|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
95-406 |
4.84e-139 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 415.09 E-value: 4.84e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 95 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQK-HAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHI 173
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 174 EEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAELLAQLQASHATVER 253
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 254 KDYLKTDLTTALKEIRAQLECQSDHNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 333
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099376549 334 ESLERQLSDIEERHNNDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 406
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
625-749 |
3.04e-18 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 90.13 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 625 EKPATPKvtSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKP 704
Cdd:PTZ00449 577 KKPEFPK--DPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKII 654
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2099376549 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 |
1.31e-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: 78.20 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 12 SYRRVMTEtrATYSRASASPSSGFR---SQSWSRGSGSTVSSSYKRTNLGAPRTAYGSTVlssAESLDVSQSSLLNGaaE 88
Cdd:pfam04732 5 SYRRMFGD--SSSSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSSRSSSRSSYPSLA---ADSLDFSLADALNQ--E 77
|
....*.
gi 2099376549 89 LKLSRS 94
Cdd:pfam04732 78 FKATRT 83
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-346 |
5.41e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 99 QLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQ 178
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 179 RLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHATVERKDYLK 258
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 259 TDLTTALKEIRAQLEcQSDHNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLER 338
Cdd:COG1196 389 LEALRAAAELAAQLE-ELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
....*...
gi 2099376549 339 QLSDIEER 346
Cdd:COG1196 464 LLAELLEE 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
91-382 |
8.25e-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: 78.95 E-value: 8.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 91 LSRSNEKEQLQglndrfagyiEKVHYLEQQNKEIEAELAALRQKHagraqlgDAYEQELRELRGALEQVSHEKAQIQLDS 170
Cdd:TIGR02168 673 LERRREIEELE----------EKIEELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 171 EHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHAT 250
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 251 VERKDYLKTDLTTALKEIRAQLECQSDHNMHQAEEWfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVR 330
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQI-----EELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2099376549 331 GTKESLERQLSDIEErhnnDLTTYQDTIHQLENELRGTKWEMARHLREYQDL 382
Cdd:TIGR02168 887 EALALLRSELEELSE----ELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
626-719 |
3.42e-14 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 77.04 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 626 KPATPKVTSpEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPA 705
Cdd:PTZ00449 568 KPSKIPTLS-KKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPE 646
|
90
....*....|....
gi 2099376549 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 |
2.67e-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: 74.32 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 62 TAYGSTVLSSAESLDVSQSSLlngaAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAgraql 141
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKL----EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE----- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 142 gdAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQS 221
Cdd:TIGR02168 320 --ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 222 LQdevaflrgnheEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQlECQSDHNMHQAEEwfkcryAKLTEAAEQN 301
Cdd:TIGR02168 398 LN-----------NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEEL------EELQEELERL 459
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2099376549 302 KEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNN 349
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
118-414 |
3.20e-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: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 118 EQQNKEIEAELAALRQKHAGRAQLG---DAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDET 194
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 195 EATIRALRKEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLEc 274
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 275 qsdhnmHQAEEWFKCRYAKLTEAAEQnkEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTY 354
Cdd:COG1196 376 ------EAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099376549 355 QDTIHQLENELRGTKWEMARHLRE---YQDLLNVKMALDIEIAAYRKLLEGEETRFSAFSGSI 414
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEaalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-388 |
9.06e-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: 69.32 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 117 LEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQ--LDS-----EHIEEDIQRLRERFEDEAR 189
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkeLYAlaneiSRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 190 LRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKE-- 267
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQia 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 268 -IRAQLECQSDHnMHQAEEwfkcRYAKLTEAAEQNKEAIRSAkeEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEER 346
Cdd:TIGR02168 397 sLNNEIERLEAR-LERLED----RRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2099376549 347 ---HNNDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMA 388
Cdd:TIGR02168 470 leeAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-406 |
1.27e-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: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 123 EIEAELAALRQKhAGRAQLGDAYEQELRELRGALeqvshekaqIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALR 202
Cdd:COG1196 197 ELERQLEPLERQ-AEKAERYRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 203 KEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLEcqsdhnmhQ 282
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEY----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE--------E 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 283 AEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLE 362
Cdd:COG1196 335 LEE----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2099376549 363 NELRgtkwEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 406
Cdd:COG1196 411 ALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-350 |
3.20e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 72 AESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRE 151
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 152 LRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRG 231
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 232 NHEEEVAELLAQLQashATVERKDYLKTDLTTALKEIRAQLECQSDHNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEE 311
Cdd:COG1196 408 AEEALLERLERLEE---ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE------EALLELLAELLEEAALLEAA 478
|
250 260 270
....*....|....*....|....*....|....*....
gi 2099376549 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 |
1.90e-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: 63.63 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 136 AGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAEL 215
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 216 DKKVQSLQDEVA----FLRGNHEEEVAELLAQLQASHATVERKDYLKtDLTTALKEIRAQLEcqsdhnmhqaeewfkcry 291
Cdd:COG4942 96 RAELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELR------------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 292 aKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLENELRGTKWE 371
Cdd:COG4942 157 -ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
...
gi 2099376549 372 MAR 374
Cdd:COG4942 236 AAA 238
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
144-383 |
2.66e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 144 AYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLrdetEATIRALRKEMEEASLMRAELDKKVQSLQ 223
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL----EAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 224 DEVAFLrgnhEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQL-ECQSDHNMH--QAE------EWFKCRYAKL 294
Cdd:PRK02224 286 ERLEEL----EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLeECRVAAQAHneEAEslredaDDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 295 TEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHnNDLTTYQDTIHQLENELRGTKWEMAR 374
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERDELREREAELEATLRTARE 440
|
....*....
gi 2099376549 375 HLREYQDLL 383
Cdd:PRK02224 441 RVEEAEALL 449
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
624-754 |
3.14e-10 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 63.94 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 624 PEKPATPKV-TSPEKPATPEKPPTPEKAITPEKVRSPEKPTTP------------------------------EKVVSPE 672
Cdd:PTZ00449 627 PESPKSPKRpPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPkfkekfyddyldaaaksketkttvvldesfESILKET 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 673 KPASPEKPRTPEKPASPEKPATPEKPRTPEKPATPEKPrSPEKPSSPLKDEKAVVEESITVTKVTKVTAEvevskEARKE 752
Cdd:PTZ00449 707 LPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQP-DDIEFFTPPEEERTFFHETPADTPLPDILAE-----EFKEE 780
|
..
gi 2099376549 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 |
7.67e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 65 GSTVLSSAESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAgyiEKVHYLEQQNKEIEA----ELAALRQK----HA 136
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE---EIEQLLEELNKKIKDlgeeEQLRVKEKigelEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 137 GRAQLGDAYEQELRELRGALEQVshekAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELD 216
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERL----AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 217 KKVQSLQDEVAFLRGNHE---EEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQL-ECQSDHNMHQAE----EWFK 288
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInELEEEKEDKALEikkqEWKL 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099376549 289 CRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQL 361
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
|
| 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 2099376549 624 PEKPATPKVTSPEKPATPEKPPTPEKAITPEKVR---SPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPrT 700
Cdd:PHA03247 2722 PPGPAAARQASPALPAAPAPPAVPAGPATPGGPArpaRPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLP-S 2800
|
90
....*....|....*....
gi 2099376549 701 PEKPATPEKPRSPEKPSSP 719
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAALP 2819
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
82-325 |
8.24e-09 |
|
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: 58.62 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 82 LLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSH 161
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 162 EKAQIQLDSEHIEEDIQRL------------------RERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQ 223
Cdd:COG4942 91 EIAELRAELEAQKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 224 DEvaflrgnhEEEVAELLAQLQASHATVERkdyLKTDLTTALKEIRAQLECQSDhnmhqaeewfkcRYAKLTEAAEQNKE 303
Cdd:COG4942 171 AE--------RAELEALLAELEEERAALEA---LKAERQKLLARLEKELAELAA------------ELAELQQEAEELEA 227
|
250 260
....*....|....*....|..
gi 2099376549 304 AIRSAKEEIAEYRRQLQSKSIE 325
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFA 249
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-383 |
8.65e-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: 59.31 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 112 EKVHYLEQQNKEIEAELAALRQKHAGRaqlgdayEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLR 191
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRI-------ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 192 DETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFL-RGNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEI-- 268
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtl 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 269 -RAQLECQSDHNMHQAEEWfKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERH 347
Cdd:TIGR02169 827 eKEYLEKEIQELQEQRIDL-KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270
....*....|....*....|....*....|....*.
gi 2099376549 348 NNDLTTYQDTIHQLeNELRGTKWEMARHLREYQDLL 383
Cdd:TIGR02169 906 EELEAQIEKKRKRL-SELKAKLEALEEELSEIEDPK 940
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
623-730 |
1.38e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.18 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTP-EKVVSPEKPASPEKP--RTPEKPASPEKP-----AT 694
Cdd:PHA03247 2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlGGSVAPGGDVRRRPPsrSPAAKPAAPARPpvrrlAR 2888
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2099376549 695 PEKPRTPEK----PATPEKPRSPEKPSSPLKDEKAVVEES 730
Cdd:PHA03247 2889 PAVSRSTESfalpPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-384 |
1.53e-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: 58.54 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 88 ELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQ 167
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 168 LDSEHIEEDIQRLRERFED-EARLRDE------------------TEATIRALRKEMEEASLMRAELDKKVQSLQDEVAF 228
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDlEARLSHSripeiqaelskleeevsrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 229 L---RGNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLECQSDH--NMHQAEEWFKCRYAKLTEAAEQNKE 303
Cdd:TIGR02169 845 LkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQlrELERKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 304 AIRSAKEEIAEYRRQLQSKSIE------LESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLeNELRGTKWEMARHLR 377
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERK 1003
|
....*..
