|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
27-130 |
2.42e-45 |
|
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.
Pssm-ID: 465482 Cd Length: 102 Bit Score: 157.41 E-value: 2.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 27 VIFQNVGKSFLPQAALECHYTLTPFITPHPKDWVGIFKVGWSSARDYYTFLWSpmPENYTEGSTVHRTIIFQGYYVPRSD 106
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 251765105 107 GEFYQFCYVTHTGEIRGASTPFQF 130
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
154-450 |
3.78e-26 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 113.07 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQ------ELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELD 227
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYKELSAsseelsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 228 CLRDKLQKVISerdslqtQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDT-- 305
Cdd:pfam07888 154 RMKERAKKAGA-------QRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTah 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 306 -HPAET-GLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMK 383
Cdd:pfam07888 227 rKEAENeALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQER 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251765105 384 NQTSQEMGRAGGGVGVASE----LEAELQKE-VEELKLRLNMAAE------HYKEKYRECQRLRRQVTKLTQQQETQQ 450
Cdd:pfam07888 307 ETLQQSAEADKDRIEKLSAelqrLEERLQEErMEREKLEVELGREkdcnrvQLSESRRELQELKASLRVAQKEKEQLQ 384
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
157-453 |
1.86e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 157 EVQQECKELQKALRLLtqERDQLQEKQRQQNQELQKsLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQKV 236
Cdd:COG1196 217 ELKEELKELEAELLLL--KLRELEAELEELEAELEE-LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 237 ISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDThpAETGLKEQL 316
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE--AEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 317 RQAEEQLQATRQQAAMLGSELRDASGGRDRtMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGG 396
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 251765105 397 VGVASELEAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQQETQQGDA 453
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-424 |
3.71e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 152 LVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQK------SLIEEKEEAQSRVRQLEQDLLKITQKAVLKETE 225
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEElrleleELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 226 LDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDT 305
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 306 H-PAETGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKN 384
Cdd:COG1196 391 AlRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 251765105 385 QTSQEmgragggVGVASELEAELQKEVEELKLRLNMAAEH 424
Cdd:COG1196 471 EAALL-------EAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
164-461 |
1.81e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.87 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 164 ELQKALRLLTQERDQLQEKQRQQNQELQKsLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQKVISERDSL 243
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 244 QTQLKNERDERELYKSHVRSAELEntklsaelqmLKAVelnrEVTIAQYQEELHRLRTERDThpaetgLKEQLRQAEEQL 323
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEE----------LAEA----EAEIEELEAQIEQLKEELKA------LREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 324 QATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMknqtSQEMGRAGGGVGVASEL 403
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL----ESELEALLNERASLEEA 888
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 251765105 404 EAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKL-TQQQETQQGDANRNDASTE 461
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLeLRLEGLEVRIDNLQERLSE 947
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
166-389 |
7.47e-14 |
|
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: 74.03 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 166 QKALRLLTQERDQLQEKQRQQNQELQKsLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQKVISERDSLQT 245
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 246 QLKNERDE-----RELYKSHVRSAEL------ENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTerdthpaetgLKE 314
Cdd:COG4942 98 ELEAQKEElaellRALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----------LRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251765105 315 QLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELyrvRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQE 389
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
151-385 |
1.63e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 151 ILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQK------SLIEEKEEAQSRVRQLEQDLLKITQKAVLKET 224
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARleqdiaRLEERRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 225 ELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERD 304
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 305 ThpaetgLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKN 384
Cdd:COG1196 418 R------LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
.
gi 251765105 385 Q 385
Cdd:COG1196 492 R 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-385 |
4.50e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 155 VEEVQQECKELQKALRLLTQE----RDQLQEKQRQQN---------QELQKSLIEEKEEAQSRVRQLEQDLLKIT----- 216
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKleelRLEVSELEEEIEelqkelyalANEISRLEQQKQILRERLANLERQLEELEaqlee 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 217 --QKAVLKETELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAEL-QMLKAVELNREvTIAQYQ 293
Cdd:TIGR02168 328 leSKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaQLELQIASLNN-EIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 294 EELHRLRTERDTHPAETGLKEQlRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECR 373
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
250
....*....|..
