|
Name |
Accession |
Description |
Interval |
E-value |
| MAP70 |
pfam07058 |
Microtubule-associated protein 70; This family represents a family of plant ... |
47-583 |
0e+00 |
|
Microtubule-associated protein 70; This family represents a family of plant microtubule-associated proteins of size 70 kDa. The proteins contain four predicted coiled-coil domains, and truncation studies identify a central domain that targets the proteins to microtubules. It has no predicted trans-membrane domains, and the region between the coils from approximately residues 240-483 is the targetting region.
Pssm-ID: 399798 [Multi-domain] Cd Length: 544 Bit Score: 705.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 47 GSDPVRIELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKK 126
Cdd:pfam07058 1 GSDPVKVELNRLENEVRDKDRELGEALAEIKALRLSERLKEKAVEELTDELLKLDEKLKASENLLESKNLEIKKINDEKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 127 ASMAAQFAAEASLRRVHAAQKDDDMPPIEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAERTVQSALAK 206
Cdd:pfam07058 81 AALAAQFAAEATLRRVHAAQKDEDMPPIEAILAPLEAELKLARQEINKLQDDNKALDRLTKSKEAALLEAERAVQIALAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 207 ASMVDDLQNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEAVLAGGAAANAVRDYQRKFQEMNEERKIL 286
Cdd:pfam07058 161 ASLVDDLQNKNQELMKQIEICQEENKILDKAHRQKVAEVEKLSQTVRELEEAVLAGGAAANAVRDYQRKVKEMNEERRTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 287 ERELARAKVNANRVATVVANEWKDSNDKVMPVRQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKEKFLLRLRVLEES 366
Cdd:pfam07058 241 ERELARAKVVANRVATVVANEWKDANDKVMPVKQWLEERRFLQGEMQQLRDKLAISERTAKAEAQLKEKVQLRLKVLEEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 367 LKGPTSSSSRGTSVGRSSSNGPTRRQSLGGAETSPKITSNGSLIKRTPSSQLRS-LTASASTVLKHAKGTSRSFDGGTRS 445
Cdd:pfam07058 321 LRSSLSGSGRSFSEGRSRSNGPSRRQSLGGASNNGLLSSNGFSSRRRSSSSSSSsLSSSHAKGLKHAKGGSKSFDGGSKS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 446 LDRSKVLINGPRSNFPLNhKSSEGTSRGESPSSIKGEEESAD----KATNNDSVPGVLYDLLQKEVITLRKAAHEKDQSL 521
Cdd:pfam07058 401 LGRGKHLLNGSTENSDAV-RDCDTNDSWKGNADEGTIENTNSntdeSNDETDNVSGQLYDMLQKEVIHLRKASHEKDQSL 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18394168 522 RDKDEAIEMLAKKVETLTKAMDVEAKKMRREVAVMGKEVAAMRVvdKGQQDSKTRRLSVSKG 583
Cdd:pfam07058 480 KDKDDAIEMLAKKVDTLTKAMEVEAKKMRREVAAMEKEVAAMRV--DKEHLGRSKRTGSSKG 539
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
54-352 |
1.74e-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: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 54 ELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMAAQF 133
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 134 AAEASLRRVHAAQKDddmppIEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAERTVQSALAKAsmvDDL 213
Cdd:COG1196 313 ELEERLEELEEELAE-----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL---EEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 214 QNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEAVLAGGAAANAVRDYQRKFQEMNEERKILERELARA 293
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 18394168 294 KVNANRVATVVANEWKDSNDKvmpvRQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQL 352
Cdd:COG1196 465 LAELLEEAALLEAALAELLEE----LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-340 |
6.59e-09 |
|
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: 58.91 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 65 KDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMAAQFAAEASLRRVHA 144
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 145 AQKD--DDMPPIEAILAPLEAELKLSRQEIAKLQDD-NKSLDRLTKSKEAalLDAERTVQSALAKAsmVDDLQNKNQELM 221
Cdd:TIGR02168 755 ELTEleAEIEELEERLEEAEEELAEAEAEIEELEAQiEQLKEELKALREA--LDELRAELTLLNEE--AANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 222 KQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEavlaggaaanAVRDYQRKFQEMNEERKILERELARAKvnanrva 301
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE----------LIEELESELEALLNERASLEEALALLR------- 893
|
250 260 270
....*....|....*....|....*....|....*....