gi 2099376549 378 EYQDLLN 384
Cdd:TIGR02169 1004 AILERIE 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
68-273 |
2.36e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 68 VLSSAESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQ 147
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 148 ELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVA 227
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2099376549 228 flrgNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLE 273
Cdd:COG1196 453 ----ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
630-730 |
2.37e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.41 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 630 PKVTSPEKPATPEKPPtpekaitpekVRSPEKPTTPEKVVS-PEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPatPE 708
Cdd:PHA03247 2867 PSRSPAAKPAAPARPP----------VRRLARPAVSRSTESfALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP--PP 2934
|
90 100
....*....|....*....|..
gi 2099376549 709 KPRSPEKPSSPLKDEKAVVEES 730
Cdd:PHA03247 2935 PPPRPQPPLAPTTDPAGAGEPS 2956
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
626-719 |
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 2099376549 626 KPATPKVTSPEKPATPEKPPTPekaitPEKVRSPEKPTTP-EKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKP 704
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPTPEP-----APHALVSATPLPPgPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT 2763
|
90
....*....|....*
gi 2099376549 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 2099376549 624 PEKPATPKVTsPEKPATPEKP-PTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPE 702
Cdd:PHA03247 2704 PPPTPEPAPH-ALVSATPLPPgPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
|
90 100 110
....*....|....*....|....*....|
gi 2099376549 703 KPATPEKPRSPEKPSSPLKDEKAVVEESIT 732
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVL 2812
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
66-379 |
3.66e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 66 STVLSSAESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAY 145
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 146 EQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERfedearlRDETEATIRALRKEMEEASLMRA------------ 213
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER-------EAELEATLRTARERVEEAEALLEagkcpecgqpve 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 214 ---------ELDKKVQSLQDEVAFLRGNHE--EEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLECQSDhnmhQ 282
Cdd:PRK02224 463 gsphvetieEDRERVEELEAELEDLEEEVEevEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE----R 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 283 AEEWFKcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNndlttYQDTIHQLe 362
Cdd:PRK02224 539 AEELRE-RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-----AEDEIERL- 611
|
330
....*....|....*..
gi 2099376549 363 NELRGTKWEMARHLREY 379
Cdd:PRK02224 612 REKREALAELNDERRER 628
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-345 |
1.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 67 TVLSSAESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYE 146
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 147 QELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERF--------------EDEARLRDETEATIRALRKEMEEASLMR 212
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlrerleslerriAATERRLEDLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 213 AELDKKVQSLQDEVA---FLRGNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLEcqsDHNMHQAE----- 284
Cdd:TIGR02168 862 EELEELIEELESELEallNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA---QLELRLEGlevri 938
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099376549 285 ----EWFKCRYAKLTEAAEQNKEAI----RSAKEEIAEYRRQLQS------KSI-ELESVRGTKESLERQLSDIEE 345
Cdd:TIGR02168 939 dnlqERLSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKElgpvnlAAIeEYEELKERYDFLTAQKEDLTE 1014
|
|
| 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 2099376549 623 SPEKPATPKVT-SPEKPATPEKPPTPEKAITPEKVRSPEKPTTP--------------EKVVSPEKPASPEKPRTPEKPA 687
Cdd:PHA03247 2738 APAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRrltrpavaslsesrESLPSPWDPADPPAAVLAPAAA 2817
|
90 100 110
....*....|....*....|....*....|....*
gi 2099376549 688 SP--EKPATPEKPRTPEKPATPEKPRSPEKPSSPL 720
Cdd:PHA03247 2818 LPpaASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL 2852
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-273 |
3.17e-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: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 117 LEQQNKEIEAELAALRQKHAGraqlgdaYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEdeaRLRDETEa 196
Cdd:COG1579 22 LEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG---NVRNNKE- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099376549 197 tIRALRKEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHATVERKdylKTDLTTALKEIRAQLE 273
Cdd:COG1579 91 -YEALQKEIESLKRRISDLEDEILELMERIE----ELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
88-383 |
4.70e-07 |
|
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: 53.36 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 88 ELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQ 167
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 168 LDSEHIEEDIQRL-RERFEDEARLRD------ETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLR------GNHE 234
Cdd:pfam07888 150 TELERMKERAKKAgAQRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttaHRKE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 235 EEVAELLAQLQAS----HATVERKDYLKTDLTTA----------LKEIR---AQLECQ-SDHNMHQAEEwfKCRYAKLTE 296
Cdd:pfam07888 230 AENEALLEELRSLqerlNASERKVEGLGEELSSMaaqrdrtqaeLHQARlqaAQLTLQlADASLALREG--RARWAQERE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 297 AAEQNKEAirsAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLENELRGTKWEMARHL 376
Cdd:pfam07888 308 TLQQSAEA---DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQ 384
|
....*..
gi 2099376549 377 REYQDLL 383
Cdd:pfam07888 385 AEKQELL 391
|
|
| 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 2099376549 637 KPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPATPEKPRSPEKP 716
Cdd:PRK12270 37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDE 116
|
90 100
....*....|....*....|....*....
gi 2099376549 717 SSPLKD-EKAVV---EESITVTKVTKVTA 741
Cdd:PRK12270 117 VTPLRGaAAAVAknmDASLEVPTATSVRA 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
96-249 |
5.33e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 96 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYE--QELRELRGALEQVSHEKAQIQLDSEHI 173
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 174 EEDIQRLRERFEDEARLRDETEATIR----ALRKEMEEASLMRAELDKKVQSLQDEVAFLR---GNHEEEVAELLAQLQA 246
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEEAQeelEELEEELEQLENELEA 238
|
...
gi 2099376549 247 SHA 249
Cdd:COG4717 239 AAL 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
122-328 |
7.50e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 122 KEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRA- 200
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLl 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 201 -LRKEMEEASLMRAELDKKVQSLQDEVaflrgnheEEVAELLAQLQASHATVERkdylktdLTTALKEIRAQLECQSDHN 279
Cdd:COG4717 129 pLYQELEALEAELAELPERLEELEERL--------EELRELEEELEELEAELAE-------LQEELEELLEQLSLATEEE 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2099376549 280 MHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELES 328
Cdd:COG4717 194 LQDLAE----ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
87-240 |
9.92e-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: 50.69 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 87 AELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAgraqlgdAYEQELRELRGA--LEQVSHEKA 164
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-------KYEEQLGNVRNNkeYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099376549 165 QIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEAslmRAELDKKVQSLQDEVAFLRGNHEEEVAEL 240
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELEELEAEREELAAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
82-401 |
1.33e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 82 LLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIE---AELAALRQK--HAGRAQLGDAyEQELRELRGAL 156
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAelqEELEELLEQlsLATEEELQDL-AEELEELQQRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 157 EQVSHEKAQIQLDSEHIEEDIQRLR---ERFEDEARLRDET--------------------------------------- 194
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLEnelEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllal 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 195 --------EATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAELLAQLQASHATVERKDYLKTDLTTA-- 264
Cdd:COG4717 289 lflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEel 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 265 LKEIRAQLECQSDHNMHQAEEWfkcryAKLTEAAEQNKEAIRSAKEEIAEYR--RQLQSKSIELESVRGTKESLERQLSD 342
Cdd:COG4717 369 EQEIAALLAEAGVEDEEELRAA-----LEQAEEYQELKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEE 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2099376549 343 IEERHNNDLTTYQDTIHQLENELRGTKWEMARHlrEYQDLLNVKMALDIEIAAYRKLLE 401
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQ--ELEELKAELRELAEEWAALKLALE 500
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
93-348 |
1.52e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 93 RSNEKEQLQGLNDRFAGYIEKVHYLEqqnkEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEH 172
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 173 IEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRgnheEEVAELLAQLQASHATVE 252
Cdd:PRK02224 305 DDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR----EEAAELESELEEAREAVE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 253 RKDYLKTDLTTALKEIRAQLEcQSDHNMHQAEEWFKCRYAKLTEAAEQNKE---AIRSAKEEIAEYRRQLQS-------K 322
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFG-DAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecgQ 459
|
250 260 270
....*....|....*....|....*....|...
gi 2099376549 323 SIE-------LESVRGTKESLERQLSDIEERHN 348
Cdd:PRK02224 460 PVEgsphvetIEEDRERVEELEAELEDLEEEVE 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
99-349 |
1.97e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 99 QLQGLNDRFAGYIekvhyLEQqnKEIEAELAALrQKHagRAQLGDAYEQ--ELRELRGALEQV-----SHEKAQIQLDse 171
Cdd:COG4913 205 PIGDLDDFVREYM-----LEE--PDTFEAADAL-VEH--FDDLERAHEAleDAREQIELLEPIrelaeRYAAARERLA-- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 172 HIEEDIQRLR-----ERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAELLAQLQA 246
Cdd:COG4913 273 ELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 247 SHATVERKdylKTDLTTALKEIRAQLEcqsdhnmHQAEEWfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 326
Cdd:COG4913 353 ELEERERR---RARLEALLAALGLPLP-------ASAEEF-----AALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
250 260
....*....|....*....|...
gi 2099376549 327 esvRGTKESLERQLSDIEERHNN 349
Cdd:COG4913 418 ---RRELRELEAEIASLERRKSN 437
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-244 |
2.35e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 97 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAG---------RAQLGDAyEQELRELRGALEQVSHEKAQIQ 167
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqlEREIERL-ERELEERERRRARLEALLAALG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 168 LDSEHIEEDIQRLRERFedeARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRG---NHEEEVAELLAQL 244
Cdd:COG4913 373 LPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksNIPARLLALRDAL 449
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
110-370 |
2.39e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 110 YIEkvHYLEQQNKEIEAELAALRQkhagraQLgDAYEQELRELRGALE--QVSHEKAQIQLDSEHIEEDIQRLRERFEDE 187
Cdd:COG3206 161 YLE--QNLELRREEARKALEFLEE------QL-PELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 188 ARLRDETEATIRALRKEMEEASLMRAEL--DKKVQSLQDEVAFLrgnhEEEVAELLAQLQASHATVerkdylktdlttal 265
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAEL----EAELAELSARYTPNHPDV-------------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 266 KEIRAQLEcqsdhnmhQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEE 345
Cdd:COG3206 294 IALRAQIA--------ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
250 260
....*....|....*....|....*
gi 2099376549 346 RHNNDLTTYQDTihQLENELRGTKW 370
Cdd:COG3206 366 LYESLLQRLEEA--RLAEALTVGNV 388
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
627-707 |
2.93e-06 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 50.34 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 627 PATPkvtspekPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPAspekPATPEKPRTPEKPAT 706
Cdd:PHA03291 205 PATP-------RPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPEAEGTPA----PPTPGGGEAPPANAT 273
|
.
