|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
95-406 |
9.55e-140 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 416.63 E-value: 9.55e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 95 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQK-HAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHI 173
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 174 EEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAELLAQLQASHATVER 253
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 254 KDYLKTDLTTALKEIRAQLECQSDHNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 333
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 128146 334 ESLERQLSDIEERHNNDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 406
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
625-749 |
2.37e-18 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 90.52 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 625 EKPATPKvtSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKP 704
Cdd:PTZ00449 577 KKPEFPK--DPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKII 654
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 128146 705 ATPEKPRSPEKPSSPLKDEKAVVE--ESITVTKVTKVTAEVEVSKEA 749
Cdd:PTZ00449 655 KSPKPPKSPKPPFDPKFKEKFYDDylDAAAKSKETKTTVVLDESFES 701
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
12-94 |
1.55e-17 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 77.82 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 12 SYRRVMTEtrATYSRASASPSSGFR---SQSWSRGSGSTVSSSYKRTNLGAPRTAYGSTVlssAESLDVSQSSLLNGaaE 88
Cdd:pfam04732 5 SYRRMFGD--SSSSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSSRSSSRSSYPSLA---ADSLDFSLADALNQ--E 77
|
....*.
gi 128146 89 LKLSRS 94
Cdd:pfam04732 78 FKATRT 83
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-346 |
2.53e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 99 QLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQ 178
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 179 RLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHATVERKDYLK 258
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 259 TDLTTALKEIRAQLEcQSDHNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLER 338
Cdd:COG1196 389 LEALRAAAELAAQLE-ELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
....*...
gi 128146 339 QLSDIEER 346
Cdd:COG1196 464 LLAELLEE 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
91-403 |
4.58e-15 |
|
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: 79.72 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 91 LSRSNEKEQLQglndrfagyiEKVHYLEQQNKEIEAELAALRQKHagraqlgDAYEQELRELRGALEQVSHEKAQIQLDS 170
Cdd:TIGR02168 673 LERRREIEELE----------EKIEELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 171 EHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHAT 250
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 251 VERKDYLKTDLTTALKEIRAQLECQSDHNMHQAEEWfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVR 330
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQI-----EELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 331 GTKESLERQLSDIE------ERHNNDLTTY----QDTIHQLENELRGTKWEMARHLR----EYQDLLNVKMALDIEIAAY 396
Cdd:TIGR02168 887 EALALLRSELEELSeelrelESKRSELRREleelREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDD 966
|
....*..
gi 128146 397 RKLLEGE 403
Cdd:TIGR02168 967 EEEARRR 973
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
626-719 |
2.71e-14 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 77.42 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 626 KPATPKVTSpEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPA 705
Cdd:PTZ00449 568 KPSKIPTLS-KKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPE 646
|
90
....*....|....
gi 128146 706 TPEKPRSPEKPSSP 719
Cdd:PTZ00449 647 RPEGPKIIKSPKPP 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-349 |
2.90e-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: 73.94 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 62 TAYGSTVLSSAESLDVSQSSLlngaAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAgraql 141
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKL----EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE----- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 142 gdAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQS 221
Cdd:TIGR02168 320 --ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 222 LQdevaflrgnheEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQlECQSDHNMHQAEEwfkcryAKLTEAAEQN 301
Cdd:TIGR02168 398 LN-----------NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEEL------EELQEELERL 459
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 128146 302 KEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNN 349
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
118-414 |
3.14e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 118 EQQNKEIEAELAALRQKHAGRAQLG---DAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDET 194
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 195 EATIAALRKEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLEc 274
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 275 qsdhnmHQAEEWFKCRYAKLTEAAEQnkEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTY 354
Cdd:COG1196 376 ------EAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 128146 355 QDTIHQLENELRGTKWEMARHLRE---YQDLLNVKMALDIEIAAYRKLLEGEETRFSAFSGSI 414
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEaalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-345 |
8.79e-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: 72.40 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 93 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEH 172
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 173 IEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEvaflRGNHEEEVAELLAQLQASHATVE 252
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE----RASLEEALALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 253 RKDYLKTDLTTALKEIRAQLEcqsDHNMHQAE---------EWFKCRYAKLTEAAEQNKEAI----RSAKEEIAEYRRQL 319
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLA---QLELRLEGlevridnlqERLSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKI 981
|
250 260 270
....*....|....*....|....*....|...
gi 128146 320 QS------KSI-ELESVRGTKESLERQLSDIEE 345
Cdd:TIGR02168 982 KElgpvnlAAIeEYEELKERYDFLTAQKEDLTE 1014
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-388 |
4.95e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 117 LEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQ--LDS-----EHIEEDIQRLRERFEDEAR 189
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkeLYAlaneiSRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 190 LRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKE-- 267
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQia 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 268 -IRAQLECQSDHnMHQAEEwfkcRYAKLTEAAEQNKEAIRSAkeEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEER 346
Cdd:TIGR02168 397 sLNNEIERLEAR-LERLED----RRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 128146 347 ---HNNDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMA 388
Cdd:TIGR02168 470 leeAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-406 |
1.26e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 123 EIEAELAALRQKhAGRAQLGDAYEQELRELRGALeqvshekaqIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALR 202
Cdd:COG1196 197 ELERQLEPLERQ-AEKAERYRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 203 KEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLEcqsdhnmhQ 282
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEY----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE--------E 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 283 AEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLE 362
Cdd:COG1196 335 LEE----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 128146 363 NELRgtkwEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 406
Cdd:COG1196 411 ALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-350 |
2.22e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 72 AESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRE 151
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 152 LRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLRG 231
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 232 NHEEEVAELLAQLQashATVERKDYLKTDLTTALKEIRAQLECQSDHNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEE 311
Cdd:COG1196 408 AEEALLERLERLEE---ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE------EALLELLAELLEEAALLEAA 478
|
250 260 270
....*....|....*....|....*....|....*....
gi 128146 312 IAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNND 350
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
136-374 |
1.29e-10 |
|
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: 64.01 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 136 AGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAEL 215
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 216 DKKVQSLQDEVA----FLRGNHEEEVAELLAQLQASHATVERKDYLKtDLTTALKEIRAQLEcqsdhnmhqaeewfkcry 291
Cdd:COG4942 96 RAELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELR------------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 292 aKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLENELRGTKWE 371
Cdd:COG4942 157 -ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
...
gi 128146 372 MAR 374
Cdd:COG4942 236 AAA 238
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
624-754 |
2.71e-10 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 64.33 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKV-TSPEKPATPEKPPTPEKAITPEKVRSPEKPTTP------------------------------EKVVSPE 672
Cdd:PTZ00449 627 PESPKSPKRpPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPkfkekfyddyldaaaksketkttvvldesfESILKET 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 673 KPASPEKPRTPEKPASPEKPATPEKPRTPEKPATPEKPrSPEKPSSPLKDEKAVVEESITVTKVTKVTAEvevskEARKE 752
Cdd:PTZ00449 707 LPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQP-DDIEFFTPPEEERTFFHETPADTPLPDILAE-----EFKEE 780
|
..
gi 128146 753 DI 754
Cdd:PTZ00449 781 DI 782
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-361 |
2.74e-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: 64.32 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 65 GSTVLSSAESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAgyiEKVHYLEQQNKEIEA----ELAALRQK----HA 136
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE---EIEQLLEELNKKIKDlgeeEQLRVKEKigelEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 137 GRAQLGDAYEQELRELRGALEQVshekAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELD 216
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERL----AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 217 KKVQSLQDEVAFLRGNHE---EEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQL-ECQSDHNMHQAE----EWFK 288
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInELEEEKEDKALEikkqEWKL 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 128146 289 CRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQL 361
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-364 |
3.01e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 111 IEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEkaqiqLDSEHIEEDIQRLRERFEdeaRL 190
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-----IDVASAEREIAELEAELE---RL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 191 rDETEATIAALRKEMEEASLMRAELDKKVQSLQDEvaflRGNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRA 270
Cdd:COG4913 681 -DASSDDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 271 QLECQsDHNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEE-IAEYRRQLQSKSIELESVrgtkESLERQLSDIEerhNN 349
Cdd:COG4913 756 AAALG-DAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESL----PEYLALLDRLE---ED 827
|
250
....*....|....*
gi 128146 350 DLTTYQDTIHQLENE 364
Cdd:COG4913 828 GLPEYEERFKELLNE 842
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
624-719 |
2.25e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.49 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTSPEKPATPEKPPTPEKAITPEKVR---SPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPrT 700
Cdd:PHA03247 2722 PPGPAAARQASPALPAAPAPPAVPAGPATPGGPArpaRPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLP-S 2800
|
90
....*....|....*....
gi 128146 701 PEKPATPEKPRSPEKPSSP 719
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAALP 2819
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-383 |
2.54e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 112 EKVHYLEQQNKEIEAELAALRQKHAGRaqlgdayEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLR 191
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRI-------ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 192 DETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFL-RGNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEI-- 268
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtl 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 269 -RAQLECQSDHNMHQAEEWfKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERH 347
Cdd:TIGR02169 827 eKEYLEKEIQELQEQRIDL-KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270
....*....|....*....|....*....|....*.
gi 128146 348 NNDLTTYQDTIHQLeNELRGTKWEMARHLREYQDLL 383
Cdd:TIGR02169 906 EELEAQIEKKRKRL-SELKAKLEALEEELSEIEDPK 940
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
145-476 |
6.94e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 145 YEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLR------ERFEDEARLRDETEATIAALRKEMEEASlmRAELDKK 218
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRrerekaERYQALLKEKREYEGYELLKEKEALERQ--KEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 219 VQSLQDEVA---FLRGNHEEEVAELLAQLQASHATVERK-DYLKTDLTTALKEIRAQLE-CQS-----DHNMHQAEEwfk 288
Cdd:TIGR02169 246 LASLEEELEkltEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIAsLERsiaekERELEDAEE--- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 289 cRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNndltTYQDTIHQLENELRGT 368
Cdd:TIGR02169 323 -RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA----ETRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 369 KWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSAFSGSITGPIFTHRQPSVTIASTKIQKTKIEPPKLKVQHK 448
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340
....*....|....*....|....*...
gi 128146 449 FVEEIIEETKVEDEKSEMEDALSAIAEE 476
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
623-730 |
1.40e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.18 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTP-EKVVSPEKPASPEKP--RTPEKPASPEKP-----AT 694
Cdd:PHA03247 2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlGGSVAPGGDVRRRPPsrSPAAKPAAPARPpvrrlAR 2888
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 128146 695 PEKPRTPEK----PATPEKPRSPEKPSSPLKDEKAVVEES 730
Cdd:PHA03247 2889 PAVSRSTESfalpPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
82-325 |
1.68e-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: 57.47 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 82 LLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSH 161
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 162 EKAQIQLDSEHIEEDIQRL------------------RERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQ 223
Cdd:COG4942 91 EIAELRAELEAQKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 224 DEvaflrgnhEEEVAELLAQLQASHATVERkdyLKTDLTTALKEIRAQLECQSDhnmhqaeewfkcRYAKLTEAAEQNKE 303
Cdd:COG4942 171 AE--------RAELEALLAELEEERAALEA---LKAERQKLLARLEKELAELAA------------ELAELQQEAEELEA 227
|
250 260
....*....|....*....|..
