVELQRQLKIKTVEIDML 184
Cdd:TIGR02168 270 EELRLEVSELEEEIeELQKELYAlaNEISRLEQQKQILRERLANLERQLEELeAQLEELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 185 NITINSLQAE----RKKLQEELSQNGIVRKELEVARNKIKELQRQIqldaNQTKGQLLLLKQHVSSLQMKEEEAMNKDTE 260
Cdd:TIGR02168 350 KEELESLEAEleelEAELEELESRLEELEEQLETLRSKVAQLELQI----ASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 261 VERKL--KAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNmtESDKVAKVREEVNNLKHNNEDLLKQVEG 338
Cdd:TIGR02168 426 LLKKLeeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ--ALDAAERELAQLQARLDSLERLQENLEG 503
|
..
gi 1063713717 339 LQ 340
Cdd:TIGR02168 504 FS 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-342 |
6.96e-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: 66.62 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 118 KERKYEVE--MAYNDGELERLKQLVKELEEREVKLEGE---LLEYYGLKEQES---------DIVELQRQLKIKTVEIDM 183
Cdd:TIGR02168 171 KERRKETErkLERTRENLDRLEDILNELERQLKSLERQaekAERYKELKAELRelelallvlRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 184 LNITINSLQAERKKLQEELSQN-----------GIVRKELEVARNKIKELQRQIQ--------LDANQTKGQLLLLKQHV 244
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELrlevseleeeiEELQKELYALANEISRLEQQKQilrerlanLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 245 SSLQMKEEEAMNKD------TEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNmtesdKVAKV 318
Cdd:TIGR02168 331 KLDELAEELAELEEkleelkEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-----EIERL 405
|
250 260
....*....|....*....|....
gi 1063713717 319 REEVNNLKHNNEDLLKQVEGLQMN 342
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKK 429
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
129-321 |
8.37e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 129 NDGELERLKQLVKELEEREVKLEGELLEyygLKEQESDIVELQRQLKIKTVEIDMLNITIN--SLQAERKKLQEELSQng 206
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEE---LEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAE-- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 207 iVRKELEVARNKIKELQRQIQldanqtkgQLLLLKQHVSSLQMKEEEAMNKDTEVERklKAVQDLEVQVMELKRKNRELQ 286
Cdd:COG4717 144 -LPERLEELEERLEELRELEE--------ELEELEAELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELE 212
|
170 180 190
....*....|....*....|....*....|....*
gi 1063713717 287 HEKRELSIKLDSAEARIATLSNMTESDKVAKVREE 321
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-351 |
3.39e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 88 DDILPEFEDLLSG--EIEYPLPDDDNNLEKAEKE-RKYEVEMAYNDGELERLKQLVKELEEREVKLEGELleyyglKEQE 164
Cdd:TIGR02168 708 EELEEELEQLRKEleELSRQISALRKDLARLEAEvEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL------AEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 165 SDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHV 244
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN---LRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 245 SSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnmteSDKVAKVREEVNN 324
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL-----REKLAQLELRLEG 933
|
250 260
....*....|....*....|....*..
gi 1063713717 325 LKHNNEDLLKQVEGLQMNRFSEVEELV 351
Cdd:TIGR02168 934 LEVRIDNLQERLSEEYSLTLEEAEALE 960
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
130-306 |
5.78e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 130 DGELERLKQLVKELEEREVKLEGELLEYYG-LKEQESDIVELQRQL-----KIKTVEIDMLNITINSLQAERKKLQEELS 203
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSeLKELEARIEELEEDLhkleeALNDLEARLSHSRIPEIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 204 QNGIVRKELEVARNKiKELQRQIQLDANQTK-GQLLLLKQHVSSLQmKEEEAMNK-----DTEVERKLKAVQDLEVQVME 277
Cdd:TIGR02169 809 RIEARLREIEQKLNR-LTLEKEYLEKEIQELqEQRIDLKEQIKSIE-KEIENLNGkkeelEEELEELEAALRDLESRLGD 886
|
170 180
....*....|....*....|....*....
gi 1063713717 278 LKRKNRELQHEKRELSIKLDSAEARIATL 306
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKK 915
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-354 |
9.08e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 132 ELERLKQLVKELEEREVKLEGELLEYYGLKEQ-ESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRK 210
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEElEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 211 ELEVarnKIKELQRQIqldaNQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDlevQVMELKRKNRELQHEKR 290
Cdd:TIGR02168 758 ELEA---EIEELEERL----EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063713717 291 ELSIKLDSAEARIATLSNMTE--SDKVAKVREEVNNLKHNNEDLLKQVEGLQMNRFSEVEELVYLR 354
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEelSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-350 |
3.58e-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: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 93 EFEDLLSGEIEYPLPDDDNNLEKAEKERK-YEVEMAYNDGELERLK----QLVKELEEREVKLEGELLEYYGLKEQEsdI 167
Cdd:TIGR02169 212 RYQALLKEKREYEGYELLKEKEALERQKEaIERQLASLEEELEKLTeeisELEKRLEEIEQLLEELNKKIKDLGEEE--Q 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 168 VELQRQLKIKTVEIDMLNITINSLQAERKKLQEElsqngivRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSL 247
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEER-------LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 248 QMKEEEAMNKDTEVERKLKA----VQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNmtesdKVAKVREEVN 323
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAEtrdeLKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA-----AIAGIEAKIN 437
|
250 260
....*....|....*....|....*..
gi 1063713717 324 NLKHNNEDLLKQVEGLQMNRFSEVEEL 350
Cdd:TIGR02169 438 ELEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-350 |
3.61e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 113 LEK-AEKERKYeveMAYNDgELERLKQ--LVKELEEREVKLEGELLEyygLKEQESDIVELQRQLKIKTVEIDMLNITIN 189
Cdd:COG1196 205 LERqAEKAERY---RELKE-ELKELEAelLLLKLRELEAELEELEAE---LEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 190 SLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAmnkDTEVERKLKAVQ 269
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL---EEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 270 DLEVQVMELKRKNRELQHEKRELSIKLDSAEARIAtlsnmTESDKVAKVREEVNNLKHNNEDLLKQVEGLQMNRFSEVEE 349
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
.
