|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
95-404 |
3.84e-112 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 334.20 E-value: 3.84e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 95 NEKETMQILNERLANYLQKVRMLERENAELESKIQEESNKELPVLCPDYLSYYTTIEELQQKILCTKAENSRLVSQIDNT 174
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 175 KLTADDLRAKYEAEVSLRQLVESDANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNHKEEINSLQCQLG-ERLDIEV 253
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 254 TAAPSADLNQVLQEMRCQYEPIMETNRKDVEQWFNTQIEELNQQVVTSSQQQQCCQKEIIELRRSVNTLEVELQAQHRMR 333
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148277620 334 DSQECILTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSLLESSD 404
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-406 |
7.57e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 103 LNERLANYLQKVRMLERENAELESKIQ------EESNKELPVLcpdylsyYTTIEELQQKILCTKAENSRLVSQIDNTKL 176
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQeleeklEELRLEVSEL-------EEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 177 TADDLRAKYEAEVSLRQLVESDANGLKQILNVLTLGKADLEAQVQSLKEELlclknnhkeeinslqcqlgerldievtaa 256
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL----------------------------- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 257 psADLNQVLQEmrcqyepiMETNRKDVEQwfntQIEELNQQVVTSSQQQQCCQKEIIELRRSVNTLEVELQAQHRMRDSQ 336
Cdd:TIGR02168 361 --EELEAELEE--------LESRLEELEE----QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 337 ECILTETEarytalLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSLLESSDGK 406
Cdd:TIGR02168 427 LKKLEEAE------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-406 |
6.81e-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: 51.98 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 151 EELQQKILCTKAENSRLVSQIDNTKLTADDLRAKY-EAEVSLRQLvESDANGLKQILNVLTLGKADLEAQVQSLKEELlc 229
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALaELRKELEEL-EEELEQLRKELEELSRQISALRKDLARLEAEV-- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 230 lkNNHKEEINSLQCQLGERLD-IEVTAAPSADLNQVLQEMrcqyepimETNRKDVEQwfntQIEELNQQVVTSSQQQQCC 308
Cdd:TIGR02168 743 --EQLEERIAQLSKELTELEAeIEELEERLEEAEEELAEA--------EAEIEELEA----QIEQLKEELKALREALDEL 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 309 QKEIIELRRSVNTLEVELQAQHRMRDSQECILTETEARytalLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSR 388
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250
....*....|....*...
gi 148277620 389 LECEITTYRSLLESSDGK 406
Cdd:TIGR02168 885 LEEALALLRSELEELSEE 902
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
142-390 |
1.51e-06 |
|
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: 50.84 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 142 DYLSYYTTIEELQQKILCTKAENSRLVSQIDNTKLTADDLRAKY-EAEVSLRQLvESDANGLKQILNVLTLGKADLEAQV 220
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsDASRKIGEI-EKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 221 QSLKEELLclknNHKEEINSLQCQLGER-LDI----EVTAAPSADLN-QVLQEMRCQYEPIMETNRKDVEQwfntqIEEL 294
Cdd:TIGR02169 747 SSLEQEIE----NVKSELKELEARIEELeEDLhkleEALNDLEARLShSRIPEIQAELSKLEEEVSRIEAR-----LREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 295 NQQVVTSSQQQQCCQKEIIELRRSVNTLE---VELQAQ-----HRMRDSQEcILTETEARYTAL---LTQIQSLIDNLEA 363
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKeqiKSIEKEienlnGKKEELEE-ELEELEAALRDLesrLGDLKKERDELEA 896
|
250 260
....*....|....*....|....*..
gi 148277620 364 QLAEIRCALERQNQEYEILLDVKSRLE 390
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-408 |
2.16e-06 |
|
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: 49.76 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 150 IEELQQKILCTKAENSRLVSQIDNTKLTADDLRAKYEAEVSLRQLVESDANGLKQILNVLTLGKADLEAQVQSLKEELlc 229
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 230 lknnhKEEINSLQcQLGERLDIEVTAAPSaDLNQVLQEMRcQYEPIMETNRKdveqwfntQIEELNqqvvtssqqqqccq 309
Cdd:COG4942 107 -----AELLRALY-RLGRQPPLALLLSPE-DFLDAVRRLQ-YLKYLAPARRE--------QAEELR-------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 310 KEIIELRRSVNTLEVELQAQHRMRDSQEciltETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRL 389
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELE----EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|....*....