gi 18394168 302 tvvanewKDSNDKVMPVRQWLEERRFLQGEMQQLRDKLA 340
Cdd:TIGR02168 894 -------SELEELSEELRELESKRSELRRELEELREKLA 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
52-295 |
2.38e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 52 RIELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMAA 131
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 132 QFAAEASLRRVHAAQKDDdmppIEAILAPLEAELKLSRQEI---AKLQDDNKSLDRLTKSKEAALLDAERTVQSALAKAS 208
Cdd:COG1196 360 LAEAEEALLEAEAELAEA----EEELEELAEELLEALRAAAelaAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 209 MVDDLQNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEAVLAGGAAANAVRDYQRKFQEMNEERKILER 288
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
....*..
gi 18394168 289 ELARAKV 295
Cdd:COG1196 516 LAGLRGL 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-354 |
4.13e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 58 LENEVRDKDRELSegQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMAAQFAAEA 137
Cdd:COG1196 218 LKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 138 SLRRvhaaqkdddmppIEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAERTVQSALAKASMVddLQNKN 217
Cdd:COG1196 296 ELAR------------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 218 QELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEAVLAGGAAANAVRDYQRKFQEMNEERKILERELARAKVNA 297
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 18394168 298 NRVATVVANEWKDSNDKVMPVRQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKE 354
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-339 |
5.85e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 49 DPVRIELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEElgkmaekLKLIENLLESKNLEIKKINEEKKAS 128
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 129 MAAQFAAEASLRRvHAAQKDDDmppiEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAERTVQSAlakAS 208
Cdd:TIGR02168 315 ERQLEELEAQLEE-LESKLDEL----AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL---RS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 209 MVDDLQNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSV----------------RELEEAVLAGGAAANAVRDY 272
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelkelqaeleeleEELEELQEELERLEEALEEL 466
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18394168 273 QRKFQEMNEERKILERELARAKVNANRVATVVANEWKDSNDkvmpVRQWLEERRFLQGEMQQLRDKL 339
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG----VKALLKNQSGLSGILGVLSELI 529
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-355 |
2.24e-07 |
|
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: 54.30 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 20 GGSKGMSRRRSMRPSFDADNEFMNllHGSDPVRIELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGK 99
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAELQRLR--ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 100 MAEKLKLIENLLESKNLEIkkinEEKKASMAAQFAAEASLRRVHAAqkdddmppIEAILAPLEAelKLSRQEIAKLQDDN 179
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEI----ENVKSELKELEARIEELEEDLHK--------LEEALNDLEA--RLSHSRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 180 KSLDRLTKSKEAALLDAERTVQSALAKASMVDD----LQNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVREL 255
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKeiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 256 EEAvLAGGAA-----ANAVRDYQRKFQEMNEE----RKILERELARAKVNANRVATVVANEWKDSND--KVMPVRQWLEE 324
Cdd:TIGR02169 881 ESR-LGDLKKerdelEAQLRELERKIEELEAQiekkRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeEELSLEDVQAE 959
|
330 340 350
....*....|....*....|....*....|....*
gi 18394168 325 RRFLQGEMQQLRD--KLAIAD--RAAKSEAQLKEK 355
Cdd:TIGR02169 960 LQRVEEEIRALEPvnMLAIQEyeEVLKRLDELKEK 994
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
60-267 |
2.85e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 60 NEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMAAQFAAEASL 139
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 140 --------RRVHAAQKDDDMPPIEAILAP------------LEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAERT 199
Cdd:COG4942 100 eaqkeelaELLRALYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18394168 200 VQSALAKASMVDDLQNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEAVLAGGAAAN 267
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
54-299 |
1.93e-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: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 54 ELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMAAQF 133
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 134 AAEASL-RRVHAAQKDDDMPPIEAILAPLEAELKLSRQEIAK--LQDDNKSLDRLTKSKEAalLDAERtvqsalakasmv 210
Cdd:COG4942 101 AQKEELaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKylAPARREQAEELRADLAE--LAALR------------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 211 DDLQNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEAVLAGGAAAnavRDYQRKFQEMNEERKILEREL 290
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA---EELEALIARLEAEAAAAAERT 243
|
....*....