gi 1063713717 350 L 350
Cdd:COG1196 430 L 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-352 |
3.68e-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: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 114 EKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYGLKEqesdivELQRQLKIKTVEIDMLNITINSLQA 193
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS------RLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 194 ErkkLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQ---TKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKA--- 267
Cdd:TIGR02168 324 Q---LEELESKLDELAEELAELEEKLEELKEELESLEAEleeLEAELEELESRLEELEEQLETLRSKVAQLELQIASlnn 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 268 -VQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARiatlsnmTESDKVAKVREEVNNLKHNNEDLLKQVEGLQmNRFSE 346
Cdd:TIGR02168 401 eIERLEARLERLEDRRERLQQEIEELLKKLEEAELK-------ELQAELEELEEELEELQEELERLEEALEELR-EELEE 472
|
....*.
gi 1063713717 347 VEELVY 352
Cdd:TIGR02168 473 AEQALD 478
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
116-319 |
5.43e-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: 56.31 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 116 AEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELleyyglKEQESDIVELQRQLKIKTVEIDMLNITINSLQAER 195
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL------AALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 196 KKLQEELSQNGIVRKELEVA------------------------------------RNKIKELQRQIQLDANQTKGQLLL 239
Cdd:COG4942 93 AELRAELEAQKEELAELLRAlyrlgrqpplalllspedfldavrrlqylkylaparREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 240 LKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVR 319
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-340 |
8.03e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 114 EKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELleyyglKEQESDIVELQRQLKIKTVEIDmlnitinSLQA 193
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI------EELEELIEELESELEALLNERA-------SLEE 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 194 ERKKLQEELSQngiVRKELEVARNKIKELQRQIQldanqtkgqllLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEV 273
Cdd:TIGR02168 888 ALALLRSELEE---LSEELRELESKRSELRRELE-----------ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063713717 274 QVMELKRKNRELqhEKRELSIKLDSAEARIATLS--NMTESDKVAKVREEVNNLKHNNEDLLKQVEGLQ 340
Cdd:TIGR02168 954 EEAEALENKIED--DEEEARRRLKRLENKIKELGpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-339 |
1.36e-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: 55.83 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 122 YEVEMAYNDGELERLKQLVKELEEREVKLEGELLEY--------YGLKEQESDIVELQRQLKIKTVEIDMLNITINSLQA 193
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELeeeleqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 194 ERKKLQEELSQNgivRKELEVARNKIKELQRQI---QLDANQTKGQLLLLKQHVSSLQMK----EEEAMNKDTEVERKLK 266
Cdd:TIGR02168 755 ELTELEAEIEEL---EERLEEAEEELAEAEAEIeelEAQIEQLKEELKALREALDELRAEltllNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063713717 267 AVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTE--SDKVAKVREEVNNLKHNNEDLLKQVEGL 339
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEalLNERASLEEALALLRSELEELSEELREL 906
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-340 |
2.97e-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: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 110 DNNLEKAEKE-RKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYG--------LKEQESDIVELQRQLKIKTVE 180
Cdd:COG1196 252 EAELEELEAElAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarleerRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 181 IDMLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAM----N 256
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEeaeeA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 257 KDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnmteSDKVAKVREEVNNLKHNNEDLLKQV 336
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL-----LELLAELLEEAALLEAALAELLEEL 486
|
....
gi 1063713717 337 EGLQ 340
Cdd:COG1196 487 AEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
146-394 |
5.35e-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: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 146 REVKLEGELLEYYG--------LKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQngiVRKELEVARN 217
Cdd:TIGR02169 640 RMVTLEGELFEKSGamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE---LSQELSDASR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 218 KIKELQRQIQL---DANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKL-----------KAVQDLEV-----QVMEL 278
Cdd:TIGR02169 717 KIGEIEKEIEQleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeeleedlhkleEALNDLEArlshsRIPEI 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 279 KRKNRELQHEKRELSIKLDSAEARIATLSNMTES----------------DKVAKVREEVNNLKHNNEDLLKQVEGLQMN 342
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYlekeiqelqeqridlkEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063713717 343 RFSEVEELVYLRWVNACLRYELRNYQTPAGKISA-----RDLSKNLSPKSQAKAKRL 394
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAqiekkRKRLSELKAKLEALEEEL 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
106-302 |
6.91e-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: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 106 LPDDDNNLEKAEKER-KYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYG-LKEQESDIVELQRQLKIKTVEIDM 183
Cdd:TIGR02169 317 LEDAEERLAKLEAEIdKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAeLEEVDKEFAETRDELKDYREKLEK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 184 LNITINSLQAERKKLQEELSQngiVRKELEVARNKIKELQRQIqldanqtkgqllllKQHVSSLQMKEEEAMNKDTEVER 263
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQR---LSEELADLNAAIAGIEAKI--------------NELEEEKEDKALEIKKQEWKLEQ 459
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063713717 264 KLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEAR 302
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
111-340 |
1.37e-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: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 111 NNLEK----AEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEgelleyyglkEQESDIVELQRQLKIKTVEIDMLNI 186
Cdd:TIGR04523 357 ENSEKqrelEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ----------NQEKLNQQKDEQIKKLQQEKELLEK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 187 TINSLQAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLK 266
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKD---LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 267 AVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDK-----------VAKVREEVNNLKHNNEDLLKQ 335
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelkkenlekeIDEKNKEIEELKQTQKSLKKK 583
|
....*
gi 1063713717 336 VEGLQ 340
Cdd:TIGR04523 584 QEEKQ 588
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
113-321 |
4.47e-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: 50.89 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 113 LEKAEKERKYEvEMAYNDGELERLKQLVKELEEREVKLEGELLEYyglKEQESDIVELQRQL-------------KIKTV 179
Cdd:pfam17380 293 FEKMEQERLRQ-EKEEKAREVERRRKLEEAEKARQAEMDRQAAIY---AEQERMAMERERELerirqeerkreleRIRQE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 180 EIDMLNITINSLQaerkKLQEELSQ-NGIVRKELEVARN-KIKELQRQIQLDANQTKGQLLLLKQHVS---SLQMKEEEA 254
Cdd:pfam17380 369 EIAMEISRMRELE----RLQMERQQkNERVRQELEAARKvKILEEERQRKIQQQKVEMEQIRAEQEEArqrEVRRLEEER 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063713717 255 MN-----KDTEVERKlKAVQDLEVQVMELKRKNRELQHEKRElsiKLDSAEARIATLSNMTESDKVAKVREE 321
Cdd:pfam17380 445 ARemervRLEEQERQ-QQVERLRQQEEERKRKKLELEKEKRD---RKRAEEQRRKILEKELEERKQAMIEEE 512
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
167-325 |
6.54e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 167 IVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSS 246
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQ---LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 247 LQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQH-------EKRELSIKLDSAEARIATLSNMTESDKVAKVR 319
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSeiaereeELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
....*.
