|
Name |
Accession |
Description |
Interval |
E-value |
| Colicin |
pfam01024 |
Colicin pore forming domain; |
345-517 |
3.07e-12 |
|
Colicin pore forming domain;
Pssm-ID: 425995 Cd Length: 185 Bit Score: 65.22 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 345 IKDAVDATVSFYQTLTEKYGEKYSKMAQELADKSKGKKIGNVNEALAAFEKYKDVLNKKFSKADRDAIFNALASVKYDDW 424
Cdd:pfam01024 11 LQDAAKFPADFYAEETEKFDAAASAGAMFGAEGAREINIQKNAEAIKRFEFEKDAKEKKEILKDRQAIADAFDKLDKQGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 425 AKHLDQFAKYLKITGHVSFGYDVVSDILKIKDTGDWKPLFLTLEKKAADAGVSYVVALLFSLLAGTTLGIWGIAIVTGIL 504
Cdd:pfam01024 91 AEALEKERKDFGSAGKAIDAADLEGEFKIFTEGGDIDPEFQKIESIAAAAAAIWEKGIAEARAKAPFIGILGDALEMAVA 170
|
170
....*....|...
gi 2242546895 505 CSYIDKNKLNTIN 517
Cdd:pfam01024 171 GAKIDEDLEAKAN 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
87-341 |
1.33e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 87 RDALTQRLKDIVNEALRHNASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAE 166
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 167 TERQLKLAEAEEKRLAA-LSEEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASA 245
Cdd:COG1196 328 LEEELEELEEELEELEEeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 246 KYKELDELVKKLSPRANdplqnrpffEATRRRVGAGKIREEKQKQVTASETRINRINADITQIQKAISQVSNNRNAGIAR 325
Cdd:COG1196 408 AEEALLERLERLEEELE---------ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250
....*....|....*.
gi 2242546895 326 VHEAEENLKKAQNNLL 341
Cdd:COG1196 479 LAELLEELAEAAARLL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
124-348 |
9.26e-09 |
|
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: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 124 QAE-AERLRLAKAEEKaRKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAE--------EKRLAALSEEAKAVEIA 194
Cdd:COG1196 208 QAEkAERYRELKEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAElaeleaelEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 195 QKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRANDPLQNRpfFEAT 274
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL--AEAE 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2242546895 275 RRRVGAGKIREEKQKQVTASETRINRINADITQIQKAISQVSNNRNAGIARVHEAEENLKKAQNNLLNSQIKDA 348
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
126-341 |
1.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 126 EAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEkRLAALSEEAKAVEIAQKKLSAAQSEV 205
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAER-EIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 206 VKMDGEIKTLNSRlsssihaRDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRANDPLqnRPFFEATRRRVGA----G 281
Cdd:COG4913 695 EELEAELEELEEE-------LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGdaveR 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2242546895 282 KIREEKQKQVTASETRINRINADITQIQKAISQV----SNNRNAGIARVHEAEENLKKAQNNLL 341
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESLPEYLALLDRLEEDGL 829
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-313 |
1.41e-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: 54.29 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 88 DALTQRLKDIVNEALRHNASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAET 167
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 168 ERQLKLAEAEEKRL-AALSEEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAK 246
Cdd:TIGR02168 802 REALDELRAELTLLnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2242546895 247 YKELDELVKKLSPRANDplQNRPFFEATRRRVGAGKIREEKQKQVTASETRINRINADITQIQKAIS 313
Cdd:TIGR02168 882 RASLEEALALLRSELEE--LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-351 |
3.60e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 70 AARAKAAAEAQAKAKANRDALTQRLKDIVNEALRHNASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKA 149
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 150 FQEAEQRRK-EIEREKAETERQLKLAEAEEKRLAALSEEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDA 228
Cdd:COG1196 297 LARLEQDIArLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 229 EMKTLAGKRNELAQASAKYKELDELVKKLSPRANDplqnrpffeATRRRVGAGKIREEKQKQVTASETRINRINADITQI 308
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEA---------LLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2242546895 309 QKAISQVSNNRNAGIARVHEAEENLKKAQNNLLNSQIKDAVDA 351
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
131-246 |
4.87e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 52.64 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 131 RLAKAEEKARK-EAEAAEKAFQEAEQRRKEIEREKAetERQLKLAEAEEKRLAALSEEAKAVEIAQKKLSAAQSEVVKMD 209
Cdd:PRK05035 432 RQAKAEIRAIEqEKKKAEEAKARFEARQARLEREKA--AREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIK 509
|
90 100 110
....*....|....*....|....*....|....*..