gi 148277620 390 ECEITTYRSLLESSDGKRP 408
Cdd:COG4942 233 EAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-401 |
2.43e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 74 NNFNARF-SLDDCSWYGEGINS--NEKETMQILNERlanylQKVRMLERENAELESKIqEESNKELPVLcpdylsyYTTI 150
Cdd:TIGR02168 641 LRPGYRIvTLDGDLVRPGGVITggSAKTNSSILERR-----REIEELEEKIEELEEKI-AELEKALAEL-------RKEL 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 151 EELQQKILCTKAENSRLVSQIDNTKLTADDLRAKYEAEVSLRQLVESDANGLKQILNVLTLGKADLEAQVQSLKEELLCL 230
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 231 K---NNHKEEINSLQCQLGErLDIEVTaapsaDLNQVLQEMRCQYEPiMETNRKDVEQwfntQIEELNQQVVTSSQQQQC 307
Cdd:TIGR02168 788 EaqiEQLKEELKALREALDE-LRAELT-----LLNEEAANLRERLES-LERRIAATER----RLEDLEEQIEELSEDIES 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 308 CQKEIIELRRSVNTLEVELQAQHRMRDSQECILTETEARYTALLTQIQSL----------IDNLEAQLAEIRCAL----- 372
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELeskrselrreLEELREKLAQLELRLeglev 936
|
330 340 350
....*....|....*....|....*....|....*
gi 148277620 373 ------ERQNQEYEILLDVKSRLECEITTYRSLLE 401
Cdd:TIGR02168 937 ridnlqERLSEEYSLTLEEAEALENKIEDDEEEAR 971
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-390 |
1.25e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 96 EKETMQILNERLANYLQKVRMLERENAELESKIQEESNKelpvlcpdylsyyttIEELQQKILCTKAENSRLVSQIDNTK 175
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELE---------------LEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 176 LTADDLRAKYEAEVSLRQLVESDANGLKQILNVLTLGKADLEAQVQSLKEELlclknnhKEEINSLQCQLGERLDIEVTA 255
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL-------AEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 256 ApsADLNQVLQEMRcqyepimetnrkdveqwfntQIEELNQQVVTSSQQQQCCQKEIIELRRSVNTLEVELQAQHRMRDS 335
Cdd:COG1196 382 E--ELAEELLEALR--------------------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 148277620 336 QECILTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLE 390
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
90-281 |
1.99e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 90 EGINSNEKETMQILNERLANYLQKVRMLERENAELESKIQE------ESNKELPVLCPDYLSYYTTIEELQQKILCTKAE 163
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSEserqraELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 164 NSRLVSQIDNTK-LTADDLRAKYEAEVSLRQLvESDANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNHKEEINSLQ 242
Cdd:pfam01576 463 VSSLESQLQDTQeLLQEETRQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLE 541
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148277620 243 cQLGE---RLDIEVTAapsadLNQVLQEMRCQYEPIMETNRK 281
Cdd:pfam01576 542 -ALEEgkkRLQRELEA-----LTQQLEEKAAAYDKLEKTKNR 577
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-273 |
2.21e-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: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 95 NEKETM-QILNERLANYLQKVRMLERENAELESKiQEESNKELPVLCPDylsyyttIEELQQKILCTKAENSRLVSQIDN 173
Cdd:TIGR02168 298 SRLEQQkQILRERLANLERQLEELEAQLEELESK-LDELAEELAELEEK-------LEELKEELESLEAELEELEAELEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 174 TKLTADDLRAKYEAevslrqlVESDANGLKQILNVLTLGKADLEAQVQSLKEELlclkNNHKEEINSLQCQLgERLDIEV 253