gi 128146 304 AIRSAKEEIAEYRRQLQSKSIE 325
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFA 249
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
68-273 |
1.98e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 68 VLSSAESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQ 147
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 148 ELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVA 227
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 128146 228 flrgNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLE 273
Cdd:COG1196 453 ----ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-384 |
2.17e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 88 ELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQ 167
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 168 LDSEHIEEDIQRLRERFED-EARLRDE------------------TEATIAALRKEMEEASLMRAELDKKVQSLQDEVAF 228
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDlEARLSHSripeiqaelskleeevsrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 229 L---RGNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLECQSDH--NMHQAEEWFKCRYAKLTEAAEQNKE 303
Cdd:TIGR02169 845 LkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQlrELERKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 304 AIRSAKEEIAEYRRQLQSKSIE------LESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLeNELRGTKWEMARHLR 377
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERK 1003
|
....*..
gi 128146 378 EYQDLLN 384
Cdd:TIGR02169 1004 AILERIE 1010
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
630-730 |
2.43e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.03 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 630 PKVTSPEKPATPEKPPtpekaitpekVRSPEKPTTPEKVVS-PEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPatPE 708
Cdd:PHA03247 2867 PSRSPAAKPAAPARPP----------VRRLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP--PP 2934
|
90 100
....*....|....*....|..
gi 128146 709 KPRSPEKPSSPLKDEKAVVEES 730
Cdd:PHA03247 2935 PPPRPQPPLAPTTDPAGAGEPS 2956
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
626-719 |
2.45e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.03 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 626 KPATPKVTSPEKPATPEKPPTPekaitPEKVRSPEKPTTP-EKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKP 704
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPTPEP-----APHALVSATPLPPgPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT 2763
|
90
....*....|....*
gi 128146 705 ATPEKPRSPEKPSSP 719
Cdd:PHA03247 2764 AGPPAPAPPAAPAAG 2778
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
624-732 |
2.90e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.03 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTsPEKPATPEKP-PTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPE 702
Cdd:PHA03247 2704 PPPTPEPAPH-ALVSATPLPPgPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
|
90 100 110
....*....|....*....|....*....|
gi 128146 703 KPATPEKPRSPEKPSSPLKDEKAVVEESIT 732
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVL 2812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-340 |
3.16e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 117 LEQQNKEIEAeLAALRQKHAGRAQLgdayEQELRELRGALEQVSHEKAQIQLDS-----EHIEEDIQRLRERFEDEARLR 191
Cdd:COG4913 244 LEDAREQIEL-LEPIRELAERYAAA----RERLAELEYLRAALRLWFAQRRLELleaelEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 192 DETEATIAALRKEMEEASLMR-AELDKKVQSLQDEVAfLRGNHEEEVAELLAQLQASHATVERkdylktDLTTALKEIRA 270
Cdd:COG4913 319 DALREELDELEAQIRGNGGDRlEQLEREIERLERELE-ERERRRARLEALLAALGLPLPASAE------EFAALRAEAAA 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 271 QLEcqsdhnmhqaeewfkcryaKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQL 340
Cdd:COG4913 392 LLE-------------------ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
136-383 |
6.93e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 136 AGRAQLGdaYEQELRELRGALEQVSHEKAQIQLDSEH------------IEEDIQRLRERFEDEARLRDETEATIAALRK 203
Cdd:PRK02224 171 ASDARLG--VERVLSDQRGSLDQLKAQIEEKEEKDLHerlngleselaeLDEEIERYEEQREQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 204 EMEEASLMRAELDK----------KVQSLQDEVAFLR---GNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRA 270
Cdd:PRK02224 249 RREELETLEAEIEDlretiaeterEREELAEEVRDLRerlEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 271 QL-ECQSDHNMH--QAE------EWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLS 341
Cdd:PRK02224 329 RLeECRVAAQAHneEAEslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 128146 342 DIEERHnNDLTTYQDTIHQLENELRGTKWEMARHLREYQDLL 383
Cdd:PRK02224 409 NAEDFL-EELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-361 |
7.59e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 97 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQEL--RELRGALEQVSHEKAQIQLDS---E 171
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 172 HIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVA----------FLRGNHEEEVAELL 241
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelralleerFAAALGDAVERELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 242 AQLQASHATVERK-DYLKTDLTTALK---------------------EIRAQLECQSDHNMHQAEEWFKcRYakLTEAAE 299
Cdd:COG4913 769 ENLEERIDALRARlNRAEEELERAMRafnrewpaetadldadleslpEYLALLDRLEEDGLPEYEERFK-EL--LNENSI 845
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 128146 300 QNKEAIRSA-KEEIAEYRRQLQSKSIELESVR-GTKESLerQLsDIEERHNNDLTTYQDTIHQL 361
Cdd:COG4913 846 EFVADLLSKlRRAIREIKERIDPLNDSLKRIPfGPGRYL--RL-EARPRPDPEVREFRQELRAV 906
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
66-379 |
1.44e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 66 STVLSSAESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAY 145
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 146 EQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERfedearlRDETEATIAALRKEMEEASLMRA------------ 213
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER-------EAELEATLRTARERVEEAEALLEagkcpecgqpve 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 214 ---------ELDKKVQSLQDEVAFLRGNHE--EEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLECQSDhnmhQ 282
Cdd:PRK02224 463 gsphvetieEDRERVEELEAELEDLEEEVEevEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE----R 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 283 AEEWFKcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNndlttYQDTIHQLe 362
Cdd:PRK02224 539 AEELRE-RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-----AEDEIERL- 611
|
330
....*....|....*..
gi 128146 363 NELRGTKWEMARHLREY 379
Cdd:PRK02224 612 REKREALAELNDERRER 628
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
623-720 |
2.42e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.94 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVT-SPEKPATPEKPPTPEKAITPEKVRSPEKPTTP--------------EKVVSPEKPASPEKPRTPEKPA 687
Cdd:PHA03247 2738 APAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRrltrpavaslsesrESLPSPWDPADPPAAVLAPAAA 2817
|
90 100 110
....*....|....*....|....*....|....*
gi 128146 688 SP--EKPATPEKPRTPEKPATPEKPRSPEKPSSPL 720
Cdd:PHA03247 2818 LPpaASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL 2852
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
144-483 |
2.55e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 144 AYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLrdetEATIAALRKEMEEASLMRAELDKKVQSLQ 223
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL----EAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 224 DEVAFLrgnhEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQL-ECQSDHNMH--QAE------EWFKCRYAKL 294
Cdd:PRK02224 286 ERLEEL----EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLeECRVAAQAHneEAEslredaDDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 295 TEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNnDLTTYQDTIHQLENELRGTKWEMAR 374
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE-ELREERDELREREAELEATLRTARE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 375 HLREYQDLLN----------VKMALDIE--------IAAYRKLLEGEETRFSAFSGSITgpifthrqpsvtiASTKIQKT 436
Cdd:PRK02224 441 RVEEAEALLEagkcpecgqpVEGSPHVEtieedrerVEELEAELEDLEEEVEEVEERLE-------------RAEDLVEA 507
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 128146 437 KIEPPKLKVQHKFVEEIIEETKVE-DEKSEMEDALSAIAEEMAAKAQE 483
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETiEEKRERAEELRERAAELEAEAEE 555
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
87-240 |
2.56e-07 |
|
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: 52.62 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 87 AELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAgraqlgdAYEQELRELRGA--LEQVSHEKA 164
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-------KYEEQLGNVRNNkeYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 128146 165 QIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEAslmRAELDKKVQSLQDEVAFLRGNHEEEVAEL 240
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELEELEAEREELAAKI 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-273 |
3.26e-07 |
|
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: 52.23 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 117 LEQQNKEIEAELAALRQKHAGraqlgdaYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEdeaRLRDETEA 196
Cdd:COG1579 22 LEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG---NVRNNKEY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 128146 197 TiaALRKEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHATVERKdylKTDLTTALKEIRAQLE 273
Cdd:COG1579 92 E--ALQKEIESLKRRISDLEDEILELMERIE----ELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
637-741 |
4.98e-07 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 53.74 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 637 KPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPATPEKPRSPEKP 716
Cdd:PRK12270 37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDE 116
|
90 100
....*....|....*....|....*....
gi 128146 717 SSPLKD-EKAVV---EESITVTKVTKVTA 741
Cdd:PRK12270 117 VTPLRGaAAAVAknmDASLEVPTATSVRA 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
122-328 |
6.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 122 KEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAA- 200
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLl 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 201 -LRKEMEEASLMRAELDKKVQSLQDEVaflrgnheEEVAELLAQLQASHATVERkdylktdLTTALKEIRAQLECQSDHN 279
Cdd:COG4717 129 pLYQELEALEAELAELPERLEELEERL--------EELRELEEELEELEAELAE-------LQEELEELLEQLSLATEEE 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 128146 280 MHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELES 328
Cdd:COG4717 194 LQDLAE----ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
96-249 |
6.66e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 96 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYE--QELRELRGALEQVSHEKAQIQLDSEHI 173
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 174 EEDIQRLRERFEDEARLRDETEATI----AALRKEMEEASLMRAELDKKVQSLQDEVAFLR---GNHEEEVAELLAQLQA 246
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEAQeelEELEEELEQLENELEA 238
|
...
gi 128146 247 SHA 249
Cdd:COG4717 239 AAL 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
82-401 |
7.31e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 82 LLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIE---AELAALRQK--HAGRAQLGDAyEQELRELRGAL 156
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAelqEELEELLEQlsLATEEELQDL-AEELEELQQRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 157 EQVSHEKAQIQLDSEHIEEDIQRLR---ERFEDEARLRDETEATIAA--------------------------------- 200
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLEnelEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlgllal 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 201 -----------LRKEMEEASLMRAELD---KKVQSLQDEVAFLRGNHEEEVAELLAQLQASHATVERKDYLKTDLTTA-- 264
Cdd:COG4717 289 lflllarekasLGKEAEELQALPALEEleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEel 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 265 LKEIRAQLECQSDHNMHQAEEWfkcryAKLTEAAEQNKEAIRSAKEEIAEYR--RQLQSKSIELESVRGTKESLERQLSD 342
Cdd:COG4717 369 EQEIAALLAEAGVEDEEELRAA-----LEQAEEYQELKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEE 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 128146 343 IEERHNNDLTTYQDTIHQLENELRGTKWEMARHlrEYQDLLNVKMALDIEIAAYRKLLE 401
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQ--ELEELKAELRELAEEWAALKLALE 500
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
93-348 |
8.86e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 93 RSNEKEQLQGLNDRFAGYIEKVHYLEqqnkEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEH 172
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 173 IEEDIQRLRERfedearlRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHE---EEVAELLAQLQASHA 249
Cdd:PRK02224 305 DDADAEAVEAR-------REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEelrEEAAELESELEEARE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 250 TVERKDYLKTDLTTALKEIRAQLEcQSDHNMHQAEEWFKCRYAKLTEAAEQNKE---AIRSAKEEIAEYRRQLQS----- 321
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFG-DAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpe 456
|
250 260 270
....*....|....*....|....*....|....*.