gi 2242546895 210 GEIKTLNsrlSSSIHARDAEMKTLAGKRNELAQASAK 246
Cdd:PRK05035 510 AGARPDN---SAVIAAREARKAQARARQAEKQAAAAA 543
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
114-250 |
1.53e-06 |
|
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: 49.54 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 114 ELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAKavei 193
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR---- 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2242546895 194 AQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKEL 250
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
126-409 |
1.53e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 126 EAERLRLAKAEEKARKeAEAAEKA--------FQEAEQRRKEIEREKAETERQLKLA-EAEEKRLAalsEEAKAVEIAQK 196
Cdd:PTZ00121 1162 DARKAEEARKAEDAKK-AEAARKAeevrkaeeLRKAEDARKAEAARKAEEERKAEEArKAEDAKKA---EAVKKAEEAKK 1237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 197 KLSAA-QSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRANDPLQNRPffEATR 275
Cdd:PTZ00121 1238 DAEEAkKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA--EEAK 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 276 RRVGAGKIREEKQKQVTA----SETRINRINADITQIQKAISQVSNNRNAGIARVHEAEENLKKAQNNLLNSQIKDAVDA 351
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAakkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2242546895 352 tvsfyqtlTEKYGEKYSKMAQELADKSKGKKIGNVNEALAAFEKYKDVLNKKFSKADR 409
Cdd:PTZ00121 1396 --------AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
104-249 |
2.33e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 50.25 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 104 HNASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKlaEAEEKRLAA 183
Cdd:PRK12472 174 HPALFVPKAEALAAAPARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELK--RADKALAAA 251
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2242546895 184 LSEEAKA-VEIAQKKLSAAQSEVvkmdgeiktlNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKE 249
Cdd:PRK12472 252 KTDEAKArAEERQQKAAQQAAEA----------ATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAE 308
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
124-345 |
3.66e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 124 QAE-AERLRLAKAEEKArKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRL-AALSEEAKAVEIAQKKLSAA 201
Cdd:TIGR02168 208 QAEkAERYKELKAELRE-LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 202 QSEVVKMDGEIKTLNSR----------LSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRANDPLQNRP-- 269
Cdd:TIGR02168 287 QKELYALANEISRLEQQkqilrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEae 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2242546895 270 FFEATRRRVGAGKIREEKQKQVTASETRINRINADITQIQKAISQVSNNRNAGIARVHEAEENLKKAQNNLLNSQI 345
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
190-361 |
3.98e-06 |
|
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: 48.96 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 190 AVEIAQKKLSAAQSEVVKMDGEIKtlnsRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRAND--PLQN 267
Cdd:pfam00529 59 ALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrrVLAP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 268 RPFFEAtRRRVGAGKIREEKQKQVTASETRINRINADITQIQKA-ISQVSNNRNAGIARVHEAEENLKKAQNNLLNSQIK 346
Cdd:pfam00529 135 IGGISR-ESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAEnQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIR 213
|
170
....*....|....*
gi 2242546895 347 DAVDATVSFYQTLTE 361
Cdd:pfam00529 214 APVDGTVAFLSVTVD 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
134-337 |
5.06e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 134 KAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLaalsEEAKAVEIAQKKLSAAQSEVVKMDGEIK 213
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----EKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 214 TLNSRLsSSIHARDAEMKTLagkRNELAQASAkykELDELVKKLSPRANDPLQnrpffEATRRrvgagkiREEKQKQVTA 293
Cdd:COG4717 150 ELEERL-EELRELEEELEEL---EAELAELQE---ELEELLEQLSLATEEELQ-----DLAEE-------LEELQQRLAE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2242546895 294 SETRINRINADITQIQKAISQVSNNrnagiARVHEAEENLKKAQ 337
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENE-----LEAAALEERLKEAR 249
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
118-203 |
6.03e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 118 ANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAKAVEIAQKK 197
Cdd:PRK09510 156 AAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAK 235
|
....*.
gi 2242546895 198 LSAAQS 203
Cdd:PRK09510 236 AAAEKA 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
87-249 |
6.06e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 87 RDALTQRLKDIVNEALRHNASRTPSATEL----AHANNAAMQAEAERLRLAKAE-EKARKEAEAAEKAFQEAEQRRKEIE 161
Cdd:COG4913 633 LEALEAELDALQERREALQRLAEYSWDEIdvasAEREIAELEAELERLDASSDDlAALEEQLEELEAELEELEEELDELK 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 162 REKAETERQLKLAEAEEKRLAALSEEA-KAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEmktLAGKRNEL 240
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR---LNRAEEEL 789
|
....*....
gi 2242546895 241 AQASAKYKE 249
Cdd:COG4913 790 ERAMRAFNR 798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-337 |
1.18e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 121 AAMQAEAERLRLAKAE-EKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAKAVEiaqkKLS 199
Cdd:PRK03918 224 EKLEKEVKELEELKEEiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI----KLS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 200 AAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRA---NDPLQNRPFFEATRR 276
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKK 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2242546895 277 RVGaGKIREEKQKQVTASETRINRINADITQIQKAISQVSNNrnagIARVHEAEENLKKAQ 337
Cdd:PRK03918 380 RLT-GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE----IKELKKAIEELKKAK 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
124-314 |
1.21e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 124 QAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQlkLAEAEEKRLAALSEEAKAveiAQKKLSAAQS 203
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ--IRGNGGDRLEQLEREIER---LERELEERER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 204 EVVKMDGEIKTLNsrlsssiHARDAEMKTLAGKRNELAQASAKYKELDELVKKLsprandplqnrpFFEATRRRVGAGKI 283
Cdd:COG4913 360 RRARLEALLAALG-------LPLPASAEEFAALRAEAAALLEALEEELEALEEA------------LAEAEAALRDLRRE 420
|
170 180 190
....*....|....*....|....*....|.