gi 2099376549 707 P 707
Cdd:PHA03291 274 P 274
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-361 |
3.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 97 KEQLQGLNDRFAGY--IEKVHYLEQQNKEIEAELAALRQKHAG-----------RAQLgDAYEQELRELRGALEQVSHEK 163
Cdd:COG4913 637 EAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAELERldassddlaalEEQL-EELEAELEELEEELDELKGEI 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 164 AQIQLDSEHIEEDIQRLRERFED-----EARLRDETEATIRALRKEmEEASLMRAELDKKVQSLQDEvaflRGNHEEEVA 238
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEAaedlaRLELRALLEERFAAALGD-AVERELRENLEERIDALRAR----LNRAEEELE 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 239 ELLAQLQashatvERKDYLKTDLTTALK---EIRAQLECQSDHNMHQAEEWFKcRYakLTEAAEQNKEAIRSA-KEEIAE 314
Cdd:COG4913 791 RAMRAFN------REWPAETADLDADLEslpEYLALLDRLEEDGLPEYEERFK-EL--LNENSIEFVADLLSKlRRAIRE 861
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2099376549 315 YRRQLQSKSIELESVR-GTKESLerQLsDIEERHNNDLTTYQDTIHQL 361
Cdd:COG4913 862 IKERIDPLNDSLKRIPfGPGRYL--RL-EARPRPDPEVREFRQELRAV 906
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
97-345 |
7.20e-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: 49.95 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 97 KEQLQGLNdrfaGYIEKVHYL-----EQQNKEIEAELAALRQKHAGRAQLGDAYEQ-------------ELRELRGALEQ 158
Cdd:COG3096 870 KEQLQLLN----KLLPQANLLadetlADRLEELREELDAAQEAQAFIQQHGKALAQleplvavlqsdpeQFEQLQADYLQ 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 159 VSHEKAQIQLDSEHIEEDIQRlRERF--EDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAflrgnheeE 236
Cdd:COG3096 946 AKEQQRRLKQQIFALSEVVQR-RPHFsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYS--------Q 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 237 VAELLAQLQASHATverkdylKTDLTTALKEIRAQLECQSDHNmhqAEEWFKCRYAKLTEAAEQNkeaiRSAKEEIaeyR 316
Cdd:COG3096 1017 YNQVLASLKSSRDA-------KQQTLQELEQELEELGVQADAE---AEERARIRRDELHEELSQN----RSRRSQL---E 1079
|
250 260
....*....|....*....|....*....
gi 2099376549 317 RQLQSKSIELESVRGTKESLERQLSDIEE 345
Cdd:COG3096 1080 KQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
|
|
| Cornifin |
pfam02389 |
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ... |
624-723 |
7.69e-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: 46.20 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 624 PEKPATPKVTSPEKPATPE--KPPTPEKAITpeKVRSPEKPTTPE----KVVSPEKPASPE--KPRTPEkPASPEKPaTP 695
Cdd:pfam02389 13 PQEPCVPTTKEPCHSKVPEpcNPKVPEPCCP--KVPEPCCPKVPEpccpKVPEPCCPKVPEpcYPKVPE-PCSPKVP-EP 88
|
90 100 110
....*....|....*....|....*....|..
gi 2099376549 696 EKPRTPE--KPATPEK--PRSPEkPSSPLKDE 723
Cdd:pfam02389 89 CHPKAPEpcHPKVPEPcyPKAPE-PCQPKVPE 119
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
635-719 |
8.12e-06 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 49.69 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 635 PEKPATPEKPPT-PEKAITPEKVRSPEKPT-TPEKVVSPEKPASPEKPRTPeKPASPEKPAT-------PEKPRTPEKPA 705
Cdd:PTZ00449 511 PEGPEASGLPPKaPGDKEGEEGEHEDSKESdEPKEGGKPGETKEGEVGKKP-GPAKEHKPSKiptlskkPEFPKDPKHPK 589
|
90
....*....|....
gi 2099376549 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 |
1.05e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 188 ARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAflrgNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKE 267
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 268 IRAQLECQSDHNMHQAEEWFKC---RYAKLTEAAEQNKEAIRSAK--EEIAEYRRQ----LQSKSIELESVRGT----KE 334
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgrqPPLALLLSPEDFLDAVRRLQylKYLAPARREqaeeLRADLAELAALRAEleaeRA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 335 SLERQLSDIEERHN---NDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGeeTRFSAFS 411
Cdd:COG4942 175 ELEALLAELEEERAaleALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA--AGFAALK 252
|
....*..
gi 2099376549 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 |
1.13e-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: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTSPEKPATPEKPPTPEkAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPrTPE 702
Cdd:COG3266 264 ASAPATTSLGEQQEVSLPPAVAAQPA-AAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKPVVTETAAPAAP-APE 341
|
90 100
....*....|....*....|....
gi 2099376549 703 KPATPEKPRSPEKPSSPLKDEKAV 726
Cdd:COG3266 342 AAAAAAAPAAPAVAKKLAADEQWL 365
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
53-401 |
1.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 53 KRTNLGAPRTAYGSTVLSSAESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALR 132
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 133 QK--------HAGRAQLGDA---YEQELR---EL----------RGALEQV------------SHEKA----------QI 166
Cdd:COG4913 433 RRksniparlLALRDALAEAlglDEAELPfvgELievrpeeerwRGAIERVlggfaltllvppEHYAAalrwvnrlhlRG 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 167 QLDSEHIEEDI-----------------------------QRLRERF-----EDEARLRDET------------------ 194
Cdd:COG4913 513 RLVYERVRTGLpdperprldpdslagkldfkphpfrawleAELGRRFdyvcvDSPEELRRHPraitragqvkgngtrhek 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 195 ----------------EATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHE-----EEVAELLAQLQASHATVER 253
Cdd:COG4913 593 ddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlAEYSWDEIDVASAEREIAE 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 254 KDYLKTDLTTA---LKEIRAQLE-CQSDHNmhQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSI----- 324
Cdd:COG4913 673 LEAELERLDASsddLAALEEQLEeLEAELE--ELEE----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarle 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 325 ---ELESVRGTkESLERQLSDIEERHNNDLTTYQDTIHQLENELRGTkweMARHLREYQDLLNvkmALDIEIAA---YRK 398
Cdd:COG4913 747 lraLLEERFAA-ALGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETA---DLDADLESlpeYLA 819
|
...
gi 2099376549 399 LLE 401
Cdd:COG4913 820 LLD 822
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
623-741 |
1.21e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKvvSPEKPASPEKPRTPEKPASPEKPATPEKPRTPE 702
Cdd:PHA03247 2890 AVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP--PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
|
90 100 110
....*....|....*....|....*....|....*....
gi 2099376549 703 KPATPEKPRSPEKPSSPLKDEKAVVEESITVTKVTKVTA 741
Cdd:PHA03247 2968 VPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSS 3006
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
623-718 |
1.52e-05 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 47.37 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTSPEkpatPEKPPTPEKaiTPEKVRSPEKP---------TTPEKVVSPE-KPAS--PEKPRTPEKPASPe 690
Cdd:PRK10819 54 APADLEPPQAVQPP----PEPVVEPEP--EPEPIPEPPKEapvvipkpePKPKPKPKPKpKPVKkvEEQPKREVKPVEP- 126
|
90 100
....*....|....*....|....*...
gi 2099376549 691 KPATPEKPRTPEKPATPEKPRSPEKPSS 718
Cdd:PRK10819 127 RPASPFENTAPARPTSSTATAAASKPVT 154
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
657-728 |
1.66e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 48.37 E-value: 1.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099376549 657 RSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPATPEKPRSPeKPSSPLKDEKAVVE 728
Cdd:PRK01297 11 KGEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKP-KPASLWKLEDFVVE 81
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
624-719 |
1.93e-05 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 46.98 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 624 PEKPATPKVTSPEKPATPEKPPTPEkaitPEKVRS-PEKPTTPEKVVSPeKPASPEKPRTPEKPASPEKPATPEKPrTPE 702
Cdd:PRK10819 82 PEPPKEAPVVIPKPEPKPKPKPKPK----PKPVKKvEEQPKREVKPVEP-RPASPFENTAPARPTSSTATAAASKP-VTS 155
|
90
....*....|....*..
gi 2099376549 703 KPATPeKPRSPEKPSSP 719
Cdd:PRK10819 156 VSSGP-RALSRNQPQYP 171
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-406 |
2.08e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 171 EHIEE--DIQRLRERfedearlRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVA------FLRGNHEE-EVAELL 241
Cdd:COG1196 159 AIIEEaaGISKYKER-------KEEAERKLEATEENLERLEDILGELERQLEPLERQAEkaeryrELKEELKElEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 242 AQLQASHATVERKDYLKTDLTTALKEIRAQLEcQSDHNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQS 321
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELA-ELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 322 KSIELESVRGTKESLERQLSDIEERHNND---LTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRK 398
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
....*...
gi 2099376549 399 LLEGEETR 406
Cdd:COG1196 387 ELLEALRA 394
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
628-720 |
2.19e-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: 45.55 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 628 ATPKVtSPEKPATPEKP--PTP-EKAITPEKVRSPEKPTTPEKVVSPEkPASPEKPRTPEKPASPEKPATPEKPRTPEKP 704
Cdd:smart00818 57 HIPVL-PAQQPVVPQQPlmPVPgQHSMTPTQHHQPNLPQPAQQPFQPQ-PLQPPQPQQPMQPQPPVHPIPPLPPQPPLPP 134
|
90
....*....|....*.
