|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
95-406 |
1.76e-136 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 394.29 E-value: 1.76e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 95 NEKETMQFLNDRLASYLTRVRQLEQENAELESRIQEASHSQVLTMTPDYQSHFRTIEELQQKILCTKAENARMVVNIDNA 174
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 175 KLAADDFRAKYEAELAMRQLVEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKKNHEEEVGSLRCQLGD-RLNIEV 253
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDtQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 254 DAAPPVDLTRVLEEMRCQYEAMVEANRRDVEEWFNMQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLR 333
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116488398 334 DSLENTLTESEARYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLEGEINTYRSLLENEDCK 406
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-401 |
5.90e-13 |
|
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: 71.24 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 106 RLASYLTRVRQLEQENAELESRIQEASHsqvltmtpDYQSHFRTIEELQQKILctkaenarmvvnidnaklaaddfraky 185
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEE--------ELEELTAELQELEEKLE--------------------------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 186 EAELAMRQLvEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKKNhEEEVGSLRCQLGDRLNIevDAAPPVDLTRVL 265
Cdd:TIGR02168 271 ELRLEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQ-LEELEAQLEELESKLDE--LAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 266 EEMRCQYEAMVEANRRdveewFNMQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQ----HSLRDSLENTLT 341
Cdd:TIGR02168 347 EELKEELESLEAELEE-----LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLearlERLEDRRERLQQ 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116488398 342 ESEA-----------RYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLEGEINTYRSLLE 401
Cdd:TIGR02168 422 EIEEllkkleeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-391 |
7.48e-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: 67.77 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 50 VCLPTTFRPA--SCLSKTYLSSSCQAASGISGSMGPGS---------WYSEGAFNGNEKET---MQFLNDRLASYLTRVR 115
Cdd:TIGR02168 608 VKFDPKLRKAlsYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlVRPGGVITGGSAKTnssILERRREIEELEEKIE 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 116 QLEQENAELESRIQEASHSQvLTMTPDYQSHFRTIEELQQKILCTKAENARMVVNIDNAKLAADDFRAKYEAELAMRQLV 195
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 196 EADINGLRRILDDLTLCKADLEAQVESLKEELmclkKNHEEEVGSLRCQLgDRLNIEVDaappvDLTRVLEEMrcqyeam 275
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEEL----KALREALDELRAEL-TLLNEEAA-----NLRERLESL------- 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 276 vEANRRDVEEwfnmQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARYSSQLAQMQ 355
Cdd:TIGR02168 830 -ERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
330 340 350
....*....|....*....|....*....|....*.
gi 116488398 356 cmitNVEAQLAEIRADLERQNQEyqvLLDVRARLEG 391
Cdd:TIGR02168 905 ----ELESKRSELRRELEELREK---LAQLELRLEG 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
78-379 |
2.34e-10 |
|
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: 62.78 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 78 SGSMGPGSWYSEGA--FNGNEKETMQFLNDR-------LASYLTRVRQLEQENAELESRIQEASHSQVLTMtpdyqshfR 148
Cdd:TIGR02169 652 SGAMTGGSRAPRGGilFSRSEPAELQRLRERleglkreLSSLQSELRRIENRLDELSQELSDASRKIGEIE--------K 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 149 TIEELQQKILCTK---AENARMVVNIDNAKLAADDFRAKYEAELAMRqlvEADINGLRRILDDLtlcKADL-EAQVESLK 224
Cdd:TIGR02169 724 EIEQLEQEEEKLKerlEELEEDLSSLEQEIENVKSELKELEARIEEL---EEDLHKLEEALNDL---EARLsHSRIPEIQ 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 225 EELMCLKKNHEEEVGSLRcQLGDRLN-IEVDAAPPVDLTRVLEEMRCQYEAMVEANRRDVEEwFNMQMEELNQQVATSSE 303
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLR-EIEQKLNrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEA 875
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116488398 304 QLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARYSSQLAQMQcmitNVEAQLAEIrADLERQNQEY 379
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE----ALEEELSEI-EDPKGEDEEI 946
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-375 |
1.79e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 150 IEELQQKILCTKAENARMVVNIDNAKLAADDFRAKYEAELAMRQLVEADINGLRRILDDLTLCKADLEAQVESLKEELmc 229
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 230 lkknhEEEVGSL-RCQLGDRLNIEVDAAPPVDLTRVLEEMRcqyeAMVEANRRDVEEwfnmqMEELNQQVATSSEQLQNY 308
Cdd:COG4942 107 -----AELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEE-----LRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116488398 309 QSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARYSSQLAQMQCMITNVEAQLAEIRADLERQ 375
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-404 |
2.81e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 96 EKETMQFLNDRLASYLTRVRQLEQENAELESRIQEAShsqvltmtpdyqshfRTIEELQQKILCTKAENARMVVNIDNAK 175
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELE---------------LELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 176 LAADDFRAKYEAELAMRQLVEADINGLRRILDDLTLCKADLEAQVESLKEELmclkKNHEEEVGSLRCQLGDRLNIEVDA 255
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL----AEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 256 AppvdltrvLEEMRCQYEAMVEANRRDVEEwfnMQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDS 335
Cdd:COG1196 385 A--------EELLEALRAAAELAAQLEELE---EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116488398 336 LENTLTESEARYSSQLAQmqcmITNVEAQLAEIRADLERQNQEYQVLLDVRARLEGEINTYRSLLENED 404
Cdd:COG1196 454 LEEEEEALLELLAELLEE----AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
105-400 |
