|
Name |
Accession |
Description |
Interval |
E-value |
| SH3BP5 |
pfam05276 |
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ... |
43-271 |
2.08e-108 |
|
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 domain-binding protein 5 or c-Jun N-terminal kinase (JNK)-interacting proteins (SH3BP5 or Sab). Sab binds to and serves as a substrate for JNK in vitro, and has been found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine-proline JNK phosphorylation sites in the C-terminal half of the molecule.
Pssm-ID: 461608 [Multi-domain] Cd Length: 231 Bit Score: 320.38 E-value: 2.08e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 43 VDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQ 122
Cdd:pfam05276 3 LDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 123 DFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKK 202
Cdd:pfam05276 83 RFERANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149034180 203 LKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNAMGPR 271
Cdd:pfam05276 163 LKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
44-266 |
4.83e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 44 DPRIQGELEKLNQSTDDINRRETELEDARQKFR--SVLVEATVKLDELAKKIGK--AVEDSKPYWEARRVARQAQLEAQK 119
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAEleYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 120 ATQDFQRATEVLRAAKETISLAEQRLleddkrqfDSAWQEMLNHATQRVMEAEQtktrsELVHKE-TAARYNAAMGRMRQ 198
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREEL--------DELEAQIRGNGGDRLEQLER-----EIERLErELEERERRRARLEA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149034180 199 LEKKLKRAINKSKPYF-ELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIH--ERRRSN 266
Cdd:COG4913 367 LLAALGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKSN 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-266 |
1.95e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 66 TELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKpywearrvarQAQLEAQKATQDFQRATEVLRAAKETISLAEQRL 145
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLE----------ELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 146 LE-DDKRQFDSAWQEMLNHATQrvmEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQL 224
Cdd:TIGR02168 305 QIlRERLANLERQLEELEAQLE---ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 149034180 225 EQLKKTVDDLQAKLALAKGEYKAALKSLERISDEiHERRRSN 266
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDR-RERLQQE 422
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-264 |
6.17e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 50 ELEKLNQSTDDINRRETELEDARQKfrsvlVEATVKLDELAK-KIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRAT 128
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKA-----AEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 129 EVlRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEA-----EQTKTRSELVHKETAARYNAAMGR-------- 195
Cdd:PTZ00121 1556 EL-KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKkaeeekkk 1634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149034180 196 MRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRR 264
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SH3BP5 |
pfam05276 |
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ... |
43-271 |
2.08e-108 |
|
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 domain-binding protein 5 or c-Jun N-terminal kinase (JNK)-interacting proteins (SH3BP5 or Sab). Sab binds to and serves as a substrate for JNK in vitro, and has been found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine-proline JNK phosphorylation sites in the C-terminal half of the molecule.
Pssm-ID: 461608 [Multi-domain] Cd Length: 231 Bit Score: 320.38 E-value: 2.08e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 43 VDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQ 122
Cdd:pfam05276 3 LDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 123 DFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKK 202
Cdd:pfam05276 83 RFERANSAHAAAKEMVALAEQGLLNNDEGTFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLEKK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149034180 203 LKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNAMGPR 271
Cdd:pfam05276 163 LKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
44-266 |
4.83e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 44 DPRIQGELEKLNQSTDDINRRETELEDARQKFR--SVLVEATVKLDELAKKIGK--AVEDSKPYWEARRVARQAQLEAQK 119
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAEleYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 120 ATQDFQRATEVLRAAKETISLAEQRLleddkrqfDSAWQEMLNHATQRVMEAEQtktrsELVHKE-TAARYNAAMGRMRQ 198
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREEL--------DELEAQIRGNGGDRLEQLER-----EIERLErELEERERRRARLEA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149034180 199 LEKKLKRAINKSKPYF-ELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIH--ERRRSN 266
Cdd:COG4913 367 LLAALGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKSN 437
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
50-264 |
7.97e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 50 ELEKLNQStddinRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATE 129
Cdd:pfam17380 349 ELERIRQE-----ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 130 VLRAAKETISLAEQRLLEDDK-RQFDSAWQEMLNHATQ----RVMEAEQTKTRSELvHKETAARYNAAMGRMRQLEKKLK 204
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERaREMERVRLEEQERQQQverlRQQEEERKRKKLEL-EKEKRDRKRAEEQRRKILEKELE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 205 RaiNKSKPYFELKAKyyvqlEQLKKTVDDLQAklALAKGEYKAALKSLERISDEIHERRR 264
Cdd:pfam17380 503 E--RKQAMIEEERKR-----KLLEKEMEERQK--AIYEEERRREAEEERRKQQEMEERRR 553
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-267 |
1.54e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 37 LEeeeevdpRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARrvaRQAQLE 116
Cdd:COG1196 248 LE-------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR---RELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 117 AQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQfdSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRM 196
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEEL--EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149034180 197 RQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNA 267
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-266 |
1.95e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 66 TELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKpywearrvarQAQLEAQKATQDFQRATEVLRAAKETISLAEQRL 145
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLE----------ELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 146 LE-DDKRQFDSAWQEMLNHATQrvmEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQL 224
Cdd:TIGR02168 305 QIlRERLANLERQLEELEAQLE---ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 149034180 225 EQLKKTVDDLQAKLALAKGEYKAALKSLERISDEiHERRRSN 266
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDR-RERLQQE 422
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
46-242 |
2.48e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 46 RIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQ 125
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 126 RATEVLRAAKETISLAEQRLLEDDKRQfdsawQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKR 205
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAEL-----EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
170 180 190
....*....|....*....|....*....|....*..