gi 1063713717 320 EEVNNL 325
Cdd:COG4372 183 QALDEL 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
160-340 |
1.39e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 160 LKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNgivRKELEVARNKIKELQRQI--QLDANQTKG-- 235
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---QAEIAEAEAEIEERREELgeRARALYRSGgs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 236 ----QLLLLKQHVSSLqMKEEEAMNKDTEVERKLkaVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnmte 311
Cdd:COG3883 102 vsylDVLLGSESFSDF-LDRLSALSKIADADADL--LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL----- 173
|
170 180
....*....|....*....|....*....
gi 1063713717 312 SDKVAKVREEVNNLKHNNEDLLKQVEGLQ 340
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
132-328 |
1.50e-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: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 132 ELERLKQLVKELEEREVKLEgELLEYYGLKEQESDIVELQRQLK------IKTVEIDMLNITINSLQAERKKLQEELSQn 205
Cdd:COG4913 236 DLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRaalrlwFAQRRLELLEAELEELRAELARLEAELER- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 206 giVRKELEVARNKIKELQRQIQLDANQTKGQlllLKQHVSSLQMKEEEAMNKDTEVERKLKAV--------QDLEVQVME 277
Cdd:COG4913 314 --LEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALglplpasaEEFAALRAE 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063713717 278 LKRKNRELQHEKRELSIKLDSAEARIATLSNmtesdKVAKVREEVNNLKHN 328
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRR-----ELRELEAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-343 |
1.65e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 172 RQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQI-----QLDANQTKGQLLLLKQHVSS 246
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELeklekLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 247 LQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEK--------RELSIKLDSAEARIATLSNmtesdKVAKV 318
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslateeelQDLAEELEELQQRLAELEE-----ELEEA 218
|
170 180
....*....|....*....|....*
gi 1063713717 319 REEVNNLKHNNEDLLKQVEGLQMNR 343
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEE 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
111-328 |
1.87e-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: 48.91 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 111 NNLEKAEKERKYEVEmaYNDGELERLKQLVKELEEREVKLEGELLEYYGLKEqesdivELQRQLKIKTVEIDMLNITINS 190
Cdd:TIGR02169 815 REIEQKLNRLTLEKE--YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE------ELEEELEELEAALRDLESRLGD 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 191 LQAERKKLQEELSQNGIVRKELEVARNKIKELQrqiqldaNQTKGQLLLLKQHVSSLQ--MKEEEAMNKDTEVERKLKA- 267
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRL-------SELKAKLEALEEELSEIEdpKGEDEEIPEEELSLEDVQAe 959
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063713717 268 VQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnMTESDKVAKVREEVNNLKHN 328
Cdd:TIGR02169 960 LQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL--EEERKAILERIEEYEKKKRE 1018
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
113-290 |
1.93e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 113 LEKAEKERKYEVEmAYND--GELERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVE---LQRQLKIKTVEIDMLNIT 187
Cdd:COG4717 76 LEEELKEAEEKEE-EYAElqEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleaLEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 188 InslqAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQTkgqlllLKQHVSSLQMKEEEAMNKDTEVERKLKA 267
Cdd:COG4717 155 L----EELRELEEELEE---LEAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180
....*....|....*....|...
gi 1063713717 268 VQDLEVQVMELKRKNRELQHEKR 290
Cdd:COG4717 222 LEELEEELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
114-350 |
1.96e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 114 EKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELL---EYYGLKEQESDIVELQRQLKI--------KTVEID 182
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkesELIKLKELAEQLKELEEKLKKynleelekKAEEYE 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 183 MLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRqiqldanqtkgQLLLLKQHVSSLQMKEEEamnkdtEVE 262
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE-----------ELAELLKELEELGFESVE------ELE 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 263 RKLKAVQDLEVQVMELKRKNRELQHEKRELSI---KLDSAEARIATLSNMTEsdkvaKVREEVNNLKHN-NEDLLKQVEG 338
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKELEREEKELKKleeELDKAFEELAETEKRLE-----ELRKELEELEKKySEEEYEELRE 666
|
250
....*....|..
gi 1063713717 339 LQMNRFSEVEEL 350
Cdd:PRK03918 667 EYLELSRELAGL 678
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
130-306 |
2.25e-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: 46.84 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 130 DGELERLKQLVKELEERevklegelleyygLKEQESDIVELQRQLKIKTVEIDmlnitinSLQAERKKLQEELSQngiVR 209
Cdd:COG1579 16 DSELDRLEHRLKELPAE-------------LAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIEE---VE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 210 KELEVARNKIKELQRQIQLDANQtkGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDlevqvmELKRKNRELQHEK 289
Cdd:COG1579 73 ARIKKYEEQLGNVRNNKEYEALQ--KEIESLKRRISDLEDEILELMERIEELEEELAELEA------ELAELEAELEEKK 144
|
170
....*....|....*..