gi 251765105 374 HAQDQLDRMKNQ 385
Cdd:TIGR02168 486 QLQARLDSLERL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-342 |
5.34e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 138 EELLTVEDDGNSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQ 217
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 218 KAVLKETELDCLRDKLQKViSERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELH 297
Cdd:COG1196 381 LEELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 251765105 298 RLRTERDTHPAET-GLKEQLRQAEEQLQATRQQAAMLGSELRDASG 342
Cdd:COG1196 460 ALLELLAELLEEAaLLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-448 |
5.67e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 138 EELLTVEDDGNSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQK--SLIEEKEEAQSRVRQLEQDLLKI 215
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleEAEEELAEAEAEIEELEAQIEQL 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 216 TQKAVLKETELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRsaELENTKLSAELQMLKAvelnrEVTIAQYQEE 295
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE--DLEEQIEELSEDIESL-----AAEIEELEEL 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 296 LHRLRTERDthpaetGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHA 375
Cdd:TIGR02168 868 IEELESELE------ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 376 QDQLdrmKNQTSQEMGRAGGGVGVASELEAELQKEVEELKLRL------NMAA----EHYKEKYREcqrLRRQVTKLTQQ 445
Cdd:TIGR02168 942 QERL---SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvNLAAieeyEELKERYDF---LTAQKEDLTEA 1015
|
...
gi 251765105 446 QET 448
Cdd:TIGR02168 1016 KET 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
136-476 |
1.23e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 136 TGEELLTVED--DGNSDILVRVEE--VQQECKELQKALRLLTQERDQLQ------EKQRQQNQELQ---KSLIEEKEEAQ 202
Cdd:PRK02224 171 ASDARLGVERvlSDQRGSLDQLKAqiEEKEEKDLHERLNGLESELAELDeeieryEEQREQARETRdeaDEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 203 SRVRQLEQDLLKITQKAVLKETELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVE 282
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 283 LNREVTIAQYQEELHRLRTERDTHPAE-TGLKEQLRQAEEQLQATRQQA-------AMLGSELRDASGG----------- 343
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERaEELREEAAELESELEEAREAVedrreeiEELEEEIEELRERfgdapvdlgna 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 344 ---RDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQT-------SQEMGRAGGGVGVASELEAELQK---E 410
Cdd:PRK02224 411 edfLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEcgqpvegSPHVETIEEDRERVEELEAELEDleeE 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251765105 411 VEELKLRLNmAAEHYKEKYRECQRLRRQVTKLTQQQETQQgdaNRNDASTETTLELHTPDAETPSE 476
Cdd:PRK02224 491 VEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAERR---ETIEEKRERAEELRERAAELEAE 552
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
744-770 |
3.74e-10 |
|
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.
Pssm-ID: 412016 Cd Length: 27 Bit Score: 55.25 E-value: 3.74e-10
10 20
....*....|....*....|....*..
gi 251765105 744 RVCPVCSEQFPLDCQQQLYEKHVHTHF 770
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTHF 27
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
719-742 |
1.37e-09 |
|
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the first one.
Pssm-ID: 412015 Cd Length: 24 Bit Score: 53.57 E-value: 1.37e-09
10 20
....*....|....*....|....
gi 251765105 719 CPLCEVIFPPHFEQSSFERHVESH 742
Cdd:cd21969 1 CPLCELVFPPNYDQSKFEQHVESH 24
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
150-368 |
1.74e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 150 DILVRVEEVQQECKELQKALRLLTQERDQLQ--EKQRQQNQELQKsLIEEKEEAQSRVRQLeqDLLKITQKAVLKETELD 227
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAA-ARERLAELEYLRAAL--RLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 228 CLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELEN-TKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDTH 306
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251765105 307 PAE-----TGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQ-------EAEELRAHLAEA 368
Cdd:COG4913 379 AEEfaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksnipaRLLALRDALAEA 452
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
717-743 |
5.03e-09 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 51.88 E-value: 5.03e-09
10 20
....*....|....*....|....*..