gi 149034180 206 AINKSKpyfELKAKYYVQLEQLKKTVDDLQAKLALAK 242
Cdd:COG1196 482 LLEELA---EAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-264 |
6.17e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 50 ELEKLNQSTDDINRRETELEDARQKfrsvlVEATVKLDELAK-KIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRAT 128
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKA-----AEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 129 EVlRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEA-----EQTKTRSELVHKETAARYNAAMGR-------- 195
Cdd:PTZ00121 1556 EL-KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKkaeeekkk 1634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149034180 196 MRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRR 264
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
114-264 |
8.42e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.76 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 114 QLEAQKATQDFQRATEVLRAAKETI-SLAEQRLLEDDKRQF----DSAWQEMLNHATQR----VMEAEQTKTRSELVHKE 184
Cdd:pfam06160 248 ENLALLENLELDEAEEALEEIEERIdQLYDLLEKEVDAKKYveknLPEIEDYLEHAEEQnkelKEELERVQQSYTLNENE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 185 TAaRYNAAMGRMRQLEKKL----KRAINKSKPYFELKAKY---YVQLEQLKKTVDDLQAKLA-LAKGEyKAALKSLERIS 256
Cdd:pfam06160 328 LE-RVRGLEKQLEELEKRYdeivERLEEKEVAYSELQEELeeiLEQLEEIEEEQEEFKESLQsLRKDE-LEAREKLDEFK 405
|
....*...
gi 149034180 257 DEIHERRR 264
Cdd:pfam06160 406 LELREIKR 413
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-263 |
1.25e-03 |
|
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: 41.58 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 47 IQGELEKLNQstdDINRRETELEDARQKFRSV---LVEATVKLDELAKKIGKAVEDskpywEARRVARQAQLEAQKATQ- 122
Cdd:TIGR02168 286 LQKELYALAN---EISRLEQQKQILRERLANLerqLEELEAQLEELESKLDELAEE-----LAELEEKLEELKEELESLe 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 123 -DFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEqtKTRSELVHKETAARYNAAMGRMRQLEK 201
Cdd:TIGR02168 358 aELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR--LERLEDRRERLQQEIEELLKKLEEAEL 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149034180 202 K-LKRAINKSKPyfelkakyyvQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERR 263
Cdd:TIGR02168 436 KeLQAELEELEE----------ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
50-265 |
1.55e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 50 ELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKAT-------- 121
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagve 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 122 --QDFQRATEVLRAAKETisLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELvhKETAARYNAAMGRMRQL 199
Cdd:COG4717 383 deEELRAALEQAEEYQEL--KEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--EELEEELEELREELAEL 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149034180 200 EKKLKRAINkSKPYFELKAKYYVQLEQLKKTVDDLQAklalakgeYKAALKSLERISDEIHERRRS 265
Cdd:COG4717 459 EAELEQLEE-DGELAELLQELEELKAELRELAEEWAA--------LKLALELLEEAREEYREERLP 515
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
69-262 |
2.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 69 EDARQkfrsvLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEV-----LRAAKETISLAEQ 143
Cdd:PTZ00121 1137 EDARK-----AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELrkaedARKAEAARKAEEE 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 144 RLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQ 223
Cdd:PTZ00121 1212 RKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK 1291
|
170 180 190
....*....|....*....|....*....|....*....
gi 149034180 224 LEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHER 262
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
76-261 |
2.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 76 RSVLVEATVK-LDELAKKIGK----AVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLE-DD 149
Cdd:COG4717 44 RAMLLERLEKeADELFKPQGRkpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 150 KRQFDSAWQEMlnHATQRVMEAEQTKTRSelvHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFE-LKAKYYVQLEQLK 228
Cdd:COG4717 124 LLQLLPLYQEL--EALEAELAELPERLEE---LEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLA 198
|
170 180 190
....*....|....*....|....*....|...
gi 149034180 229 KTVDDLQAKLALAKGEYKAALKSLERISDEIHE 261
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
46-206 |
9.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 46 RIQGELEKLNQSTDDINRRETELEDARQKFRSVL---------VEATVKLDELAKKIGKAVEDSKPYwearrvaRQAQLE 116
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLqllplyqelEALEAELAELPERLEELEERLEEL-------RELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149034180 117 AQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHatqrvmEAEQTKTRSELVHKETAARYNAAMGRM 196
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL------EEELEEAQEELEELEEELEQLENELEA 238
|
170
....*....|
gi 149034180 197 RQLEKKLKRA 206
Cdd:COG4717 239 AALEERLKEA 248
|
|
|