gi 2099376549 705 ATPEKPRSPEKPSSPL 720
Cdd:smart00818 135 MFPMQPLPPLLPDLPL 150
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
630-719 |
2.27e-05 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 46.60 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 630 PKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPttpEKVVSPEKPASPE-------KP--RTPEKPASPEKPATPeKPRT 700
Cdd:PRK10819 55 PADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKE---APVVIPKPEPKPKpkpkpkpKPvkKVEEQPKREVKPVEP-RPAS 130
|
90 100
....*....|....*....|..
gi 2099376549 701 PEKPATPEKP---RSPEKPSSP 719
Cdd:PRK10819 131 PFENTAPARPtssTATAAASKP 152
|
|
| PTZ00441 |
PTZ00441 |
sporozoite surface protein 2 (SSP2); Provisional |
633-733 |
2.59e-05 |
|
sporozoite surface protein 2 (SSP2); Provisional
Pssm-ID: 240420 [Multi-domain] Cd Length: 576 Bit Score: 47.65 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 633 TSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPAspEKPATPEKPRTpEKPATPEKPRS 712
Cdd:PTZ00441 353 EVPDESNVPPNPPNVPGGSNSEFSSDVENPPNPPNPDIPEQEPNIPEDSNKEVPE--DVPMEPEDDRD-NNFNEPKKPEN 429
|
90 100
....*....|....*....|....*..
gi 2099376549 713 -----PEKPS-SPLKDEKAVVEESITV 733
Cdd:PTZ00441 430 kgdgqNEPVIpKPLDNERDQSNKNKQV 456
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
580-719 |
3.29e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.01 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 580 PKSPPKSPVTEQAKAVQKAAAEVGKDQKAEKAAEKAAKEEKAASPEKPATPKVTSPEKPATPEK---------------- 643
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRprrraarptvgsltsl 2698
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099376549 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 2099376549 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKvvsPEKPASPEKPRTPEKPaSPEKPATPEKPRTPE 702
Cdd:pfam13254 245 STDKEQSPAPTSASEPPPKTKELPKDSEEPAAPSKSAEASTEKKE---PDTESSPETSSEKSAP-SLLSPVSKASIDKPL 320
|
90 100
....*....|....*....|...
gi 2099376549 703 KPATPEKPRSPEKPSSPLKDEKA 725
Cdd:pfam13254 321 SSPDRDPLSPKPKPQSPPKDFRA 343
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
112-346 |
3.42e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 112 EKVHYLEQQNKEIEAELAALRqkhaGRAQLGDA-----------YEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRL 180
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLL----AEAGLDDAdaeavearreeLEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 181 RERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFL---RGNHEEEVAELLAQLQASHATVerkdyl 257
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDApvdLGNAEDFLEELREERDELRERE------ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 258 kTDLTTALKEIRAQLEcqsdhnmhQAEEWF---KC-------RYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELE 327
Cdd:PRK02224 429 -AELEATLRTARERVE--------EAEALLeagKCpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
250
....*....|....*....
gi 2099376549 328 SVRGTKEsLERQLSDIEER 346
Cdd:PRK02224 500 RAEDLVE-AEDRIERLEER 517
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
98-366 |
5.56e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 98 EQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDA--------------YEQELRELRGALEQVSHEK 163
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAEL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 164 AQIQLDSEHIEEDI-------------QRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLR 230
Cdd:PRK02224 485 EDLEEEVEEVEERLeraedlveaedriERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 231 GNHE---EEVAELLAQLQASHATVERKDYLKT------DLTTALKEIRAQLECQSDHNMHQAEEWFKCRYAKLTEAAEQN 301
Cdd:PRK02224 565 EEAEearEEVAELNSKLAELKERIESLERIRTllaaiaDAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 302 KEAIRSAKE-----------------EIAEYRRQLQSK------SIE-LESVRGTKESLERQLSDIEERHNNdLTTYQDT 357
Cdd:PRK02224 645 EARIEEAREdkeraeeyleqveekldELREERDDLQAEigavenELEeLEELRERREALENRVEALEALYDE-AEELESM 723
|
....*....
gi 2099376549 358 IHQLENELR 366
Cdd:PRK02224 724 YGDLRAELR 732
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
627-723 |
5.70e-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: 46.69 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 627 PATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRtPEKPaSPEKPATPEKPRTPEKPaT 706
Cdd:NF033839 281 QDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQ-PEKP-KPEVKPQLETPKPEVKP-Q 357
|
90 100
....*....|....*....|..
gi 2099376549 707 PEKPR-----SPEKPSSPLKDE 723
Cdd:NF033839 358 PEKPKpevkpQPEKPKPEVKPQ 379
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
625-713 |
6.58e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 625 EKPATPKVTSPEKPATPEKPP-TPEKAI-TPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPE 702
Cdd:PHA03247 2541 EELASDDAGDPPPPLPPAAPPaAPDRSVpPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPD 2620
|
90
....*....|.
gi 2099376549 703 KPATPEKPRSP 713
Cdd:PHA03247 2621 THAPDPPPPSP 2631
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-364 |
7.40e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 123 EIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALR 202
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 203 KEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAELLAQLQASHATVErkdylktdlttaLKEIRAQLECQSDHNMHQ 282
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE------------EELEEEALEEQLEAEREE 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 283 AEEWFKCRYAKLTEAAEQNKEA---IRSAKEEIAEYRRQLQS------KSI-ELESVRGTKESLERQLSDIEERhnndLT 352
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEppdLEELERELERLEREIEAlgpvnlLAIeEYEELEERYDFLSEQREDLEEA----RE 812
|
250
....*....|..
gi 2099376549 353 TYQDTIHQLENE 364
Cdd:COG1196 813 TLEEAIEEIDRE 824
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
623-720 |
7.41e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTSPEKPATPEKPPTPEKAIT----PEKVRSPEkPTTPEKVVSPEKPASPEKPRTPEKPASPEKPatPEKP 698
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANepdpHPPPTVPP-PERPRDDPAPGRVSRPRRARRLGRAAQASSP--PQRP 2683
|
90 100 110
....*....|....*....|....*....|..
gi 2099376549 699 RTPEKPAT----------PEKPRSPEKPSSPL 720
Cdd:PHA03247 2684 RRRAARPTvgsltsladpPPPPPTPEPAPHAL 2715
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
624-730 |
8.53e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.32 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 624 PEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPT-----TPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKP 698
Cdd:PHA03307 71 PPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGpsspdPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAA 150
|
90 100 110
....*....|....*....|....*....|..
gi 2099376549 699 RTPEKPATPEKPRSPEKPSSPLKDEKAVVEES 730
Cdd:PHA03307 151 SPPAAGASPAAVASDAASSRQAALPLSSPEET 182
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
86-349 |
9.21e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 86 AAELKLSRSNEKEQLQGLNDrfagYIEKVHYLEQQNKEIEAELAALrQKHAGRAQL--GDAYEQELRELRGALEQVSHEK 163
Cdd:PRK04863 836 EAELRQLNRRRVELERALAD----HESQEQQQRSQLEQAKEGLSAL-NRLLPRLNLlaDETLADRVEEIREQLDEAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 164 AQIQldsEHieediQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAflRGNH---EEEV--- 237
Cdd:PRK04863 911 RFVQ---QH-----GNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQ--RRAHfsyEDAAeml 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 238 ---AELLAQLQASHatvERKDYLKTDLTTALKEIRAQLEcqsdhnmhQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEI-- 312
Cdd:PRK04863 981 aknSDLNEKLRQRL---EQAEQERTRAREQLRQAQAQLA--------QYNQ----VLASLKSSYDAKRQMLQELKQELqd 1045
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2099376549 313 --------AEYRRQLQSKSI--ELESVRGTKESLERQLSDIEERHNN 349
Cdd:PRK04863 1046 lgvpadsgAEERARARRDELhaRLSANRSRRNQLEKQLTFCEAEMDN 1092
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
624-723 |
1.04e-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: 45.92 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 624 PEKPATPKVTSPEKPAtPEKPPTPEKAiTPEKVRSPEKPTtPEKVVSPEKPaSPEKPRTPEKPaSPEKPATPEKPRTPEK 703
Cdd:NF033839 314 PETPKPEVKPQLEKPK-PEVKPQPEKP-KPEVKPQLETPK-PEVKPQPEKP-KPEVKPQPEKP-KPEVKPQPETPKPEVK 388
|
90 100
....*....|....*....|....*
gi 2099376549 704 PaTPEKPR-----SPEKPSSPLKDE 723
Cdd:NF033839 389 P-QPEKPKpevkpQPEKPKPEVKPQ 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
87-401 |
1.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 87 AELKLSRSNEKEQLQGLND--RFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKA 164
Cdd:COG4717 105 EELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 165 QIQLDSEH----IEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASlMRAELDKKVQSLQDEVAFLR---------- 230
Cdd:COG4717 185 QLSLATEEelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERLKEARLLLLiaaallallg 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 231 -----GNHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLECQSDHNMHQAEEWFKCRYAKLTEAAEQNKEAI 305
Cdd:COG4717 264 lggslLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 306 RSAKE------EIAEYRRQLQSKSIELESVR-------GTKESLERQLSDIEERHNNdLTTYQDTIHQLENELRGTKWEM 372
Cdd:COG4717 344 DRIEElqellrEAEELEEELQLEELEQEIAAllaeagvEDEEELRAALEQAEEYQEL-KEELEELEEQLEELLGELEELL 422
|
330 340 350
....*....|....*....|....*....|.
gi 2099376549 373 ARHLRE--YQDLLNVKMALDIEIAAYRKLLE 401
Cdd:COG4717 423 EALDEEelEEELEELEEELEELEEELEELRE 453
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
642-719 |
1.24e-04 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 45.46 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 642 EKPPTPEKAITPEKVRSPEKPTT--PEKVVSPEKpaSPEKPRTPEKPASPEK--PATPEKPRTPEKPATPEKPRSPEKPS 717
Cdd:PRK06347 54 ETAPADEASKSAEANTTKEAPATatPENTTEPTV--EPKQTETKEQTKTPEEkqPAAKQVEKAPAEPATVSNPDNATSSS 131
|
..