gi 251765105 717 KQCPLCEVIFPPHFEQSSFERHVESHW 743
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
149-435 |
1.35e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 56.84 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 149 SDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKsLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDC 228
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEERDELNEKLNELREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 229 LRDKLQKVISERDSLQtQLKnERDERELYKshvrsaeLENTKLSAELQMlKAVElnrevTIAQYQEELHRLRTERDTHPA 308
Cdd:COG1340 97 LRKELAELNKAGGSID-KLR-KEIERLEWR-------QQTEVLSPEEEK-ELVE-----KIKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 309 ETGLKEQLRQAEEQLQATRQQAamlgSELRDASGGRDRTMTELYrvrQEAEELRAHLAEAQEECRHAQDQLDRMKNQ--- 385
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKI----KELAEEAQELHEEMIELY---KEADELRKEADELHKEIVEAQEKADELHEEiie 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 251765105 386 TSQEMGRAGGGVGVASELEAELQKEVEELKLRlnMAAEHYKEKYRECQRL 435
Cdd:COG1340 235 LQKELRELRKELKKLRKKQRALKREKEKEELE--EKAEEIFEKLKKGEKL 282
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-564 |
2.18e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDcLRDKL 233
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA-LLERL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 234 QKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDT-HPAETGL 312
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaAARLLLL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 313 KEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRV-----------------RQEAEELRAHLAEAQEEcRHA 375
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaalaaalqnivvedDEVAAAAIEYLKAAKAG-RAT 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 376 QDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEEL--------------KLRLNMAAEHYKEKYRECQRLRRQVTK 441
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARyyvlgdtllgrtlvAARLEAALRRAVTLAGRLREVTLEGEG 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 442 LTQQQETQQGDANRNDASTETTLELHTPDAETPSESYPAEIKTVARDVEKSRdeEGNEQEEEDEEEEECSLSVEAELACM 521
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER--ELAEAEEERLEEELEEEALEEQLEAE 733
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 251765105 522 EEKWREQCTINENLKLLLANEEKRFKTQVAEKDREVSALRESL 564
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
196-458 |
7.89e-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: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 196 EEKEEAQSRVRQLEQDLLKItqKAVLKEteldcLRDKLqkviserDSLQTQLKNERDERELykshvrSAELENTKLSaeL 275
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRL--EDILNE-----LERQL-------KSLERQAEKAERYKEL------KAELRELELA--L 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 276 QMLKAVELNREvtIAQYQEELHRLRTERDThpaetgLKEQLRQAEEQLQATRQQAAMLGSELRDASGgrdrtmtELYRVR 355
Cdd:TIGR02168 230 LVLRLEELREE--LEELQEELKEAEEELEE------LTAELQELEEKLEELRLEVSELEEEIEELQK-------ELYALA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 356 QEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAE----------LQKEVEELKLRLNMAAEHY 425
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKleelkeelesLEAELEELEAELEELESRL 374
|
250 260 270
....*....|....*....|....*....|...
gi 251765105 426 KEKYRECQRLRRQVTKLTQQQETQQGDANRNDA 458
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
154-371 |
8.28e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLiEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKL 233
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL-AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 234 QKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDThpaetgLK 313
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED------KA 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 251765105 314 EQLRQAEEQLQATRQQaamlgselrdasggRDRTMTELYRVRQEAEELRAHLAEAQEE 371
Cdd:TIGR02169 448 LEIKKQEWKLEQLAAD--------------LSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-593 |
9.91e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 138 EELLTVEDDGNSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLI--EEKEEAQsRVRQLEQdllkI 215
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkaEEARKAD-ELKKAEE----K 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 216 TQKAVLKETELDCLRDKLQKVISERDSLQtQLKNERDERElYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEE 295
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAK-KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 296 LHRLRTERDTHPAETGLK--EQLRQAEEqLQATRQQAAMLGSELRDASGGRDRTMtelyRVRQEAEELRA--HLAEAQEE 371