3.79e-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: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 105 DRLASYLTRVRQLEQENAELESRIQEAshSQVLTMTPDYQSHFRTIEELQQKIlctkaenarmvvnIDNAKLAADdfRAK 184
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEAL--EAELDALQERREALQRLAEYSWDE-------------IDVASAERE--IAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 185 YEAELamRQLVEA--DINGLRRILDDLTLCKADLEAQVESLKEELMCLKKNHEEEVGSLRcQLGDRLNIEVDAAPPVDLT 262
Cdd:COG4913 673 LEAEL--ERLDASsdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD-ELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 263 RvLEEMRcqYEAMVEANRRDVEEWFNMQMEELNQQVATSSEQLQN--------YQSDIIDLRRTVNTLEiELQAqhsLRD 334
Cdd:COG4913 750 L-LEERF--AAALGDAVERELRENLEERIDALRARLNRAEEELERamrafnreWPAETADLDADLESLP-EYLA---LLD 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 335 SLENT-LTESEARYSSQLAqmQCMITNV-------EAQLAEIRADLERQNQE-----------YQvlLDVRARLEGEINT 395
Cdd:COG4913 823 RLEEDgLPEYEERFKELLN--ENSIEFVadllsklRRAIREIKERIDPLNDSlkripfgpgryLR--LEARPRPDPEVRE 898
|
....*
gi 116488398 396 YRSLL 400
Cdd:COG4913 899 FRQEL 903
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
170-390 |
4.16e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 170 NIDNAKLAADDFRAKY-------EAELAMRQLVEadinglrrilddltlckadLEAQVESLKEELmclkknheEEVGSLR 242
Cdd:COG3206 190 ELEEAEAALEEFRQKNglvdlseEAKLLLQQLSE-------------------LESQLAEARAEL--------AEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 243 CQLGDRLNIEVDAAPPVDLTRVLEEMRCQYeAMVEANRRDVEEWF---NMQMEELNQQVATSSEQLQNyqsdiiDLRRTV 319
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQL-AELEAELAELSARYtpnHPDVIALRAQIAALRAQLQQ------EAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116488398 320 NTLEIELQAQHSLRDSLENTLteseARYSSQLAQMQcmitNVEAQLAEIRADLERQNQEYQVLLdvrARLE 390
Cdd:COG3206 316 ASLEAELEALQAREASLQAQL----AQLEARLAELP----ELEAELRRLEREVEVARELYESLL---QRLE 375
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
290-404 |
7.55e-07 |
|
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: 50.92 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 290 QMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARyssqlaqmqcmITNVEAQLAEIR 369
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE-----------LAELEKEIAELR 96
|
90 100 110
....*....|....*....|....*....|....*
gi 116488398 370 ADLERQNQEYQVLLDVRARLeGEINTYRSLLENED 404
Cdd:COG4942 97 AELEAQKEELAELLRALYRL-GRQPPLALLLSPED 130
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-401 |
1.24e-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: 51.22 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 95 NEKETMQFLNDRLASY-----LTRVRQLEQENAELESRIQEAShsqvltmtpdyqshfRTIEELQQKIlctkAENARMVV 169
Cdd:TIGR02169 208 EKAERYQALLKEKREYegyelLKEKEALERQKEAIERQLASLE---------------EELEKLTEEI----SELEKRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 170 NIdNAKLAADDFRAKYEAELAMRQL------VEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKKNHEEEVGSLRC 243
Cdd:TIGR02169 269 EI-EQLLEELNKKIKDLGEEEQLRVkekigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 244 QLGDRLNIEVDAAppvDLTRVLEEMRCQYEAMVEANRrdveEWFNMQMEElnqqvatsSEQLQNYQSDIIDLRRTVNTLE 323
Cdd:TIGR02169 348 ERKRRDKLTEEYA---ELKEELEDLRAELEEVDKEFA----ETRDELKDY--------REKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 324 IELQAQHSLRDSLENTLTESEAR---YSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLEGEINTYRSLL 400
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
.
gi 116488398 401 E 401
Cdd:TIGR02169 493 A 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
183-403 |
1.86e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 183 AKYEAELAMRQLVEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKKNHEEEVGSLRCQLGDRLNIEVDAappvdlt 262
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI------- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 263 RVLEEMRcqyeamvEANRRDVEEwFNMQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTE 342
Cdd:COG1196 305 ARLEERR-------RELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116488398 343 SEARYSSQLAQMQcmitNVEAQLAEIRADLERQNQEYQVLLDVRARLEGEINTYRSLLENE 403
Cdd:COG1196 377 AEEELEELAEELL----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
148-401 |
2.45e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 148 RTIEELQQKIlctKAENARM--VVNI----DNAKLAADdfRAKYEAELAMRQLVEADINGLRRILDDLTLCKADLEAQVE 221
Cdd:COG3206 118 AAIERLRKNL---TVEPVKGsnVIEIsytsPDPELAAA--VANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 222 SLKEELMCLKKNH-----EEEVGSLRCQLgdrlnievdaappVDLTRVLEEMRCQYeAMVEANRRDVEEWFNMQMEELNQ 296
Cdd:COG3206 193 EAEAALEEFRQKNglvdlSEEAKLLLQQL-------------SELESQLAEARAEL-AEAEARLAALRAQLGSGPDALPE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 297 qvATSSEQLQNYQSDIIDLRRTVNTLEIELQAQH----SLRDSLENTLTESEARYSSQLAQMQCMITNVEAQLAEIRADL 372
Cdd:COG3206 259 --LLQSPVIQQLRAQLAELEAELAELSARYTPNHpdviALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQL 336
|
250 260 270
....*....|....*....|....*....|..
gi 116488398 373 ERQNQEYQVLLDVRA---RLEGEINTYRSLLE 401
Cdd:COG3206 337 AQLEARLAELPELEAelrRLEREVEVARELYE 368
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
144-375 |
4.82e-06 |
|
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: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 144 QSHFRTIEELQQKILctKAENARMV--------VNIDNAKLAADDFRA------KYEAELAmRQLVEADINGLRRILDDL 209
Cdd:COG4913 231 VEHFDDLERAHEALE--DAREQIELlepirelaERYAAARERLAELEYlraalrLWFAQRR-LELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 210 TLCKADLEAQVESLKEELMCLKKNHEEevgslrcQLGDRLNievdaappvDLTRVLEEMRCQYEAmVEANRRDVEEWfnm 289
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRG-------NGGDRLE---------QLEREIERLERELEE-RERRRARLEAL--- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 290 qMEELNQQVATSSEQLQNYQSdiiDLRRTVNTLEIELQAQHSLRDSLENTLTESEARY---SSQLAQMQCMITNVEAQLA 366
Cdd:COG4913 368 -LAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELrelEAEIASLERRKSNIPARLL 443
|
....*....