gi 2099376549 718 SP 719
Cdd:PRK06347 132 TP 133
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
638-739 |
1.33e-04 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 45.33 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 638 PATPEKPP--TPEKAITPEKVRSP-EKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPE--KPATPEKPRS 712
Cdd:PHA03291 188 PALPLSAPrlGPADVFVPATPRPTpRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPEAEGtpAPPTPGGGEA 267
|
90 100
....*....|....*....|....*..
gi 2099376549 713 PEKPSSPLKDEKavvEESITVTKVTKV 739
Cdd:PHA03291 268 PPANATPAPEAS---RYELTVTQIIQI 291
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
638-754 |
1.35e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 45.57 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 638 PATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPA--TPEKPRSPEK 715
Cdd:PRK14950 362 PVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPklTRAAIPVDEK 441
|
90 100 110
....*....|....*....|....*....|....*....
gi 2099376549 716 PSSPLKDEKAvvEESITVTKVTKVTAEVEVSKEARKEDI 754
Cdd:PRK14950 442 PKYTPPAPPK--EEEKALIADGDVLEQLEAIWKQILRDV 478
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
144-273 |
1.37e-04 |
|
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: 44.15 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 144 AYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALRKEME--EASLMRAELDKKVQS 221
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVRNNKEYEA 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2099376549 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, ... |
624-719 |
1.49e-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: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 624 PEKPATPKVTSPEKPaTPEKPPTPEKAiTPEKVRSPEKPTtPEKVVSPEKPASPEKPRtPEKPASPEKPaTPEKPRtPEK 703
Cdd:NF033839 347 LETPKPEVKPQPEKP-KPEVKPQPEKP-KPEVKPQPETPK-PEVKPQPEKPKPEVKPQ-PEKPKPEVKP-QPEKPK-PEV 420
|
90
....*....|....*.
gi 2099376549 704 PATPEKPRSPEKPSSP 719
Cdd:NF033839 421 KPQPEKPKPEVKPQPE 436
|
|
| 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 2099376549 626 KPATPKVTSPekPATPEKPPTPEKAITPEKVRspeKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPA 705
Cdd:PRK14951 404 AAAPAAAASA--PAAPPAAAPPAPVAAPAAAA---PAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPA 478
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2099376549 706 TPEKPRSPEKPSSPLKDE-KAVVEESITVTKVTKVTAEVEVSKEARKED 753
Cdd:PRK14951 479 PAAAPAAARLTPTEEGDVwHATVQQLAAAEAITALARELALQSELVARD 527
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
626-720 |
1.92e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 626 KPATPKVTSP------------EKPATPEKPPTPEKAITPEKV-RSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKP 692
Cdd:PHA03247 385 RRSARHAATPfargpggddqtrPAAPVPASVPTPAPTPVPASApPPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPD 464
|
90 100
....*....|....*....|....*...
gi 2099376549 693 ATPEKprTPEKPATPEKPRSPEKPSSPL 720
Cdd:PHA03247 465 DPDDA--TRKALDALRERRPPEPPGADL 490
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
623-740 |
2.30e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTSPEKPAT-----PEKPPTPEKAITPEKVR-----SPEKPTTPEKVVSPEKPASPEKP-RTPEKPASPEK 691
Cdd:PHA03247 2612 APPSPLPPDTHAPDPPPPspspaANEPDPHPPPTVPPPERprddpAPGRVSRPRRARRLGRAAQASSPpQRPRRRAARPT 2691
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2099376549 692 PAT-PEKPRTPEKPATPEKPRSPEKPSSPLKDEKAVVEESITVTKVTKVT 740
Cdd:PHA03247 2692 VGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP 2741
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
624-728 |
2.39e-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: 44.76 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 624 PEKPATPKVTSPEKPaTPEKPPTPEKAiTPEKVRSPEKPTtPEKVVSPEKPaSPEKPRTPEKPaSPEKPATPE--KPRTP 701
Cdd:NF033839 380 PETPKPEVKPQPEKP-KPEVKPQPEKP-KPEVKPQPEKPK-PEVKPQPEKP-KPEVKPQPEKP-KPEVKPQPEkpKPEVK 454
|
90 100
....*....|....*....|....*..
gi 2099376549 702 EKPATPeKPRSPEKPSSPLKDEKAVVE 728
Cdd:NF033839 455 PQPETP-KPEVKPQPEKPKPEVKPQPE 480
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-245 |
2.46e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 47 TVSSSYKRTNLGAPRTAYGSTVLSSAESLDVSQSSLLngAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEA 126
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEFLEEQLPELRKELE--EAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 127 ELAALRQKHAG-RAQLGDAYEQ--------ELRELRGALEQVSHEKAQIQ--LDSEH-----IEEDIQRLRERFEDEA-R 189
Cdd:COG3206 234 ELAEAEARLAAlRAQLGSGPDAlpellqspVIQQLRAQLAELEAELAELSarYTPNHpdviaLRAQIAALRAQLQQEAqR 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099376549 190 LRDETEATIRALRKEMEEASLMRAELDKKVQS----------LQDEVAFLRGNHEeevaELLAQLQ 245
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAElpeleaelrrLEREVEVARELYE----SLLQRLE 375
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
624-714 |
2.48e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 44.80 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 624 PEKPATPKVTSP----EKPATPEKPPTPEKAITPEKvrsPEKPTTPEKVVSPEKPASPekPRTPEKPASPekPATPEKPR 699
Cdd:PRK14950 365 APQPAKPTAAAPspvrPTPAPSTRPKAAAAANIPPK---EPVRETATPPPVPPRPVAP--PVPHTPESAP--KLTRAAIP 437
|
90
....*....|....*
gi 2099376549 700 TPEKPATPEKPRSPE 714
Cdd:PRK14950 438 VDEKPKYTPPAPPKE 452
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
193-406 |
2.52e-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: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 193 ETEATIRALRKEMEEasLMRAEldKKVQSLQDEVAFLrgnheEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQL 272
Cdd:COG4913 222 DTFEAADALVEHFDD--LERAH--EALEDAREQIELL-----EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 273 ------ECQSDHNMHQAE-EWFKCRYAKLTEAAEQNKEAIRSAK-EEIAEYRRQLQSKSIELESVRGTKESLERQLSDIE 344
Cdd:COG4913 293 leaeleELRAELARLEAElERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099376549 345 ERHNNDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 406
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
83-226 |
2.87e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 83 LNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKhagraqlgdayEQELRELRGALEQVSHE 162
Cdd:PRK04863 550 LDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR-----------APAWLAAQDALARLREQ 618
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099376549 163 KAQIQLDSEHIEEDIQRLRERfEDEARL-RDETEATIRALRKEMEEASLMRAELDKKVQSLQDEV 226
Cdd:PRK04863 619 SGEEFEDSQDVTEYMQQLLER-ERELTVeRDELAARKQALDEEIERLSQPGGSEDPRLNALAERF 682
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-521 |
2.98e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 72 AESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRE 151
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 152 LRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLrg 231
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL-- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 232 nhEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLECQSDHNMHQA---EEWFKCRYAKLTEAAEQNKEAIRSA 308
Cdd:COG1196 476 --EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavLIGVEAAYEAALEAALAAALQNIVV 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 309 KEEIAEYRRQLQSKSIELEsvRGTKESLERQLSDIEERHNNDLTTYQDTIHQLENELRGTkwEMARHLREYQDLLNVKMA 388
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAG--RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA--DARYYVLGDTLLGRTLVA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 389 LDIEIAAYRKLLEGEETRFSAFSGSITGPifthrQPSVTIASTKIQKTKIEppklkvqhkfVEEIIEETKVEDEKSEMED 468
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSA-----GGSLTGGSRRELLAALL----------EAEAELEELAERLAEEELE 694
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2099376549 469 ALSAIAEEMAAKAQEEEQEEEKAEEEAVEEEAVSEKAAEQAAEEEEKEEEEAE 521
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
120-347 |
3.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 120 QNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLdsEHIEEDIQRLRERF----EDEARLRDETE 195
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAgvedEEELRAALEQA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 196 ATIRALRKEMEEASLMRAELDKKVQSLqdevafLRGNHEEEVAELLAQLQASHATVERKdylKTDLTTALKEIRAQLEcq 275
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEEL------LEALDEEELEEELEELEEELEELEEE---LEELREELAELEAELE-- 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099376549 276 sdhnmhQAEEwfkcryaklteaaeqnKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERH 347
Cdd:COG4717 464 ------QLEE----------------DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| ISET-FN3_linker |
pfam16625 |
Unstructured linking region I-set and fnIII on Brother of CDO; ISET-FN3_linker is a short ... |
637-693 |
4.10e-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: 4.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2099376549 637 KPATPEKPPTPEKAITPEKVRSPEKPTTPEKVvsPEKPASPEKPRTPEKPASPEKPA 693
Cdd:pfam16625 2 RPGTTLRPWQDAKLATATPPAPPSRPSSPDQM--LRGKPGLPRPPTSVQPASPQCPG 56
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
626-719 |
4.30e-04 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 43.79 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 626 KPATPKV--TSPEKPATPEKPPTPEKaITPEKVRSPEKPTTPekvvspekPASPEKPRTPEKPASPEKPATPEKPRTPEK 703
Cdd:PHA03291 171 TLAAPPLgeGSADGSCDPALPLSAPR-LGPADVFVPATPRPT--------PRTTASPETTPTPSTTTSPPSTTIPAPSTT 241
|
90
....*....|....*.