Cdd:TIGR02168 370 LESRLEELEEQLET-------LRSKVAQLELQIASLNNEIERLEARLERLEDRR----ERLQQEIEELLKKL-EEAELKE 437
|
170 180
....*....|....*....|
gi 148277620 254 TAAPSADLNQVLQEMRCQYE 273
Cdd:TIGR02168 438 LQAELEELEEELEELQEELE 457
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
105-378 |
2.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 105 ERLANYLQKVRMLERENAELESKIQeESNKELPVLcPDYLSYYTTIEEL---QQKILCTKAENSRLVSQIDNTKLTADDL 181
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLE-ALEAELDAL-QERREALQRLAEYswdEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 182 RAkyeaevsLRQLVEsdanGLKQILNVLTLGKADLEAQVQSLKEELlclkNNHKEEINSLQCQLgERLDIEVTAAPSADL 261
Cdd:COG4913 688 AA-------LEEQLE----ELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRL-EAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 262 NQVLQemrcqyEPIMETNRKDVEQWFNTQIEELNQqvvtssqqqqccqkeiiELRRSVNTLEvELQAQHRMR---DSQEc 338
Cdd:COG4913 752 EERFA------AALGDAVERELRENLEERIDALRA-----------------RLNRAEEELE-RAMRAFNREwpaETAD- 806
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 148277620 339 ILTETEAR--YTALLTQIQSliDNLEAQLAEIRCALERQNQE 378
Cdd:COG4913 807 LDADLESLpeYLALLDRLEE--DGLPEYEERFKELLNENSIE 846
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
148-443 |
2.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 148 TTIEELQQKILCTKAENSRLVSQIDNTKLTADDLRAKY-EAEVSLRQLVESDANGLKQIlnvltlgkADLEAQVQSLKEE 226
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnELQAELEALQAEIDKLQAEI--------AEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 227 LlclknnhKEEINSLQCQLGERLDIEVTAApSADLNQVLQemRCQY-EPIMETNRKDVEQwFNTQIEELNqqvvtssqqq 305
Cdd:COG3883 88 L-------GERARALYRSGGSVSYLDVLLG-SESFSDFLD--RLSAlSKIADADADLLEE-LKADKAELE---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 306 qccqkeiiELRRSVNTLEVELQAQHRMRDSQECILTETEARYTALLTQIQSLIDNLEAQLAEIrcALERQNQEYEILLDV 385
Cdd:COG3883 147 --------AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL--EAELAAAEAAAAAAA 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148277620 386 KSRLECEITTYRSLLESSDGKRPCYPRATKCEPSPWTSCKSGAIESTAPACTSSSPCS 443
Cdd:COG3883 217 AAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
94-401 |
5.46e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 94 SNEKETMQILNERLANYLQKVRMLERENAELESKIQ--EESNKELPvlcpdylsyyTTIEELQQKI-----LCTKAENSR 166
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRelEERIEELK----------KEIEELEEKVkelkeLKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 167 LVSqidntKLTADDLRAKYEAEVSLRQLvESDANGLKQILNVLTLGKA---DLEAQVQSLKEELLCLKNNHK--EEINSL 241
Cdd:PRK03918 297 KLS-----EFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEErleELKKKLKELEKRLEELEERHElyEEAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 242 QCQLgERLDIEVTAAPSADLNQVLQEMRCQYEPIMEtnrkdveqwfntQIEELNQQVVTSSQQQQCCQKEIIELRRSVNT 321
Cdd:PRK03918 371 KEEL-ERLKKRLTGLTPEKLEKELEELEKAKEEIEE------------EISKITARIGELKKEIKELKKAIEELKKAKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 322 LEV---ELQAQHRmrdsqecilTETEARYTALLTQIQSLIDNLEAQLAEIRcaleRQNQEYEILLDVKSRLeceiTTYRS 398
Cdd:PRK03918 438 CPVcgrELTEEHR---------KELLEEYTAELKRIEKELKEIEEKERKLR----KELRELEKVLKKESEL----IKLKE 500
|
...