gi 2242546895 284 REEKQKQVTASETRINRINADITQIQKAISQ 314
Cdd:COG4913 421 LRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
140-348 |
1.54e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 140 RKEAEAAEKAFQ-EAEQRRKEIE---REKAETERQLKLAEAEEKRLAALSEEAKA-VEIAQKKLSAAQSEVVKMDGEIKT 214
Cdd:COG1196 206 ERQAEKAERYRElKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAeLAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 215 LNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRANDPLQNRPffEATRRRVGAGKIREEKQKQVTAS 294
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2242546895 295 ETRINRINADITQIQKAISQVSNNRNAGIARVHEAEENLKKAQNNLLNSQIKDA 348
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
112-337 |
1.62e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 112 ATELAHANNAAMQAEAERlrlaKAEEKARK--EAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAK 189
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAK----KADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 190 AVEIAQKKLSAAQSEVVKMDG------EIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKyKELDELVKKLSPRAND 263
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADelkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKM 1607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2242546895 264 PLQNRPFFEATRRRVGAGKIREEKQKQVTASETRINRINADITQIQKAiSQVSNNRNAGIARvhEAEENLKKAQ 337
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAK--KAEEDKKKAE 1678
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
106-331 |
1.80e-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: 47.07 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 106 ASRTPSATELAHANNAAMQAEAERLRLAKAE-EKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAAL 184
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKElAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 185 SEEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSS---IHARDAE-MKTLAGKRNELAQA-SAKYKELDELVKKLSP 259
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdflDAVRRLQyLKYLAPARREQAEElRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2242546895 260 RANDPLQNRPFFEATRRRVgaGKIREEKQKQVTASETRINRINADITQIQKAISQVSNNRNAGIARVHEAEE 331
Cdd:COG4942 172 ERAELEALLAELEEERAAL--EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
119-409 |
1.84e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 119 NNAAMQAEAERLRL----AKAEEKARKEAEAAEKAfqEAEQRRKEIEREKAETERQLKLAEAEEK------RLAALSEEA 188
Cdd:pfam02463 145 EIIAMMKPERRLEIeeeaAGSRLKRKKKEALKKLI--EETENLAELIIDLEELKLQELKLKEQAKkaleyyQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 189 KAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRANdplqnr 268
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE------ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 269 pffEATRRRVGAGKIREEKQKQVTASETRINRINADITQIQKAISQVSN-NRNAGIARVHEAEENLKKAQNNLLNSQIKD 347
Cdd:pfam02463 297 ---ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKeLKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2242546895 348 AVDATvsfYQTLTEKYGEKYSKMAQELADKSKGKKIgnVNEALAAFEKYKDVLNKKFSKADR 409
Cdd:pfam02463 374 ELLAK---KKLESERLSSAAKLKEEELELKSEEEKE--AQLLLELARQLEDLLKEEKKEELE 430
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
123-246 |
1.98e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 123 MQAEAERL-----RLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAeterqlKLAEAEEKRLAALSEEakaveiAQKK 197
Cdd:PRK00409 511 IGEDKEKLneliaSLEELERELEQKAEEAEALLKEAEKLKEELEEKKE------KLQEEEDKLLEEAEKE------AQQA 578
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2242546895 198 LSAAQSEVVKMDGEIKTLNSRLSSSIHARDA-EMKTLAGKRNELAQASAK 246
Cdd:PRK00409 579 IKEAKKEADEIIKELRQLQKGGYASVKAHELiEARKRLNKANEKKEKKKK 628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
124-346 |
1.98e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 124 QAEAERlRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAE----TERQLKLAEAEEKRLAALSEEAKAVEIAQKKLS 199
Cdd:TIGR02169 310 IAEKER-ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 200 AAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRANdplqnrpffEATRRRVG 279
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK---------KQEWKLEQ 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2242546895 280 AGKIREEKQKQVTASETRINRINADITQIQKAISQVSNNRNAGIARVHEAeenlkKAQNNLLNSQIK 346
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG-----RAVEEVLKASIQ 521
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
124-202 |
2.29e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.87 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 124 QAEAER---LRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQ------LKLAEaEEKRLAALSEEAKaVEIA 194
Cdd:pfam15709 403 QEEEERkqrLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQrqkeleMQLAE-EQKRLMEMAEEER-LEYQ 480
|
....*...
gi 2242546895 195 QKKLSAAQ 202
Cdd:pfam15709 481 RQKQEAEE 488
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
121-205 |
2.43e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 121 AAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAKAVEIAQKKLSA 200
Cdd:PRK09510 175 AAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
....*
gi 2242546895 201 AQSEV 205
Cdd:PRK09510 255 AAAEV 259
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
87-257 |
3.78e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 87 RDALTQRLKDIVNEALRHNASRTPSATELAHAN---NAAMQAeaerLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIERE 163
Cdd:PRK04863 302 LAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlNLVQTA----LRQQEKIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 164 KAETERQLKLAEAEEKRLAA-LSEEAKAVEIAQKKLSAAQSEVVKMDgEIKTLN-------SRLSSSIHARDAEMKTLAG 235
Cdd:PRK04863 378 QEENEARAEAAEEEVDELKSqLADYQQALDVQQTRAIQYQQAVQALE-RAKQLCglpdltaDNAEDWLEEFQAKEQEATE 456
|
170 180
....*....|....*....|....*....
gi 2242546895 236 KRNELAQ-------ASAKYKELDELVKKL 257
Cdd:PRK04863 457 ELLSLEQklsvaqaAHSQFEQAYQLVRKI 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-219 |
7.04e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 106 ASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALS 185
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
90 100 110
....*....|....*....|....*....|....
gi 2242546895 186 EEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSRL 219
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
112-433 |
7.76e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 112 ATELAHANNAAMQAEAERlrlAKAEEKARKEAEA--AEKAFQEAEQRRKEIE-REKAETERQLKLAE--AEEKR----LA 182
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDK---KKADELKKAAAAKkkADEAKKKAEEKKKADEaKKKAEEAKKADEAKkkAEEAKkaeeAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 183 ALSEEAKAVEIAQKKLSAAQ--SEVVKMDGEIKTLNSRLSSSIHAR---DAEMKTLAGKRNELAQASAKYKELDELVKKL 257
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 258 SPRANDPLQN-RPFFEATRRRVGAGKIREEKQKQVTASETRINRiNADITQIQKAISQVSNNRNAGIARVHEAEENLKKA 336
Cdd:PTZ00121 1544 EKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 337 QnnllnsQIKDAVDATVSFYQTLTEKYGEKysKMAQELADKSKGKKIGNVNEALAAFEKYKDVlnKKFSKADRDAIFNAL 416
Cdd:PTZ00121 1623 E------ELKKAEEEKKKVEQLKKKEAEEK--KKAEELKKAEEENKIKAAEEAKKAEEDKKKA--EEAKKAEEDEKKAAE 1692
|
330
....*....|....*..
gi 2242546895 417 ASVKYDDWAKHLDQFAK 433
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKK 1709
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
143-319 |
7.86e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 143 AEAAEKAFQEAEQRRKEIEREKAETERQLKLAEA------EEKRLAALSEEAKAV----EIAQKKLSAAQSEVVKMDGEI 212
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefrQKNGLVDLSEEAKLLlqqlSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 213 KTLNSRLSSSIHARDAEMK--TLAGKRNELAQASAKYKELDELVKKLSPRANDpLQNRpfFEATRRRVG--AGKIREEKQ 288
Cdd:COG3206 243 AALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIA-LRAQ--IAALRAQLQqeAQRILASLE 319
|
170 180 190
....*....|....*....|....*....|.