gi 128146 322 --KSIE-------LESVRGTKESLERQLSDIEERHN 348
Cdd:PRK02224 457 cgQPVEgsphvetIEEDRERVEELEAELEDLEEEVE 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
147-366 |
9.24e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 147 QELRELRGALEQVSHEKAQI-QLdsehieEDIQRLRERFEDEARLRDETEATIAALRkeMEEASLMRAELDKKVQSLQDE 225
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIeLL------EPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 226 VAFLrgnhEEEVAELLAQLQASHATVE--RKDYLKTDlTTALKEIRAQLEcqsdhnmhQAEEwfkcRYAKLTEAAEQNKE 303
Cdd:COG4913 304 LARL----EAELERLEARLDALREELDelEAQIRGNG-GDRLEQLEREIE--------RLER----ELEERERRRARLEA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 128146 304 AIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLENELR 366
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
99-349 |
9.81e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 99 QLQGLNDRFAGYIekvhyLEQqnKEIEAELAALrQKHagRAQLGDAYEQ--ELRELRGALEQV-----SHEKAQIQLDse 171
Cdd:COG4913 205 PIGDLDDFVREYM-----LEE--PDTFEAADAL-VEH--FDDLERAHEAleDAREQIELLEPIrelaeRYAAARERLA-- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 172 HIEEDIQRLR-----ERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAELLAQLQA 246
Cdd:COG4913 273 ELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 247 SHATVERKdylKTDLTTALKEIRAQLEcqsdhnmHQAEEWfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 326
Cdd:COG4913 353 ELEERERR---RARLEALLAALGLPLP-------ASAEEF-----AALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
250 260
....*....|....*....|...
gi 128146 327 esvRGTKESLERQLSDIEERHNN 349
Cdd:COG4913 418 ---RRELRELEAEIASLERRKSN 437
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-244 |
1.36e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 97 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAG---------RAQLGDAyEQELRELRGALEQVSHEKAQIQ 167
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqlEREIERL-ERELEERERRRARLEALLAALG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 168 LDSEHIEEDIQRLRERFedeARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLRG---NHEEEVAELLAQL 244
Cdd:COG4913 373 LPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksNIPARLLALRDAL 449
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
88-383 |
1.69e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 88 ELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQ 167
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 168 LDSEHIEEDIQRL-RERFEDEARLRD------ETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLR------GNHE 234
Cdd:pfam07888 150 TELERMKERAKKAgAQRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttaHRKE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 235 EEVAELLAQLQAS----HATVERKDYLKTDLTTA----------LKEIR---AQLECQ-SDHNMHQAEEwfKCRYAKLTE 296
Cdd:pfam07888 230 AENEALLEELRSLqerlNASERKVEGLGEELSSMaaqrdrtqaeLHQARlqaAQLTLQlADASLALREG--RARWAQERE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 297 AAEQNKEAirsAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLENELRGTKWEMARHL 376
Cdd:pfam07888 308 TLQQSAEA---DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQ 384
|
....*..
gi 128146 377 REYQDLL 383
Cdd:pfam07888 385 AEKQELL 391
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
110-370 |
2.12e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 110 YIEkvHYLEQQNKEIEAELAALRQkhagraQLgDAYEQELRELRGALE--QVSHEKAQIQLDSEHIEEDIQRLRERFEDE 187
Cdd:COG3206 161 YLE--QNLELRREEARKALEFLEE------QL-PELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 188 ARLRDETEATIAALRKEMEEASLMRAEL--DKKVQSLQDEVAFLrgnhEEEVAELLAQLQASHATVerkdylktdlttal 265
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAEL----EAELAELSARYTPNHPDV-------------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 266 KEIRAQLEcqsdhnmhQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEE 345
Cdd:COG3206 294 IALRAQIA--------ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
250 260
....*....|....*....|....*
gi 128146 346 RHNNDLTTYQDTihQLENELRGTKW 370
Cdd:COG3206 366 LYESLLQRLEEA--RLAEALTVGNV 388
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
627-707 |
2.91e-06 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 50.72 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 627 PATPkvtspekPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPAspekPATPEKPRTPEKPAT 706
Cdd:PHA03291 205 PATP-------RPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPEAEGTPA----PPTPGGGEAPPANAT 273
|
.
gi 128146 707 P 707
Cdd:PHA03291 274 P 274
|
|
| Cornifin |
pfam02389 |
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ... |
624-723 |
5.82e-06 |
|
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.
Pssm-ID: 280537 [Multi-domain] Cd Length: 135 Bit Score: 46.58 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTSPEKPATPE--KPPTPEKAITpeKVRSPEKPTTPE----KVVSPEKPASPE--KPRTPEkPASPEKPaTP 695
Cdd:pfam02389 13 PQEPCVPTTKEPCHSKVPEpcNPKVPEPCCP--KVPEPCCPKVPEpccpKVPEPCCPKVPEpcYPKVPE-PCSPKVP-EP 88
|
90 100 110
....*....|....*....|....*....|..
gi 128146 696 EKPRTPE--KPATPEK--PRSPEkPSSPLKDE 723
Cdd:pfam02389 89 CHPKAPEpcHPKVPEPcyPKAPE-PCQPKVPE 119
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
97-345 |
6.39e-06 |
|
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: 50.34 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 97 KEQLQGLNdrfaGYIEKVHYL-----EQQNKEIEAELAALRQKHAGRAQLGDAYEQ-------------ELRELRGALEQ 158
Cdd:COG3096 870 KEQLQLLN----KLLPQANLLadetlADRLEELREELDAAQEAQAFIQQHGKALAQleplvavlqsdpeQFEQLQADYLQ 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 159 VSHEKAQIQLDSEHIEEDIQRlRERF--EDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAflrgnheeE 236
Cdd:COG3096 946 AKEQQRRLKQQIFALSEVVQR-RPHFsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYS--------Q 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 237 VAELLAQLQASHATverkdylKTDLTTALKEIRAQLECQSDHNmhqAEEWFKCRYAKLTEAAEQNkeaiRSAKEEIaeyR 316
Cdd:COG3096 1017 YNQVLASLKSSRDA-------KQQTLQELEQELEELGVQADAE---AEERARIRRDELHEELSQN----RSRRSQL---E 1079
|
250 260
....*....|....*....|....*....
gi 128146 317 RQLQSKSIELESVRGTKESLERQLSDIEE 345
Cdd:COG3096 1080 KQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
635-719 |
7.08e-06 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 635 PEKPATPEKPPT-PEKAITPEKVRSPEKPT-TPEKVVSPEKPASPEKPRTPeKPASPEKPAT-------PEKPRTPEKPA 705
Cdd:PTZ00449 511 PEGPEASGLPPKaPGDKEGEEGEHEDSKESdEPKEGGKPGETKEGEVGKKP-GPAKEHKPSKiptlskkPEFPKDPKHPK 589
|
90
....*....|....
gi 128146 706 TPEKPRSPEKPSSP 719
Cdd:PTZ00449 590 DPEEPKKPKRPRSA 603
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
188-418 |
9.06e-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: 48.99 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 188 ARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKE 267
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 268 IRAQLECQSDHNMHQAEEWFKC---RYAKLTEAAEQNKEAIRSAK--EEIAEYRRQ----LQSKSIELESVRGT----KE 334
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgrqPPLALLLSPEDFLDAVRRLQylKYLAPARREqaeeLRADLAELAALRAEleaeRA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 335 SLERQLSDIEERHN---NDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGeeTRFSAFS 411
Cdd:COG4942 175 ELEALLAELEEERAaleALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA--AGFAALK 252
|
....*..
gi 128146 412 GSITGPI 418
Cdd:COG4942 253 GKLPWPV 259
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
623-726 |
1.11e-05 |
|
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442497 [Multi-domain] Cd Length: 455 Bit Score: 48.69 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPATPEKPPTPEkAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPrTPE 702
Cdd:COG3266 264 ASAPATTSLGEQQEVSLPPAVAAQPA-AAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKPVVTETAAPAAP-APE 341
|
90 100
....*....|....*....|....
gi 128146 703 KPATPEKPRSPEKPSSPLKDEKAV 726
Cdd:COG3266 342 AAAAAAAPAAPAVAKKLAADEQWL 365
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
623-741 |
1.20e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKvvSPEKPASPEKPRTPEKPASPEKPATPEKPRTPE 702
Cdd:PHA03247 2890 AVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP--PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
|
90 100 110
....*....|....*....|....*....|....*....
gi 128146 703 KPATPEKPRSPEKPSSPLKDEKAVVEESITVTKVTKVTA 741
Cdd:PHA03247 2968 VPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSS 3006
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
623-718 |
1.34e-05 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 47.37 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEkpatPEKPPTPEKaiTPEKVRSPEKP---------TTPEKVVSPE-KPAS--PEKPRTPEKPASPe 690
Cdd:PRK10819 54 APADLEPPQAVQPP----PEPVVEPEP--EPEPIPEPPKEapvvipkpePKPKPKPKPKpKPVKkvEEQPKREVKPVEP- 126
|
90 100
....*....|....*....|....*...
gi 128146 691 KPATPEKPRTPEKPATPEKPRSPEKPSS 718
Cdd:PRK10819 127 RPASPFENTAPARPTSSTATAAASKPVT 154
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
112-346 |
1.46e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 112 EKVHYLEQQNKEIEAELAALRqkhaGRAQLGDA-----------YEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRL 180
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLL----AEAGLDDAdaeavearreeLEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 181 RERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFL---RGNHEEEVAELLAQLQASHATVerkdyl 257
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDApvdLGNAEDFLEELREERDELRERE------ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 258 kTDLTTALKEIRAQLEcqsdhnmhQAEEWF---KC-------RYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELE 327
Cdd:PRK02224 429 -AELEATLRTARERVE--------EAEALLeagKCpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
250
....*....|....*....
gi 128146 328 SVRGTKEsLERQLSDIEER 346
Cdd:PRK02224 500 RAEDLVE-AEDRIERLEER 517
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
657-728 |
1.59e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 48.37 E-value: 1.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 128146 657 RSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPATPEKPRSPeKPSSPLKDEKAVVE 728
Cdd:PRK01297 11 KGEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKP-KPASLWKLEDFVVE 81
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
624-719 |
1.73e-05 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 46.98 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTSPEKPATPEKPPTPEkaitPEKVRS-PEKPTTPEKVVSPeKPASPEKPRTPEKPASPEKPATPEKPrTPE 702
Cdd:PRK10819 82 PEPPKEAPVVIPKPEPKPKPKPKPK----PKPVKKvEEQPKREVKPVEP-RPASPFENTAPARPTSSTATAAASKP-VTS 155
|
90
....*....|....*..
gi 128146 703 KPATPeKPRSPEKPSSP 719
Cdd:PRK10819 156 VSSGP-RALSRNQPQYP 171
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
86-349 |
1.78e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 86 AAELKLSRSNEKEQLQGLNDrfagYIEKVHYLEQQNKEIEAELAALrQKHAGRAQL--GDAYEQELRELRGALEQVSHEK 163
Cdd:PRK04863 836 EAELRQLNRRRVELERALAD----HESQEQQQRSQLEQAKEGLSAL-NRLLPRLNLlaDETLADRVEEIREQLDEAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 164 AQIQldsEHieediQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAflRGNH---EEEV--- 237
Cdd:PRK04863 911 RFVQ---QH-----GNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQ--RRAHfsyEDAAeml 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 238 ---AELLAQLQASHatvERKDYLKTDLTTALKEIRAQLEcqsdhnmhQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEI-- 312
Cdd:PRK04863 981 aknSDLNEKLRQRL---EQAEQERTRAREQLRQAQAQLA--------QYNQ----VLASLKSSYDAKRQMLQELKQELqd 1045
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 128146 313 --------AEYRRQLQSKSI--ELESVRGTKESLERQLSDIEERHNN 349
Cdd:PRK04863 1046 lgvpadsgAEERARARRDELhaRLSANRSRRNQLEKQLTFCEAEMDN 1092
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
628-720 |
1.97e-05 |
|
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.
Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 45.94 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 628 ATPKVtSPEKPATPEKP--PTP-EKAITPEKVRSPEKPTTPEKVVSPEkPASPEKPRTPEKPASPEKPATPEKPRTPEKP 704
Cdd:smart00818 57 HIPVL-PAQQPVVPQQPlmPVPgQHSMTPTQHHQPNLPQPAQQPFQPQ-PLQPPQPQQPMQPQPPVHPIPPLPPQPPLPP 134
|
90
....*....|....*.
gi 128146 705 ATPEKPRSPEKPSSPL 720
Cdd:smart00818 135 MFPMQPLPPLLPDLPL 150
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
630-719 |
2.03e-05 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 46.98 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 630 PKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPttpEKVVSPEKPASPE-------KP--RTPEKPASPEKPATPeKPRT 700
Cdd:PRK10819 55 PADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKE---APVVIPKPEPKPKpkpkpkpKPvkKVEEQPKREVKPVEP-RPAS 130
|
90 100
....*....|....*....|..
gi 128146 701 PEKPATPEKP---RSPEKPSSP 719
Cdd:PRK10819 131 PFENTAPARPtssTATAAASKP 152
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
98-366 |
2.09e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 98 EQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDA--------------YEQELRELRGALEQVSHEK 163
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAEL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 164 AQIQLDSEHIEEDI-------------QRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLR 230
Cdd:PRK02224 485 EDLEEEVEEVEERLeraedlveaedriERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 231 GNHE---EEVAELLAQLQASHATVERKDYLKT------DLTTALKEIRAQLECQSDHNMHQAEEWFKCRYAKLTEAAEQN 301
Cdd:PRK02224 565 EEAEearEEVAELNSKLAELKERIESLERIRTllaaiaDAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 302 KEAIRSAKE-----------------EIAEYRRQLQSK------SIE-LESVRGTKESLERQLSDIEERHNNdLTTYQDT 357
Cdd:PRK02224 645 EARIEEAREdkeraeeyleqveekldELREERDDLQAEigavenELEeLEELRERREALENRVEALEALYDE-AEELESM 723
|
....*....
gi 128146 358 IHQLENELR 366
Cdd:PRK02224 724 YGDLRAELR 732
|
|
| PTZ00441 |
PTZ00441 |
sporozoite surface protein 2 (SSP2); Provisional |
633-733 |
2.61e-05 |
|
sporozoite surface protein 2 (SSP2); Provisional
Pssm-ID: 240420 [Multi-domain] Cd Length: 576 Bit Score: 47.65 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 633 TSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEkvvSPEKPASPEKPRTPEKPASPEK-PATPEKPRTpEKPATPEKPR 711
Cdd:PTZ00441 353 EVPDESNVPPNPPNVPGGSNSEFSSDVENPPNPP---NPDIPEQEPNIPEDSNKEVPEDvPMEPEDDRD-NNFNEPKKPE 428
|
90 100
....*....|....*....|....*...
gi 128146 712 S-----PEKPS-SPLKDEKAVVEESITV 733
Cdd:PTZ00441 429 NkgdgqNEPVIpKPLDNERDQSNKNKQV 456
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
136-467 |
2.72e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 136 AGRAQLGDA----YEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLM 211
Cdd:TIGR02169 631 AARRLMGKYrmvtLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 212 RAELDKKVQSLQDEVAFLrGNHEEEVAELLAQLQASHATVERKdylKTDLTTALKEIRAQLEcQSDHNMHQAEEWFKCRY 291
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQL-EQEEEKLKERLEELEEDLSSLEQE---IENVKSELKELEARIE-ELEEDLHKLEEALNDLE 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 292 AKLTEAAEQNKEA-IRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERhNNDLTTYQDTIHQLENELRGTKW 370
Cdd:TIGR02169 786 ARLSHSRIPEIQAeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKE 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 371 EMARHLREYQDLLNvkmaldiEIAAYRKLLEGEETRFSAFSGSItgpifthrQPSVTIASTKIQKTKIEPPKLKVQHKFV 450
Cdd:TIGR02169 865 ELEEELEELEAALR-------DLESRLGDLKKERDELEAQLREL--------ERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
330
....*....|....*..
gi 128146 451 EEiiEETKVEDEKSEME 467
Cdd:TIGR02169 930 EE--ELSEIEDPKGEDE 944
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
580-719 |
3.26e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.01 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 580 PKSPPKSPVTEQAKAVQKAAAEVGKDQKAEKAAEKAAKEEKAASPEKPATPKVTSPEKPATPEK---------------- 643
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRprrraarptvgsltsl 2698
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 128146 644 --PPTPEKaiTPEKVRSPEKPTTPEKVV-SPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPATPEKPRSPEKPSSP 719
Cdd:PHA03247 2699 adPPPPPP--TPEPAPHALVSATPLPPGpAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAP 2775
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
623-725 |
3.32e-05 |
|
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.
Pssm-ID: 433066 [Multi-domain] Cd Length: 415 Bit Score: 47.08 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKvvsPEKPASPEKPRTPEKPaSPEKPATPEKPRTPE 702
Cdd:pfam13254 245 STDKEQSPAPTSASEPPPKTKELPKDSEEPAAPSKSAEASTEKKE---PDTESSPETSSEKSAP-SLLSPVSKASIDKPL 320
|
90 100
....*....|....*....|...
gi 128146 703 KPATPEKPRSPEKPSSPLKDEKA 725
Cdd:pfam13254 321 SSPDRDPLSPKPKPQSPPKDFRA 343
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-406 |
3.65e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 171 EHIEE--DIQRLRERfedearlRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVA------FLRGNHEE-EVAELL 241
Cdd:COG1196 159 AIIEEaaGISKYKER-------KEEAERKLEATEENLERLEDILGELERQLEPLERQAEkaeryrELKEELKElEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 242 AQLQASHATVERKDYLKTDLTTALKEIRAQLEcQSDHNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQS 321
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELA-ELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 322 KSIELESVRGTKESLERQLSDIEERHNND---LTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRK 398
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
....*...
gi 128146 399 LLEGEETR 406
Cdd:COG1196 387 ELLEALRA 394
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
627-723 |
4.84e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 47.07 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 627 PATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRtPEKPaSPEKPATPEKPRTPEKPaT 706
Cdd:NF033839 281 QDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQ-PEKP-KPEVKPQLETPKPEVKP-Q 357
|
90 100
....*....|....*....|..
gi 128146 707 PEKPR-----SPEKPSSPLKDE 723
Cdd:NF033839 358 PEKPKpevkpQPEKPKPEVKPQ 379
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
625-713 |
6.41e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 625 EKPATPKVTSPEKPATPE-KPPTPEKAI-TPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPE 702
Cdd:PHA03247 2541 EELASDDAGDPPPPLPPAaPPAAPDRSVpPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPD 2620
|
90
....*....|.
gi 128146 703 KPATPEKPRSP 713
Cdd:PHA03247 2621 THAPDPPPPSP 2631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
87-401 |
6.60e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 87 AELKLSRSNEKEQLQGLND--RFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKA 164
Cdd:COG4717 105 EELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 165 QIQLDSEH----IEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASlMRAELDKKVQSLQDEVAFLR---------- 230
Cdd:COG4717 185 QLSLATEEelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERLKEARLLLLiaaallallg 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 231 -----GNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLECQSDHNMHQAEEWFKCRYAKLTEAAEQNKEAI 305
Cdd:COG4717 264 lggslLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 306 RSAKE------EIAEYRRQLQSKSIELESVR-------GTKESLERQLSDIEERHNNdLTTYQDTIHQLENELRGTKWEM 372
Cdd:COG4717 344 DRIEElqellrEAEELEEELQLEELEQEIAAllaeagvEDEEELRAALEQAEEYQEL-KEELEELEEQLEELLGELEELL 422
|
330 340 350
....*....|....*....|....*....|.
gi 128146 373 ARHLRE--YQDLLNVKMALDIEIAAYRKLLE 401
Cdd:COG4717 423 EALDEEelEEELEELEEELEELEEELEELRE 453
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
623-720 |
7.53e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPATPEKPPTPEKAIT----PEKVRSPEkPTTPEKVVSPEKPASPEKPRTPEKPASPEKPatPEKP 698
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANepdpHPPPTVPP-PERPRDDPAPGRVSRPRRARRLGRAAQASSP--PQRP 2683
|
90 100 110
....*....|....*....|....*....|..
gi 128146 699 RTPEKPAT----------PEKPRSPEKPSSPL 720
Cdd:PHA03247 2684 RRRAARPTvgsltsladpPPPPPTPEPAPHAL 2715
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
144-273 |
7.67e-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: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 144 AYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEME--EASLMRAELDKKVQS 221
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVRNNKEYEA 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 128146 222 LQDEVAFL---RGNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLE 273
Cdd:COG1579 94 LQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
624-723 |
8.60e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 46.30 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTSPEKPAtPEKPPTPEKAiTPEKVRSPEKPTtPEKVVSPEKPaSPEKPRTPEKPaSPEKPATPEKPRTPEK 703
Cdd:NF033839 314 PETPKPEVKPQLEKPK-PEVKPQPEKP-KPEVKPQLETPK-PEVKPQPEKP-KPEVKPQPEKP-KPEVKPQPETPKPEVK 388
|
90 100
....*....|....*....|....*
gi 128146 704 PaTPEKPR-----SPEKPSSPLKDE 723
Cdd:NF033839 389 P-QPEKPKpevkpQPEKPKPEVKPQ 412
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
624-730 |
8.75e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.32 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPT-----TPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKP 698
Cdd:PHA03307 71 PPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGpsspdPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAA 150
|
90 100 110
....*....|....*....|....*....|..
gi 128146 699 RTPEKPATPEKPRSPEKPSSPLKDEKAVVEES 730
Cdd:PHA03307 151 SPPAAGASPAAVASDAASSRQAALPLSSPEET 182
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-334 |
1.05e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 92 SRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHagraqlgdayeQELRELRGALEQVSHEKAQIQLDSE 171
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-----------KELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 172 HIEEDIQRLRERFED-EARLRD--ETEATIAALRKEMEEASLMRAELDKKVQSLQdEVAFLRGNHEEEVAELLAQLQASH 248
Cdd:PRK03918 256 KLEEKIRELEERIEElKKEIEEleEKVKELKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 249 ATVERKDYLKTDLTTALKEI-----RAQLECQSDHNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKS 323
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLeeleeRHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414
|
250
....*....|.
gi 128146 324 IELESVRGTKE 334
Cdd:PRK03918 415 GELKKEIKELK 425
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
624-719 |
1.23e-04 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 45.53 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTSPEKPaTPEKPPTPEKAiTPEKVRSPEKPTtPEKVVSPEKPASPEKPRtPEKPASPEKPaTPEKPRtPEK 703
Cdd:NF033839 347 LETPKPEVKPQPEKP-KPEVKPQPEKP-KPEVKPQPETPK-PEVKPQPEKPKPEVKPQ-PEKPKPEVKP-QPEKPK-PEV 420
|
90
....*....|....*.