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKkaEEKKKADE-AKKKAEEDKKKADELKKAAAAKKKAD----EAKKKAEEKKKadEAKKKAEE 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 372 CRHAQDQLDRMKN-QTSQEMGRAGGGVGVASEL--EAELQKEVEELKLRlnmaAEHYKEKYRECQRL---RRQVTKLTQQ 445
Cdd:PTZ00121 1443 AKKADEAKKKAEEaKKAEEAKKKAEEAKKADEAkkKAEEAKKADEAKKK----AEEAKKKADEAKKAaeaKKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 446 QETQQGDANRNDASTETTLELHTPDAETPSEsypaEIKTvARDVEKSRDEEGNEQEEEDEEEEECSLSVEAELACMEEKW 525
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKAD----ELKK-AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251765105 526 REQCtinenlkLLLANEEKRFKTQVAEKDREVSALRESLVVVTKEKERLEKQYMREGTTRSRRLEVRE 593
Cdd:PTZ00121 1594 IEEV-------MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-423 |
1.22e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 216 TQKAVLKETELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQmlkavelnrevtIAQYQEE 295
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE------------IAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 296 LHRLRterDTHPAETGLKEQLRQAEEQLQATRQQAAmlgselrdasggrdrtmtelyRVRQEAEELRAHLAEAQEECRHA 375
Cdd:COG4913 677 LERLD---ASSDDLAALEEQLEELEAELEELEEELD---------------------ELKGEIGRLEKELEQAEEELDEL 732
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 251765105 376 QDQLDRMKNQTSQ-------EMGRAGGGVGVASELEAELQKEVEELKLRLNMAAE 423
Cdd:COG4913 733 QDRLEAAEDLARLelralleERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
155-455 |
2.15e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 155 VEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELqKSLIEEKEEAQSRVRQleqdllkitqkavlketeldcLRDKLQ 234
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEEL-KELAEKRDELNAQVKE---------------------LREEAQ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 235 KVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDTHPAETGLKE 314
Cdd:COG1340 61 ELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 315 QLRQAEEQLQAtRQQAAMLGSELRDasggrdrTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAG 394
Cdd:COG1340 141 KIKELEKELEK-AKKALEKNEKLKE-------LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAD 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251765105 395 ggvgvaseleaELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQQETQQGDANR 455
Cdd:COG1340 213 -----------ELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
153-370 |
2.32e-07 |
|
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: 54.46 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 153 VRVEEVQQECKELQKALR-LLTQERDQLQEKQRQQNQEL--QKSLIEEKEE----AQSRVRQLEQD-----------LLK 214
Cdd:pfam12128 272 TLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELsaADAAVAKDRSeleaLEDQHGAFLDAdietaaadqeqLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 215 ITQKAVLKETELDCLRDKLQKVISERDSLQtQLKNERDERELYKSHVRSAELENTK---LSAELQMLKAVE--------- 282
Cdd:pfam12128 352 WQSELENLEERLKALTGKHQDVTAKYNRRR-SKIKEQNNRDIAGIKDKLAKIREARdrqLAVAEDDLQALEselreqlea 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 283 LNREVTIAQYQ--EELHRLRTERDTHPAETGLKEQLRQ-------AEEQLQATRQQAAMLGSELRDASGGRDRTMTELYR 353
Cdd:pfam12128 431 GKLEFNEEEYRlkSRLGELKLRLNQATATPELLLQLENfderierAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
250
....*....|....*..
gi 251765105 354 VRQEAEELRAHLAEAQE 370
Cdd:pfam12128 511 ASRRLEERQSALDELEL 527
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
138-450 |
3.21e-07 |
|
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: 54.21 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 138 EELLTVEDDGNSDILVRVEEVQQECKEL-QKALRLLTQERDQLQEKQRQQN---QELQKSLIEEKEEAQSRVRQLEQDLL 213
Cdd:pfam02463 674 ELLEIQELQEKAESELAKEEILRRQLEIkKKEQREKEELKKLKLEAEELLAdrvQEAQDKINEELKLLKQKIDEEEEEEE 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 214 KITQKAVLKETELDCLRDKlQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQ 293
Cdd:pfam02463 754 KSRLKKEEKEEEKSELSLK-EKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 294 EELHRLRTERDTHPAETGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECR 373
Cdd:pfam02463 833 EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLL 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 374 HAQDQLDRMKNQTSQEMGRAGGGVGVASELEAE-------------------LQKEVEELKLRLNMAAEHYKEKYRECQR 434
Cdd:pfam02463 913 EEKENEIEERIKEEAEILLKYEEEPEELLLEEAdekekeennkeeeeernkrLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
330
....*....|....*.