gi 2242546895 289 KQVTASETRINRINADITQIQKAISQVSNNR 319
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELE 350
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
63-337 |
1.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 63 KKTQAEQAARAKAAAEAQAKAKANRDALTQRLKDIVNEALRHNASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKE 142
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 143 AEAAEKafqEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAKAveiAQKKLSAAQSEVVKMDGEIKTLNSRLSSS 222
Cdd:PTZ00121 1317 ADEAKK---KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA---AEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 223 IHARDAEMKTLAGKR--NELAQASAKYKELDELVKKLSP-RANDPLQNRPffEATRRRVGAGKIREEKQKQVTASETRIN 299
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKkaDELKKAAAAKKKADEAKKKAEEkKKADEAKKKA--EEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
250 260 270
....*....|....*....|....*....|....*...
gi 2242546895 300 RINADitqiqKAISQVSNNRNAGIARvHEAEENLKKAQ 337
Cdd:PTZ00121 1469 AKKAD-----EAKKKAEEAKKADEAK-KKAEEAKKKAD 1500
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
96-343 |
1.15e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 96 DIVNEALRHNASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRrKEIEREKAETERQLKLAE 175
Cdd:COG5185 264 DLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAE-QELEESKRETETGIQNLT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 176 AEEKRLAALSEEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAK-YKELDELV 254
Cdd:COG5185 343 AEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtLKAADRQI 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 255 KKL-------------SPRANDPLQNRPFFEATRRRVGAGKIREEKQKQVTAS-ETRINRINADITQIQKAISQVSNNRN 320
Cdd:COG5185 423 EELqrqieqatssneeVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSvRSKKEDLNEELTQIESRVSTLKATLE 502
|
250 260
....*....|....*....|...
gi 2242546895 321 AGIARVHEAEENLKKAQNNLLNS 343
Cdd:COG5185 503 KLRAKLERQLEGVRSKLDQVAES 525
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
113-409 |
1.31e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 113 TELAHANNAAMQAEAERLRLA---KAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETE-----RQLKLAE---AEEKRL 181
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQMAekdKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEkeindRRLELQEfkiLKDKKD 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 182 AALSE-EAKA--VEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAG-----KRNELAQASAKYKELDEL 253
Cdd:pfam15921 618 AKIRElEARVsdLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyevlKRNFRNKSEEMETTTNKL 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 254 VKKLSPRANDPLQNRPFFEATRRRVG-AGKIREEKQKQVTASETRINRINADITQIQKAISQVSNnrnagiarvheaEEN 332
Cdd:pfam15921 698 KMQLKSAQSELEQTRNTLKSMEGSDGhAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANK------------EKH 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 333 LKKAQNNLLNSQIkdavdATVSfyqtlTEKygekySKMAQEL-----ADKSKGKKIGNVNEAL----AAFEKYKDVLNKK 403
Cdd:pfam15921 766 FLKEEKNKLSQEL-----STVA-----TEK-----NKMAGELevlrsQERRLKEKVANMEVALdkasLQFAECQDIIQRQ 830
|
....*.
gi 2242546895 404 FSKADR 409
Cdd:pfam15921 831 EQESVR 836
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
92-266 |
1.61e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 92 QRLKDIVNEALRHNASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQL 171
Cdd:PRK09510 114 QEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 172 KLAEAEEKRLAALSEEAKAVEIAQKKLSAAQSEVVKMDGEIKtlnsrlsssihaRDAEmKTLAGKRNELAQASAKYKELD 251
Cdd:PRK09510 194 KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAK------------AAAE-KAAAAKAAEKAAAAKAAAEVD 260
|
170
....*....|....*
gi 2242546895 252 ELVKKLSPRANDPLQ 266
Cdd:PRK09510 261 DLFGGLDSGKNAPKT 275
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
114-242 |
1.83e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 114 ELAHANNAAMQAEAERLRLAKAE-EKARKEAEAAEKAFQEAeqrrKEIEREKAETERQLKLAEAEEKRLAALSEEAKAVE 192
Cdd:PRK09039 82 SVANLRASLSAAEAERSRLQALLaELAGAGAAAEGRAGELA----QELDSEKQVSARALAQVELLNQQIAALRRQLAALE 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2242546895 193 IAqkkLSAAQSEVVKMDGEIKTLNSRLSSSihardaemktLAGKRNELAQ 242
Cdd:PRK09039 158 AA---LDASEKRDRESQAKIADLGRRLNVA----------LAQRVQELNR 194
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-320 |
2.13e-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: 44.28 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 92 QRLKDIVNEALRHNASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIErEKAETERQl 171
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE-EQLETLRS- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 172 KLAEAEEKRLAALSEeakaVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSsiHARDAEMKTLAGKRNELAQASAKYKELD 251
Cdd:TIGR02168 387 KVAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLE 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2242546895 252 ELVKKLSPRandplqnrpFFEATRRRVGAGKIREEKQKQVTASETRINRINaditQIQKAISQVSNNRN 320
Cdd:TIGR02168 461 EALEELREE---------LEEAEQALDAAERELAQLQARLDSLERLQENLE----GFSEGVKALLKNQS 516
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
137-347 |
4.25e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 137 EKARKEAEAAEKaFQEAEQRRKEIEREKA--ETERQLKLAEAEEKRLAALSEEAKAVeiaqkklsaAQSEVVKMDGEIKT 214
Cdd:pfam17380 281 QKAVSERQQQEK-FEKMEQERLRQEKEEKarEVERRRKLEEAEKARQAEMDRQAAIY---------AEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 215 LNSRLSSsihaRDAEMKTLagKRNELAQASAKYKELDELVKKlspRANDPLQNRPFFEATRRRvgagKIRE-EKQKQVTA 293
Cdd:pfam17380 351 ERIRQEE----RKRELERI--RQEEIAMEISRMRELERLQME---RQQKNERVRQELEAARKV----KILEeERQRKIQQ 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2242546895 294 SETRINRINADITQI-QKAISQVSNNRNAGIARVHEaEENLKKAQNNLLNSQIKD 347