gi 128146 704 PATPEKPRSPEKPSSP 719
Cdd:NF033839 421 KPQPEKPKPEVKPQPE 436
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
642-719 |
1.30e-04 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 45.46 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 642 EKPPTPEKAITPEKVRSPEKPTT--PEKVVSPEKpaSPEKPRTPEKPASPEK--PATPEKPRTPEKPATPEKPRSPEKPS 717
Cdd:PRK06347 54 ETAPADEASKSAEANTTKEAPATatPENTTEPTV--EPKQTETKEQTKTPEEkqPAAKQVEKAPAEPATVSNPDNATSSS 131
|
..
gi 128146 718 SP 719
Cdd:PRK06347 132 TP 133
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
638-754 |
1.30e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 45.57 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 638 PATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPA--TPEKPRSPEK 715
Cdd:PRK14950 362 PVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPklTRAAIPVDEK 441
|
90 100 110
....*....|....*....|....*....|....*....
gi 128146 716 PSSPLKDEKAvvEESITVTKVTKVTAEVEVSKEARKEDI 754
Cdd:PRK14950 442 PKYTPPAPPK--EEEKALIADGDVLEQLEAIWKQILRDV 478
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
638-739 |
1.32e-04 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 45.33 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 638 PATPEKPP--TPEKAITPEKVRSP-EKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPE--KPATPEKPRS 712
Cdd:PHA03291 188 PALPLSAPrlGPADVFVPATPRPTpRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPEAEGtpAPPTPGGGEA 267
|
90 100
....*....|....*....|....*..
gi 128146 713 PEKPSSPLKDEKavvEESITVTKVTKV 739
Cdd:PHA03291 268 PPANATPAPEAS---RYELTVTQIIQI 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-245 |
1.66e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 47 TVSSSYKRTNLGAPRTAYGSTVLSSAESLDVSQSSLLngAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEA 126
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEFLEEQLPELRKELE--EAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 127 ELAALRQKHAG-RAQLGDAYEQ--------ELRELRGALEQVSHEKAQIQ--LDSEH-----IEEDIQRLRERFEDEA-R 189
Cdd:COG3206 234 ELAEAEARLAAlRAQLGSGPDAlpellqspVIQQLRAQLAELEAELAELSarYTPNHpdviaLRAQIAALRAQLQQEAqR 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 128146 190 LRDETEATIAALRKEMEEASLMRAELDKKVQS----------LQDEVAFLRGNHEeevaELLAQLQ 245
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAElpeleaelrrLEREVEVARELYE----SLLQRLE 375
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
626-753 |
1.92e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 45.09 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 626 KPATPKVTSPekPATPEKPPTPEKAITPEKVRspeKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPA 705
Cdd:PRK14951 404 AAAPAAAASA--PAAPPAAAPPAPVAAPAAAA---PAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPA 478
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 128146 706 TPEKPRSPEKPSSPLKDE-KAVVEESITVTKVTKVTAEVEVSKEARKED 753
Cdd:PRK14951 479 PAAAPAAARLTPTEEGDVwHATVQQLAAAEAITALARELALQSELVARD 527
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
626-720 |
1.94e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 626 KPATPKVTSP------------EKPATPEKPPTPEKAITPEKV-RSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKP 692
Cdd:PHA03247 385 RRSARHAATPfargpggddqtrPAAPVPASVPTPAPTPVPASApPPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPD 464
|
90 100
....*....|....*....|....*...
gi 128146 693 ATPEKprTPEKPATPEKPRSPEKPSSPL 720
Cdd:PHA03247 465 DPDDA--TRKALDALRERRPPEPPGADL 490
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
624-728 |
1.96e-04 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 45.14 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTSPEKPaTPEKPPTPEKAiTPEKVRSPEKPTtPEKVVSPEKPaSPEKPRTPEKPaSPEKPATPE--KPRTP 701
Cdd:NF033839 380 PETPKPEVKPQPEKP-KPEVKPQPEKP-KPEVKPQPEKPK-PEVKPQPEKP-KPEVKPQPEKP-KPEVKPQPEkpKPEVK 454
|
90 100
....*....|....*....|....*..
gi 128146 702 EKPATPeKPRSPEKPSSPLKDEKAVVE 728
Cdd:NF033839 455 PQPETP-KPEVKPQPEKPKPEVKPQPE 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
95-273 |
2.22e-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: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 95 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAG-RAQLGDAyEQELRELRGALEQVS-------HEKAQI 166
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlEKELEQA-EEELDELQDRLEAAEdlarlelRALLEE 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 167 QLDSEHIEEDIQRLRERFEDEarlRDETEATIAALRKEMEEAslMRA---ELDKKVQSLQDEVAFLrgnheEEVAELLAQ 243
Cdd:COG4913 754 RFAAALGDAVERELRENLEER---IDALRARLNRAEEELERA--MRAfnrEWPAETADLDADLESL-----PEYLALLDR 823
|
170 180 190
....*....|....*....|....*....|...
gi 128146 244 LQAS--HATVER-KDYLKTDLTTALKEIRAQLE 273
Cdd:COG4913 824 LEEDglPEYEERfKELLNENSIEFVADLLSKLR 856
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
623-740 |
2.32e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPAT-----PEKPPTPEKAITPEKVR-----SPEKPTTPEKVVSPEKPASPEKP-RTPEKPASPEK 691
Cdd:PHA03247 2612 APPSPLPPDTHAPDPPPPspspaANEPDPHPPPTVPPPERprddpAPGRVSRPRRARRLGRAAQASSPpQRPRRRAARPT 2691
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 128146 692 PAT-PEKPRTPEKPATPEKPRSPEKPSSPLKDEKAVVEESITVTKVTKVT 740
Cdd:PHA03247 2692 VGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP 2741
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
624-714 |
2.41e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 44.80 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTSP----EKPATPEKPPTPEKAITPEKvrsPEKPTTPEKVVSPEKPASPekPRTPEKPASPekPATPEKPR 699
Cdd:PRK14950 365 APQPAKPTAAAPspvrPTPAPSTRPKAAAAANIPPK---EPVRETATPPPVPPRPVAP--PVPHTPESAP--KLTRAAIP 437
|
90
....*....|....*
gi 128146 700 TPEKPATPEKPRSPE 714
Cdd:PRK14950 438 VDEKPKYTPPAPPKE 452
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
146-365 |
4.03e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.07 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 146 EQELRELRGALEQVSHEKAQIQLDS-----EHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQ 220
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLELDEaeealEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 221 SLQ-------DEVAFLRGnHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLE-CQSDHnmhqaEEWFKcrya 292
Cdd:pfam06160 316 RVQqsytlneNELERVRG-LEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEeIEEEQ-----EEFKE---- 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 128146 293 KLTEAAEQNKEairsAKEEIAEYRRQLqsksielesvRGTKESLERQ-LSDIEERHNNDLTTYQDTIHQLENEL 365
Cdd:pfam06160 386 SLQSLRKDELE----AREKLDEFKLEL----------REIKRLVEKSnLPGLPESYLDYFFDVSDEIEDLADEL 445
|
|
| TALPID3 |
pfam15324 |
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ... |
627-746 |
4.09e-04 |
|
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for Hedgehog signalling. Mutations in this gene noticed first in chickens lead to multiple abnormalities of development.
Pssm-ID: 434634 [Multi-domain] Cd Length: 1288 Bit Score: 44.11 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 627 PATPKVTSPEKPATPeKPPTPEKAITPEKVRSPEKPTTPEkvvSPEKPASPEKPRTP----------------EKPASPE 690
Cdd:pfam15324 1047 PTVTPIATPPPAATP-TPPLSENSIDKLKSPSPELPKPWE---DSDLPLEEENPNSEqeelhpravvmsvardEEPESVV 1122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 128146 691 KPATP--EKPRTPEkPATPEKPRSPEKPSSplkdEKAVVEESITVTKVTKVTAEVEVS 746
Cdd:pfam15324 1123 LPASPpePKPLAPP-PLGAAPPSPPQSPSS----SSSTLESSSSLTVTETETADRPIS 1175
|
|
| ISET-FN3_linker |
pfam16625 |
Unstructured linking region I-set and fnIII on Brother of CDO; ISET-FN3_linker is a short ... |
637-693 |
4.18e-04 |
|
Unstructured linking region I-set and fnIII on Brother of CDO; ISET-FN3_linker is a short section of natively unstructured sequence on Biregional cell adhesion molecule-related/down-regulated by oncogenes (Cdon) binding proteins or Brother of CDO. It is found in higher eukaryotes and lies between the second I-set and the first fnIII domains, pfam07679 and pfam00041. The function is not known.
Pssm-ID: 435475 [Multi-domain] Cd Length: 65 Bit Score: 39.40 E-value: 4.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 128146 637 KPATPEKPPTPEKAITPEKVRSPEKPTTPEKVvsPEKPASPEKPRTPEKPASPEKPA 693
Cdd:pfam16625 2 RPGTTLRPWQDAKLATATPPAPPSRPSSPDQM--LRGKPGLPRPPTSVQPASPQCPG 56
|
|
| Metal_resist |
pfam13801 |
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to ... |
125-205 |
4.34e-04 |
|
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to heavy-metal ions. The protein forms a four-helix hooked hairpin, consisting of two long alpha helices each flanked by a shorter alpha helix. It binds a metal ion in a type-2 like centre. It contains two copies of an LTXXQ motif.
Pssm-ID: 433488 [Multi-domain] Cd Length: 119 Bit Score: 40.74 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 125 EAELAALRQKHAGRAQLGDAYEQELRELRGALEQVShekAQIQLDSEHIEEDIQRLRERfedEARLRDETEATIAALRKE 204
Cdd:pfam13801 41 AEQRERLRAALRDHARELRALRRELRAARRELAALL---AAPPFDPAAIEAALAEARQA---RAALQAQIEEALLEFAAT 114
|
.
gi 128146 205 M 205
Cdd:pfam13801 115 L 115
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
626-719 |
4.34e-04 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 43.79 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 626 KPATPKV--TSPEKPATPEKPPTPEKaITPEKVRSPEKPTTPekvvspekPASPEKPRTPEKPASPEKPATPEKPRTPEK 703
Cdd:PHA03291 171 TLAAPPLgeGSADGSCDPALPLSAPR-LGPADVFVPATPRPT--------PRTTASPETTPTPSTTTSPPSTTIPAPSTT 241
|
90
....*....|....*.
gi 128146 704 PATPEKPRSPEKPSSP 719
Cdd:PHA03291 242 IAAPQAGTTPEAEGTP 257
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-406 |
4.89e-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: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 127 ELAALRQKHAGR-AQLGDAYEQELRELRGALEqVSHEKA-----QIQ----------------LDSEHIEEDIQRLRERF 184
Cdd:COG4913 156 DIRALKARLKKQgVEFFDSFSAYLARLRRRLG-IGSEKAlrllhKTQsfkpigdlddfvreymLEEPDTFEAADALVEHF 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 185 EDEARLRDE---TEATIAALRkEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAELLAQLQAshatverkdylktDL 261
Cdd:COG4913 235 DDLERAHEAledAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE-------------EL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 262 TTALKEIRAQLEcqsdhnmhQAEEwfkcRYAKLTEAAEQNKEAIRSAK-EEIAEYRRQLQSKSIELESVRGTKESLERQL 340
Cdd:COG4913 301 RAELARLEAELE--------RLEA----RLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALL 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 128146 341 SDIEERHNNDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 406
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
626-721 |
4.92e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 626 KPATPKVTS----PEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKvVSPEKPASPEKPRtPEKPASPEKPATPEKPRTP 701
Cdd:PHA03247 2576 RPSEPAVTSrarrPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDT-HAPDPPPPSPSPA-ANEPDPHPPPTVPPPERPR 2653
|
90 100
....*....|....*....|....*...