gi 18394168 291 ARAKVNANR 299
Cdd:COG4942 244 PAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-368 |
5.67e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 54 ELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMAAQF 133
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 134 AAEASLRRVHAAQK-DDDMPPIEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAERTVQSAL----AKAS 208
Cdd:PRK03918 291 KAEEYIKLSEFYEEyLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyeeAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 209 M--------------VDDLQNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEA---------VLAGGAA 265
Cdd:PRK03918 371 KeelerlkkrltgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 266 ANAVRDYQRKFQEMNEERKILERELARAKVNANRVATVVANEwkdsnDKVMPVRQWLEERRFLQGEMQQLrdKLAIADRA 345
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-----SELIKLKELAEQLKELEEKLKKY--NLEELEKK 523
|
330 340
....*....|....*....|....*.
gi 18394168 346 AKSEAQLKEKFLL---RLRVLEESLK 368
Cdd:PRK03918 524 AEEYEKLKEKLIKlkgEIKSLKKELE 549
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
49-367 |
3.09e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 49 DPVRIELNRLENEVRDK-----------DRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLE 117
Cdd:TIGR02169 194 DEKRQQLERLRREREKAeryqallkekrEYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 118 IKKINEEkkasmaaqfaaeaslrrvhaaqkdddmppieaILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAE 197
Cdd:TIGR02169 274 LEELNKK--------------------------------IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 198 RTVQSALAKasmVDDLQNKNQELMKQIEicqEENRIIDKMHRQKVAEVEKLMQSVRELEEAVLAGGAAANAVRDYQRKFQ 277
Cdd:TIGR02169 322 ERLAKLEAE---IDKLLAEIEELEREIE---EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 278 EMNEERKILERELARAKVNANRVATVVAnewkDSNDKVMPVRQWLEErrfLQGEMQQLRDKLAIADRAAKSEAQLKEKFL 357
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELA----DLNAAIAGIEAKINE---LEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330
....*....|
gi 18394168 358 LRLRVLEESL 367
Cdd:TIGR02169 469 QELYDLKEEY 478
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-294 |
3.54e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 38 DNEFMNLLHGSDPVRIELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAE--------------- 102
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvkekigelea 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 103 KLKLIENLLESKNLEIKKINEEKKASMA----AQFAAEASLRRVHAAQKDDDmpPIEAILAPLEAELKLSRQEIAKLQDD 178
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAeidkLLAEIEELEREIEEERKRRD--KLTEEYAELKEELEDLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 179 NKSLDRLTKSKEAALLDAERTVQSALAKasmvddlQNKNQELMKQIEICQEENRIIDKMHRQKVAEVE--------KLMQ 250
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRE-------LDRLQEELQRLSEELADLNAAIAGIEAKINELEeekedkalEIKK 452
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 18394168 251 SVRELEEAVLAGGAAANAVRDYQRKFQEMNEERKILERELARAK 294
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-368 |
4.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 54 ELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMAAQF 133
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 134 AAEASLRRVHAAQKDDDMPPIEAilAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEaalldaertvqsalaKASMVDDL 213
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE---------------EAKKADEA 1488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 214 QNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEAVLAGGA-AANAVR--DYQRKFQEMNEERKILEREL 290
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAkKAEEKKkaDELKKAEELKKAEEKKKAEE 1568
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18394168 291 ARAKVNANRVATVVANEWKDSNDK-VMPVRQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKEKFLLRLRVLEESLK 368
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-355 |
4.33e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 54 ELNRLENEVRDKDRELSEGQAEIKALRLSERQREKaveELTEELGKMAEKLKLIENLlESKNLEIKKINEEKKASMAAQF 133
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA---KKAEEAKKKAEEAKKADEA-KKKAEEAKKADEAKKKAEEAKK 1497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 134 AAEASLRRVHAAQKDDDMPPIEAILAPLE---AELKLSRQEIAKLQDDNKSlDRLTKSKEAALLDAERTVQSAlAKASMV 210
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEakkAEEAKKADEAKKAEEKKKA-DELKKAEELKKAEEKKKAEEA-KKAEED 1575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 211 DDLQNKNQELMKQIE-------ICQEENRIIDKMHRQKVAEVEKL-MQSVRELEEAVLAGGAAANAVRDYQRKFQEM--- 279