Cdd:pfam17380 418 QKVEMEQIRAEQEEArQREVRRLEEERAREMERVRL-EEQERQQQVERLRQQEEE 471
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
99-335 |
5.18e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 99 NEALRHNASRTPSATELAHANNAamQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEE 178
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQA--AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 179 KRLA-----ALSEEAKAVEIAQKKLSAAQSE----------------VVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKR 237
Cdd:pfam12128 677 KDSAnerlnSLEAQLKQLDKKHQAWLEEQKEqkreartekqaywqvvEGALDAQLALLKAAIAARRSGAKAELKALETWY 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 238 -NELA------QASAKYK-ELDELVKKLSPRANDPLQNRPFFEATRRRVGAGKIReeKQKQVTASETRINRINADITQIQ 309
Cdd:pfam12128 757 kRDLAslgvdpDVIAKLKrEIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPR--LATQLSNIERAISELQQQLARLI 834
|
250 260 270
....*....|....*....|....*....|
gi 2242546895 310 KA----ISQVSNNRNAGIARVHEAEENLKK 335
Cdd:pfam12128 835 ADtklrRAKLEMERKASEKQQVRLSENLRG 864
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
114-250 |
6.02e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 114 ELAHANNAAMQAEAERL--RLAkaeEKARKEAEA-AEKAFQEAEQRRKEIERE-------------KAETERQLKLAEAE 177
Cdd:COG3524 150 EDAQAIAEALLAESEELvnQLS---ERAREDAVRfAEEEVERAEERLRDAREAllafrnrngildpEATAEALLQLIATL 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2242546895 178 EKRLAALSEEAKAveiAQKKLSAAQSEVVKMDGEIKTLNSRlsssIHARDAEMkTLAGKRNELAQASAKYKEL 250
Cdd:COG3524 227 EGQLAELEAELAA---LRSYLSPNSPQVRQLRRRIAALEKQ----IAAERARL-TGASGGDSLASLLAEYERL 291
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
123-262 |
6.65e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.37 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 123 MQAEAERLRLaKAEEKARKEAEAAEKAFQEAEQRRKEIERE-KAETERQLKLAEAEEKRLAALSEEA----------KAV 191
Cdd:pfam05622 287 LQHENKMLRL-GQEGSYRERLTELQQLLEDANRRKNELETQnRLANQRILELQQQVEELQKALQEQGskaedssllkQKL 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2242546895 192 EIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKT-LAGKRNELAQASAKYKELDE----LVKKLSPRAN 262
Cdd:pfam05622 366 EEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEaLRKKDEDMKAMEERYKKYVEkaksVIKTLDPKQN 441
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
126-411 |
6.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 126 EAERLRLAKAEEkARKEAEA---AEKAFQEAEQRRKEIERE-----KAETERQLKLA-EAEEKRLAalsEEAKAVEIAQK 196
Cdd:PTZ00121 1102 EAKKTETGKAEE-ARKAEEAkkkAEDARKAEEARKAEDARKaeearKAEDAKRVEIArKAEDARKA---EEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 197 KLSAAQSEVVKMDGEI-KTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDElVKKLSPRANDPLQNRPFFEATR 275
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEE-AKKDAEEAKKAEEERNNEEIRK 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 276 RRVGAGKIREEKQKQVTASETRinriNADitQIQKAISQVSNNRNAGIARVHEAEENLKKAQNNLLNSQIKDAVDATVSF 355
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEAR----KAD--ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2242546895 356 YQTLTEKYGEKYSKM-AQELADKSKGKKIGNVNEALAAFEKYKDVLNKKFSKADRDA 411
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
126-410 |
6.74e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 126 EAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLA-EAEEKRLAalsEEAKAVEIAQKKLSAAQSE 204
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArKAEEARKA---EDAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 205 VVKMDGEIKTLNSRlSSSIHARDAE--MKTLAGKRNELAQASAKYKELDELVKklsprandplqnrpfFEATRRRVGAGK 282
Cdd:PTZ00121 1168 EARKAEDAKKAEAA-RKAEEVRKAEelRKAEDARKAEAARKAEEERKAEEARK---------------AEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 283 IREEKQKQVTASETRINRINADITQIQKAISQVSNNRNAGI-ARVHEAEENLKKAQNNLLNSQIKDAVDatVSFYQTLTE 361
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkAEEARKADELKKAEEKKKADEAKKAEE--KKKADEAKK 1309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2242546895 362 KYGEKysKMAQELADKS-KGKKIGNVNEALAAFEKYKDVLNKKFSKADRD 410
Cdd:PTZ00121 1310 KAEEA--KKADEAKKKAeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
86-212 |
7.17e-04 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 41.75 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 86 NRDALTQRLKDIVNEALR-----------HNAsrTPSAtELAHANNAAMQAEAERLRlakAEEKARKEAEAAE-KAFQEA 153
Cdd:COG0330 132 GRDEINAEIREELQEALDpygievvdveiKDI--DPPE-EVQDAMEDRMKAEREREA---AILEAEGYREAAIiRAEGEA 205
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 154 EQRrkeIEREKAETERQLKLAEAEEKRLAALSEEAKAVE-IAQKKLSAAQSEVVKMDGEI 212
Cdd:COG0330 206 QRA---IIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPfVLFYRSLEALEEVLSPNSKV 262
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
126-320 |
8.76e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 126 EAERLRLAKAE--EKARKEAEAAEKAFQEAEQRRKEIEREKAETER-QLKLAEAEEKRLAALSEEakaveiAQKKLSAAQ 202
Cdd:pfam17380 379 ELERLQMERQQknERVRQELEAARKVKILEEERQRKIQQQKVEMEQiRAEQEEARQREVRRLEEE------RAREMERVR 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 203 SEVVKMDGEIKTLNSrlsssihaRDAEMKTlagKRNELAQASAKYKELDELVKKLSPRANDPlQNRPFFEATRRRVGAGK 282
Cdd:pfam17380 453 LEEQERQQQVERLRQ--------QEEERKR---KKLELEKEKRDRKRAEEQRRKILEKELEE-RKQAMIEEERKRKLLEK 520
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2242546895 283 --------IREEKQKQVTASETRINRINADITQIQKAISQVSNNRN 320
Cdd:pfam17380 521 emeerqkaIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
88-185 |
1.01e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 39.61 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 88 DALTQRLKDIVNE------ALRHNASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIE 161
Cdd:TIGR02473 30 ERLETQLQQLIKYreeyeqQALEKVGAGTSALELSNYQRFIRQLDQRIQQQQQELALLQQEVEAKRERLLEARRELKALE 109
|
90 100
....*....|....*....|....*.