gi 148277620 399 LLE 401
Cdd:PRK03918 501 LAE 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
98-399 |
5.78e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 98 ETMQILNERLANYLQKVRMlERENAELESKIQEESNK-ELPVLCPDYLSYYTTIEELQQKIlctkaenSRLVSQIDNTKL 176
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRR-EREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQL-------ASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 177 TADDLRAKYEA-EVSLRQLVES-DANGLKQILNVLTlGKADLEAQVQSLKEELlclknnhkEEINSLQCQLGERL----- 249
Cdd:TIGR02169 259 EISELEKRLEEiEQLLEELNKKiKDLGEEEQLRVKE-KIGELEAEIASLERSI--------AEKERELEDAEERLaklea 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 250 DIEVTAAPSADLNQVLQEMRCQYEPIME--TNRKDVEQWFNTQIEELNQQVVTSSQQQQCCQKEIIELRRSVNTLEVE-- 325
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREld 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148277620 326 -LQAQHRMRDSQeciLTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSL 399
Cdd:TIGR02169 410 rLQEELQRLSEE---LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
88-384 |
6.44e-04 |
|
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: 42.25 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 88 YGEGINSNEKETMQILNERLANYLQKVRMLERENAELESKIQEESNKELPVLcpdylsyYTTIEELQQKilctKAENSRL 167
Cdd:COG5185 219 STLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKL-------GENAESSKRL----NENANNL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 168 VSQIDNTKltadDLRAKYEAEVSLRQLVESDANGLKQ--ILNVLTLGKADLEAQVQSLKEELLCLKNNHKEEINSLQCQL 245
Cdd:COG5185 288 IKQFENTK----EKIAEYTKSIDIKKATESLEEQLAAaeAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEI 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 246 GERLDIEVTAAPSADLNQVLQEMRCQYEPIMETNR------KDVEQWFN-------TQIEELNQQVVTSSQQQQCCQKEI 312
Cdd:COG5185 364 ENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQnqrgyaQEILATLEdtlkaadRQIEELQRQIEQATSSNEEVSKLL 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148277620 313 IELRRSVNTLEVELQAQHRMRDSQECILTETEARYTA-----LLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLD 384
Cdd:COG5185 444 NELISELNKVMREADEESQSRLEEAYDEINRSVRSKKedlneELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLD 520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-369 |
9.10e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 92 INSNEKETMQI---LNERLANYLQKVRMLERENAELESKIQEESN---KELPVLCPDYLSYYTTIEELQQKILCTKAENS 165
Cdd:TIGR02169 246 LASLEEELEKLteeISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 166 RLVSQIDNTKLTADDLRAKYEAEVSLRQLVESDANGLKQILNvltlgkaDLEAQVQSLKEELLCLKNNHKeeinslqcQL 245
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE-------DLRAELEEVDKEFAETRDELK--------DY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 246 GERLDievtaapsaDLNQVLQEMRCQYEPIMETNRKDVEqwfntQIEELNQQVVTSSQQQQCCQKEIIELRRSVNTLEVE 325
Cdd:TIGR02169 391 REKLE---------KLKREINELKRELDRLQEELQRLSE-----ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 148277620 326 LQAQHRMRDSQECILTETEARYTAL---LTQIQSLIDNLEAQLAEIR 369
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVekeLSKLQRELAEAEAQARASE 503
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
89-264 |
2.10e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 89 GEGINSNEKETMQ----ILNERLANYLQKVRMLERENAELESKIQEESNKELPVLCpdylSYYTTIEELQQKILCTKAEN 164
Cdd:pfam09787 41 SSTALTLELEELRqerdLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQ----ELEEQLATERSARREAEAEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 165 SRLVSQIDNTKltaDDLRAKYEAEVSLRQLVESDANGLKQILNVLTLG---KADLEAQVQSLKEELLCLKNNHKE---EI 238
Cdd:pfam09787 117 ERLQEELRYLE---EELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSsssQSELENRLHQLTETLIQKQTMLEAlstEK 193
|
170 180
....*....|....*....|....*.