gi 251765105 435 LRRQVTKLTQQQETQQ 450
Cdd:pfam02463 993 DELEKERLEEEKKKLI 1008
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
150-499 |
4.94e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 150 DILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKE------EAQSRVRQLEQDLLKITQKAVLKE 223
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEeeealeEAAEEEAELEEEEEALLELLAELL 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 224 TELDCLRDKLQKVISERDSLQTQ---LKNERDERELYKSHVRSAELE--NTKLSAELQMLKAVELNREVTIAQYQEELHR 298
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARlllLLEAEADYEGFLEGVKAALLLagLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 299 LRTERDTHPAET---GLKEQ---------LRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLA 366
Cdd:COG1196 550 NIVVEDDEVAAAaieYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 367 EAQEECRHAQDQLDRMKNQTSQEMGRAGG----GVGVASELEAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKL 442
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAggslTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 251765105 443 TQQQETQQGDANRNDASTETTLELHTPDAETPSESYPAEIKTVARDVEKSRDEEGNE 499
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-580 |
4.95e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 152 LVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQelqksLIEEKEEAQSRVRQLEQ--DLLKITQKAVLKETELDCL 229
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-----LEAELEELREELEKLEKllQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 230 RDKLQKV---ISERDSLQTQLKNERDERELYKSHVRSAELENT--------KLSAELQMLKAVELNREVTIAQYQEELHR 298
Cdd:COG4717 145 PERLEELeerLEELRELEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 299 LRTERDTHPAETGLKEQLRQAEEQLQATRQQAAMLGseLRDASGGRDRTMTELYRVRQEAEELRAHLAEAqeecrhaqdq 378
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLA--LLGLGGSLLSLILTIAGVLFLVLGLLALLFLL---------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 379 LDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQQEtqqgDANRNDA 458
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE----ELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 459 STETTLELHTPDAETPsESYPAEIKTVARDVEKSRDEEGNEQEEEDEEEEECSLSVEAELACMEEKWREqctINENLKLL 538
Cdd:COG4717 369 EQEIAALLAEAGVEDE-EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE---LEEELEEL 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 251765105 539 ------LANEEKRFKTQV--AEKDREVSALRESLVVVTKEKERLEKQYMR 580
Cdd:COG4717 445 eeeleeLREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
163-454 |
5.05e-07 |
|
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: 53.44 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 163 KELQKALRLLTQERDQLQEKQ---RQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQKVISE 239
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIidlEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 240 RDSlQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQyQEELHRLRTERDTHPAETGLKEQLRQA 319
Cdd:pfam02463 249 EQE-EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK-SELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 320 EEQLQATRQQAAMLGSELrdasggrdrtmTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGGVGV 399
Cdd:pfam02463 327 EKELKKEKEEIEELEKEL-----------KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 251765105 400 ASELEAELQKEVEELKLRLNMAAEHYKEkyrECQRLRRQVTKLTQQQETQQGDAN 454
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKE---EKKEELEILEEEEESIELKQGKLT 447
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
154-445 |
6.52e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQE----RDQL---QEKQRQQNQE--LQKSL--IEEKEEAQSRVRQLEQDllkitqkavlk 222
Cdd:PRK04863 308 RLVEMARELAELNEAESDLEQDyqaaSDHLnlvQTALRQQEKIerYQADLeeLEERLEEQNEVVEEADE----------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 223 etELDCLRDKLQKVISERDSLQTQLKNerderelyksHVRSAELENTKLSAELQMLKAVELNRE------VTIAQYQEEL 296
Cdd:PRK04863 377 --QQEENEARAEAAEEEVDELKSQLAD----------YQQALDVQQTRAIQYQQAVQALERAKQlcglpdLTADNAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 297 HRLRTERDThpaetgLKEQLRQAEEQL---QATRQQAAMLGSELRDASGGRDR---------TMTELYRVRQEAEE---L 361
Cdd:PRK04863 445 EEFQAKEQE------ATEELLSLEQKLsvaQAAHSQFEQAYQLVRKIAGEVSRseawdvareLLRRLREQRHLAEQlqqL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 362 RAHLAEAQEECRhAQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTK 441
Cdd:PRK04863 519 RMRLSELEQRLR-QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
....
gi 251765105 442 LTQQ 445
Cdd:PRK04863 598 LAAR 601
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
165-450 |
7.37e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 165 LQKALRLLTQERDQLQEKQRQQN--QELQKSL-IEEKEE-------AQSRVRQLEQDLLKITQKAVLKETeldcLRDKLQ 234
Cdd:COG3206 96 LERVVDKLNLDEDPLGEEASREAaiERLRKNLtVEPVKGsnvieisYTSPDPELAAAVANALAEAYLEQN----LELRRE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 235 KVISERDSLQTQLKNERDErelykshVRSAElentklsAELQMLKA----VELNREVTiaQYQEELHRLRTERDThpaet 310
Cdd:COG3206 172 EARKALEFLEEQLPELRKE-------LEEAE-------AALEEFRQknglVDLSEEAK--LLLQQLSELESQLAE----- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 311 gLKEQLRQAEEQLQATRQQAAMLGSELRD--ASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQ 388
Cdd:COG3206 231 -ARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251765105 389 EMgragggvgvaSELEAELQKEVEELKLRLNM---AAEHYKEKYRECQRLRRQVTKLTQQQETQQ 450
Cdd:COG3206 310 EA----------QRILASLEAELEALQAREASlqaQLAQLEARLAELPELEAELRRLEREVEVAR 364
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-383 |
8.19e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 138 EELLTVEDDGNSDILVRVEEVQ--QECKELQKALR------LLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLE 209
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKaeedknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 210 QDLLKITQkaVLKETELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTI 289
Cdd:PTZ00121 1617 EAKIKAEE--LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 290 AQYQEELHRLRTERDTHPAETGLKEQLRQAE-------EQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELR 362
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEeenkikaEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
250 260
....*....|....*....|.