gi 2242546895 162 --REKAETERQLKLAEAEEKRLAALS 185
Cdd:TIGR02473 110 klKEKKQKEYRAEEAKREQKEMDELA 135
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
124-188 |
1.08e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.64 E-value: 1.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2242546895 124 QAEAERLRLakaEEKARKEAEaaEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEA 188
Cdd:pfam05672 37 KEEEERLRK---EELRRRAEE--ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQ 96
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
101-188 |
1.11e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 40.93 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 101 ALRHNASRTPSATELAHANNAAMQAEA-ERLRLAKAEEKARKEAEAAekafQEAEQRRKEIEREKAETERQLKLAEAEEK 179
Cdd:PRK06991 179 ARAAASAAAAAAEASAAAAPAADDAEAkKRAIIAAALERARKKKEEL----AAQGAGPKNTEGVSAAVQAQIDAAEARRK 254
|
....*....
gi 2242546895 180 RLAALSEEA 188
Cdd:PRK06991 255 RLAEQRDAP 263
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
126-319 |
1.15e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 126 EAERLRLAKaEEKAR-----KEAEAAEKAFQEAEQRRKEI----EREKAETERQLKLAEAEEKR--LAALSEEAKAVEIA 194
Cdd:pfam17380 297 EQERLRQEK-EEKAReverrRKLEEAEKARQAEMDRQAAIyaeqERMAMERERELERIRQEERKreLERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 195 Q-KKLSAAQ------SEVVKMDGE----IKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKElDELVKKLSPRAND 263
Cdd:pfam17380 376 RmRELERLQmerqqkNERVRQELEaarkVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE-EERAREMERVRLE 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2242546895 264 PLQNRPFFEATR-----RRVGAGKIREEKQKQVTASETRINRINADITQIQKAISQVSNNR 319
Cdd:pfam17380 455 EQERQQQVERLRqqeeeRKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR 515
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
141-469 |
1.34e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 141 KEAEAAEKAF----QEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAKAVEIAQKKLSAAQSEVVKMDGEIKTLN 216
Cdd:TIGR01612 1551 KEIKDAHKKFileaEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 217 SRLSS-SIHARDAEMKTLAGKRNELAQ-----------ASAKYKELDELVKKLSPRANDPLQNRPFFEatrrrVGagkIR 284
Cdd:TIGR01612 1631 KKISSfSIDSQDTELKENGDNLNSLQEfleslkdqkknIEDKKKELDELDSEIEKIEIDVDQHKKNYE-----IG---II 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 285 EEKQKQVTASETRINRINADI-TQIQKAISQVSNNRNAGIarvhEAEENLKKaqnnlLNSQIKDAVDATVSFYQTLTeKY 363
Cdd:TIGR01612 1703 EKIKEIAIANKEEIESIKELIePTIENLISSFNTNDLEGI----DPNEKLEE-----YNTEIGDIYEEFIELYNIIA-GC 1772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 364 GEKYSKMAQELaDKSKGKKIGNVNEALAAFE---KYKDVL-NKKFSKADRdaIFNALASvKYDdwakHLDqfAKYLKITG 439
Cdd:TIGR01612 1773 LETVSKEPITY-DEIKNTRINAQNEFLKIIEiekKSKSYLdDIEAKEFDR--IINHFKK-KLD----HVN--DKFTKEYS 1842
|
330 340 350
....*....|....*....|....*....|.
gi 2242546895 440 HVSFGYDVVS-DILKIKDTGDWKPLFLTLEK 469
Cdd:TIGR01612 1843 KINEGFDDISkSIENVKNSTDENLLFDILNK 1873
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
110-181 |
1.38e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 40.74 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 110 PSATELAHANNAAMqaEAERLRLAKAEEKAR---KEAE--------AAEKAFQ-------------EAEQRRKEIE---- 161
Cdd:cd03406 158 PKIPEAIRRNYEAM--EAEKTKLLIAEQHQKvveKEAEterkraviEAEKDAEvakiqmqqkimekEAEKKISEIEdemh 235
|
90 100
....*....|....*....|....*.
gi 2242546895 162 --REK----AETERQLKLAEAEEKRL 181
Cdd:cd03406 236 laREKaradAEYYRALREAEANKLKL 261
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
118-248 |
1.38e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 118 ANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLA------------ALS 185
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAeakakaeeakakAEA 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2242546895 186 EEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEM--KTLAGKRNELAQASAKYK 248
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNaeKQGGARGAAAGSEVDKYA 265
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
88-172 |
1.53e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 40.63 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 88 DALTQRLKdIVNEALRH-NASRtpsATELAHANNAAMQAEAERLRLAKAEEKarKEAEAAEKAFQEAEQRRKEIEREKae 166
Cdd:pfam07946 246 DKLAKRAK-LRPEALKKaKKTR---EEEIEKIKKAAEEERAEEAQEKKEEAK--KKEREEKLAKLSPEEQRKYEEKER-- 317
|
....*.