gi 2099376549 704 PATPEKPRSPEKPSSP 719
Cdd:PHA03291 242 IAAPQAGTTPEAEGTP 257
|
|
| TALPID3 |
pfam15324 |
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ... |
627-746 |
4.30e-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: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 627 PATPKVTSPEKPATPeKPPTPEKAITPEKVRSPEKPTTPEkvvSPEKPASPEKPRTP----------------EKPASPE 690
Cdd:pfam15324 1047 PTVTPIATPPPAATP-TPPLSENSIDKLKSPSPELPKPWE---DSDLPLEEENPNSEqeelhpravvmsvardEEPESVV 1122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2099376549 691 KPATP--EKPRTPEkPATPEKPRSPEKPSSplkdEKAVVEESITVTKVTKVTAEVEVS 746
Cdd:pfam15324 1123 LPASPpePKPLAPP-PLGAAPPSPPQSPSS----SSSTLESSSSLTVTETETADRPIS 1175
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
632-719 |
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 2099376549 632 VTSPEKPATPEKPPTPEKAITPEK----VRSPEKPTTPEKvvSPEKPASPEKPRTPEKPASpeKPATPEKPRTPEKPATP 707
Cdd:PHA03247 368 LSAGRHHPKRASLPTRKRRSARHAatpfARGPGGDDQTRP--AAPVPASVPTPAPTPVPAS--APPPPATPLPSAEPGSD 443
|
90
....*....|..
gi 2099376549 708 EKPRSPEKPSSP 719
Cdd:PHA03247 444 DGPAPPPERQPP 455
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
146-365 |
4.95e-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: 43.69 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 146 EQELRELRGALEQVSHEKAQIQLDS-----EHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQ 220
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLELDEaeealEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 221 SLQ-------DEVAFLRGnHEEEVAELLAQLQASHATVERKDYLKTDLTTALKEIRAQLE-CQSDHnmhqaEEWFKcrya 292
Cdd:pfam06160 316 RVQqsytlneNELERVRG-LEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEeIEEEQ-----EEFKE---- 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099376549 293 KLTEAAEQNKEairsAKEEIAEYRRQLqsksielesvRGTKESLERQ-LSDIEERHNNDLTTYQDTIHQLENEL 365
Cdd:pfam06160 386 SLQSLRKDELE----AREKLDEFKLEL----------REIKRLVEKSnLPGLPESYLDYFFDVSDEIEDLADEL 445
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
626-721 |
4.96e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 626 KPATPKVTS----PEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKvVSPEKPASPEKPRtPEKPASPEKPATPEKPRTP 701
Cdd:PHA03247 2576 RPSEPAVTSrarrPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDT-HAPDPPPPSPSPA-ANEPDPHPPPTVPPPERPR 2653
|
90 100
....*....|....*....|....*...
gi 2099376549 702 EKPATP--------EKPRSPEKPSSPLK 721
Cdd:PHA03247 2654 DDPAPGrvsrprraRRLGRAAQASSPPQ 2681
|
|
| 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 2099376549 625 EKPATPkvtSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVS-----------PE-----------------KPAS 676
Cdd:PHA03308 756 ESPANP---WPRAPPCDEQEPLSVSPYGPEPDRPPDDDFETRKGLKrkssedhadpiPEgnatkktcglqglpdslPPAV 832
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2099376549 677 PEKPRtpEKPASPEKPATPEKPRTP--EKPATPEKPRSPEKPS 717
Cdd:PHA03308 833 PETDR--DNPLLPPCPITPEGPPCPprEEPQQPQEPQEPQSPS 873
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
623-728 |
5.96e-04 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 42.30 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTspekPATPEKPP--TPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRT 700
Cdd:PRK11633 50 RDEPDMMPAAT----QALPTQPPegAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKV 125
|
90 100
....*....|....*....|....*...
gi 2099376549 701 PEKPATPEKPRSPEKPSSPLKDEKAVVE 728
Cdd:PRK11633 126 EAPPAPKPEPKPVVEEKAAPTGKAYVVQ 153
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
117-213 |
6.39e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 117 LEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGAleQVSHEKAQIQLDSEhIEEDIQRLRERFEDEARLRD---- 192
Cdd:PRK11637 175 LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQA--RNERKKTLTGLESS-LQKDQQQLSELRANESRLRDsiar 251
|
90 100
....*....|....*....|..
gi 2099376549 193 -ETEATIRALRkEMEEASLMRA 213
Cdd:PRK11637 252 aEREAKARAER-EAREAARVRD 272
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
638-732 |
6.57e-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: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 638 PATPEKPPTPEKAITPEKVrsPEKPTTPEKVVSPEKPASPEKPRTPEKPASPE------KPATPEKPRTP---------- 701
Cdd:PLN03209 324 PSQRVPPKESDAADGPKPV--PTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYtayedlKPPTSPIPTPPssspassksv 401
|
90 100 110
....*....|....*....|....*....|....
gi 2099376549 702 ---EKPATPEKPRSPEKPSSPLKDEKAVVEESIT 732
Cdd:PLN03209 402 davAKPAEPDVVPSPGSASNVPEVEPAQVEAKKT 435
|
|
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
656-741 |
6.84e-04 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 43.14 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 656 VRSPEKPTTPEKVVSPEKPASPEKPRTpekpASPEKPATPEkpRTPEKPATPEKPRSPEKPSSPLKDEKAVVEESITVTK 735
Cdd:PRK06347 50 VSADETAPADEASKSAEANTTKEAPAT----ATPENTTEPT--VEPKQTETKEQTKTPEEKQPAAKQVEKAPAEPATVSN 123
|
....*.
gi 2099376549 736 VTKVTA 741
Cdd:PRK06347 124 PDNATS 129
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
156-366 |
8.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 156 LEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEAslmRAELDKKVQSLQDevaflrgnHEE 235
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---QAEIAEAEAEIEE--------RRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 236 EVAELLAQLQASHATVERKDYLK--TDLTTALKEIRAqLECQSDHNMHQAEEwfkcrYAKLTEAAEQNKEAIRSAKEEIA 313
Cdd:COG3883 87 ELGERARALYRSGGSVSYLDVLLgsESFSDFLDRLSA-LSKIADADADLLEE-----LKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2099376549 314 EYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLENELR 366
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| PHA03264 |
PHA03264 |
envelope glycoprotein D; Provisional |
625-712 |
9.19e-04 |
|
envelope glycoprotein D; Provisional
Pssm-ID: 223029 [Multi-domain] Cd Length: 416 Bit Score: 42.68 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 625 EKPATPKVTSPEKPATPEKPPTPEKAIT---PEKVRSPEKPTTPEKVVSPEKPASPEKPRtPEKPASPEK-----PATPE 696
Cdd:PHA03264 265 EPPPAPSGGSPAPPGDDRPEAKPEPGPVedgAPGRETGGEGEGPEPAGRDGAAGGEPKPG-PPRPAPDADrpegwPSLEA 343
|
90
....*....|....*.
gi 2099376549 697 KPRTPEKPATPEKPRS 712
Cdd:PHA03264 344 ITFPPPTPATPAVPRA 359
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-409 |
9.32e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 173 IEE--DIQRLRERfedearlRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVaflrgnheeEVAELLAQLQASHAT 250
Cdd:TIGR02168 161 FEEaaGISKYKER-------RKETERKLERTRENLDRLEDILNELERQLKSLERQA---------EKAERYKELKAELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 251 VErKDYLKTDLTTALKEIRAQL----ECQSDHNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 326
Cdd:TIGR02168 225 LE-LALLVLRLEELREELEELQeelkEAEEELEELTAEL------QELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 327 ESVRGTKESLERQLsdieERHNNDLTTYQDTIHQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 406
Cdd:TIGR02168 298 SRLEQQKQILRERL----ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
...
gi 2099376549 407 FSA 409
Cdd:TIGR02168 374 LEE 376
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
623-723 |
1.10e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPR-TPEKPASPEKPATPEKPRTP 701
Cdd:PRK07764 409 APAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPApAPAAAPEPTAAPAPAPPAAP 488
|
90 100
....*....|....*....|..
gi 2099376549 702 EKPATPEKPRSPEKPSSPLKDE 723
Cdd:PRK07764 489 APAAAPAAPAAPAAPAGADDAA 510
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
631-723 |
1.26e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 631 KVTSPEKPATPEKPPTPekaITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTP--------EKPASPEKPA-TPEKPRTP 701
Cdd:PTZ00449 704 KETLPETPGTPFTTPRP---LPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPeeertffhETPADTPLPDiLAEEFKEE 780
|
90 100
....*....|....*....|...
gi 2099376549 702 EKPATPEKPRSPEK-PSSPLKDE 723
Cdd:PTZ00449 781 DIHAETGEPDEAMKrPDSPSEHE 803
|
|
| 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 2099376549 624 PEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEK 703
Cdd:PRK06995 56 AAAPAAAQPPPAAAPAAVSRPAAPAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARA 135
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2099376549 704 PATPEKPRSPEKPSSPLKDEkavVEESITVTKVTKVTAEVEV 745
Cdd:PRK06995 136 AAAAPRPRVPADAAAAVADA---VKARIERIVNDTVMQELRS 174
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
100-229 |
1.36e-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: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 100 LQGLNDRFAGYIEKVHYLEQQNK--EIEAE-LAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIEED 176
Cdd:pfam06785 54 LYYWEDALKEKFEKSFLEEKEAKltELDAEgFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQD 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2099376549 177 IQRLR----ERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFL 229
Cdd:pfam06785 134 FAEFRleseEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-240 |
1.43e-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: 42.36 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 95 NEKEQLQGLNDRFagyIEKVHYLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHEKAQIQLDSEHIE 174
Cdd:TIGR02169 399 REINELKRELDRL---QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099376549 175 EDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAEL 240
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAI 541
|
|
| PRK12373 |
PRK12373 |
NADH-quinone oxidoreductase subunit E; |
626-708 |
1.46e-03 |
|
NADH-quinone oxidoreductase subunit E;
Pssm-ID: 237082 [Multi-domain] Cd Length: 400 Bit Score: 42.10 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 626 KPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRT--PEK 703
Cdd:PRK12373 239 APVPPSEAARPKSADAETNAALKTPATAPKAAAKNAKAPEAQPVSGTAAAEPAPKEAAKAAAAAAKPALEDKPRPlgIAR 318
|
....*
gi 2099376549 704 PATPE 708
Cdd:PRK12373 319 PGGAD 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 2099376549 628 ATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEK-----PRTPEKPASPEKPATPEKPRTPE 702
Cdd:PHA03307 51 AAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPARegsptPPGPSSPDPPPPTPPPASPPPSP 130
|
90 100
....*....|....*....|....*...