gi 1063713717 290 RELSIKLDSAEARIATL 306
Cdd:COG1579 145 AELDEELAELEAELEEL 161
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
100-349 |
2.64e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 100 GEIEYPLPDDDNNlEKAEKE----RKYEveMAYndgelERLKQLVKELEEREVKLEGELLEYYGLKEQesdIVELQRQLK 175
Cdd:PRK03918 135 GEIDAILESDESR-EKVVRQilglDDYE--NAY-----KNLGEVIKEIKRRIERLEKFIKRTENIEEL---IKEKEKELE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 176 IKTVEIDMLNITINSLQAERKKLQEELsqngivrKELEVARNKIKELQRQIQLdanqTKGQLLLLKQHVSSLQMKEEEAM 255
Cdd:PRK03918 204 EVLREINEISSELPELREELEKLEKEV-------KELEELKEEIEELEKELES----LEGSKRKLEEKIRELEERIEELK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 256 NKDTEVERKLKAVQDLEvqvmELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESdkVAKVREEVNNLKHNNEDLLKQ 335
Cdd:PRK03918 273 KEIEELEEKVKELKELK----EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING--IEERIKELEEKEERLEELKKK 346
|
250
....*....|....
gi 1063713717 336 VEGLQmNRFSEVEE 349
Cdd:PRK03918 347 LKELE-KRLEELEE 359
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
114-306 |
2.66e-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: 47.75 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 114 EKAEKERKYEVEMAYNDgeleRLKQLVKELEEREVKLEGELLEYYG--------LKEQESDIVELQRQLKIKTVEIDMLN 185
Cdd:pfam19220 49 RLLELEALLAQERAAYG----KLRRELAGLTRRLSAAEGELEELVArlakleaaLREAEAAKEELRIELRDKTAQAEALE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 186 itiNSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIqldaNQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKL 265
Cdd:pfam19220 125 ---RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGEL----ATARERLALLEQENRRLQALSEEQAAELAELTRRL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063713717 266 K-----------AVQDLEVQVME-----------LKRKNRELQHEKRELSIKLDSAEARIATL 306
Cdd:pfam19220 198 AeletqldatraRLRALEGQLAAeqaereraeaqLEEAVEAHRAERASLRMKLEALTARAAAT 260
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
101-326 |
3.10e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 101 EIEYPLPDDDNNLEKAEKERK-----------YEVEMAYNDGELERLKQLVKELEER--EVKLEGELLE-----YYGLKE 162
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKeleelkeeieeLEKELESLEGSKRKLEEKIRELEERieELKKEIEELEekvkeLKELKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 163 QESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIqldaNQTKGQLLLLkq 242
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL----EELEERHELY-- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 243 hvsslqmkeEEAMNKDTEVERKLKAVQDLEVQvmELKRKNRELQHEKRELSIKLDSAEARIATLSNmtesdKVAKVREEV 322
Cdd:PRK03918 365 ---------EEAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKK-----EIKELKKAI 428
|
....
gi 1063713717 323 NNLK 326
Cdd:PRK03918 429 EELK 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-340 |
3.70e-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: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 163 QESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEEL------------------SQNGIVRKELEVARNKIKELQR 224
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLaalerriaalarriraleQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 225 QI---------QLDANQTKGQ----LLLLKQHvSSLQMKEEEAMNKDTEVERKlKAVQDLEVQVMELKRKNRELQHEKRE 291
Cdd:COG4942 98 ELeaqkeelaeLLRALYRLGRqpplALLLSPE-DFLDAVRRLQYLKYLAPARR-EQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063713717 292 LSIKLDSAEARIATLSNMTES--DKVAKVREEVNNLKHNNEDLLKQVEGLQ 340
Cdd:COG4942 176 LEALLAELEEERAALEALKAErqKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
130-323 |
4.28e-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: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 130 DGELERLKQLVKELEEREVKLEGElleyygLKEQESDIVELQRQLKiktvEIDmlNITINSLQAERKKLQEELsqngivr 209
Cdd:COG4913 294 EAELEELRAELARLEAELERLEAR------LDALREELDELEAQIR----GNG--GDRLEQLEREIERLEREL------- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 210 KELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEamnkdteverklkAVQDLEVQVMELKRKNRELQHEK 289
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE-------------ELEALEEALAEAEAALRDLRREL 421
|
170 180 190
....*....|....*....|....*....|....
gi 1063713717 290 RELSIKLDSAEARIatlSNMTEsdKVAKVREEVN 323
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 ... |
139-354 |
5.23e-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: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 139 LVKELEEREVKLEgELL--EYYGLKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQngivRKELEVAR 216
Cdd:pfam05483 350 VVTEFEATTCSLE-ELLrtEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----DEKLLDEK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 217 NKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMkeeEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKl 296
Cdd:pfam05483 425 KQFEKIAEELKGKEQELIFLLQAREKEIHDLEI---QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE- 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063713717 297 dsAEARIATLSNMTESDKvaKVREEVNNLKHNNEDLLKQVEGLQMNRFSEVEELVYLR 354
Cdd:pfam05483 501 --NKELTQEASDMTLELK--KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
134-347 |
5.41e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 134 ERLKQLVKELEEREVKLEgellEYyglkEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQngiVRKELE 213
Cdd:COG3206 182 EQLPELRKELEEAEAALE----EF----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA---LRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 214 VARNKIKEL----------QRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNR 283
Cdd:COG3206 251 SGPDALPELlqspviqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREA 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063713717 284 ELQHEKRELSIKLDSAEARIATLSNMTesdkvakvrEEVNNLKHNNEDLLKQVEGLQMNRFSEV 347
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELRRLE---------REVEVARELYESLLQRLEEARLAEALTV 385
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
132-266 |
9.21e-05 |
|
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: 44.51 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 132 ELERLKQLVKELEEREVKLEGELleyyglKEQESDIVELQRQLKiktveiDMLNITINSLQAERKKLQEELSQngiVRKE 211
Cdd:pfam15619 68 EVRVLRERLRRLQEKERDLERKL------KEKEAELLRLRDQLK------RLEKLSEDKNLAEREELQKKLEQ---LEAK 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063713717 212 LEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLK 266
Cdd:pfam15619 133 LEDKDEKIQDLERKLELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
114-337 |
9.80e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 114 EKAEKERKYEVEMAYNDGELERLKQLVKELEEREvKLEGELLEYYGLKEQ-ESDIVELQRQLKIKTVEIDMLNITInSLQ 192
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEE-ESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDR-TVQ 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 193 AERKKLQEELSQNGIVRKELEVARNKIKELQRQIQL---DANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQ 269
Cdd:TIGR00606 826 QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHlksKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063713717 270 DLEVQVMELKRKNRELQHEKRELSIKLDSaeariatlSNMTESDKVAKVREEVNNLKHNNEDLLKQVE 337
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKET--------SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
109-247 |
1.02e-04 |
|
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: 45.00 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 109 DDNNLEKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEyyglkeqesdiveLQRQLKIKTVEIDMLNITI 188
Cdd:pfam14932 45 EGAALDEALKTISAESPGLLNQQDVEALEESLEEIREATEDLEAELQE-------------LQKTKQLKINRLNKLQAQA 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063713717 189 NSLQAERKKLQEELSQngivrkelevARNKIKELQRQIQLDANQTKGQLLLLKQHVSSL 247
Cdd:pfam14932 112 SSLSQGLRALVAEEEE----------AAKQLEELQEELAALNAKTNNVLQSLQSEVKEL 160
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
114-349 |
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 1063713717 114 EKAEKERKYEVEMAYNDgELERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLKIKTVEI-----DMLN--- 185
Cdd:TIGR00606 229 KEAQLESSREIVKSYEN-ELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtdEQLNdly 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 186 ----ITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEE-EAMNKDTE 260
Cdd:TIGR00606 308 hnhqRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLElDGFERGPF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 261 VERKLKAVQDLEVQVMELKRKN-----RELQHEKRELSIKLDSAEARIATLSNMTESDKVaKVREEVNNLKHNNEDlLKQ 335
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTaaqlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKE-ILEKKQEELKFVIKE-LQQ 465
|
250
....*....|....