gi 2242546895 167 tERQLK 172
Cdd:pfam07946 318 -KKEQR 322
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-409 |
1.71e-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: 41.21 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 131 RLAKAEEKARK---------EAEAAE--KAFQEAEQRRKEIEREKAETERQL----KLAEAEEKRLAALSEEAKAVEIAQ 195
Cdd:TIGR02169 202 RLRREREKAERyqallkekrEYEGYEllKEKEALERQKEAIERQLASLEEELekltEEISELEKRLEEIEQLLEELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 196 KKLSAAQSEVVKMD-GEIKTLNSRLSSSIHARDAEMKTLAGKRNEL-AQASAKYKELDELVKKLSPRA--NDPLQNRpfF 271
Cdd:TIGR02169 282 KDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLeAEIDKLLAEIEELEREIEEERkrRDKLTEE--Y 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 272 EATRRRvgagkiREEKQKQVTASETRINRINADITQIQKAISQVSNNRNAGIARVHEAEENLKKAQNNL--LNSQIKDAV 349
Cdd:TIGR02169 360 AELKEE------LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELadLNAAIAGIE 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 350 DATVSFYQTLTEKyGEKYSKMAQELadKSKGKKIGNVNEALAAFEKYKDVLNKKFSKADR 409
Cdd:TIGR02169 434 AKINELEEEKEDK-ALEIKKQEWKL--EQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
153-344 |
2.00e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 153 AEQRRKEIE---------REKAETERQLKLAEAE-----------EKRLAALSEEAKA--------VEIAQKKLSAAQSE 204
Cdd:COG1196 154 PEERRAIIEeaagiskykERKEEAERKLEATEENlerledilgelERQLEPLERQAEKaeryrelkEELKELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 205 VVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKlsprandpLQNRpFFEATRRRVGAGKIR 284
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE--------AQAE-EYELLAELARLEQDI 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 285 EEKQKQVTASETRINRINADITQIQKAISQVSNNRNAGIARVHEAEENLKKAQNNLLNSQ 344
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
|
| SVIP |
pfam15811 |
Small VCP/p97-interacting protein; SVIP, small VCP/p97-interacting protein, is a family of ... |
124-179 |
2.43e-03 |
|
Small VCP/p97-interacting protein; SVIP, small VCP/p97-interacting protein, is a family of proteins found in eukaryotes. SVIP was identified by yeast two-hybrid screening to be an interactive partner of VCP/p97. Mammalian VCP/p97 and its yeast counterpart Cdc48p participate in the formation of organelles, including the endoplasmic reticulum (ER), Golgi apparatus, and nuclear envelope. Over-expression of SVIP caused the formation of large vacuoles that seemed to be derived from the ER. The family has two putative coiled-coil regions and contains proteins of approximately 80 amino acids in length.
Pssm-ID: 464888 [Multi-domain] Cd Length: 77 Bit Score: 36.96 E-value: 2.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2242546895 124 QAEAERLRLAkAEEKARKEAEAAEKAFQEAEQRR-KEIEREKAETERQLKLAEAEEK 179
Cdd:pfam15811 11 SAEEVVLTPD-AEERRQQQAEAAEKRQEEAESRGiKNPESVRRKQKRAEELEKREQE 66
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
131-340 |
2.61e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 131 RLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETER-QLKLAEAEEKRlAALSEEAK----AVEIAQKKLSAAQSEV 205
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDlRETIAETERER-EELAEEVRdlreRLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 206 VKMDGEIKTLNSRLsSSIHARDAEMktlagkRNELAQASAKYKELDELVKKLSPRANDpLQNRpffeATRRRVGAGKIRE 285
Cdd:PRK02224 303 GLDDADAEAVEARR-EELEDRDEEL------RDRLEECRVAAQAHNEEAESLREDADD-LEER----AEELREEAAELES 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2242546895 286 EKQK---QVTASETRINRINADITQIQKAIS--------------QVSNNRNAGIARVHEAEENLKKAQNNL 340
Cdd:PRK02224 371 ELEEareAVEDRREEIEELEEEIEELRERFGdapvdlgnaedfleELREERDELREREAELEATLRTARERV 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-345 |
2.62e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 137 EKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEaeekRLAALSEEAKAVEI---------AQKKLSAAQSEVVK 207
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKAE----RYKELKAELRELELallvlrleeLREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 208 MDGEIKTLNSRlsssIHARDAEMKTLAGKRNELAQASAKY-KELDELVKKLSP------RANDPLQN--RPFFEATRRRV 278
Cdd:TIGR02168 251 AEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELqKELYALANEISRleqqkqILRERLANleRQLEELEAQLE 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2242546895 279 GAGKIREEKQKQVTASETRINRINADITQIQKAIS------QVSNNRNAGIARVHE---AEENLKKAQNNLLNSQI 345
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEeleaelEELESRLEELEEQLEtlrSKVAQLELQIASLNNEI 402
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
126-369 |
2.83e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 126 EAERLRlaKAEEKARKEAEAAEkafQEAEQRRK--------EIEREKAETER-----------QLKLAEAEEKRLAalsE 186
Cdd:PTZ00121 1676 KAEEAK--KAEEDEKKAAEALK---KEAEEAKKaeelkkkeAEEKKKAEELKkaeeenkikaeEAKKEAEEDKKKA---E 1747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 187 EAKAVEIAQKKLSAAQSEVVKMDGEI-KTLNSRLSSSIHARDAEMKTLAGKRneLAQASAKYKELDELVKKLSPRANDPL 265
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIrKEKEAVIEEELDEEDEKRRMEVDKK--IKDIFDNFANIIEGGKEGNLVINDSK 1825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 266 QNrpFFEATRRRVGAGKIREEKQKQVTASETRINRINADITQIQKAISQVSNNRNAGIARVHEAEENlKKAQNNLLNSQI 345
Cdd:PTZ00121 1826 EM--EDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEI-EKIDKDDIEREI 1902
|
250 260
....*....|....*....|....
gi 2242546895 346 KDAVDATVSFYQTLTEKYGEKYSK 369
Cdd:PTZ00121 1903 PNNNMAGKNNDIIDDKLDKDEYIK 1926
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
124-246 |
3.69e-03 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 39.98 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 124 QAEAERLRLAKAEEKARK------EAEAAEKAFQEAEQRRKEIERE---KAETERQLKLAEAEEKRLAALSEEAKAVEia 194
Cdd:PRK14900 883 RARAEELREKRGKLEAHRamlsgsEANSARRDTMEIQNEQKPTQDGpaaEAQPAQENTVVESAEKAVAAVSEAAQQAA-- 960
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2242546895 195 qkklSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAK 246
Cdd:PRK14900 961 ----TAVASGIEKVAEAVRKTVRRSVKKAAATRAAMKKKVAKKAPAKKAAAK 1008
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
93-321 |
3.81e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 93 RLKDIVNEALRHNASRTPSATELAHANNAAMQAEA--ERLRLAKAEeKARKEAEAAEKAFQEAEQRRKEIEREKAETERQ 170
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTltQKLQSLCKE-LDILQREQATIDTRTSAFRDLQGQLAHAKKQQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 171 LKLAEAEEKRLAALSE--EAKAVEIAQKKLSAAQSEVVKMDGEIKTlnsrlsssIHARDAEMKTLAGKRNELAQASAKY- 247
Cdd:TIGR00618 435 LQQRYAELCAAAITCTaqCEKLEKIHLQESAQSLKEREQQLQTKEQ--------IHLQETRKKAVVLARLLELQEEPCPl 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2242546895 248 -KELDELVKKLSPRANDPLQNRPFFEATRRRVGAGKIREEKQKQVTASETRINRINADITQIQKAISQVSNNRNA 321
Cdd:TIGR00618 507 cGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR 581
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
120-215 |
4.53e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.10 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 120 NAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLK------LAEAEEKRLAALSE-----EA 188
Cdd:cd16269 184 EAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEehlrqlKEKMEEERENLLKEqeralES 263
|
90 100
....*....|....*....|....*..