gi 251765105 363 AHLAEAQEECRHAQDQLDRMK 383
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRME 1795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-381 |
1.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQ--------KSLIEEKEEAQSRVRQLEQ---DLLKITQKAVLK 222
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvASAEREIAELEAELERLDAssdDLAALEEQLEEL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 223 ETELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAElentKLSAELQMLKAVELNREVTIAQYQEELHR-LRT 301
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE----DLARLELRALLEERFAAALGDAVERELREnLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 302 ERDthpaetGLKEQLRQAEEQLQATRQQ--------AAMLGSELRDASGGRDR----TMTELYRVRQEAEELR------- 362
Cdd:COG4913 774 RID------ALRARLNRAEEELERAMRAfnrewpaeTADLDADLESLPEYLALldrlEEDGLPEYEERFKELLnensief 847
|
250 260
....*....|....*....|.
gi 251765105 363 -AHLAEA-QEECRHAQDQLDR 381
Cdd:COG4913 848 vADLLSKlRRAIREIKERIDP 868
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
164-427 |
1.27e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 164 ELQKALRLLTQERDQLQEKQRQQNQELQK--------SLIEEKEEAQSRVRQLEQDLLKitqkavlketeldcLRDKLQK 235
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvDLSEEAKLLLQQLSELESQLAE--------------ARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 236 VISERDSLQTQLKNERDErelykshvrSAELENtklSAELQMLKAVELNREVTIAQYQEELhrlrteRDTHPAETGLKEQ 315
Cdd:COG3206 238 AEARLAALRAQLGSGPDA---------LPELLQ---SPVIQQLRAQLAELEAELAELSARY------TPNHPDVIALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 316 LRQAEEQLQATRQQAamlgselrdasggrdrtmteLYRVRQEAEELRAHLAEAQEECRHAQDQLDRMkNQTSQEMgragg 395
Cdd:COG3206 300 IAALRAQLQQEAQRI--------------------LASLEAELEALQAREASLQAQLAQLEARLAEL-PELEAEL----- 353
|
250 260 270
....*....|....*....|....*....|..
gi 251765105 396 gvgvaseleAELQKEVEELKLRLNMAAEHYKE 427
Cdd:COG3206 354 ---------RRLEREVEVARELYESLLQRLEE 376
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
191-449 |
1.34e-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: 51.30 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 191 QKSLIEEKEEAQSRVRQleqdllkitqkavlketELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTK 270
Cdd:COG4942 18 QADAAAEAEAELEQLQQ-----------------EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 271 LSAELQmlkavELNREvtIAQYQEELHRLRTErdthpaetgLKEQLRQAEEQLQATRQQAAMLGSELRDASggrdRTMTE 350
Cdd:COG4942 81 LEAELA-----ELEKE--IAELRAELEAQKEE---------LAELLRALYRLGRQPPLALLLSPEDFLDAV----RRLQY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 351 LYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEELKLRLNMAAEHYKEKYR 430
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250
....*....|....*....