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEearieevMKLYEEEKKMKAEEAKKAEEAKIkAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkka 1655
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18394168 280 NEERKILERELARAKVNANRVATVVANEWKDSNDKVMPVRQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKEK 355
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
58-578 |
5.32e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 58 LENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLK----LIENLLESKNLEIKKINE---------E 124
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEaakcLKEDMLEDSNTQIEQLRKmmlshegvlQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 125 KKASMAAQFAaEASLRRVHAAQKDDDMP------PIEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALL---- 194
Cdd:pfam15921 188 EIRSILVDFE-EASGKKIYEHDSMSTMHfrslgsAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLqqhq 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 195 --------DAERTVQSALAKASMVDDLQNKNQElmkQIEICQEENRIIDKMHRQKVAEVEKLMQSVR-ELEEavlaggaa 265
Cdd:pfam15921 267 drieqlisEHEVEITGLTEKASSARSQANSIQS---QLEIIQEQARNQNSMYMRQLSDLESTVSQLRsELRE-------- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 266 anAVRDYQRKFQEMNEERKILERELARAKVNANRVATVVANeWKDSNDKVMPVRQWLEERRFLQGEM-QQLRDK---LAI 341
Cdd:pfam15921 336 --AKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGN-LDDQLQKLLADLHKREKELSLEKEQnKRLWDRdtgNSI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 342 ADRAAKSEAQLKEKFLLRLRVLEESLKgptssssrgtsvgrSSSNGPTRRQSL---GGAETSPKITSNGSLIKRTpSSQL 418
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEALLKAMK--------------SECQGQMERQMAaiqGKNESLEKVSSLTAQLEST-KEML 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 419 RSLTASASTVLKHAKGTSRSFDGGTRSLDRSKVLINGprSNFPLNHKSSEGTSRGESPSSIKGEEESADKAtnndsvpgv 498
Cdd:pfam15921 478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA--TNAEITKLRSRVDLKLQELQHLKNEGDHLRNV--------- 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 499 lydllQKEVITLRkaahekdQSLRDKDEAIEMLAKKVETLTK----------AMDVEAKKMRREVAVMGKEVAAMRVVdK 568
Cdd:pfam15921 547 -----QTECEALK-------LQMAEKDKVIEILRQQIENMTQlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKIL-K 613
|
570
....*....|
gi 18394168 569 GQQDSKTRRL 578
Cdd:pfam15921 614 DKKDAKIREL 623
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-257 |
9.38e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 54 ELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMAAQF 133
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 134 AAEASLRRVHAAQKDDDMPPIEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAERTVQSALAK------- 206
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknlesq 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18394168 207 ----ASMVDDLQNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEE 257
Cdd:TIGR04523 393 indlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
155-354 |
1.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 155 EAILAPLEAELKLSRQEIAKLQDDNKSLDrltkskEAALLDAERTVQSALAKASMVDDLQNKNQELMKQIEICQEENRII 234
Cdd:COG4717 41 AFIRAMLLERLEKEADELFKPQGRKPELN------LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 235 DKMHRQ--KVAEVEKLMQSVRELEEAVLAGGAAANAVRDYQRKFQEMNEERKILERELARAKVNANRVATVVANEWKDSn 312
Cdd:COG4717 115 REELEKleKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18394168 313 dkvmpVRQWLEERRFLQGEMQQLRDKLAIADRAAKS-EAQLKE 354
Cdd:COG4717 194 -----LQDLAEELEELQQRLAELEEELEEAQEELEElEEELEQ 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
54-356 |
1.60e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 54 ELNRLENEVRDKDRELSEGQAEI-KALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEE-------- 124
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleqlenel 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 125 ------KKASMAAQFAAEASLRRVHAAQKDDDMPPIE----------AILAPLEAELKLSRQEIAKLQDDNKSLDRLTKS 188
Cdd:COG4717 237 eaaaleERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 189 KEAAL--------LDAERTVQSALAKASMVDDLQNKNQE---LMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEE 257
Cdd:COG4717 317 EEEELeellaalgLPPDLSPEELLELLDRIEELQELLREaeeLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 258 AVLAGGAAANAVRDYQRKFQEMNEERKILERELARAKVNANRvatvvaNEWKDSNDKVmpvRQWLEERRFLQGEMQQLRD 337
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE------EELEELEEEL---EELREELAELEAELEQLEE 467
|
330
....*....|....*....