gi 1063713717 336 VEGlQMNRFSEVEE 349
Cdd:TIGR00606 466 LEG-SSDRILELDQ 478
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
137-339 |
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 1063713717 137 KQLVKELEEREVKLEGELLEYYGLKEQESDIVELQ----RQLKIKTVEIDMLNITINSLQAERKKLQEELSQ-------- 204
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQnkikKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlnnqkeqd 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 205 -NGIVRKELEVARNKIKELQRQIqldaNQTKGQLLLLKQHVSSLqmkEEEAMNKDTEVERKLKavqdlevqvmELKRKNR 283
Cdd:TIGR04523 308 wNKELKSELKNQEKKLEEIQNQI----SQNNKIISQLNEQISQL---KKELTNSESENSEKQR----------ELEEKQN 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063713717 284 ELQHEKRELSIKLDSA---EARIATL-SNMTESDKVAKVREE-VNNLKHNNEDLLKQVEGL 339
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIknlESQINDLeSKIQNQEKLNQQKDEqIKKLQQEKELLEKEIERL 431
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
52-350 |
1.25e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 52 LNDKNLQEEEEEEEEEVKLINSVINQTRGSFSDyLDDDIlpefeDLLSGEIEyplpDDDNNLEKA-EKERKYEVEMAYND 130
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAE-LEAEL-----EELRLELE----ELELELEEAqAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 131 GELERLKQLVKELEEREVKLEGELLEYYG-LKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNgivR 209
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---E 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 210 KELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEK 289
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063713717 290 RELSIKLDSAEARIATLsnmteSDKVAKVREEVNNLKhNNEDLLKQVEGLQMNRFSEVEEL 350
Cdd:COG1196 459 EALLELLAELLEEAALL-----EAALAELLEELAEAA-ARLLLLLEAEADYEGFLEGVKAA 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
115-319 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 115 KAEKERKY-EVEMAYNDGELERLKqLVKELEER-----EVKLEGELL--EYYGLKEQESDIVE----LQRQLKIKTVEID 182
Cdd:pfam15921 613 KDKKDAKIrELEARVSDLELEKVK-LVNAGSERlravkDIKQERDQLlnEVKTSRNELNSLSEdyevLKRNFRNKSEEME 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 183 MlniTINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKqhvSSLQMKEEEAMNKDTE-- 260
Cdd:pfam15921 692 T---TTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQ---SKIQFLEEAMTNANKEkh 765
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063713717 261 --VERKLKAVQDLEVQVME----------LKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVR 319
Cdd:pfam15921 766 flKEEKNKLSQELSTVATEknkmagelevLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-343 |
1.74e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 113 LEKAEKERKYEVEMAYNDGE-LERLKQLVKELEEREV-------KLEGELLEYYGLKEQESDIVELQRQLKIKTVEIdml 184
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEeKKKAEELKKAEEENKIkaaeeakKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA--- 1701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 185 nitiNSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTK------------GQLLLLKQHVSSLQMKEE 252
Cdd:PTZ00121 1702 ----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEeakkdeeekkkiAHLKKEEEKKAEEIRKEK 1777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 253 EAMNKD----------TEVERKLKAVQDLEVQVMELKRKNRELQHEKRELsikLDSAEARIATLSNMT--ESDKVAKVRE 320
Cdd:PTZ00121 1778 EAVIEEeldeedekrrMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM---EDSAIKEVADSKNMQleEADAFEKHKF 1854
|
250 260 270
....*....|....*....|....*....|....*..
gi 1063713717 321 EVNNL--------------KHNNEDLLKQVEGLQMNR 343
Cdd:PTZ00121 1855 NKNNEngedgnkeadfnkeKDLKEDDEEEIEEADEIE 1891
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
130-303 |
3.11e-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: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 130 DGELERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLkIKTVEIDMLNITINSLQAERKKLQEELSQNGIVR 209
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQSPVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 210 KELevaRNKIKELQRQIQldaNQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRK---NREL- 285
Cdd:COG3206 294 IAL---RAQIAALRAQLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREvevARELy 367
|
170 180
....*....|....*....|...