gi 116488398 367 EIRADLERQ 375
Cdd:COG4913 444 ALRDALAEA 452
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
88-405 |
5.04e-06 |
|
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: 48.80 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 88 SEGAFNGNEKETMqfLNDRLASYLTRVRQLEQ--ENAELESRIQEASHSQVLTMTPDYQSHFRTIEELQQKILCTKAENA 165
Cdd:COG5185 200 PSGTVNSIKESET--GNLGSESTLLEKAKEIIniEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 166 RMVvNIDNAKLAADDFRAK-----YEAELAMR--------QLVEADIN------------GLRRILDDLTLCKADLEAQV 220
Cdd:COG5185 278 KRL-NENANNLIKQFENTKekiaeYTKSIDIKkatesleeQLAAAEAEqeleeskretetGIQNLTAEIEQGQESLTENL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 221 ESLKEELMCLKKNH-----EEEVGSLRCQLgDRLNIEVDAAPpVDLTRVLEEMRCQYEAMVEANRRDVEEwFNMQMEELN 295
Cdd:COG5185 357 EAIKEEIENIVGEVelsksSEELDSFKDTI-ESTKESLDEIP-QNQRGYAQEILATLEDTLKAADRQIEE-LQRQIEQAT 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 296 QQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSlrDSLENTLTESEARYSSQLAQMQCMITNVEAQLAEIRADLERQ 375
Cdd:COG5185 434 SSNEEVSKLLNELISELNKVMREADEESQSRLEEAY--DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
|
330 340 350
....*....|....*....|....*....|...
gi 116488398 376 NQEYQVLLDVRARLEGEINTYRS---LLENEDC 405
Cdd:COG5185 512 LEGVRSKLDQVAESLKDFMRARGyahILALENL 544
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
97-401 |
9.02e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 97 KETMQFLNDRLASYLTRVRQLEQENAELESRIQEA-SHSQVLtmtpdyQSHFRTIEELQQkilctKAENARMVVnidnaK 175
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELkKEIEEL------EEKVKELKELKE-----KAEEYIKLS-----E 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 176 LAADDFRAKYEAELAMRQLvEADINGLRRILDDLTLCKA---DLEAQVESLKEELMCLKKNHE--EEVGSLRCQLgDRLN 250
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEErleELKKKLKELEKRLEELEERHElyEEAKAKKEEL-ERLK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 251 IEVDAAPPVDLTRVLEEMRCQYEAMVE---------ANRRDVEEWFNMQMEELNQQVAT------------SSEQLQNYQ 309
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELEKAKEEIEEeiskitariGELKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 310 SDIIDLRRTVNTL-EIELQAQHSLRDsLENTLteSEARYSSQLAQMQCMITNVEAQLAEIRA-DLERQNQEYQVLLDVRA 387
Cdd:PRK03918 459 AELKRIEKELKEIeEKERKLRKELRE-LEKVL--KKESELIKLKELAEQLKELEEKLKKYNLeELEKKAEEYEKLKEKLI 535
|
330
....*....|....
gi 116488398 388 RLEGEINTYRSLLE 401
Cdd:PRK03918 536 KLKGEIKSLKKELE 549
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
150-406 |
9.21e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 150 IEELQQKILCTKAENARMVVNIDNAKLAADDFRA-KYEAELAMRQLvEADINGLRRILDDLTLCKADLEAQveslkeelm 228
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEEELQAALARLEEETAqKNNALKKIREL-EAQISELQEDLESERAARNKAEKQ--------- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 229 clKKNHEEEVGSLRCQLGDRLnievdaappvDLTRVLEEMRCQYEAMVEANRRDVEE---WFNMQMEEL----NQQVATS 301
Cdd:pfam01576 294 --RRDLGEELEALKTELEDTL----------DTTAAQQELRSKREQEVTELKKALEEetrSHEAQLQEMrqkhTQALEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 302 SEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARYSSQlaqmqcmitnvEAQLAEIRA---DLERQNQE 378
Cdd:pfam01576 362 TEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKL-----------EGQLQELQArlsESERQRAE 430
|
250 260
....*....|....*....|....*...
gi 116488398 379 yqvLLDVRARLEGEINTYRSLLENEDCK 406
Cdd:pfam01576 431 ---LAEKLSKLQSELESVSSLLNEAEGK 455
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
290-404 |
9.46e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 290 QMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEAryssQLAQMQCMITNVEAQLAEIR 369
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA----ELAQAQEELESLQEEAEELQ 114
|
90 100 110
....*....|....*....|....*....|....*
gi 116488398 370 ADLERQNQEYQVLLDVRARLEGEINTYRSLLENED 404
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
193-393 |
3.48e-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: 44.92 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 193 QLVEADINGLRRILDDLTLCKADLEAQVESLKEELmclkKNHEEEVGSLRCQLgDRLNIEVDAappvdltrvleemrcqy 272
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARL----EAAKTELEDLEKEI-KRLELEIEE----------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 273 eamVEANRRDVEEwfnmqmeelNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARYSSQLA 352
Cdd:COG1579 71 ---VEARIKKYEE---------QLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 116488398 353 QMQCMITNVEAQLAEIRADLERQNQEyqvlldvRARLEGEI 393
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEAE-------REELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-304 |
4.34e-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: 45.53 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 103 LNDRLASYLTRVRQLEQENAELESRIQEASHSqvltmtpdyqshfrtIEELQQKILCTKAENARMVVNI--------DNA 174
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELAELEKE---------------IAELRAELEAQKEELAELLRALyrlgrqppLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 175 KLAADDFRAKYEAELAMRQLVEAD---INGLRRILDDLTLCKADLEAQVESLKEelmcLKKNHEEEVGSLRCQLGDRlni 251
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARreqAEELRADLAELAALRAELEAERAELEA----LLAELEEERAALEALKAER--- 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 116488398 252 evdaappVDLTRVLEEMRCQYEAMVEANRRDVEEwFNMQMEELNQQVATSSEQ 304
Cdd:COG4942 198 -------QKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAEAAAAAER 242
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
112-240 |
5.02e-05 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 42.77 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 112 TRVRQLEQENAELESRIQEAShsqvltmtpdyqshfRTIEELQQKilctKAENARMVVNIDNAKLAADDFRAKYEAELAM 191