gi 18394168 338 KLAIADRAAKsEAQLKEKF 356
Cdd:COG4717 468 DGELAELLQE-LEELKAEL 485
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
64-313 |
1.65e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 64 DKDRELSEGQAEIkaLRLSERQREKAVEELTEELGKM-AEKLKLIENLlESKNLEIKKINEEKKASMAAQFAAEASLRRV 142
Cdd:PTZ00121 1573 EEDKNMALRKAEE--AKKAEEARIEEVMKLYEEEKKMkAEEAKKAEEA-KIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 143 HAAQKDDDMPPIEAI-LAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAE---RTVQSALAKASMVDDLQNKNQ 218
Cdd:PTZ00121 1650 EELKKAEEENKIKAAeEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEelkKKEAEEKKKAEELKKAEEENK 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 219 ELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEAVLAGGAAANAVRDYQRKfQEMNEERKILERELARAKVN-- 296
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD-EEDEKRRMEVDKKIKDIFDNfa 1808
|
250 260
....*....|....*....|.
gi 18394168 297 ----ANRVATVVANEWKDSND 313
Cdd:PTZ00121 1809 niieGGKEGNLVINDSKEMED 1829
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
52-354 |
3.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 52 RIELNRLEnEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKinEEKKASMAa 131
Cdd:COG4717 67 ELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELA- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 132 qfAAEASLRRVHAAQKDddmppieaiLAPLEAELKLSRQEIAKLQDD-NKSLDRLTKSKEAALLDAERTVQSALAKASM- 209
Cdd:COG4717 143 --ELPERLEELEERLEE---------LRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAEl 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 210 ---VDDLQNKNQELMKQIEICQEENRIIDKMHRQK-----------VAEVEKLMQSVRELEEAV-----LAGGAAANAVR 270
Cdd:COG4717 212 eeeLEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaaLLALLGLGGSLLSLILTIagvlfLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 271 DYQRKFQEMNEERKILERELARAKVNANRVATVVANEWKD---SNDKVMPVRQWLEERRFLQGEMQQLRDKLAIADRAAK 347
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPpdlSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
....*..
gi 18394168 348 SEAQLKE 354
Cdd:COG4717 372 IAALLAE 378
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
54-438 |
3.60e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 54 ELNRLENEvrdkDRELSEGQAEIKALRLSERQREKAVEELTEELGKM---------------AEKLKLiENLLESKNLEI 118
Cdd:pfam15921 532 ELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtagamqVEKAQL-EKEINDRRLEL 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 119 K--KINEEKKASMAAQFAAEAS---LRRVH----AAQKDDDMPPIEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSK 189
Cdd:pfam15921 607 QefKILKDKKDAKIRELEARVSdleLEKVKlvnaGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNK 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 190 EAALLDAERTVQSALAKASmvDDLQNKNQELMKQIEICQEENRIIDKMHRQ---KVAEVEKLMQSVRELEEAVlaggAAA 266
Cdd:pfam15921 687 SEEMETTTNKLKMQLKSAQ--SELEQTRNTLKSMEGSDGHAMKVAMGMQKQitaKRGQIDALQSKIQFLEEAM----TNA 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 267 NAVRDYqrkfqeMNEERKILERELARAKVNANRVA---TVVANEWKDSNDKVMPVRQWLEERRFLQGEMQQlrdklaIAD 343
Cdd:pfam15921 761 NKEKHF------LKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLKEKVANMEVALDKASLQFAECQD------IIQ 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 344 RAAKSEAQLKEKFLLRLRvleeSLKGP--TSSSS------RGTSVGRSSSNGPTRRQSlggAETSPKITSNGSLIKRTPS 415
Cdd:pfam15921 829 RQEQESVRLKLQHTLDVK----ELQGPgyTSNSSmkprllQPASFTRTHSNVPSSQST---ASFLSHHSRKTNALKEDPT 901
|
410 420
....*....|....*....|...
gi 18394168 416 SQLRSLTASASTVLKHAKGTSRS 438
Cdd:pfam15921 902 RDLKQLLQELRSVINEEPTVQLS 924
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
54-207 |
3.96e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 54 ELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLK-------LIENLLESKNLE--------I 118
Cdd:COG3883 45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsYLDVLLGSESFSdfldrlsaL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 119 KKINEEKKASMAAQFAAEASLRRVHAAQKDDdmppiEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAER 198
Cdd:COG3883 125 SKIADADADLLEELKADKAELEAKKAELEAK-----LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
....*....