gi 1063713717 286 -----QHEKRELSIKLDSAEARI 303
Cdd:COG3206 368 esllqRLEEARLAEALTVGNVRV 390
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
95-231 |
4.75e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 95 EDLLSGEIEYPLPDDDNNLEKAEKE-----RKYEVEMAYNDGELERLKQLVKEL----EEREVKLEGELLEYYGLKEQES 165
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHeerelTEEEEEIRRLEEQVERLEAEVEELeaelEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063713717 166 DIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEEL-----------SQNGIVRKELE-VARNKIKELQRQIQLDAN 231
Cdd:COG2433 459 REIRKDREISRLDREIERLERELEEERERIEELKRKLerlkelwklehSGELVPVKVVEkFTKEAIRRLEEEYGLKEG 536
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
114-368 |
6.15e-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: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 114 EKAEKERKYEVEMAyndgELERLKQLVKELEEREVKLEGELL-EYYGLKEQESDIVELQRQlkiktvEIDMLNITINSLQ 192
Cdd:pfam05557 17 EKKQMELEHKRARI----ELEKKASALKRQLDRESDRNQELQkRIRLLEKREAEAEEALRE------QAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 193 AERKKLQEELSQNGIVRKELEVARNKIKELQRQIQ---LDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQ 269
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELSELRRQIQraeLELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 270 DLEVQVMELKRKNRELQHEKRELSikldSAEARIATLSNMTEsdKVAKVREE---VNNLKHNNEDLLKQVEGLQ--MNRF 344
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEIVK----NSKSELARIPELEK--ELERLREHnkhLNENIENKLLLKEEVEDLKrkLERE 240
|
250 260
....*....|....*....|....*
gi 1063713717 345 SEV-EELVYLRWVNACLRYELRNYQ 368
Cdd:pfam05557 241 EKYrEEAATLELEKEKLEQELQSWV 265
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
117-337 |
6.83e-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: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 117 EKERKYEVEMAYNDGELE-RLKQLVKELEEREVKLegelleyyglKEQESDIVELQRQLKIKTVEIDMLNITINSLQAER 195
Cdd:pfam05483 481 EKEKLKNIELTAHCDKLLlENKELTQEASDMTLEL----------KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 196 KKLQEELSQNgivRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQmkeeeamnkdTEVERKLKAVQDLEVQV 275
Cdd:pfam05483 551 ESVREEFIQK---GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK----------KQIENKNKNIEELHQEN 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063713717 276 MELKRKNRELQHEKRELSIKLDSAEARIATLSNMTEsDKVAKVREEVNNLKHNNEDLLKQVE 337
Cdd:pfam05483 618 KALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE-EIIDNYQKEIEDKKISEEKLLEEVE 678
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
113-282 |
8.49e-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: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 113 LEKAEKERKYEVEMAYNDG-ELER-LKQLVKELEEREVKLEgelleyyglkEQESDIVELQRQLKIKTVEIDMLNITINS 190
Cdd:TIGR00606 799 MELKDVERKIAQQAAKLQGsDLDRtVQQVNQEKQEKQHELD----------TVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 191 LQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQldanQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKlkavQD 270
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK----DAKEQDSPLETFLEKDQQEKEELISSKETSNKK----AQ 940
|
170
....*....|..
gi 1063713717 271 LEVQVMELKRKN 282
Cdd:TIGR00606 941 DKVNDIKEKVKN 952
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-321 |
8.51e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 113 LEKAEKERKYEVEMAYNDGELERLKQLVKELEER----EVKLEGELLEYY-GLKEQESDIVELQRQLKIKTVEIDMLNIT 187
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaeELKKAEEEKKKVeQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 188 INSLQAERKKLQEELsqngivRKELEVARNKIKELQRQIQldanqtkgqlllLKQHVSSLQMKEEEAMNKDTEVErklKA 267
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEA------KKAEEDEKKAAEALKKEAE------------EAKKAEELKKKEAEEKKKAEELK---KA 1724
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063713717 268 VQDLEVQVMELKRKNRELQHEKRELsiKLDSAEARIATLSNMTESDKVAKVREE 321
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
127-321 |
1.02e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 127 AYNDGELERLKQLVKELEEREVKLEGELLEyyglkeqesdiveLQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQng 206
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDA-------------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 207 iVRKELEVARNKIKELQRQIQLDANQTKGQLLLL----------------------KQHVSSLQMKEEEAMNKDTEVERK 264
Cdd:COG3883 77 -AEAEIEERREELGERARALYRSGGSVSYLDVLLgsesfsdfldrlsalskiadadADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063713717 265 LkavQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVREE 321
Cdd:COG3883 156 L---AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
117-352 |
1.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 117 EKERKYEVEMAYNDGELERLK-QLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLKIKTVEIDMlnitinslqaER 195
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK----------AF 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 196 KKLQEelsqngiVRKELEVARNKIKELQRqiqldanqtkgqllllKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQV 275
Cdd:PRK03918 633 EELAE-------TEKRLEELRKELEELEK----------------KYSEEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063713717 276 MELKRKNRELQHEKRElsikLDSAEARIATLSNMTEsdKVAKVREEVNNLKHN-NEDLLKQVEGLQMNRFSEVEELVY 352
Cdd:PRK03918 690 EEIKKTLEKLKEELEE----REKAKKELEKLEKALE--RVEELREKVKKYKALlKERALSKVGEIASEIFEELTEGKY 761
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
108-340 |
1.31e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 108 DDDNNLEKAEKERKYEVEMAYNDGELER------LKQLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLKiktVEI 181
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEKRdelneeLKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK---EER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 182 DMLNITINSLQAERKKLQEElsqngivRKELEVARNKIKELQRQIqldanqtkgQLLLLKQHVSSLQMKEE-EAMNKDTE 260
Cdd:COG1340 81 DELNEKLNELREELDELRKE-------LAELNKAGGSIDKLRKEI---------ERLEWRQQTEVLSPEEEkELVEKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 261 VERKLKAVQDLEvqvmELKRKNRELQHEKRELSIKLDSAEARIATLSNMTE--SDKVAKVREEVNNLKHNNEDLLKQVEG 338
Cdd:COG1340 145 LEKELEKAKKAL----EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQelHEEMIELYKEADELRKEADELHKEIVE 220
|
..
gi 1063713717 339 LQ 340
Cdd:COG1340 221 AQ 222
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
117-295 |
1.51e-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: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 117 EKERKYEVEMAYNDGELERLKQLVKELEEREVKLegelleyygLKEQESDIVElqrqlkiktveidmlnitiNSLQAERK 196
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRKR---------AEEQRRKILE-------------------KELEERKQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 197 KLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVsslqmkeEEAMNKDTEVERKLKAVQ---DLEV 273
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRI-------QEQMRKATEERSRLEAMErerEMMR 579
|
170 180
....*....|....*....|..