Cdd:pfam04871 8 SEASSLKNENTELKAELQELS---------------KQYNSLEQK----ESQAKELEAEVKKLEEALKKLKAELSEEKQK 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 116488398 192 RQLVEADinglrriLDDLTLCKADLEAQVESLKEELmclkKNHEEEVGS 240
Cdd:pfam04871 69 EKEKQSE-------LDDLLLLLGDLEEKVEKYKARL----KELGEEVLS 106
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
160-393 |
5.22e-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: 45.14 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 160 TKAENARMVVNIDNAKLAADDFRAKYEAELAMRQLVEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKKNHEEevg 239
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 240 sLRCQLGDRLnievdaappvdltRVLEEMRCQYEAMVEANRRDVEEwFNMQMEELNQQVATSSEQLQNYQSDIIDLRRTV 319
Cdd:COG4942 102 -QKEELAELL-------------RALYRLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116488398 320 NTLEIELQAQHSLRDSLE---NTLTESEARYSSQLAQMQCMITNVEAQLAEIRADLERqnqeyqvLLDVRARLEGEI 393
Cdd:COG4942 167 AELEAERAELEALLAELEeerAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-------LEALIARLEAEA 236
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
172-390 |
5.40e-05 |
|
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: 45.94 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 172 DNAKLAADDFRAKYEAELAMRQLvEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKKNHEEEVGSLRC--QLGDRL 249
Cdd:pfam01576 472 DTQELLQEETRQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEAleEGKKRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 250 NIEVDAappvdLTRVLEEMRCQYEAMVEANRRDVEEWFNMQMEELNQ-QVATSSEQLQNYQSDIIDLRRTVNTLEIE--- 325
Cdd:pfam01576 551 QRELEA-----LTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQrQLVSNLEKKQKKFDQMLAEEKAISARYAEerd 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 326 -------------LQAQHSLRDSLEnTLTESEARYSSQLAQMQCMIT-------NV----------EAQLAEIRADLERQ 375
Cdd:pfam01576 626 raeaeareketraLSLARALEEALE-AKEELERTNKQLRAEMEDLVSskddvgkNVhelerskralEQQVEEMKTQLEEL 704
|
250
....*....|....*
gi 116488398 376 NQEYQVLLDVRARLE 390
Cdd:pfam01576 705 EDELQATEDAKLRLE 719
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
95-404 |
5.81e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 95 NEKETMQFLNDRLASYLTRVRQLEQENAELESRIQEASHSQVLTMTPDYQSHFRTIEELQQKILCTKAENARM---VVNI 171
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELeeeLEQL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 172 DNAKLAADDFRAKYEAE---------LAMRQLVEADINGLRRILDDLTLC--------------KADLEAQVESLkEELM 228
Cdd:COG4717 233 ENELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVLFLVlgllallflllareKASLGKEAEEL-QALP 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 229 CLKKNHEEEVGSLRCQLGDRLNIEVDAAPpvDLTRVLEEMRCQYEAMVEANRRDVEEWFNMQMEELNQQVATSSE----Q 304
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELL--ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelrA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 305 LQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEaryssqlaqmqcmitnVEAQLAEIRADLERQNQEYQVLLD 384
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE----------------LEEELEELEEELEELEEELEELRE 453
|
330 340
....*....|....*....|
gi 116488398 385 VRARLEGEINTyrslLENED 404
Cdd:COG4717 454 ELAELEAELEQ----LEEDG 469
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
149-404 |
6.14e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 149 TIEELQQKILCTKAENARMVVNIDNA---KLAADDFRAKYEAELAMRQLVEADInglrrilDDLTLCKADLEAQVESLKE 225
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQAretRDEADEVLEEHEERREELETLEAEI-------EDLRETIAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 226 ELMCLKKNHEEevgslrcqLGDRLNievDAAPPVDLTRVLEEMrcqyeamVEANRRDVEEwfnmQMEELNQQVATSSEQL 305
Cdd:PRK02224 280 EVRDLRERLEE--------LEEERD---DLLAEAGLDDADAEA-------VEARREELED----RDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 306 QNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEA---RYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVL 382
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
250 260
....*....|....*....|..
gi 116488398 383 LDVRARLEGEINTYRSLLENED 404
Cdd:PRK02224 418 REERDELREREAELEATLRTAR 439
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
290-402 |
1.09e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 290 QMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARYSSQLAQMQcmitNVEAQLAEIR 369
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK----ELEEQLESLQ 163
|
90 100 110
....*....|....*....|....*....|...
gi 116488398 370 ADLERQNQEYQVLLDvrARLEGEINTYRSLLEN 402
Cdd:COG4372 164 EELAALEQELQALSE--AEAEQALDELLKEANR 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-403 |
1.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 199 INGLRRILDDLTLCKADLEAQVESLKEELmclkKNHEEEVGSLRcQLGDRLNIEVDAAPpvdLTRVLEEMRCQYEAMVEA 278
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL----DALQERREALQ-RLAEYSWDEIDVAS---AEREIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 279 NRrdveewfnmQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARYSSQLAQmqcmi 358
Cdd:COG4913 684 SD---------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----- 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 116488398 359 tNVEAQLAEIRADlerqnqeyQVLLDVRARLEGEINTYRSLLENE 403
Cdd:COG4913 750 -LLEERFAAALGD--------AVERELRENLEERIDALRARLNRA 785
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
103-259 |
1.42e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 103 LNDRLASYLTRVRQLEQENAELESRIQEAsHSQVLTMTPDYQSH-FRTIEELQQKI--LCTKAENARMVVNIDNAKLA-- 177
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDAL-REELDELEAQIRGNgGDRLEQLEREIerLERELEERERRRARLEALLAal 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 178 -------ADDFRAKYEAELAMRQLVEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKK---NHEEEVGSLRCQLGD 247
Cdd:COG4913 372 glplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksNIPARLLALRDALAE 451
|
170
....*....|..