gi 251765105 431 ECQRLRRQVTKLTQQQETQ 449
Cdd:COG4942 221 EAEELEALIARLEAEAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
149-358 |
1.56e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 149 SDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKsLIEEKEEAQSRVRQLEQDL---LKITQKAVLKETE 225
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-LQAEIAEAEAEIEERREELgerARALYRSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 226 LDCL------------RDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAvELNREvtIAQYQ 293
Cdd:COG3883 105 LDVLlgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA-ELEAQ--QAEQE 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251765105 294 EELHRLRTERDTHPAE-TGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEA 358
Cdd:COG3883 182 ALLAQLSAEEAAAEAQlAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
135-428 |
1.68e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 135 PTGEELLTVEDDGNSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQkslieekeEAQSRVRQLEQDLLK 214
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE--------QLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 215 ITQKAVLKETELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQE 294
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 295 ELHRLRTERDTHPAETGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRH 374
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 251765105 375 AQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEELKLRLNMAAEHYKEK 428
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
138-491 |
2.23e-06 |
|
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: 51.17 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 138 EELLTVEDDGNSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQEL---------QKSLIEEKEEAQSRVRQL 208
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqkNKSLESQISELKKQNNQL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 209 EQDLLKITQKAVLKETELDCLRDKLQKVISERDSLQTQLKNErdERELYKSHVRSAELEN--TKLSAELQMLKavelnre 286
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK--QKELEQNNKKIKELEKqlNQLKSEISDLN------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 287 vtiAQYQEELHRlrterdthpaetGLKEQLRQAEEQLQATRQQAA---MLGSELRDasggrdrtmtELYRVRQEAEELRA 363
Cdd:TIGR04523 302 ---NQKEQDWNK------------ELKSELKNQEKKLEEIQNQISqnnKIISQLNE----------QISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 364 HLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQ---KEVEELKLRLNMAAEHYKEKYRECQRLRRQVT 440
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQnqeKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 251765105 441 KLTQQQEtqqgDANRNDASTETT---LELHTPDAETPSESYPAEIKTVARDVEK 491
Cdd:TIGR04523 437 KNNSEIK----DLTNQDSVKELIiknLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
158-575 |
2.50e-06 |
|
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: 51.27 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 158 VQQECKELQKALRLLTQERDQLQEKQRQQNQ----------------ELQKSLIEEK-EEAQSRVRQLEQDLLkiTQKAV 220
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADIRRRESQsqedlrnqlqntvhelEAAKCLKEDMlEDSNTQIEQLRKMML--SHEGV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 221 LKE--TELDCLRDKLQKVISERDSLQTQlkNERDERELYKSHVRSAELENTKLSA-------ELQMLKAVELNR-EVTIA 290
Cdd:pfam15921 186 LQEirSILVDFEEASGKKIYEHDSMSTM--HFRSLGSAISKILRELDTEISYLKGrifpvedQLEALKSESQNKiELLLQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 291 QYQEELHRLRTErdtHPAE-TGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELyrvRQEAEELRAHLAEAQ 369
Cdd:pfam15921 264 QHQDRIEQLISE---HEVEiTGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDL---ESTVSQLRSELREAK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 370 eecRHAQDQLDRMKNQ---TSQEMGRAGGGVGVASELEAELQKEVEELklrlnMAAEHYKEKYrecqrlrrqvTKLTQQQ 446
Cdd:pfam15921 338 ---RMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQLQKL-----LADLHKREKE----------LSLEKEQ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 447 ETQQGDANRNDASTETTLELHTPDAETPSESYPAEIKTVARDVEKSRDEEGNEQEEEDEEEEECSlSVEAELACMEEKWR 526
Cdd:pfam15921 400 NKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVS-SLTAQLESTKEMLR 478
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 251765105 527 EQCTINENLKLLLANEEKR---FKTQVAEKDREVSALRESlvvVTKEKERLE 575
Cdd:pfam15921 479 KVVEELTAKKMTLESSERTvsdLTASLQEKERAIEATNAE---ITKLRSRVD 527
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
172-445 |
4.47e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.44 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 172 LTQERDQLQE----KQRQQNQELQKSL--IEEKEEAQSRVRQLEQ---DLLKITQKavlketeldclrdklqkviserds 242