gi 1063713717 274 QVMELKRKNRELQHEKRELSIK 295
Cdd:pfam17380 580 QIVESEKARAEYEATTPITTIK 601
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
112-333 |
1.92e-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: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 112 NLEKAEKerKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYG-LKEQESDIVELQRQLKIKTVEIDMLNITINS 190
Cdd:pfam01576 374 NLEKAKQ--ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQArLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 191 LQAERKKLQEELSQngiVRKELEVARNKIKELQRQiqldANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKlkaVQD 270
Cdd:pfam01576 452 AEGKNIKLSKDVSS---LESQLQDTQELLQEETRQ----KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQ---LST 521
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 271 LEVQVMELKRKNRE-------LQHEKRELSIKLDSAEARIAtlSNMTESDKVAKVReevNNLKHNNEDLL 333
Cdd:pfam01576 522 LQAQLSDMKKKLEEdagtleaLEEGKKRLQRELEALTQQLE--EKAAAYDKLEKTK---NRLQQELDDLL 586
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
133-337 |
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 1063713717 133 LERLKQLVKELEEREVKLEGElleyyglkEQESDIVELQRQL-KIKTVEIDMLNI--TINSLQAERKKLQEELSQN-GIV 208
Cdd:cd00176 6 LRDADELEAWLSEKEELLSST--------DYGDDLESVEALLkKHEALEAELAAHeeRVEALNELGEQLIEEGHPDaEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 209 RKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMkeEEAMNKDTEVERKLKAVQDLEvQVMELKRKNRELQHE 288
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL--EQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063713717 289 KRELSIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNNEDLLKQVE 337
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAE 203
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
95-353 |
2.70e-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: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 95 EDLLSGEIEYPLPDDDNNLEKAEKERKYEVEMAYNDGELERLKQlvkELEEREVKLEGELLEyygLKEQESDIVELQRQL 174
Cdd:COG5185 300 EYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTA---EIEQGQESLTENLEA---IKEEIENIVGEVELS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 175 KiKTVEIDMLNITINSL--------QAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSS 246
Cdd:COG5185 374 K-SSEELDSFKDTIESTkesldeipQNQRGYAQEILAT---LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 247 LQMKEEEAMNKDTeverklkavqdlEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnmteSDKVAKVREEVNNLK 326
Cdd:COG5185 450 LNKVMREADEESQ------------SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTL-----KATLEKLRAKLERQL 512
|
250 260
....*....|....*....|....*..
gi 1063713717 327 HNNEDLLKQVEGLQMNRFSEVEELVYL 353
Cdd:COG5185 513 EGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
111-352 |
2.73e-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: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 111 NNLEKAEKERKYEVEMAYNDGELERLKQLVKEL---EEREVKLEGELLEYygLKEQESDIVELQRQLKIKTVEIDMLNIT 187
Cdd:TIGR00618 449 CTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIhlqETRKKAVVLARLLE--LQEEPCPLCGSCIHPNPARQDIDNPGPL 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 188 INSLQA---ERKKLQEELSQngiVRKELEVARNKIKELQRQIQLdANQTKGQLLLLKQHVSSLQ---MKEEEAMNKDTEV 261
Cdd:TIGR00618 527 TRRMQRgeqTYAQLETSEED---VYHQLTSERKQRASLKEQMQE-IQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEK 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 262 ERKLKAVQDLEVQVMELK--------RKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNNEDLL 333
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKlqpeqdlqDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLAL 682
|
250
....*....|....*....
gi 1063713717 334 KQVEGLQMNRFSEVEELVY 352
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQ 701
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
135-397 |
2.87e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 135 RLKQLVKELEEREVKLEGELLEYYGLKEQESD---------------IVELQRQLKIKTVEIDMLNITINSL-QAERKKL 198
Cdd:PRK10929 99 PPNMSTDALEQEILQVSSQLLEKSRQAQQEQDrareisdslsqlpqqQTEARRQLNEIERRLQTLGTPNTPLaQAQLTAL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 199 QEELSQNGIVRKELEVAR---NKIKELQR-QIQL---DANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEverkLKAVQ-- 269
Cdd:PRK10929 179 QAESAALKALVDELELAQlsaNNRQELARlRSELakkRSQQLDAYLQALRNQLNSQRQREAERALESTE----LLAEQsg 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 270 DLEVQVMELKRKNREL-----QHEKRelsIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNN---EDLLKQVEGL-Q 340
Cdd:PRK10929 255 DLPKSIVAQFKINRELsqalnQQAQR---MDLIASQQRQAASQTLQVRQALNTLREQSQWLGVSNalgEALRAQVARLpE 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063713717 341 MNRFSEVE-ELVYLRwVNAcLRYELRNYQTPAGKISARDLSKNLSPK------SQAKAKRLMLE 397
Cdd:PRK10929 332 MPKPQQLDtEMAQLR-VQR-LRYEDLLNKQPQLRQIRQADGQPLTAEqnrildAQLRTQRELLN 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
133-311 |
3.02e-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: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 133 LERLKQLVKELEEREVKLEGELLEyyglKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQ----NGIV 208
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldasSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 209 R---KELEVARNKIKELQRQIQlDANQTKGQLLL----LKQHVSSLQMKEEEAMNKDTEVERklkavQDLEVQVMELKRK 281
Cdd:COG4913 688 AaleEQLEELEAELEELEEELD-ELKGEIGRLEKeleqAEEELDELQDRLEAAEDLARLELR-----ALLEERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|
gi 1063713717 282 NRElQHEKRELSIKLDSAEARIATLSNMTE 311
Cdd:COG4913 762 AVE-RELRENLEERIDALRARLNRAEEELE 790
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
85-204 |
3.08e-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: 39.80 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 85 YLDDDILPEFEDLLSGEIEYPLPDDDNNLEKA-EKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYyglkeq 163
Cdd:pfam06785 64 KFEKSFLEEKEAKLTELDAEGFKILEETLEELqSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEF------ 137
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1063713717 164 esdIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQ 204
Cdd:pfam06785 138 ---RLESEEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIEN 175
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
192-337 |
3.08e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 192 QAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLlllKQHVSSLQMKEEEAMNKDTEVERKlkaVQDL 271
Cdd:PRK12704 39 EAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNEL---QKLEKRLLQKEENLDRKLELLEKR---EEEL 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063713717 272 EVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVREEV-NNLKHNNEDLLKQVE 337
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVeEEARHEAAVLIKEIE 179
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
111-232 |
3.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 111 NNLEKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEyygLKEQESDIVELQRQLKIKTV-EIDMLNITIN 189
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE---LAELQEELEELLEQLSLATEeELQDLAEELE 202
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1063713717 190 SLQAERKKLQEELSQngiVRKELEVARNKIKELQRQIQLDANQ 232
Cdd:COG4717 203 ELQQRLAELEEELEE---AQEELEELEEELEQLENELEAAALE 242
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
181-327 |
3.71e-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: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 181 IDMLNITINSLQAERKKLQEELsqngivrkelevarNKIKELQRQIQLDANQTKGQLLLLKQHvsslqmkEEEAMNKDTE 260
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMKEL--------------ELLNSIKPKLRDRKDALEEELRQLKQL-------EDELEDCDPT 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 261 VERKLK-AVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATL-------------SNMTESDKVAKVREEVNNLK 326
Cdd:smart00787 205 ELDRAKeKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELnteiaeaekkleqCRGFTFKEIEKLKEQLKLLQ 284
|
.