gi 2242546895 189 KAVEIAQKKLSAAQSEVVKMDGEIKTL 215
Cdd:cd16269 264 KLKEQEALLEEGFKEQAELLQEEIRSL 290
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
60-236 |
4.86e-03 |
|
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: 39.36 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 60 AQLKKTQAEQAARAKAAAEAQAKAKANRDALTQRLKDIvnealrHNASRTPSATELAHANNAAmQAEAERLRLAKAEEKA 139
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRAL------YRLGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPAR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 140 RKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAAL-SEEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSR 218
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALkAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
170
....*....|....*...
gi 2242546895 219 LSSSIHARDAEMKTLAGK 236
Cdd:COG4942 229 IARLEAEAAAAAERTPAA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
115-245 |
5.51e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 115 LAHANNAAMQA-EAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAKAVEI 193
Cdd:COG3883 127 IADADADLLEElKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2242546895 194 AQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASA 245
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
120-334 |
5.60e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 120 NAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRL----AALSEEAKAVEIAQ 195
Cdd:TIGR00618 211 PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELraqeAVLEETQERINRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 196 K--KLSAAQSEVVKMDGEIKTLNSRLSSsihardaemktlagKRNELAQASAKYKELdeLVKKLSPRANDPLQNRPFFEA 273
Cdd:TIGR00618 291 KaaPLAAHIKAVTQIEQQAQRIHTELQS--------------KMRSRAKLLMKRAAH--VKQQSSIEEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 274 TRRRVGAGK---IREEKQKQvTASETRINRINADIT------QIQKAISQVSNNRNAGIARVHEAEENLK 334
Cdd:TIGR00618 355 IHIRDAHEVatsIREISCQQ-HTLTQHIHTLQQQKTtltqklQSLCKELDILQREQATIDTRTSAFRDLQ 423
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
126-401 |
6.43e-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: 39.28 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 126 EAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAAlsEEAKAVEIAQkklsaaqsev 205
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ--EEEKLKERLE---------- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 206 vkmdgEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKE-LDELVKKLSPRANDPLQNRpffeatrrrvgAGKIR 284
Cdd:TIGR02169 741 -----ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEaLNDLEARLSHSRIPEIQAE-----------LSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 285 EEKQKQvtasETRINRINADITQIQKAISQVSNNRNAGIARVHEAEENLK--KAQNNLLNSQIKDaVDATVSFYQTLTEK 362
Cdd:TIGR02169 805 EEVSRI----EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKsiEKEIENLNGKKEE-LEEELEELEAALRD 879
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2242546895 363 YGEKYSKMAQELAD-KSKGKKI-GNVNEALAAFEKYKDVLN 401
Cdd:TIGR02169 880 LESRLGDLKKERDElEAQLRELeRKIEELEAQIEKKRKRLS 920
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
131-257 |
7.69e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 131 RLAKAEEKARKEAEAAEKafqEAEQRRKEIERE--------KAETERQLKLAEAE----EKRLA----ALSEEAKAVEIA 194
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKK---EAEAIKKEALLEakeeihklRNEFEKELRERRNElqklEKRLLqkeeNLDRKLELLEKR 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2242546895 195 QKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGkrneLAQASAKYKELDELVKKL 257
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG----LTAEEAKEILLEKVEEEA 167
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
130-180 |
8.16e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 39.08 E-value: 8.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2242546895 130 LRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKR 180
Cdd:PLN02316 250 LLEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQAKAEVEKRR 300
|
|
| Transcrip_act |
pfam04949 |
Transcriptional activator; This family of proteins may act as a transcriptional activator. It ... |
137-205 |
8.31e-03 |
|
Transcriptional activator; This family of proteins may act as a transcriptional activator. It plays a role in stress response in plants.
Pssm-ID: 398553 [Multi-domain] Cd Length: 154 Bit Score: 37.04 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242546895 137 EKARKEAEAAEKAFQEAEQRRKEIEREKAE----TERQLKLAEAEEKRLAALSEE--------AKAVEIAQKKLSAAQSE 204
Cdd:pfam04949 15 EEENEDEEMSRSALSTFRAKEEEIERKKMEvrekVQAQLGRVEEETKRLAEIREElealadpmRKEVAMVRKKIDAVNRE 94
|
.
gi 2242546895 205 V 205
Cdd:pfam04949 95 L 95
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
132-187 |
8.94e-03 |
|
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.
Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 36.42 E-value: 8.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2242546895 132 LAKAEEKARKEAEAAEKAFQEAEQRR-------KEIEREKAETERQLKLAEAEEKRLAALSEE 187
Cdd:pfam17675 32 LKKLEKETPEELEELEKELEKLEKEEeellqelEELEKEREELDAELEALEEELEALDEEEEE 94
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
105-181 |
9.64e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 36.49 E-value: 9.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2242546895 105 NASRTPSATELAHANNAAMQAEAERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIE--REKAETERQLKLAEAEEKRL 181
Cdd:pfam02050 37 GAGQGISAAELRNYQAFISQLDEAIAQQQQELAQAEAQVEKAREEWQEARQERKSLEklREREKKEERKEQNRREQKQL 115
|
|
| |