gi 128146 702 EKPATP--------EKPRSPEKPSSPLK 721
Cdd:PHA03247 2654 DDPAPGrvsrprraRRLGRAAQASSPPQ 2681
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
632-719 |
5.00e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 632 VTSPEKPATPEKPPTPEKAITPEK----VRSPEKPTTPEKvvSPEKPASPEKPRTPEKPASpeKPATPEKPRTPEKPATP 707
Cdd:PHA03247 368 LSAGRHHPKRASLPTRKRRSARHAatpfARGPGGDDQTRP--AAPVPASVPTPAPTPVPAS--APPPPATPLPSAEPGSD 443
|
90
....*....|..
gi 128146 708 EKPRSPEKPSSP 719
Cdd:PHA03247 444 DGPAPPPERQPP 455
|
|
| PHA03308 |
PHA03308 |
transcriptional regulator ICP4; Provisional |
625-717 |
5.19e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 165563 [Multi-domain] Cd Length: 1463 Bit Score: 44.03 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 625 EKPATPkvtSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVS-----------PE-----------------KPAS 676
Cdd:PHA03308 756 ESPANP---WPRAPPCDEQEPLSVSPYGPEPDRPPDDDFETRKGLKrkssedhadpiPEgnatkktcglqglpdslPPAV 832
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 128146 677 PEKPRtpEKPASPEKPATPEKPRTP--EKPATPEKPRSPEKPS 717
Cdd:PHA03308 833 PETDR--DNPLLPPCPITPEGPPCPprEEPQQPQEPQEPQSPS 873
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
156-366 |
5.42e-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: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 156 LEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEAslmRAELDKKVQSLQDevaflrgnHEE 235
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---QAEIAEAEAEIEE--------RRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 236 EVAELLAQLQASHATVERKDYLK--TDLTTALKEIRAqLECQSDHNMHQAEEwfkcrYAKLTEAAEQNKEAIRSAKEEIA 313
Cdd:COG3883 87 ELGERARALYRSGGSVSYLDVLLgsESFSDFLDRLSA-LSKIADADADLLEE-----LKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 128146 314 EYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLENELR 366
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
623-728 |
6.01e-04 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 42.30 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTspekPATPEKPP--TPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRT 700
Cdd:PRK11633 50 RDEPDMMPAAT----QALPTQPPegAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKV 125
|
90 100
....*....|....*....|....*...
gi 128146 701 PEKPATPEKPRSPEKPSSPLKDEKAVVE 728
Cdd:PRK11633 126 EAPPAPKPEPKPVVEEKAAPTGKAYVVQ 153
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
86-489 |
6.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 86 AAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQK--------HAGRAQLGDAYEQELRELRGALE 157
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAlleaeaelAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 158 QVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRdETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEV 237
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALA-ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 238 AELLAQLQASHATVERKDYLKTDLTTALKEIRAQLECQSDHNMH------QAEEWFKCRYAKLTEAA------------- 298
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagavAVLIGVEAAYEAALEAAlaaalqnivvedd 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 299 EQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDI----EERHNNDLTTYQDTIHQLENELRGTKWEMAR 374
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlvaSDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 375 HLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSAfsgsitgpifthRQPSVTIASTKIQKTKIEPPKLKVQHKFVEEII 454
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL------------AALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
410 420 430
....*....|....*....|....*....|....*
gi 128146 455 EETKVEDEKSEMEDALSAIAEEMAAKAQEEEQEEE 489
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
83-226 |
6.31e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 83 LNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKhagraqlgdayEQELRELRGALEQVSHE 162
Cdd:PRK04863 550 LDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR-----------APAWLAAQDALARLREQ 618
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 128146 163 KAQIQLDSEHIEEDIQRLRERfEDEARL-RDETEATIAALRKEMEEASLMRAELDKKVQSLQDEV 226
Cdd:PRK04863 619 SGEEFEDSQDVTEYMQQLLER-ERELTVeRDELAARKQALDEEIERLSQPGGSEDPRLNALAERF 682
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
638-732 |
6.62e-04 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 43.38 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 638 PATPEKPPTPEKAITPEKVrsPEKPTTPEKVVSPEKPASPEKPRTPEKPASPE------KPATPEKPRTP---------- 701
Cdd:PLN03209 324 PSQRVPPKESDAADGPKPV--PTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYtayedlKPPTSPIPTPPssspassksv 401
|
90 100 110
....*....|....*....|....*....|....
gi 128146 702 ---EKPATPEKPRSPEKPSSPLKDEKAVVEESIT 732
Cdd:PLN03209 402 davAKPAEPDVVPSPGSASNVPEVEPAQVEAKKT 435
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
117-343 |
6.67e-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: 43.63 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 117 LEQQNKEIEAELAALRQKH-------------AGRAQLG-----DAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQ 178
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQKHtqaleelteqleqAKRNKANlekakQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 179 RLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLrGNHEEEVAELL-----AQLQASHATVER 253
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL-ESQLQDTQELLqeetrQKLNLSTRLRQL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 254 KDYlKTDLTTALKE---IRAQLECQ-SDHNMHQAEewFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESV 329
Cdd:pfam01576 495 EDE-RNSLQEQLEEeeeAKRNVERQlSTLQAQLSD--MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
250
....*....|....
gi 128146 330 RGTKESLERQLSDI 343
Cdd:pfam01576 572 EKTKNRLQQELDDL 585
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
120-347 |
6.99e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 120 QNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLdsEHIEEDIQRLRERF----EDEARLRDETE 195
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAgvedEEELRAALEQA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 196 ATIAALRKEMEEASLMRAELDKKVQSLqdevafLRGNHEEEVAELLAQLQASHATVERKdylKTDLTTALKEIRAQLEcq 275
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEEL------LEALDEEELEEELEELEEELEELEEE---LEELREELAELEAELE-- 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 128146 276 sdhnmhQAEEwfkcryaklteaaeqnKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERH 347
Cdd:COG4717 464 ------QLEE----------------DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
656-741 |
7.14e-04 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 43.14 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 656 VRSPEKPTTPEKVVSPEKPASPEKPRTpekpASPEKPATPEkpRTPEKPATPEKPRSPEKPSSPLKDEKAVVEESITVTK 735
Cdd:PRK06347 50 VSADETAPADEASKSAEANTTKEAPAT----ATPENTTEPT--VEPKQTETKEQTKTPEEKQPAAKQVEKAPAEPATVSN 123
|
....*.
gi 128146 736 VTKVTA 741
Cdd:PRK06347 124 PDNATS 129
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
73-241 |
8.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 73 ESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFA--GYIEKvhyleqqnKEIEAELAALRQKHAGRAQLGDAYEQELR 150
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRgnGGDRL--------EQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 151 ELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEarlRDETEATIAALRKEMEEASLMRAEL-------DKKVQSLQ 223
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRRELRELEAEIASLerrksniPARLLALR 446
|
170 180
....*....|....*....|.
gi 128146 224 DEVAFLRGNHEEE---VAELL 241
Cdd:COG4913 447 DALAEALGLDEAElpfVGELI 467
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
97-346 |
8.79e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 97 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHagraqlgDAYEQELRELRGALEQVSHEKAQIQLDS---EHI 173
Cdd:COG1340 42 AEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER-------DELNEKLNELREELDELRKELAELNKAGgsiDKL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 174 EEDIQRLRERFEDEA-RLRDETE--ATIAALRKEMEEAsLMRAELDKKVQSLQDEVAFLRG---NHEEEVAELLAQLQAS 247
Cdd:COG1340 115 RKEIERLEWRQQTEVlSPEEEKElvEKIKELEKELEKA-KKALEKNEKLKELRAELKELRKeaeEIHKKIKELAEEAQEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 248 HATVerkdylkTDLTTALKEIRAQLEcqsdhNMHQaeewfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELE 327
Cdd:COG1340 194 HEEM-------IELYKEADELRKEAD-----ELHK-------EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQR 254
|
250 260
....*....|....*....|.
gi 128146 328 SVRGTK--ESLERQLSDIEER 346
Cdd:COG1340 255 ALKREKekEELEEKAEEIFEK 275
|
|
| PHA03264 |
PHA03264 |
envelope glycoprotein D; Provisional |
625-712 |
9.94e-04 |
|
envelope glycoprotein D; Provisional
Pssm-ID: 223029 [Multi-domain] Cd Length: 416 Bit Score: 42.30 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 625 EKPATPKVTSPEKPATPEKPPTPEKAIT---PEKVRSPEKPTTPEKVVSPEKPASPEKPRtPEKPASPEK-----PATPE 696
Cdd:PHA03264 265 EPPPAPSGGSPAPPGDDRPEAKPEPGPVedgAPGRETGGEGEGPEPAGRDGAAGGEPKPG-PPRPAPDADrpegwPSLEA 343
|
90
....*....|....*.
gi 128146 697 KPRTPEKPATPEKPRS 712
Cdd:PHA03264 344 ITFPPPTPATPAVPRA 359
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
631-723 |
1.10e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 631 KVTSPEKPATPEKPPTPekaITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTP--------EKPASPEKPA-TPEKPRTP 701
Cdd:PTZ00449 704 KETLPETPGTPFTTPRP---LPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPeeertffhETPADTPLPDiLAEEFKEE 780
|
90 100
....*....|....*....|...
gi 128146 702 EKPATPEKPRSPEK-PSSPLKDE 723
Cdd:PTZ00449 781 DIHAETGEPDEAMKrPDSPSEHE 803
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
100-229 |
1.10e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.96 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 100 LQGLNDRFAGYIEKVHYLEQQNK--EIEAE-LAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIEED 176
Cdd:pfam06785 54 LYYWEDALKEKFEKSFLEEKEAKltELDAEgFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQD 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 128146 177 IQRLR----ERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFL 229
Cdd:pfam06785 134 FAEFRleseEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
623-723 |
1.15e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPR-TPEKPASPEKPATPEKPRTP 701
Cdd:PRK07764 409 APAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPApAPAAAPEPTAAPAPAPPAAP 488
|
90 100
....*....|....*....|..
gi 128146 702 EKPATPEKPRSPEKPSSPLKDE 723
Cdd:PRK07764 489 APAAAPAAPAAPAAPAGADDAA 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-409 |
1.15e-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: 42.74 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 173 IEE--DIQRLRERfedearlRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVaflrgnheeEVAELLAQLQASHAT 250
Cdd:TIGR02168 161 FEEaaGISKYKER-------RKETERKLERTRENLDRLEDILNELERQLKSLERQA---------EKAERYKELKAELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 251 VErKDYLKTDLTTALKEIRAQL----ECQSDHNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 326
Cdd:TIGR02168 225 LE-LALLVLRLEELREELEELQeelkEAEEELEELTAEL------QELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 327 ESVRGTKESLERQLsdieERHNNDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 406
Cdd:TIGR02168 298 SRLEQQKQILRERL----ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
...