gi 116488398 248 RLNIEVDAAPPV 259
Cdd:COG4913 452 ALGLDEAELPFV 463
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
261-372 |
1.90e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 261 LTRVLEEMRCQYEAMV----EANRRDVEEWFNMQMEELNQQvaTSSEQLQNYQSDIIDLRRTvntleiELQAQHSLRDSL 336
Cdd:pfam15921 76 IERVLEEYSHQVKDLQrrlnESNELHEKQKFYLRQSVIDLQ--TKLQEMQMERDAMADIRRR------ESQSQEDLRNQL 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 116488398 337 ENTLTESEA----------RYSSQLAQMQCMITNVEAQLAEIRADL 372
Cdd:pfam15921 148 QNTVHELEAakclkedmleDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
249-402 |
2.68e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 249 LNIEVDAAPPVDLTRVLEEMrcqYEAMVEANR-------RDVEEWFNMQMEELNQQVATSSEQLQNYQSD---------- 311
Cdd:COG3206 138 IEISYTSPDPELAAAVANAL---AEAYLEQNLelrreeaRKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlseea 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 312 ------IIDLRRTVNTLEIELQAQHSLRDSLEN------------------------------TLTESEARYSSQLAQMQ 355
Cdd:COG3206 215 klllqqLSELESQLAEARAELAEAEARLAALRAqlgsgpdalpellqspviqqlraqlaeleaELAELSARYTPNHPDVI 294
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116488398 356 cmitNVEAQLAEIRADLERQNQ--------EYQVLLDVRARLEGEINTYRSLLEN 402
Cdd:COG3206 295 ----ALRAQIAALRAQLQQEAQrilasleaELEALQAREASLQAQLAQLEARLAE 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
176-401 |
3.31e-04 |
|
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: 42.83 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 176 LAADDFRAKYEAELamrQLVEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKK---NHEEEVGSLRCQLgDRLNIE 252
Cdd:COG4942 16 AAQADAAAEAEAEL---EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAEL-AELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 253 VDAappvdLTRVLEEMRCQYEAMVEAnrrdveewfnmqMEELNQQvatSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSL 332
Cdd:COG4942 92 IAE-----LRAELEAQKEELAELLRA------------LYRLGRQ---PPLALLLSPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116488398 333 RDSLENTLTESEARySSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLdvrARLEGEINTYRSLLE 401
Cdd:COG4942 152 AEELRADLAELAAL-RAELEAERAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELA 216
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
209-374 |
4.34e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 209 LTLCKADLEAQVESLKEELMCLKKNHEeevgslrcqlgdRLNIEVDAAppvdltRVLEEMRCQYEAMVEANRRDVEEwFN 288
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVA------------RLQAELDRL------QALESELAISRQDYDGATAQLRA-AQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 289 MQMEELNQQVATSSEQLQNYQS----------DIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARY----SSQLAQM 354
Cdd:pfam00529 110 AAVKAAQAQLAQAQIDLARRRVlapiggisreSLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENqaevRSELSGA 189
|
170 180
....*....|....*....|
gi 116488398 355 QCMITNVEAQLAEIRADLER 374
Cdd:pfam00529 190 QLQIAEAEAELKLAKLDLER 209
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
94-397 |
5.97e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 94 GNEKETMQFLNDRLASYLTRVRQLEQ------ENAELESRIQEASH--SQVLTMTPDYQSHFRTIEELQQKILCTKAENA 165
Cdd:PRK01156 308 ENKKQILSNIDAEINKYHAIIKKLSVlqkdynDYIKKKSRYDDLNNqiLELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 166 RMVVNIdnaklaaddfrakyeAELAMRQLVEADI-----NGLRRILDDLTLCKADLEAQVESLKEELMCLKKNHEEEVGS 240
Cdd:PRK01156 388 RMSAFI---------------SEILKIQEIDPDAikkelNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 241 LRC-----QLGDRLNIEVDAAPPVDLTRVLEEMRcqyEAMVEANRRDVEEWFNMQMEE-LN----QQVATSSEQLQNYQS 310
Cdd:PRK01156 453 SVCpvcgtTLGEEKSNHIINHYNEKKSRLEEKIR---EIEIEVKDIDEKIVDLKKRKEyLEseeiNKSINEYNKIESARA 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 311 DIIDLRRTVNTL-EIELQAQHSLRDSLENTLTESEARYSSQLAQMQCM----ITNVEAQLAEIRA---DLERQNQEYQV- 381
Cdd:PRK01156 530 DLEDIKIKINELkDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIslidIETNRSRSNEIKKqlnDLESRLQEIEIg 609
|
330 340
....*....|....*....|...
gi 116488398 382 LLDVRA-------RLEGEINTYR 397
Cdd:PRK01156 610 FPDDKSyidksirEIENEANNLN 632
|
|
| Phage_GP20 |
pfam06810 |
Phage minor structural protein GP20; This family consists of several phage minor structural ... |
112-235 |
6.20e-04 |
|
Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.
Pssm-ID: 429131 [Multi-domain] Cd Length: 149 Bit Score: 40.03 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 112 TRVRQLEQENAELESRIQEAShsqvltmtpdyqshfRTIEELQQKIlctkAENARMVVNIDNAKLAADDFRAKYEAELAM 191
Cdd:pfam06810 18 AKFDEVNTERDTLKEQLATRD---------------KQLKDLKKVA----KDNEELQKQIDELQAKNKDAEADYEAKIAD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 116488398 192 RQLVEA-----------DINGLRRILDDLTLcKADLEAQVESLKEELMCLKKNHE 235
Cdd:pfam06810 79 LKFDNAiklalkgakakNEKAVKALLDKDKL-KLKDDGTLIGLDEQIEGLKESDK 132
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
290-403 |
8.02e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 290 QMEELNQQVATSsEQLQNYQSDIIDLRRTVNTLEIE-LQAQHSLRDSLENTLTESEARYSSQLAQMQCMITNVEAQLAEI 368
Cdd:COG1196 201 QLEPLERQAEKA-ERYRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110
....*....|....*....|....*....|....*
gi 116488398 369 RADLERQNQEYQVLLDVRARLEGEINTYRSLLENE 403
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
95-369 |
8.12e-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: 41.93 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 95 NEKET-MQFLNDRLASYLTRVRQLEQENAELESRIQEASH------SQVLTMTPDYQSHFRTIEELQQKILCTKAENARM 167
Cdd:TIGR04523 366 EEKQNeIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlnqqkdEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 168 VVNIDNAKLAADDFRAKYEAELAMRQLVEADINGLRRILDD--------------LTLCKADLEAQVESLKEELMCLKKN 233