gi 2099376549 703 KPATPEKPRSPEKPSSPLKDEKAVVEES 730
Cdd:PHA03307 131 APDLSEMLRPVGSPGPPPAASPPAAGAS 158
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
177-373 |
1.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 177 IQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHE--EEVAELLAQLQASHATVERK 254
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKelEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 255 dylKTDLTTALKEIRAQLECQSDHNMHQAE--------EWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQ------ 320
Cdd:PRK03918 254 ---KRKLEEKIRELEERIEELKKEIEELEEkvkelkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgieeri 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2099376549 321 ----SKSIELESVRGTKESLERQLSDIEERHNndltTYQDtIHQLENELRGTKWEMA 373
Cdd:PRK03918 331 keleEKEERLEELKKKLKELEKRLEELEERHE----LYEE-AKAKKEELERLKKRLT 382
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
97-346 |
1.56e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 97 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHagraqlgDAYEQELRELRGALEQVSHEKAQIQLDS---EHI 173
Cdd:COG1340 42 AEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER-------DELNEKLNELREELDELRKELAELNKAGgsiDKL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 174 EEDIQRLRERFEDEA-RLRDETE--ATIRALRKEMEEAsLMRAELDKKVQSLQDEVAFLRG---NHEEEVAELLAQLQAS 247
Cdd:COG1340 115 RKEIERLEWRQQTEVlSPEEEKElvEKIKELEKELEKA-KKALEKNEKLKELRAELKELRKeaeEIHKKIKELAEEAQEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 248 HATVerkdylkTDLTTALKEIRAQLEcqsdhNMHQaeewfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELE 327
Cdd:COG1340 194 HEEM-------IELYKEADELRKEAD-----ELHK-------EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQR 254
|
250 260
....*....|....*....|.
gi 2099376549 328 SVRGTK--ESLERQLSDIEER 346
Cdd:COG1340 255 ALKREKekEELEEKAEEIFEK 275
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
623-723 |
1.66e-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: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPrtPEKPASPEKPATPE--KPRT 700
Cdd:NF040712 238 TPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPP--APAPAAPAAPAAPEaeEPAR 315
|
90 100
....*....|....*....|...
gi 2099376549 701 PEKPATPEKPRSPEKPSSPLKDE 723
Cdd:NF040712 316 PEPPPAPKPKRRRRRASVPSWDD 338
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
117-343 |
1.67e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 117 LEQQNKEIEAELAALRQKH-------------AGRAQLG-----DAYEQELRELRGALEQVSHEKAQIQLDSEHIEEDIQ 178
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQKHtqaleelteqleqAKRNKANlekakQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 179 RLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLrGNHEEEVAELL-----AQLQASHATVER 253
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL-ESQLQDTQELLqeetrQKLNLSTRLRQL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 254 KDYlKTDLTTALKE---IRAQLECQ-SDHNMHQAEewFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESV 329
Cdd:pfam01576 495 EDE-RNSLQEQLEEeeeAKRNVERQlSTLQAQLSD--MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
250
....*....|....
gi 2099376549 330 RGTKESLERQLSDI 343
Cdd:pfam01576 572 EKTKNRLQQELDDL 585
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
72-209 |
1.73e-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: 42.25 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 72 AESLDVSQSSLLNGAAELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKhagraqlgdayEQELRE 151
Cdd:COG3096 538 LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-----------APAWLA 606
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2099376549 152 LRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEAS 209
Cdd:COG3096 607 AQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
|
| PTZ00441 |
PTZ00441 |
sporozoite surface protein 2 (SSP2); Provisional |
635-735 |
1.79e-03 |
|
sporozoite surface protein 2 (SSP2); Provisional
Pssm-ID: 240420 [Multi-domain] Cd Length: 576 Bit Score: 41.87 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 635 PEKPATPEKPPTPEKAITP--EKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEKPATPEKPRS 712
Cdd:PTZ00441 323 PDNPQDPVPPPNEGKDGNPneENLFPPGDDEVPDESNVPPNPPNVPGGSNSEFSSDVENPPNPPNPDIPEQEPNIPEDSN 402
|
90 100
....*....|....*....|...
gi 2099376549 713 PEKPSSPLKDEKAVVEESITVTK 735
Cdd:PTZ00441 403 KEVPEDVPMEPEDDRDNNFNEPK 425
|
|
| PLN02217 |
PLN02217 |
probable pectinesterase/pectinesterase inhibitor |
658-746 |
1.89e-03 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215130 [Multi-domain] Cd Length: 670 Bit Score: 42.00 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 658 SPEKPTTPEKVVSPEkpASPEKPRTPEKPASPEKPATPE-KPRTPEKPATPEKPRSPEKPSSPLKDEKAVVEESITVTKV 736
Cdd:PLN02217 582 TTFSSDSPSTVVAPS--TSPPAGHLGSPPATPSKIVSPStSPPASHLGSPSTTPSSPESSIKVASTETASPESSIKVAST 659
|
90
....*....|
gi 2099376549 737 TKVTAEVEVS 746
Cdd:PLN02217 660 ESSVSMVSMS 669
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
212-402 |
2.05e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 212 RAELDKKVQSLQDevaflRGNHEEEVAELLAQLQASHATVERKDYLKTDLTtalkEIRAQLEcQSDHNMHQAEEwfkcRY 291
Cdd:PRK11281 38 EADVQAQLDALNK-----QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETE----QLKQQLA-QAPAKLRQAQA----EL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 292 AKLTEAAEQNKEAiRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIE---ERHNNDLTTYQDTIHQLENELRGT 368
Cdd:PRK11281 104 EALKDDNDEETRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQtqpERAQAALYANSQRLQQIRNLLKGG 182
|
170 180 190
....*....|....*....|....*....|....*
gi 2099376549 369 KWEMARHLREYQDLLNVKMA-LDIEIAAYRKLLEG 402
Cdd:PRK11281 183 KVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEG 217
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
624-703 |
2.19e-03 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 41.21 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 624 PEKPATPKVTSPEKPATPEKPPTPEKAITPekvrspeKPTTPEKVVSPEKPASPEKPRTPEKPASPEK---PATPEKPRT 700
Cdd:PTZ00144 129 PAAAAAAKAEKTTPEKPKAAAPTPEPPAAS-------KPTPPAAAKPPEPAPAAKPPPTPVARADPREtrvPMSRMRQRI 201
|
...
gi 2099376549 701 PEK 703
Cdd:PTZ00144 202 AER 204
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
146-344 |
2.58e-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: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 146 EQELRELRGALEQVSHEKAQIQLDSEHIEEDIQRLRERFEDEARLR-------DET-EATIRALRKEMEEASLMRAELD- 216
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLpqanllaDETlADRLEELREELDAAQEAQAFIQq 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 217 --KKVQSLQDEVAFLRGN--HEEEVAELLAQLQASHATVERKDYLKTDLTT-----ALKEIRAQLECQSDHNmhqaeEWF 287
Cdd:COG3096 915 hgKALAQLEPLVAVLQSDpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLGENSDLN-----EKL 989
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099376549 288 KCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSksieLESVRGTK----ESLERQLSDIE 344
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAQAQYSQYNQVLAS----LKSSRDAKqqtlQELEQELEELG 1046
|
|
| PRK11901 |
PRK11901 |
hypothetical protein; Reviewed |
662-721 |
2.79e-03 |
|
hypothetical protein; Reviewed
Pssm-ID: 237015 [Multi-domain] Cd Length: 327 Bit Score: 40.82 E-value: 2.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099376549 662 PTTPEKVVSPEK----PASPEKPRTPEKPASPEKPATPEK-PRTPEKPATPEKPRSPEKPSSPLK 721
Cdd:PRK11901 175 PTAPATVAPSKGakvpATAETHPTPPQKPATKKPAVNHHKtATVAVPPATSGKPKSGAASARALS 239
|
|
| Metal_resist |
pfam13801 |
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to ... |
125-205 |
2.96e-03 |
|
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: 38.43 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 125 EAELAALRQKHAGRAQLGDAYEQELRELRGALEQVShekAQIQLDSEHIEEDIQRLRERfedEARLRDETEATIRALRKE 204
Cdd:pfam13801 41 AEQRERLRAALRDHARELRALRRELRAARRELAALL---AAPPFDPAAIEAALAEARQA---RAALQAQIEEALLEFAAT 114
|
.
gi 2099376549 205 M 205
Cdd:pfam13801 115 L 115
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
627-725 |
3.16e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.37 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 627 PATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEkprTPEKPAT 706
Cdd:PRK07003 448 PVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS---REDAPAA 524
|
90
....*....|....*....
gi 2099376549 707 PEKPRSPEKPSSPLKDEKA 725
Cdd:PRK07003 525 AAPPAPEARPPTPAAAAPA 543
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
623-722 |
3.27e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTSPEKPATPEKPPTPEK------AITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPE 696
Cdd:PHA03307 99 SPAREGSPTPPGPSSPDPPPPTPPPASpppspaPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSS 178
|
90 100
....*....|....*....|....*.