gi 128146 407 FSA 409
Cdd:TIGR02168 374 LEE 376
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
117-243 |
1.25e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 117 LEQQNKEIEAELAAL-RQKHAGRAQLGDAYEQELRELRgalEQVSHEKAQIQLDSEHIEEdIQRLRERFEDEARLRDETE 195
Cdd:COG0542 416 LERRLEQLEIEKEALkKEQDEASFERLAELRDELAELE---EELEALKARWEAEKELIEE-IQELKEELEQRYGKIPELE 491
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 128146 196 ATIAALRKEMEEASLMraeldkkvqsLQDEVAflrgnhEEEVAELLAQ 243
Cdd:COG0542 492 KELAELEEELAELAPL----------LREEVT------EEDIAEVVSR 523
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
624-745 |
1.26e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 42.26 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEK 703
Cdd:PRK06995 56 AAAPAAAQPPPAAAPAAVSRPAAPAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARA 135
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 128146 704 PATPEKPRSPEKPSSPLKDEkavVEESITVTKVTKVTAEVEV 745
Cdd:PRK06995 136 AAAAPRPRVPADAAAAVADA---VKARIERIVNDTVMQELRS 174
|
|
| PRK12373 |
PRK12373 |
NADH-quinone oxidoreductase subunit E; |
623-708 |
1.45e-03 |
|
NADH-quinone oxidoreductase subunit E;
Pssm-ID: 237082 [Multi-domain] Cd Length: 400 Bit Score: 42.10 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPttpekvVSPEKPASPEKPRTPEKPASPEKPATPEKPRT-- 700
Cdd:PRK12373 242 PPSEAARPKSADAETNAALKTPATAPKAAAKNAKAPEAQP------VSGTAAAEPAPKEAAKAAAAAAKPALEDKPRPlg 315
|
....*...
gi 128146 701 PEKPATPE 708
Cdd:PRK12373 316 IARPGGAD 323
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
628-730 |
1.47e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 628 ATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEK-----PRTPEKPASPEKPATPEKPRTPE 702
Cdd:PHA03307 51 AAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPARegsptPPGPSSPDPPPPTPPPASPPPSP 130
|
90 100
....*....|....*....|....*...
gi 128146 703 KPATPEKPRSPEKPSSPLKDEKAVVEES 730
Cdd:PHA03307 131 APDLSEMLRPVGSPGPPPAASPPAAGAS 158
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
623-723 |
1.56e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 41.68 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPrtPEKPASPEKPATPE--KPRT 700
Cdd:NF040712 238 TPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPP--APAPAAPAAPAAPEaeEPAR 315
|
90 100
....*....|....*....|...
gi 128146 701 PEKPATPEKPRSPEKPSSPLKDE 723
Cdd:NF040712 316 PEPPPAPKPKRRRRRASVPSWDD 338
|
|
| PTZ00441 |
PTZ00441 |
sporozoite surface protein 2 (SSP2); Provisional |
635-735 |
1.80e-03 |
|
sporozoite surface protein 2 (SSP2); Provisional
Pssm-ID: 240420 [Multi-domain] Cd Length: 576 Bit Score: 41.87 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 635 PEKPATPEKPPTPEKAITP--EKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPATPEKPRS 712
Cdd:PTZ00441 323 PDNPQDPVPPPNEGKDGNPneENLFPPGDDEVPDESNVPPNPPNVPGGSNSEFSSDVENPPNPPNPDIPEQEPNIPEDSN 402
|
90 100
....*....|....*....|...
gi 128146 713 PEKPSSPLKDEKAVVEESITVTK 735
Cdd:PTZ00441 403 KEVPEDVPMEPEDDRDNNFNEPK 425
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
212-402 |
1.83e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 212 RAELDKKVQSLQDevaflRGNHEEEVAELLAQLQASHATVERKDYLKTDLTtalkEIRAQLEcQSDHNMHQAEEwfkcRY 291
Cdd:PRK11281 38 EADVQAQLDALNK-----QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETE----QLKQQLA-QAPAKLRQAQA----EL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 292 AKLTEAAEQNKEAiRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIE---ERHNNDLTTYQDTIHQLENELRGT 368
Cdd:PRK11281 104 EALKDDNDEETRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQtqpERAQAALYANSQRLQQIRNLLKGG 182
|
170 180 190
....*....|....*....|....*....|....*
gi 128146 369 KWEMARHLREYQDLLNVKMA-LDIEIAAYRKLLEG 402
Cdd:PRK11281 183 KVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEG 217
|
|
| PLN02217 |
PLN02217 |
probable pectinesterase/pectinesterase inhibitor |
658-746 |
1.96e-03 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215130 [Multi-domain] Cd Length: 670 Bit Score: 42.00 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 658 SPEKPTTPEKVVSPEkpASPEKPRTPEKPASPEKPATPE-KPRTPEKPATPEKPRSPEKPSSPLKDEKAVVEESITVTKV 736
Cdd:PLN02217 582 TTFSSDSPSTVVAPS--TSPPAGHLGSPPATPSKIVSPStSPPASHLGSPSTTPSSPESSIKVASTETASPESSIKVAST 659
|
90
....*....|
gi 128146 737 TKVTAEVEVS 746
Cdd:PLN02217 660 ESSVSMVSMS 669
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
624-690 |
2.21e-03 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 41.21 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 128146 624 PEKPATPKVTSPEKPATPEKPPTPEKAITPekvrspeKPTTPEKVVSPEKPASPEKPRTPEKPASPE 690
Cdd:PTZ00144 129 PAAAAAAKAEKTTPEKPKAAAPTPEPPAAS-------KPTPPAAAKPPEPAPAAKPPPTPVARADPR 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
173-373 |
2.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 173 IEEDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHE--EEVAELLAQLQASHAT 250
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKelEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 251 VERKdylKTDLTTALKEIRAQLECQSDHNMHQAE--------EWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQ-- 320
Cdd:PRK03918 250 LEGS---KRKLEEKIRELEERIEELKKEIEELEEkvkelkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgi 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 128146 321 --------SKSIELESVRGTKESLERQLSDIEERHNndltTYQDtIHQLENELRGTKWEMA 373
Cdd:PRK03918 327 eerikeleEKEERLEELKKKLKELEKRLEELEERHE----LYEE-AKAKKEELERLKKRLT 382
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
72-209 |
2.47e-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: 41.86 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 72 AESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKhagraqlgdayEQELRE 151
Cdd:COG3096 538 LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-----------APAWLA 606
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 128146 152 LRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEAS 209
Cdd:COG3096 607 AQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
87-223 |
2.83e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 87 AELKLSRSNEKEQLQGLNDRFAGyiekvhyLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGAL---EQVSHEK 163
Cdd:PRK09039 63 AELADLLSLERQGNQDLQDSVAN-------LRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELdseKQVSARA 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 128146 164 -AQIQLDSEHIE---EDIQRLRERFEDEARLRDETEATIAALRKEMEEAslmraeLDKKVQSLQ 223
Cdd:PRK09039 136 lAQVELLNQQIAalrRQLAALEAALDASEKRDRESQAKIADLGRRLNVA------LAQRVQELN 193
|
|
| PRK11901 |
PRK11901 |
hypothetical protein; Reviewed |
662-721 |
2.84e-03 |
|
hypothetical protein; Reviewed
Pssm-ID: 237015 [Multi-domain] Cd Length: 327 Bit Score: 40.82 E-value: 2.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 128146 662 PTTPEKVVSPEK----PASPEKPRTPEKPASPEKPATPEK-PRTPEKPATPEKPRSPEKPSSPLK 721
Cdd:PRK11901 175 PTAPATVAPSKGakvpATAETHPTPPQKPATKKPAVNHHKtATVAVPPATSGKPKSGAASARALS 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
181-407 |
3.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 181 RERFE--DEARLRDE------TEATIAALRKEMEEASLMRAELDKKVQSLQDEVaflrgnheeevaELLAQLQASHATVE 252
Cdd:COG4913 587 GTRHEkdDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAEL------------DALQERREALQRLA 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 253 RKDYLKTDLTTALKEIRAqlecqsdhnmhqaeewfkcryaklteaAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGT 332
Cdd:COG4913 655 EYSWDEIDVASAEREIAE---------------------------LEAELERLDASSDDLAALEEQLEELEAELEELEEE 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 333 KESLERQLSDIEERHNNDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLN-------VKMALDIEIAAYRKLLEGEET 405
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALgdavereLRENLEERIDALRARLNRAEE 787
|
..
gi 128146 406 RF 407
Cdd:COG4913 788 EL 789
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
627-725 |
3.19e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.37 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 627 PATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEkprTPEKPAT 706
Cdd:PRK07003 448 PVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS---REDAPAA 524
|
90
....*....|....*....
gi 128146 707 PEKPRSPEKPSSPLKDEKA 725
Cdd:PRK07003 525 AAPPAPEARPPTPAAAAPA 543
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
146-344 |
3.22e-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: 41.48 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 146 EQELRELRGALEQVSHEKAQiqldsehIEEDIQRLRERFedearlrDETEATIAALRKEMEEASLM--------RAELDK 217
Cdd:COG3096 835 EAELAALRQRRSELERELAQ-------HRAQEQQLRQQL-------DQLKEQLQLLNKLLPQANLLadetladrLEELRE 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 218 KVQSLQDEVAFLR--GNHEEEVAELLAQLQashATVERKDYLKTDLTTA---LKEIRAQLECQSD------H-NMHQAE- 284
Cdd:COG3096 901 ELDAAQEAQAFIQqhGKALAQLEPLVAVLQ---SDPEQFEQLQADYLQAkeqQRRLKQQIFALSEvvqrrpHfSYEDAVg 977
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 128146 285 ---------EWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSksieLESVRGTK----ESLERQLSDIE 344
Cdd:COG3096 978 llgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAS----LKSSRDAKqqtlQELEQELEELG 1046
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
623-699 |
3.35e-03 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 40.71 E-value: 3.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 128146 623 SPEKPATPkvTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPekvvspeKPASPEKPRTPEKPASPekpaTPEKPR 699
Cdd:PHA03291 217 SPETTPTP--STTTSPPSTTIPAPSTTIAAPQAGTTPEAEGTP-------APPTPGGGEAPPANATP----APEASR 280
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
623-722 |
3.35e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPATPEKPPTPEK------AITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPE 696
Cdd:PHA03307 99 SPAREGSPTPPGPSSPDPPPPTPPPASpppspaPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSS 178
|
90 100
....*....|....*....|....*.
gi 128146 697 KPRTPEKPATPEKPRSPEKPSSPLKD 722
Cdd:PHA03307 179 PEETARAPSSPPAEPPPSTPPAAASP 204
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
670-736 |
3.74e-03 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 40.82 E-value: 3.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 128146 670 SPEKPASPE--KPRTPEKPASPEKPATPEKPRTPeKPATPEKPRSPEKPSSPLKDEKAVVEESITVTKV 736
Cdd:PTZ00144 125 PAAAPAAAAaaKAEKTTPEKPKAAAPTPEPPAAS-KPTPPAAAKPPEPAPAAKPPPTPVARADPRETRV 192
|
|
| PHA02030 |
PHA02030 |
hypothetical protein |
659-719 |
3.79e-03 |
|
hypothetical protein
Pssm-ID: 222843 [Multi-domain] Cd Length: 336 Bit Score: 40.35 E-value: 3.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 128146 659 PEKPTTPEKVVSPEKPASPEKPrTPEKPASPEKPATPEKPRTPEKP-----ATPEKPRSPEKPSSP 719
Cdd:PHA02030 267 PAVPNVAADAGSAAAPAVPAAA-AAVAQAAPSVPQVPNVAVLPDVPqvapvAAPAAPEVPAVPVVP 331
|
|
| PHA02030 |
PHA02030 |
hypothetical protein |
627-701 |
3.99e-03 |
|
hypothetical protein
Pssm-ID: 222843 [Multi-domain] Cd Length: 336 Bit Score: 40.35 E-value: 3.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 128146 627 PATPKVTSPEKPATPEKPPTPEKAITPE--KVRSPEKPTTPEKVVSPEKPASPEKPRTPEK--PASPEKPATPEKPRTP 701
Cdd:PHA02030 256 KPKSKAAGSNLPAVPNVAADAGSAAAPAvpAAAAAVAQAAPSVPQVPNVAVLPDVPQVAPVaaPAAPEVPAVPVVPAAP 334
|
|
| Pneumo_att_G |
pfam05539 |
Pneumovirinae attachment membrane glycoprotein G; |
625-724 |
4.01e-03 |
|
Pneumovirinae attachment membrane glycoprotein G;
Pssm-ID: 114270 [Multi-domain] Cd Length: 408 Bit Score: 40.42 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 625 EKPATPKVTSPE---KPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASP-EKPATPEKPRT 700
Cdd:pfam05539 222 QGTTTSSNPEPQtepPPSQRGPSGSPQHPPSTTSQDQSTTGDGQEHTQRRKTPPATSNRRSPHSTATPpPTTKRQETGRP 301
|
90 100
....*....|....*....|....