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekelkkLNEEKKELEEKVKDLTKKISSLKEK 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 234 hEEEVGSLRCQLGDRLnievdaappVDLTRVLEEM-----RCQYEAMVEANRRDVEEWFNMQMEELNQQvATSSEQLQNY 308
Cdd:TIGR04523 526 -IEKLESEKKEKESKI---------SDLEDELNKDdfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQ-EEKQELIDQK 594
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116488398 309 QSDIIDLRRTVNTLEIELqaqhslrDSLENTLTESEARY---SSQLAQMQCMITNVEAQLAEIR 369
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKI-------SSLEKELEKAKKENeklSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
178-378 |
1.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 178 ADDFRAKYEAELAMRQLVEADING-LRRILDDLtlckADLEAQVESLKEELmclkKNHEEEVGSLRCQLgDRLNIEVDAA 256
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAeLDALQAEL----EELNEEYNELQAEL----EALQAEIDKLQAEI-AEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 257 ppvdlTRVLEE-MRCQY---------EAMVEANrrDVEEwFNMQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIEL 326
Cdd:COG3883 85 -----REELGErARALYrsggsvsylDVLLGSE--SFSD-FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116488398 327 QAQHSLRDSLENTLTESEARYSSQ---LAQMQCMITNVEAQLAEIRADLERQNQE 378
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQealLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
105-399 |
1.35e-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: 41.11 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 105 DRLASYLTRVRQLEQENAELESRIQEASHSQVLTMTP-----DYQSHFRTIEELQQKILCTKAENArmvvnidnAKLAAD 179
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPeqdlqDVRLHLQQCSQELALKLTALHALQ--------LTLTQE 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 180 DFRAKY----EAELAMRQLVEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKKN--HEEEVGSLRCQLGDRLNIEV 253
Cdd:TIGR00618 659 RVREHAlsirVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYdrEFNEIENASSSLGSDLAARE 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 254 DAAPPVdLTRVLEEMRCQYEAMVEANRRDVE-------------------EWFNMQMEELNQQVATSSEQLQNYQSDIID 314
Cdd:TIGR00618 739 DALNQS-LKELMHQARTVLKARTEAHFNNNEevtaalqtgaelshlaaeiQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 315 LRrtvnTLEIELQAQhslrdSLENTLTESEaryssQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLldvrARLEGEIN 394
Cdd:TIGR00618 818 IL----NLQCETLVQ-----EEEQFLSRLE-----EKSATLGEITHQLLKYEECSKQLAQLTQEQAKI----IQLSDKLN 879
|
....*
gi 116488398 395 TYRSL 399
Cdd:TIGR00618 880 GINQI 884
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
109-399 |
1.44e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.99 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 109 SYLTRvRQLEQENAELESRIQEASHSQV---------LTMTPDYQSHFRTIEELQQKILctkaenARMVVNIDNAKLAAD 179
Cdd:pfam06160 1 GLLLR-KKIYKEIDELEERKNELMNLPVqeelskvkkLNLTGETQEKFEEWRKKWDDIV------TKSLPDIEELLFEAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 180 DFRAKY----------EAELAMrQLVEADINGLRRILDDLTLCKADLEAQVESLKEELMCLKKN---HEEEVGSLRCQLG 246
Cdd:pfam06160 74 ELNDKYrfkkakkaldEIEELL-DDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTllaNRFSYGPAIDELE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 247 DRL-NIEVDAAPPVDLT---------RVLEEMRCQYEAM------VEANRRDVEEWFNMQMEEL---------------- 294
Cdd:pfam06160 153 KQLaEIEEEFSQFEELTesgdylearEVLEKLEEETDALeelmedIPPLYEELKTELPDQLEELkegyremeeegyaleh 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 295 ---NQQVATSSEQLQNYQSDIIDLRrtVNTLEIELQAQHSLRDSLENTL-TESEARYS--SQLAQMQCMITNVEAQLAEI 368
Cdd:pfam06160 233 lnvDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERIDQLYDLLeKEVDAKKYveKNLPEIEDYLEHAEEQNKEL 310
|
330 340 350
....*....|....*....|....*....|.
gi 116488398 369 RADLERQNQEYQvlLDvrarlEGEINTYRSL 399
Cdd:pfam06160 311 KEELERVQQSYT--LN-----ENELERVRGL 334
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
105-378 |
1.49e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 105 DRLASYLTRVRQLEQENAELESRIQEAShsqvltmtpDYQSHFRTIEELQQK--ILCTKAENARMVVNIDNAKLA----- 177
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAE---------DLVEAEDRIERLEERreDLEELIAERRETIEEKRERAEelrer 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 178 ADDFRAKYEAELAMRQLVEADINGLRRILDDLTLCKADLEAQVESLK--EELMCLKKNHEEEVGSLRCQLGDRLNIEVDA 255
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREALAELNDER 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 256 APPVDLTRvleEMRCQYEAMVEANRrdVEEWFNmQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRD- 334
Cdd:PRK02224 626 RERLAEKR---ERKRELEAEFDEAR--IEEARE-DKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELREr 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 116488398 335 --SLENTLTESEARYSSqlaqmqcmITNVEAQLAEIRADLERQNQE 378
Cdd:PRK02224 700 reALENRVEALEALYDE--------AEELESMYGDLRAELRQRNVE 737
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-404 |
2.53e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 96 EKETMQFLNDRLASYLTRVRQLEQENAELESRIQEashsqvLTMT-----PDYQSHFRTIEELQQKILCTKAENARMVvn 170
Cdd:PRK02224 228 QREQARETRDEADEVLEEHEERREELETLEAEIED------LRETiaeteREREELAEEVRDLRERLEELEEERDDLL-- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 171 idnAKLAADDfrAKYEAELAMRQLVEADINGLRRILDDLTLCKADLEAQVESLKEELmclkKNHEEEVGSLRCQlGDRLN 250
Cdd:PRK02224 300 ---AEAGLDD--ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA----DDLEERAEELREE-AAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 251 IEVDAAppvdltrvleemrcqyEAMVEANRRDVEEwFNMQMEELNQQVATSSEQLQN-------YQSDIIDLRRTVNTLE 323
Cdd:PRK02224 370 SELEEA----------------REAVEDRREEIEE-LEEEIEELRERFGDAPVDLGNaedfleeLREERDELREREAELE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 324 IELQaqhSLRDSLENTLTESEARYSSQLAQ------MQCMITNVEAQLAEIRADLERqnqeyqvLLDVRARLEGEINTYR 397
Cdd:PRK02224 433 ATLR---TARERVEEAEALLEAGKCPECGQpvegspHVETIEEDRERVEELEAELED-------LEEEVEEVEERLERAE 502
|
....*..