gi 2099376549 697 KPRTPEKPATPEKPRSPEKPSSPLKD 722
Cdd:PHA03307 179 PEETARAPSSPPAEPPPSTPPAAASP 204
|
|
| 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 2099376549 623 SPEKPATPkvTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPekvvspeKPASPEKPRTPEKPASPekpaTPEKPR 699
Cdd:PHA03291 217 SPETTPTP--STTTSPPSTTIPAPSTTIAAPQAGTTPEAEGTP-------APPTPGGGEAPPANATP----APEASR 280
|
|
| PHA02030 |
PHA02030 |
hypothetical protein |
659-719 |
3.66e-03 |
|
hypothetical protein
Pssm-ID: 222843 [Multi-domain] Cd Length: 336 Bit Score: 40.35 E-value: 3.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099376549 659 PEKPTTPEKVVSPEKPASPEKPrTPEKPASPEKPATPEKPRTPEKP-----ATPEKPRSPEKPSSP 719
Cdd:PHA02030 267 PAVPNVAADAGSAAAPAVPAAA-AAVAQAAPSVPQVPNVAVLPDVPqvapvAAPAAPEVPAVPVVP 331
|
|
| PHA02030 |
PHA02030 |
hypothetical protein |
627-701 |
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 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099376549 627 PATPKVTSPEKPATPEKPPTPEKAITPE--KVRSPEKPTTPEKVVSPEKPASPEKPRTPEK--PASPEKPATPEKPRTP 701
Cdd:PHA02030 256 KPKSKAAGSNLPAVPNVAADAGSAAAPAvpAAAAAVAQAAPSVPQVPNVAVLPDVPQVAPVaaPAAPEVPAVPVVPAAP 334
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
670-736 |
3.80e-03 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 40.44 E-value: 3.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099376549 670 SPEKPASPE--KPRTPEKPASPEKPATPEKPRTPeKPATPEKPRSPEKPSSPLKDEKAVVEESITVTKV 736
Cdd:PTZ00144 125 PAAAPAAAAaaKAEKTTPEKPKAAAPTPEPPAAS-KPTPPAAAKPPEPAPAAKPPPTPVARADPRETRV 192
|
|
| 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 2099376549 625 EKPATPKVTSPE---KPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASP-EKPATPEKPRT 700
Cdd:pfam05539 222 QGTTTSSNPEPQtepPPSQRGPSGSPQHPPSTTSQDQSTTGDGQEHTQRRKTPPATSNRRSPHSTATPpPTTKRQETGRP 301
|
90 100
....*....|....*....|....
gi 2099376549 701 PEKPATPEKPRSPEKPSSPLKDEK 724
Cdd:pfam05539 302 TPRPTATTQSGSSPPHSSPPGVQA 325
|
|
| 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 2099376549 624 PEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPEKPRTPEK 703
Cdd:PRK07003 427 PAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAA 506
|
90
....*....|....*.
gi 2099376549 704 PATPEKPRSPEKPSSP 719
Cdd:PRK07003 507 VPDARAPAAASREDAP 522
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
623-712 |
4.88e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATPKVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEkPRTPEKPASPEKPATPEKPRTPE 702
Cdd:PRK07764 426 AAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPA-PAPPAAPAPAAAPAAPAAPAAPA 504
|
90
....*....|
gi 2099376549 703 KPATPEKPRS 712
Cdd:PRK07764 505 GADDAATLRE 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-404 |
5.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 88 ELKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKhAGRAQLGDAYEQELRELRGALEQVSHEKAQIQ 167
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 168 LDSEHIEEDIQRLRERFEDearlRDETEATIRALRKEMEEASLMRAELDKKVQSLQD---EVAFLRGNHEEEVAELLAQL 244
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRLTGLTPEKL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 245 QASHATVERKdylKTDLTTALKEI---RAQLECQSDHNMHQAEEWFKCRY------AKLTEaaEQNKEAIRSAKEEIAEY 315
Cdd:PRK03918 390 EKELEELEKA---KEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGkcpvcgRELTE--EHRKELLEEYTAELKRI 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 316 RRQLQSKSIELESVRGTKESLERQLSdiEERHNNDLTTYQDTIHQLENELRG-TKWEMARHLREYQDLLNVKMALDIEIA 394
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLK--KESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
330
....*....|
gi 2099376549 395 AYRKLLEGEE 404
Cdd:PRK03918 543 SLKKELEKLE 552
|
|
| 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 2099376549 648 EKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPATPE---KPRTPEKPATPEKPRSPEkPSSPLKDEK 724
Cdd:PRK14950 357 EALLVPVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVREtatPPPVPPRPVAPPVPHTPE-SAPKLTRAA 435
|
....*
gi 2099376549 725 AVVEE 729
Cdd:PRK14950 436 IPVDE 440
|
|
| PHA01929 |
PHA01929 |
putative scaffolding protein |
627-703 |
5.92e-03 |
|
putative scaffolding protein
Pssm-ID: 177328 Cd Length: 306 Bit Score: 39.65 E-value: 5.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099376549 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 |
6.33e-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: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 117 LEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVSHekaqiqLDSEHIEEDIQRLRERFeDEArlrDETEA 196
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANL------LADETLADRLEELREEL-DAA---QEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 197 TIRALRKEMEeaslmraELDKKVQSLQ---DEVAFLRGNHEEEVAELLAQLQASHA---TVERKDYL-----------KT 259
Cdd:COG3096 911 FIQQHGKALA-------QLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFAlseVVQRRPHFsyedavgllgeNS 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 260 DLTTALKE--IRAQLEC-QSDHNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL-----ESVRG 331
Cdd:COG3096 984 DLNEKLRArlEQAEEARrEAREQLRQAQA----QYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAdaeaeERARI 1059
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2099376549 332 TKESLERQLSDIEERHNNDLTTYQDTihqlENELRGTKWEMARHLREYQDL 382
Cdd:COG3096 1060 RRDELHEELSQNRSRRSQLEKQLTRC----EAEMDSLQKRLRKAERDYKQE 1106
|
|
| NESP55 |
pfam06390 |
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ... |
636-724 |
7.03e-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: 39.08 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 636 EKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKPRTPEKPASPEKPAT--PEKPRT---PEKPATPEKP 710
Cdd:pfam06390 135 EPETEPDTAPTTEPETEPEDEPGPVVPKGATFHQSLTERLHALKLQSADASPRRAPPSTqePESAREgeePERGPLDKDP 214
|
90
....*....|....
gi 2099376549 711 RSPEKPSSPLKDEK 724
Cdd:pfam06390 215 RDPEEEEEEKEEEK 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
212-407 |
7.21e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 212 RAELDKKVQSLQDEVAflrgnheeEVAELLAQLQASHATVERKDYlktdlttALKEIRAQLECQSDHNMHQAEEwfkcry 291
Cdd:COG4913 612 LAALEAELAELEEELA--------EAEERLEALEAELDALQERRE-------ALQRLAEYSWDEIDVASAEREI------ 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 292 akltEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNNDLTTYQDTIHQLENELRGTKWE 371
Cdd:COG4913 671 ----AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2099376549 372 MARHLREYQDLLN-------VKMALDIEIAAYRKLLEGEETRF 407
Cdd:COG4913 747 LRALLEERFAAALgdavereLRENLEERIDALRARLNRAEEEL 789
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
116-273 |
7.22e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 39.33 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 116 YLEQQNKEIEAELAALRQKHAGRAQLGDAYEQELRELRGALEQVshEKAQIQLDSehIEEDIQRLRERFEDEARLRdETE 195
Cdd:pfam00529 69 KAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAV--KAAQAQLAQ--AQIDLARRRVLAPIGGISR-ESL 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099376549 196 ATIRALRKEMEeaslmrAELDKKVQSLQDEVAFLRGNHEEEVAELLAQLQASHATVErkdylktDLTTALKEIRAQLE 273
Cdd:pfam00529 144 VTAGALVAQAQ------ANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIA-------EAEAELKLAKLDLE 208
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
170-272 |
7.43e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.93 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 170 SEHIEEDIQRLRERFEDEARLRDETEATIRALRKEMEEASLMRAELDKKVQSLQDEVAFLRGNHEEEVAELLAQL-QASH 248
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRkEITD 223
|
90 100
....*....|....*....|....
gi 2099376549 249 ATVERKDyLKTDLTTALkeIRAQL 272
Cdd:PRK11448 224 QAAKRLE-LSEEETRIL--IDQQL 244
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
623-721 |
8.88e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 39.77 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPATP-----KVTSPEKPATPEKPPTPEKAITPEKVRSPEKPTTPEKVVSPEKPASPEKP---RTPeKPASPEKPAT 694
Cdd:PHA03307 283 GPASSSSSprersPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPspsRSP-SPSRPPPPAD 361
|
90 100
....*....|....*....|....*..
gi 2099376549 695 PEKPRTPEKPATPEKPRSPEKPSSPLK 721
Cdd:PHA03307 362 PSSPRKRPRPSRAPSSPAASAGRPTRR 388
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
623-719 |
9.49e-03 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 39.07 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 623 SPEKPaTPKVTSPeKPATPE-KPPTPEKAIT---PEKVRSP-EKPTTPEKVV--SPEKPASPEKPRTPEKPASPEKPaTP 695
Cdd:PHA02682 80 SPLAP-SPACAAP-APACPAcAPAAPAPAVTcpaPAPACPPaTAPTCPPPAVcpAPARPAPACPPSTRQCPPAPPLP-TP 156
|
90 100
....*....|....*....|....
gi 2099376549 696 eKPRTPEKPATPEKPRSPekPSSP 719
Cdd:PHA02682 157 -KPAPAAKPIFLHNQLPP--PDYP 177
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
92-346 |
9.66e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 92 SRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAELAALRQKHagraqlgDAYEQELRELRGALEQVSHEKAQIQldse 171
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKR-------DELNAQVKELREEAQELREKRDELN---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 172 hieEDIQRLRERfedearlRDETEATIRALRKEMEEASLMRAELDKKVQSLQD------------EVAFLRGNHEEEVAE 239
Cdd:COG1340 71 ---EKVKELKEE-------RDELNEKLNELREELDELRKELAELNKAGGSIDKlrkeierlewrqQTEVLSPEEEKELVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099376549 240 LLAQLQASHATVERKDYLKTDLTTALKEIRAQLECQSDHNMHQAE-------------EWFKcRYAKLTEAAEQNKEAIR 306
Cdd:COG1340 141 KIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElaeeaqelheemiELYK-EADELRKEADELHKEIV 219
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2099376549 307 SAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEER 346
Cdd:COG1340 220 EAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE 259
|
|
| |