gi 128146 701 PEKPATPEKPRSPEKPSSPLKDEK 724
Cdd:pfam05539 302 TPRPTATTQSGSSPPHSSPPGVQA 325
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-240 |
4.11e-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: 40.82 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 95 NEKEQLQGLNDRFagyIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIE 174
Cdd:TIGR02169 399 REINELKRELDRL---QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 128146 175 EDIQRLRERFEDEARLRDETEATIAALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAEL 240
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAI 541
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
624-719 |
4.18e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 40.99 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 624 PEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEK 703
Cdd:PRK07003 427 PAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAA 506
|
90
....*....|....*.
gi 128146 704 PATPEKPRSPEKPSSP 719
Cdd:PRK07003 507 VPDARAPAAASREDAP 522
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
95-346 |
4.82e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 95 NEKEQLQGLnDRFAG---YIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELrgaleqvshEKAQIQLDSE 171
Cdd:COG0497 139 DPDAQRELL-DAFAGleeLLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL---------EAAALQPGEE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 172 hieEDIQRLRERFEDEARLRDETEATIAALRKEmeEASLMRAeLDKKVQSLQDEVAflrgnHEEEVAELLAQLQASHATV 251
Cdd:COG0497 209 ---EELEEERRRLSNAEKLREALQEALEALSGG--EGGALDL-LGQALRALERLAE-----YDPSLAELAERLESALIEL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 252 ErkdylktDLTTALKEIRAQLEcqsdhnmhqAEEwfkcryAKLtEAAEQNKEAIRSAK-------EEIAEYRRQLQSKSI 324
Cdd:COG0497 278 E-------EAASELRRYLDSLE---------FDP------ERL-EEVEERLALLRRLArkygvtvEELLAYAEELRAELA 334
|
250 260
....*....|....*....|..
gi 128146 325 ELESVRGTKESLERQLSDIEER 346
Cdd:COG0497 335 ELENSDERLEELEAELAEAEAE 356
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
623-712 |
5.00e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEkPRTPEKPASPEKPATPEKPRTPE 702
Cdd:PRK07764 426 AAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPA-PAPPAAPAPAAAPAAPAAPAAPA 504
|
90
....*....|
gi 128146 703 KPATPEKPRS 712
Cdd:PRK07764 505 GADDAATLRE 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
76-253 |
5.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 76 DVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIE-AELAALRQKHAGRAQLGDAYE-------- 146
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQlEELEQEIAALLAEAGVEDEEElraaleqa 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 147 QELRELRGALEQVSHEKAQI---------QLDSEHIEEDIQRLRERFEDEARLRDETEATIAALRKEMEEaslmrAELDK 217
Cdd:COG4717 395 EEYQELKEELEELEEQLEELlgeleelleALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ-----LEEDG 469
|
170 180 190
....*....|....*....|....*....|....*.
gi 128146 218 KVQSLQDEVAFLRGNHEEEVAELLAqLQASHATVER 253
Cdd:COG4717 470 ELAELLQELEELKAELRELAEEWAA-LKLALELLEE 504
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
117-214 |
5.47e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 38.23 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 117 LEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRG-ALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEAR--LRDE 193
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAeAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEaeIEQE 108
|
90 100
....*....|....*....|.
gi 128146 194 TEATIAALRKEMEEASLMRAE 214
Cdd:COG0711 109 RAKALAELRAEVADLAVAIAE 129
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
68-413 |
5.66e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 68 VLSSAESLDVSQSSLLNGAAELKLSRSNEKE---QLQGLNDRFAGYIEKvhyLEQQNKEI--EAELAALRQKhagraqlg 142
Cdd:PRK04863 295 LYTSRRQLAAEQYRLVEMARELAELNEAESDleqDYQAASDHLNLVQTA---LRQQEKIEryQADLEELEER-------- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 143 dAYEQELrelrgALEQVSHEKAQIQLDSEHIEEDIQRLR-------ERFE----------------DEAR----LRDET- 194
Cdd:PRK04863 364 -LEEQNE-----VVEEADEQQEENEARAEAAEEEVDELKsqladyqQALDvqqtraiqyqqavqalERAKqlcgLPDLTa 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 195 ---EATIAALRKEMEEASLMRAELDKKVQSLQD-----EVAF---------------------LRGNHEEE--VAELLAQ 243
Cdd:PRK04863 438 dnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfEQAYqlvrkiagevsrseawdvareLLRRLREQrhLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 244 LQASHATVERKDYLKTDLTTALKEIraqleCQSDHNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKS 323
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEF-----CKRLGKNLDDED----ELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 324 IELESVRGTKESLERQ-------LSDIEERHNNDLTTYQDTIHQLENelrgtkweMARHLREYQdllnvkmALDIEIAAY 396
Cdd:PRK04863 589 EQLQARIQRLAARAPAwlaaqdaLARLREQSGEEFEDSQDVTEYMQQ--------LLERERELT-------VERDELAAR 653
|
410
....*....|....*..
gi 128146 397 RKLLEGEETRFSAFSGS 413
Cdd:PRK04863 654 KQALDEEIERLSQPGGS 670
|
|
| NESP55 |
pfam06390 |
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ... |
636-724 |
5.84e-03 |
|
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian neuroendocrine-specific golgi protein P55 (NESP55) sequences. NESP55 is a novel member of the chromogranin family and is a soluble, acidic, heat-stable secretory protein that is expressed exclusively in endocrine and nervous tissues, although less widely than chromogranins.
Pssm-ID: 115071 [Multi-domain] Cd Length: 261 Bit Score: 39.46 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 636 EKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPAT--PEKPRT---PEKPATPEKP 710
Cdd:pfam06390 135 EPETEPDTAPTTEPETEPEDEPGPVVPKGATFHQSLTERLHALKLQSADASPRRAPPSTqePESAREgeePERGPLDKDP 214
|
90
....*....|....
gi 128146 711 RSPEKPSSPLKDEK 724
Cdd:pfam06390 215 RDPEEEEEEKEEEK 228
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
648-729 |
5.88e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 40.18 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 648 EKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPE---KPRTPEKPATPEKPRSPEkPSSPLKDEK 724
Cdd:PRK14950 357 EALLVPVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVREtatPPPVPPRPVAPPVPHTPE-SAPKLTRAA 435
|
....*
gi 128146 725 AVVEE 729
Cdd:PRK14950 436 IPVDE 440
|
|
| PHA01929 |
PHA01929 |
putative scaffolding protein |
627-703 |
6.19e-03 |
|
putative scaffolding protein
Pssm-ID: 177328 Cd Length: 306 Bit Score: 39.65 E-value: 6.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 128146 627 PATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPekPASPEKPATPEKPRTPEK 703
Cdd:PHA01929 27 PQPNPVIQPQAPVQPGQPGAPQQLAIPTQQPQPVPTSAMTPHVVQQAPAQPAPAAPP--AAGAALPEALEVPPPPAF 101
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
117-382 |
6.78e-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: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 117 LEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHekaqiqLDSEHIEEDIQRLRERFeDEArlrDETEA 196
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANL------LADETLADRLEELREEL-DAA---QEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 197 TIAALRKEMEeaslmraELDKKVQSLQ---DEVAFLRGNHEEEVAELLAQLQASHA---TVERKDYL-----------KT 259
Cdd:COG3096 911 FIQQHGKALA-------QLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFAlseVVQRRPHFsyedavgllgeNS 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 260 DLTTALKE--IRAQLEC-QSDHNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL-----ESVRG 331
Cdd:COG3096 984 DLNEKLRArlEQAEEARrEAREQLRQAQA----QYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAdaeaeERARI 1059
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 128146 332 TKESLERQLSDIEERHNNDLTTYQDTihqlENELRGTKWEMARHLREYQDL 382
Cdd:COG3096 1060 RRDELHEELSQNRSRRSQLEKQLTRC----EAEMDSLQKRLRKAERDYKQE 1106
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
117-230 |
7.03e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.48 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 117 LEQQNKEIEAElaalRQKHAGRAQLGDAYEQELRELRGALEQVshEKAQiqldsehiEEDIQRLRERFEDEAR-LRDETE 195
Cdd:cd16269 193 LTEKEKEIEAE----RAKAEAAEQERKLLEEQQRELEQKLEDQ--ERSY--------EEHLRQLKEKMEEEREnLLKEQE 258
|
90 100 110
....*....|....*....|....*....|....*
gi 128146 196 ATIAALRKEMEEasLMRAELDKKVQSLQDEVAFLR 230
Cdd:cd16269 259 RALESKLKEQEA--LLEEGFKEQAELLQEEIRSLK 291
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
117-213 |
8.46e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 117 LEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGAleQVSHEKAQIQLDSEhIEEDIQRLRERFEDEARLRD---- 192
Cdd:PRK11637 175 LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQA--RNERKKTLTGLESS-LQKDQQQLSELRANESRLRDsiar 251
|
90 100
....*....|....*....|..
gi 128146 193 -ETEATIAALRkEMEEASLMRA 213
Cdd:PRK11637 252 aEREAKARAER-EAREAARVRD 272
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
623-719 |
9.08e-03 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 39.07 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPaTPKVTSPeKPATPE-KPPTPEKAIT---PEKVRSP-EKPTTPEKVV--SPEKPASPEKPRTPEKPASPEKPaTP 695
Cdd:PHA02682 80 SPLAP-SPACAAP-APACPAcAPAAPAPAVTcpaPAPACPPaTAPTCPPPAVcpAPARPAPACPPSTRQCPPAPPLP-TP 156
|
90 100
....*....|....*....|....
gi 128146 696 eKPRTPEKPATPEKPRSPekPSSP 719
Cdd:PHA02682 157 -KPAPAAKPIFLHNQLPP--PDYP 177
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
623-721 |
9.27e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 39.77 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128146 623 SPEKPATP-----KVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKP---RTPeKPASPEKPAT 694
Cdd:PHA03307 283 GPASSSSSprersPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPspsRSP-SPSRPPPPAD 361
|
90 100
....*....|....*....|....*..
gi 128146 695 PEKPRTPEKPATPEKPRSPEKPSSPLK 721
Cdd:PHA03307 362 PSSPRKRPRPSRAPSSPAASAGRPTRR 388
|
|
| |