gi 148277620 239 NSLQCQLgERLDIEVTAAPSADLNQV 264
Cdd:pfam09787 194 NSLVLQL-ERMEQQIKELQGEGSNGT 218
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
97-367 |
5.12e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 97 KETMQILNERLANYLQKVRmlerenaELESKIQE--ESNkelpvlcpDYLSYYTTIEELQQKIlctkaenSRLVSQIDNT 174
Cdd:COG3206 174 RKALEFLEEQLPELRKELE-------EAEAALEEfrQKN--------GLVDLSEEAKLLLQQL-------SELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 175 KLTADDLRAKYEAevsLRQLVESDANGLKQILN--VLTLGKADLEAQVQSLKEELLCLKNNH------KEEINSLQCQLG 246
Cdd:COG3206 232 RAELAEAEARLAA---LRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHpdvialRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 247 ERLDievtaapsadlnQVLQEMRCQYEpIMETNRKDVEQwfntQIEELNqqvvtssqqqqccqkeiiELRRSVNTLEVEL 326
Cdd:COG3206 309 QEAQ------------RILASLEAELE-ALQAREASLQA----QLAQLE------------------ARLAELPELEAEL 353
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 148277620 327 QAQhrMRDsqeciLTETEARYTALLTQIQslidnlEAQLAE 367
Cdd:COG3206 354 RRL--ERE-----VEVARELYESLLQRLE------EARLAE 381
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
93-402 |
5.73e-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: 39.23 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 93 NSNEKETMQILNERLANYLQKVRMLERENAELESKIQEESN------KELPVLCPDYLSYYTTIEELQQKILCTKAENSR 166
Cdd:TIGR04523 302 NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 167 LVSQIDNTKLTADDLRAKYEAEVSLRQLVESDANGLKQILNVLtlgkadlEAQVQSLKEEllclKNNHKEEINSLQCQLG 246
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL-------EKEIERLKET----IIKNNSEIKDLTNQDS 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 247 E-RLDIEVTAAPSADLNQVLQEMRCQYEPImETNRKDVEQWF---NTQIEELNQQVVTSSQQQQCCQKEIIELRRSVNTL 322
Cdd:TIGR04523 451 VkELIIKNLDNTRESLETQLKVLSRSINKI-KQNLEQKQKELkskEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 323 EVE-LQAQHRMRDSQECILT-ETEARYTALLTQIQSLIDNLEaQLAEIRCALERQNQEYEILLDVKSR----LECEITTY 396
Cdd:TIGR04523 530 ESEkKEKESKISDLEDELNKdDFELKKENLEKEIDEKNKEIE-ELKQTQKSLKKKQEEKQELIDQKEKekkdLIKEIEEK 608
|
....*.
gi 148277620 397 RSLLES 402
Cdd:TIGR04523 609 EKKISS 614
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
152-402 |
7.13e-03 |
|
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: 38.95 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 152 ELQQKILCTKAENSRLVSQIDNTKLTADDLRAKYEAEVSLRQLVESDANGLKQILNVLTLGKADLEAQVQSLKEELLCLK 231
Cdd:pfam15921 427 EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 232 NNHK--EEINSLQCQLGERLDIEVtaapsadlnQVLQEMR------------CQYEPIMETNRKDVEQWFNTQIEELNQQ 297
Cdd:pfam15921 507 EKERaiEATNAEITKLRSRVDLKL---------QELQHLKnegdhlrnvqteCEALKLQMAEKDKVIEILRQQIENMTQL 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 298 VVTSSQQQQCCQKEIIELRRSVNTLEVELQAQHRMRDSQECILTETEARYTALLTQIQSLIDNLEAQLAeircALERQNQ 377
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR----AVKDIKQ 653
|
250 260
....*....|....*....|....*
gi 148277620 378 EYEILLDvksrlecEITTYRSLLES 402
Cdd:pfam15921 654 ERDQLLN-------EVKTSRNELNS 671
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-407 |
7.38e-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: 39.27 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 146 YYTTIEELQQKILCTKAENSRLVSQIDNTKLTADDLRAKYEAEVSLRQLVESDANGLKQILNVLTLGKADLEAQVQSLKE 225
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 226 ELLCLKNNhKEEINSLQCQLGERLDIEvtaapSADLNQVlqemrcqyepimetnrkdveqwfNTQIEELNqqvvtssqqq 305
Cdd:TIGR02168 310 RLANLERQ-LEELEAQLEELESKLDEL-----AEELAEL-----------------------EEKLEELK---------- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 306 qccqKEIIELRRSVNTLEVELQAQHRMRDSQEciltetearytALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDV 385
Cdd:TIGR02168 351 ----EELESLEAELEELEAELEELESRLEELE-----------EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
250 260
....*....|....*....|..