gi 1063713717 327 H 327
Cdd:smart00787 285 S 285
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
114-300 |
4.19e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 114 EKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLeyygLKEQESDIVELQRQLKIKTVEIDMLNITINSLQA 193
Cdd:COG1340 89 ELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVL----SPEEEKELVEKIKELEKELEKAKKALEKNEKLKE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 194 ERKKLQEelsqngiVRKELEVARNKIKELQRQIQldanQTKGQLLLLKQHVSSLqMKEEEAMNKdtEVERKLKAVQDLEV 273
Cdd:COG1340 165 LRAELKE-------LRKEAEEIHKKIKELAEEAQ----ELHEEMIELYKEADEL-RKEADELHK--EIVEAQEKADELHE 230
|
170 180
....*....|....*....|....*..
gi 1063713717 274 QVMELKRKNRELQHEKRELSIKLDSAE 300
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALK 257
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
171-313 |
4.69e-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: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 171 QRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKELEVARN------KIKELQRQIQlDANQTKGQLLLLKQHV 244
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIA-ELEAELERLDASSDDL 687
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063713717 245 SSLQMKEEEAmnkdteverkLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESD 313
Cdd:COG4913 688 AALEEQLEEL----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
136-350 |
5.85e-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: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 136 LKQLVKELEEREVKLEGELlEYYGLK--EQESDIVELQ-------------RQLKIktvEIDML-------NITINSLQA 193
Cdd:pfam05622 64 LQKQLEQLQEENFRLETAR-DDYRIKceELEKEVLELQhrneeltslaeeaQALKD---EMDILressdkvKKLEATVET 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 194 ERKKLqEELSQngiVRKELEVARNKIKE-LQRQIQLD-----ANQTKGQLLLLKQHVSSLQMKEEEAMNK-------DTE 260
Cdd:pfam05622 140 YKKKL-EDLGD---LRRQVKLLEERNAEyMQRTLQLEeelkkANALRGQLETYKRQVQELHGKLSEESKKadklefeYKK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 261 VERKLKAVQD----LEVQVMELKRKNREL---QHEKRELSIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNNEDLL 333
Cdd:pfam05622 216 LEEKLEALQKekerLIIERDTLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
250
....*....|....*..
gi 1063713717 334 KQVEGLQMNRFSEVEEL 350
Cdd:pfam05622 296 LGQEGSYRERLTELQQL 312
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
132-341 |
6.85e-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: 40.51 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 132 ELERLKQLVKELeeREVKLEGELleyyglkeqesdivelqrQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKE 211
Cdd:pfam07111 74 ELRRLEEEVRLL--RETSLQQKM------------------RLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 212 LEVARNK-IKELQRqiqldanqtkgqllLLKQHVSSLQMKEEEAMNKDTEVERKL-KAVQDLEV----QVMELKRKNREL 285
Cdd:pfam07111 134 LEEGSQReLEEIQR--------------LHQEQLSSLTQAHEEALSSLTSKAEGLeKSLNSLETkragEAKQLAEAQKEA 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063713717 286 QHEKRELSIKLDSAEARIATLSNMTE--SDKV-------------AKVREEVNNLKHNNEDLLKQVEGLQM 341
Cdd:pfam07111 200 ELLRKQLSKTQEELEAQVTLVESLRKyvGEQVppevhsqtwelerQELLDTMQHLQEDRADLQATVELLQV 270
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
188-351 |
8.42e-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: 39.14 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 188 INSLQAERKKLQEELSQngivrkelevARNKIKELQRQIqldaNQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKA 267
Cdd:COG1579 19 LDRLEHRLKELPAELAE----------LEDELAALEARL----EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 268 V------QDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLsnmteSDKVAKVREEVNNLKHNNEDLLKQVEGLQM 341
Cdd:COG1579 85 VrnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAEL-----EAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|
gi 1063713717 342 NRFSEVEELV 351
Cdd:COG1579 160 ELEAEREELA 169
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
50-234 |
8.53e-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: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 50 YNLNDKNLQEEEEEEEEEVKLINSVINQTRGSFS--DYLDDDI--LPEFEDLLSGEI---EYPLPDDDNNLEKAEKERKY 122
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEkvKDLTKKIssLKEKIEKLESEKkekESKISDLEDELNKDDFELKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713717 123 ---EVEMAYNDGELERLKQLVKELEEREVKLEGELleyyglKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQ 199
Cdd:TIGR04523 557 enlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI------DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
170 180 190
....*....|....*....|....*....|....*
gi 1063713717 200 EELsqngivrKELEVARNKIKELQRQIQLDANQTK 234
Cdd:TIGR04523 631 SII-------KNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| |