gi 116488398 398 SLLENED 404
Cdd:PRK02224 503 DLVEAED 509
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
123-401 |
2.65e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 123 ELESRIQEASHSQVLTMTPDYQSHFRTIEELQQKILCTKAENARMVVNiDNAKLAADDFRAKY------EAELAMRQLVE 196
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL-KKEILEKKQEELKFvikelqQLEGSSDRILE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 197 ADiNGLRRILDDLTlcKADLEAQVESLKEELMCLKKNH----------EEEVGSLRCQLGDRLNIEVDAAPPVDLTRVLE 266
Cdd:TIGR00606 476 LD-QELRKAERELS--KAEKNSLTETLKKEVKSLQNEKadldrklrklDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 267 EMRCQYEAMVEA------NRRDVEEWFNMQMEELNQQvatsseqlqnyQSDIIDLRRTVNTLEielQAQHSLRDSLEnTL 340
Cdd:TIGR00606 553 KIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQT-----------RDRLAKLNKELASLE---QNKNHINNELE-SK 617
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116488398 341 TESEARYSSQLAQMqCMITNVEAQLAEIRADLERQNQEyqvlldvRARLEGEINTYRSLLE 401
Cdd:TIGR00606 618 EEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEKSSKQ-------RAMLAGATAVYSQFIT 670
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
103-375 |
2.70e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 103 LNDRLASYLTRVRQLEQENAELESriQEASHSQVL----TMTPDYQSHFRTIEELQQkiLCTKAEnarmvVNIDNAKLAA 178
Cdd:COG3096 373 AAEQLAEAEARLEAAEEEVDSLKS--QLADYQQALdvqqTRAIQYQQAVQALEKARA--LCGLPD-----LTPENAEDYL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 179 DDFRAKYEAE----LAMRQ---LVEADINGLRRILDDLTLCKADLE-AQVESLKEELMCLKKNHE---EEVGSLRCQLGD 247
Cdd:COG3096 444 AAFRAKEQQAteevLELEQklsVADAARRQFEKAYELVCKIAGEVErSQAWQTARELLRRYRSQQalaQRLQQLRAQLAE 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 248 rlnIEVDAAPPVDLTRVLEEMrCQYEAMVEANRRDVEEwfnmQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEI--- 324
Cdd:COG3096 524 ---LEQRLRQQQNAERLLEEF-CQRIGQQLDAAEELEE----LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRArik 595
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116488398 325 ELQAQ----HSLRDSLENTLTESEARYSSQLAQMQCMITNVEA---------QLAEIRADLERQ 375
Cdd:COG3096 596 ELAARapawLAAQDALERLREQSGEALADSQEVTAAMQQLLERereatverdELAARKQALESQ 659
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
118-401 |
3.51e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 118 EQENAELESRIQEASHSQVLTMTPDYQSHFRTIEELQQKILCTKaenaRMVVNIDNAKLAADDFRAKYEAELAMRQLVEA 197
Cdd:pfam01576 326 EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAK----RNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 198 DINGLRRilddltlckaDLEAQVESLKeelmcLKKNHEEEVgslRCQLGDRLN---IEVDAappvdLTRVLEEMrcqyEA 274
Cdd:pfam01576 402 DSEHKRK----------KLEGQLQELQ-----ARLSESERQ---RAELAEKLSklqSELES-----VSSLLNEA----EG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 275 MVEANRRDVeewfnmqmEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIElqaQHSLRDSLENtltESEARyssqlAQM 354
Cdd:pfam01576 455 KNIKLSKDV--------SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDE---RNSLQEQLEE---EEEAK-----RNV 515
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 116488398 355 QCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLEGEINTYRSLLE 401
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
96-402 |
3.67e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 96 EKETMQFLNDRLASYLTRVRQLEQENAELESRiqeasHSQVLTMTPDYQSHFRTIEElqqkiLCTKAENARmvvnidnAK 175
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKK-----HQQLCEEKNALQEQLQAETE-----LCAEAEEMR-------AR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 176 LAA---------DDFRAKYEAE-------LAMRQLVEADINGLRRILDD-------LTLCKADLEAQVESLKEELMCLkk 232
Cdd:pfam01576 66 LAArkqeleeilHELESRLEEEeersqqlQNEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTEAKIKKLEEDILLL-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 233 nhEEEVGSL---RCQLGDRLN-IEVDAAPPVDLTRVLEEMRCQYEAMVE--ANRRDVEEWFNMQMEELNQQVATSS---- 302
Cdd:pfam01576 144 --EDQNSKLskeRKLLEERISeFTSNLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEEKGRQELEKAKRKLEGEStdlq 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 303 EQLQNYQSDIIDLRRTVNTLEIELQAqhslrdslenTLTESEARySSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVL 382
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQA----------ALARLEEE-TAQKNNALKKIRELEAQISELQEDLESERAARNKA 290
|
330 340
....*....|....*....|
gi 116488398 383 LDVRARLEGEINTYRSLLEN 402
Cdd:pfam01576 291 EKQRRDLGEELEALKTELED 310
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
290-401 |
4.10e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 290 QMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARYSSQLAQmqcmITNVEAQLAEIR 369
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGR----AGELAQELDSEK 129
|
90 100 110
....*....|....*....|....*....|..
gi 116488398 370 ADLERQNQEYQVLLDVRARLEGEINTYRSLLE 401
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALD 161
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
101-412 |
5.58e-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: 39.18 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 101 QFLNDRLASYLTRVRQLEQENAELESRIQEASHSQvltmtpdyqshfrtiEELQQKilcTKAENARmvvniDNAKLAADD 180
Cdd:TIGR00618 208 LCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH---------------AYLTQK---REAQEEQ-----LKKQQLLKQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 181 FRAK---YEAELAMRQLVEADINGLRRILDDLTLCKA--DLEAQVESLKEELMCLKKNHEEEVGSLRCQLGDRLNIEVDA 255
Cdd:TIGR00618 265 LRARieeLRAQEAVLEETQERINRARKAAPLAAHIKAvtQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 256 APPVDLTRVLEEMRCQYEamVEANRRDVeewFNMQMEE------LNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQ 329
Cdd:TIGR00618 345 RLLQTLHSQEIHIRDAHE--VATSIREI---SCQQHTLtqhihtLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 330 HSLRDSLENTLTESEA--RYSSQLAQ-MQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARL--EGEINTYRSLLENED 404
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELqqRYAELCAAaITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHlqETRKKAVVLARLLEL 499
|
....*...