gi 148277620 386 KSRLECEITTYRSLLESSDGKR 407
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKE 437
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
76-390 |
7.89e-03 |
|
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: 38.90 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 76 FNARFSLDDCSwygEGINSNEKETMQI------LNERLANYLQKVRMLERENAELESKIQEeSNKELPvlcpdylSYYTT 149
Cdd:TIGR02169 705 DELSQELSDAS---RKIGEIEKEIEQLeqeeekLKERLEELEEDLSSLEQEIENVKSELKE-LEARIE-------ELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 150 IEELQQKILCTKAENSRlvSQIDNtkltaddLRAKYEAEVSLRQLVESDANGLKQILNVLTLGKADLEAQVQSLKEELLC 229
Cdd:TIGR02169 774 LHKLEEALNDLEARLSH--SRIPE-------IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 230 LKNNHKE---EINSLQCQLGErldievtaapsadlnqvlqemrcqyepimetnrkdveqwFNTQIEELnqqvvtsSQQQQ 306
Cdd:TIGR02169 845 LKEQIKSiekEIENLNGKKEE---------------------------------------LEEELEEL-------EAALR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 307 CCQKEIIELRRSVNTLEVELQAQHRMRDSQECILTETEARYTALLTQIQSLIDNLeAQLAEIRCALERQNQEYEILLDVK 386
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLEDVQ 957
|
....
gi 148277620 387 SRLE 390
Cdd:TIGR02169 958 AELQ 961
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
94-386 |
8.53e-03 |
|
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: 38.95 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 94 SNEKETMQILNERLANYLQKVRMLER-------ENAELESKIQEE--SNKELPVLCPDYLSyytTIEELQQKILCTKAEN 164
Cdd:pfam15921 558 AEKDKVIEILRQQIENMTQLVGQHGRtagamqvEKAQLEKEINDRrlELQEFKILKDKKDA---KIRELEARVSDLELEK 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 165 SRLVSQidntklTADDLRAKYEAEVSLRQLVeSDANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNHKEEINSLQCQ 244
Cdd:pfam15921 635 VKLVNA------GSERLRAVKDIKQERDQLL-NEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 245 LgERLDIEVTAAPSADLNQVLQEMRCQYEPIMETNRKDVEQwfnTQIEELNQQVVTSSQQQQCCQKEIIELRRSVNTLEV 324
Cdd:pfam15921 708 L-EQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQ---SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVAT 783
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148277620 325 ElqaQHRMRDSQEcILTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEIL-----LDVK 386
Cdd:pfam15921 784 E---KNKMAGELE-VLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLklqhtLDVK 846
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
90-397 |
9.62e-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: 38.80 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 90 EGINSNEKETMQILNERLANYLQKVRMLERENAELESKIQEESNkeLPVLCPDYLSYYTTIEELQQKILCTKAENSRLVS 169
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN--PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 170 QIDNTKLTADDLRAKYEAEVSLRQLVESDANGLKQILN-VLTLGKADLEAQVQSLKE--ELLCLKNN--HKEEINSLQCQ 244
Cdd:TIGR00618 557 QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVrLQDLTEKLSEAEDMLACEqhALLRKLQPeqDLQDVRLHLQQ 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 245 LGERLDIEVTAAPSADLNQVLQEMR----------------CQYEPIMETNRKDVEQWFNTQIEELNQQVVTSSQQQQCC 308
Cdd:TIGR00618 637 CSQELALKLTALHALQLTLTQERVRehalsirvlpkellasRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277620 309 QKEIIELRRSVNTLEVELQAQ-----------HRMRDSQECILTETEAR-YTALLTQIQSLidnleAQLAEIRCALERQN 376
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAARedalnqslkelMHQARTVLKARTEAHFNnNEEVTAALQTG-----AELSHLAAEIQFFN 791
|
330 340
....*....|....*....|.
gi 148277620 377 QEYEILLDVKSRLECEITTYR 397
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEI 812
|
|
| |