gi 18394168 199 TVQSALAKA 207
Cdd:COG3883 200 ELEAELAAA 208
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
61-353 |
5.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 61 EVRDKDRELSEGQAEIKALRLSERQREKAVEELTeelgKMAEKLKLIENLLESKNLEIKKINEEKKASMAAQFAAEASLR 140
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAK----KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 141 RVHAAQKDDDMPPIEAILAPLE-AELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAERTVQSALAKASmVDDLQNKNQE 219
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK-ADEAKKKAEE 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 220 LMKQIEICQ--EENRIIDKMhRQKVAEVEKLMQSVRELEEAVLAGGAAANAvrDYQRKFQEMN---EERKILERELARAK 294
Cdd:PTZ00121 1430 KKKADEAKKkaEEAKKADEA-KKKAEEAKKAEEAKKKAEEAKKADEAKKKA--EEAKKADEAKkkaEEAKKKADEAKKAA 1506
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 18394168 295 VNANRVATVVANEWKDSNDKVMPVRQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLK 353
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
85-355 |
5.42e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 85 QREKAVE-ELTEELGKMAEklklienllESKNLEIKKINEEKKASMAAQFAAEAslRRVHAAQKDDDMPPIEAILAPLEA 163
Cdd:PTZ00121 1083 AKEDNRAdEATEEAFGKAE---------EAKKTETGKAEEARKAEEAKKKAEDA--RKAEEARKAEDARKAEEARKAEDA 1151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 164 ElklsRQEIAKLQDDNKSLDRLTKSKEAALLDAERTVQSaLAKASMVddlqnKNQELMKQIEICQ--EENRIIDKMHRqk 241
Cdd:PTZ00121 1152 K----RVEIARKAEDARKAEEARKAEDAKKAEAARKAEE-VRKAEEL-----RKAEDARKAEAARkaEEERKAEEARK-- 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 242 vAEVEKLMQSVRELEEAVLAGGAAanavrdyqRKFQEMNEERKILERELARAKVNANRVATVVANEWKDSND--KVMPVR 319
Cdd:PTZ00121 1220 -AEDAKKAEAVKKAEEAKKDAEEA--------KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElkKAEEKK 1290
|
250 260 270
....*....|....*....|....*....|....*.
gi 18394168 320 QWLEERRflqGEMQQLRDKLAIADRAAKSEAQLKEK 355
Cdd:PTZ00121 1291 KADEAKK---AEEKKKADEAKKKAEEAKKADEAKKK 1323
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-257 |
5.48e-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: 40.04 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 51 VRIELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMA 130
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 131 AQFAAEASLRRvhaaqKDDDMPPIEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTkSKEAALLDAERTVQSALAKASmV 210
Cdd:TIGR02168 902 ELRELESKRSE-----LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT-LEEAEALENKIEDDEEEARRR-L 974
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18394168 211 DDLQNKNQEL----MKQIEICQEENRIIDKMHRQK---VAEVEKLMQSVRELEE 257
Cdd:TIGR02168 975 KRLENKIKELgpvnLAAIEEYEELKERYDFLTAQKedlTEAKETLEEAIEEIDR 1028
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
87-331 |
7.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 87 EKAVEELTEELGKMAEKLKLIENLLEsknleikkineekkaSMAAQFAAEASLRRVHAAQKDddmppieaiLAPLEAELK 166
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELD---------------ALQERREALQRLAEYSWDEID---------VASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 167 LSRQEIAKLQDDNKSLDRLTKSKEAALLDAERTVQSalakasmVDDLQNKNQELMKQIEICQEEnriIDKMHRQKVAEVE 246
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEE-------LDELKGEIGRLEKELEQAEEE---LDELQDRLEAAED 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394168 247 KLMQSVRELEEAVLAGGAAANAVRDYQRKFQemnEERKILERELARAKVNANRVATVVANEWKDSNDKVMP----VRQWL 322
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLE---ERIDALRARLNRAEEELERAMRAFNREWPAETADLDAdlesLPEYL 818
|
....*....
gi 18394168 323 EERRFLQGE 331
Cdd:COG4913 819 ALLDRLEED 827
|
|
| |