gi 116488398 405 CKLPCNPC 412
Cdd:TIGR00618 500 QEEPCPLC 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
107-393 |
5.88e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 107 LASYLTRVRQLEQENAELESRIQEASHSQV-LTMTPDYQSHFRTIEELQQKIlcTKAENARMVVNIDNAKLAADDFRaKY 185
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELReLEKVLKKESELIKLKELAEQL--KELEEKLKKYNLEELEKKAEEYE-KL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 186 EAELAMrqlVEADINGLRRILDDLTLCK---ADLEAQVESLKEELMCLKKNHEEEVGSLRCQLGDRLN---------IEV 253
Cdd:PRK03918 531 KEKLIK---LKGEIKSLKKELEKLEELKkklAELEKKLDELEEELAELLKELEELGFESVEELEERLKelepfyneyLEL 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 254 DAAPPvDLTRVLEEM-RCQYEA-MVEANRRDVEEWFNMQMEELNQ-QVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQH 330
Cdd:PRK03918 608 KDAEK-ELEREEKELkKLEEELdKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELE 686
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116488398 331 SLRDSLENTLTESEAryssQLAQMQCMITNVEaQLAEIRADLER---QNQEYQVLLDVRA-----RLEGEI 393
Cdd:PRK03918 687 KRREEIKKTLEKLKE----ELEEREKAKKELE-KLEKALERVEElreKVKKYKALLKERAlskvgEIASEI 752
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
265-392 |
7.09e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 265 LEEMRCQYEAMVEAnRRDVEEWfnmqmEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESE 344
Cdd:COG4717 114 LREELEKLEKLLQL-LPLYQEL-----EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 116488398 345 ARYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLEGE 392
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
271-407 |
8.08e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 38.12 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 271 QYEAMVEANRRDVEEWFNMQMEELNQQVAtssEQLQNYQSDIIDLRRTVNTLEIELQAQHSLRDSLENTLTESEARYSSQ 350
Cdd:cd22656 92 YYAEILELIDDLADATDDEELEEAKKTIK---ALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDL 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 116488398 351 LAQMQCMITNveAQLAEIRADLERQNQEYqvlldvRARLEGEINTYRSLLENEDCKL 407
Cdd:cd22656 169 LTDEGGAIAR--KEIKDLQKELEKLNEEY------AAKLKAKIDELKALIADDEAKL 217
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
280-355 |
8.16e-03 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 38.02 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 280 RRDVEEWF---NMQMEELNQQVATSSEQLQNYQSDIIDLRRTVNTLEIE----LQAQHSLRDSLENTLTESEaRYSSQLA 352
Cdd:cd22654 43 KENVREWLdeyNPKLIDLNQDMINFSQRFNNYYDKLYDLAGKINEDEQAkedfLNGINKLQSQLQTIQNSME-QTSSNLN 121
|
...
gi 116488398 353 QMQ 355
Cdd:cd22654 122 RFK 124
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
213-400 |
8.64e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 38.74 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 213 KADLEAQVESLKEelmclKKNHEEEVGSLRCQL----------------GDRLNIEVDAAPpvdltRVLEEMRCQYEAMV 276
Cdd:PRK11281 38 EADVQAQLDALNK-----QKLLEAEDKLVQQDLeqtlalldkidrqkeeTEQLKQQLAQAP-----AKLRQAQAELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 277 EANRRDVEEWF-NMQMEELNQQVATSSEQLQNYQSDIIDLrrtvNTLEIELQ-----AQHSL----------RDSLENTL 340
Cdd:PRK11281 108 DDNDEETRETLsTLSLRQLESRLAQTLDQLQNAQNDLAEY----NSQLVSLQtqperAQAALyansqrlqqiRNLLKGGK 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116488398 341 TESEARYSSQLAQMQCMITNVEAQLAEIRADLERQNQeYQVLLDVR--------ARLEGEINTYRSLL 400
Cdd:PRK11281 184 VGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQ-LQDLLQKQrdyltariQRLEHQLQLLQEAI 250
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
110-403 |
8.69e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 38.28 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 110 YLTRVRQLEQENAELESR-----IQEASHsqvLTMTPDYQSHFrtiEELQQKIlctkaenarmvVNIDNAKLAADDFRAk 184
Cdd:PRK04778 27 NYKRIDELEERKQELENLpvndeLEKVKK---LNLTGQSEEKF---EEWRQKW-----------DEIVTNSLPDIEEQL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 185 YEAELAMRQL----VEADINGLRRILDDLtlckadlEAQVESLKEELMCLKKNHEE---EVGSLRCQLGdrlnievdaap 257
Cdd:PRK04778 89 FEAEELNDKFrfrkAKHEINEIESLLDLI-------EEDIEQILEELQELLESEEKnreEVEQLKDLYR----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 258 pvDLTRVLEEMRCQY-EAM--VEANRRDVEEWFNmQMEELNQQ--VATSSEQLQNYQSDIIDLRRTVN-------TLEIE 325
Cdd:PRK04778 151 --ELRKSLLANRFSFgPALdeLEKQLENLEEEFS-QFVELTESgdYVEAREILDQLEEELAALEQIMEeipellkELQTE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 326 LQAQhsLRDsLENTLTE-SEARY-------SSQLAQMQCMITNVEAQLAEIRAD-LERQNQEyqvlldvrarLEGEINTY 396
Cdd:PRK04778 228 LPDQ--LQE-LKAGYRElVEEGYhldhldiEKEIQDLKEQIDENLALLEELDLDeAEEKNEE----------IQERIDQL 294
|
....*..
gi 116488398 397 RSLLENE 403
Cdd:PRK04778 295 YDILERE 301
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
179-396 |
9.09e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 38.67 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 179 DDFRAKYEAELAMRQLVEADINglrrilDDLTLCKADLEAQVESLKEELMCLKKNHEEEVGSLrcqlgdrlniEVDAAPP 258
Cdd:pfam12128 707 EQKREARTEKQAYWQVVEGALD------AQLALLKAAIAARRSGAKAELKALETWYKRDLASL----------GVDPDVI 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116488398 259 VDLTRVLEEMRCQYEAmVEANRRDVEEWFNMQMEelnqqvaTSSEQLQNYQSDIIDLRRTVNTLEIELQAQHS----LRD 334
Cdd:pfam12128 771 AKLKREIRTLERKIER-IAVRRQEVLRYFDWYQE-------TWLQRRPRLATQLSNIERAISELQQQLARLIAdtklRRA 842
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116488398 335 SLENTLTESEA---RYSSQLAQMQCMITNV----EAQLAEiRADLERQNQEYQV--LLDVRARLEGEINTY 396
Cdd:pfam12128 843 KLEMERKASEKqqvRLSENLRGLRCEMSKLatlkEDANSE-QAQGSIGERLAQLedLKLKRDYLSESVKKY 912
|
|
| |