Cdd:PRK10929 28 ITQELEQAKAaktpAQAEIVEALQSALnwLEERKGSLERAKQYQQvidNFPKLSAE------------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 243 LQTQLKNERDERELYKSHVRSAELENTKLSAELQMLkavELNRevtiaQYQEELHRLRTERD---THPAE-TGLKEQLRQ 318
Cdd:PRK10929 84 LRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLL---EKSR-----QAQQEQDRAREISDslsQLPQQqTEARRQLNE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 319 AEEQLQA--------TRQQAAMLGSElrdaSGGRDRTMTELYRV------RQEAEELRAHLAEAQEECRHAQDQLDR--M 382
Cdd:PRK10929 156 IERRLQTlgtpntplAQAQLTALQAE----SAALKALVDELELAqlsannRQELARLRSELAKKRSQQLDAYLQALRnqL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 383 KNQTSQEMGRAGGGVGVASELEAELQKE-VEELKLRLNMAAEHYKekyrECQRL------RRQVTKLTQQ 445
Cdd:PRK10929 232 NSQRQREAERALESTELLAEQSGDLPKSiVAQFKINRELSQALNQ----QAQRMdliasqQRQAASQTLQ 297
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
163-385 |
4.92e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 163 KELQKALRLLTQERDQLQEKQRQQNQELQKsLIEEKEEAQSRVRQLEQDLLKItqkavlkETELDCLRDKLQKVISERDS 242
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEE-ELKEAEEKEEEYAELQEELEEL-------EEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 243 LQTQLKNERDERELykshvrsaelentklsaelqmlkaVELNREvtIAQYQEELHRLRTERDthpAETGLKEQLRQAEEQ 322
Cdd:COG4717 121 LEKLLQLLPLYQEL------------------------EALEAE--LAELPERLEELEERLE---ELRELEEELEELEAE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251765105 323 LQATRQQAAMLGSELRDASGGRDRTMTE-LYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQ 385
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEeLEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
143-381 |
6.88e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 143 VEDDGNSDILVRVEEVQQECKELQKALRlltQERDQLQE--KQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAV 220
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEELRDRLE---ECRVAAQAhnEEAESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 221 LKETELDCLRDKLQKVISERDSLQTQLKNERDERELYKS-----HVRSAELENTKLSAELQMLKAVEL------------ 283
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdelREREAELEATLRTARERVEEAEALleagkcpecgqp 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 284 -----------NREVTIAQYQEELHRLRTERDTHPAETGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELY 352
Cdd:PRK02224 461 vegsphvetieEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
250 260
....*....|....*....|....*....
gi 251765105 353 RVRQEAEELRAHLAEAQEECRHAQDQLDR 381
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-340 |
7.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 145 DDGNSDILV---RVEEVQQECKELQKALRLLTQERDQLqEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVL 221
Cdd:COG4913 681 DASSDDLAAleeQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 222 KETELDCLRDKLQKvisERDSLQTQLKNERDE-RELYKSHVRSAELENTKLSAELQmlkavelnrevTIAQYQEELHRLR 300
Cdd:COG4913 760 GDAVERELRENLEE---RIDALRARLNRAEEElERAMRAFNREWPAETADLDADLE-----------SLPEYLALLDRLE 825
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 251765105 301 TErdthpaetGLKEQLRQAEEQL-QATRQQAAMLGSELRDA 340
Cdd:COG4913 826 ED--------GLPEYEERFKELLnENSIEFVADLLSKLRRA 858
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-593 |
7.48e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 144 EDDGNSDILVRVEEVQQeCKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDllkiTQKAVLKE 223
Cdd:PTZ00121 1275 EEARKADELKKAEEKKK-ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAK 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 224 TELDCLRDKLQKviSERDSLQTQLKNERDER---ELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLR 300
Cdd:PTZ00121 1350 AEAEAAADEAEA--AEEKAEAAEKKKEEAKKkadAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 301 TERDTHPAETGLKEQLRQAEEqlqATRQQAAMLGSELRDASGGRDRTMTELYRVRQE---AEELRAHLAEAQEECRHAQD 377
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADE---AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkADEAKKKAEEAKKKADEAKK 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 378 QLDRMKNqtSQEMGRAGGGVGVASELEAELQKEVEELKlrlnmAAEHYK--EKYRECQRLRR-QVTKLTQQQETQQGDAN 454
Cdd:PTZ00121 1505 AAEAKKK--ADEAKKAEEAKKADEAKKAEEAKKADEAK-----KAEEKKkaDELKKAEELKKaEEKKKAEEAKKAEEDKN 1577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 455 RNDASTETTLELHTPDAETPSESYPAEIKTVARDVEKSRDEEGNEQEEEDEEEEECSLSVEAELACMEEKWREQCTINEN 534
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 251765105 535 LKLLLANEEKRfktQVAEKDREVSALRESlvvvTKEKERLEKQYMREGTTRSRRLEVRE 593
Cdd:PTZ00121 1658 ENKIKAAEEAK---KAEEDKKKAEEAKKA----EEDEKKAAEALKKEAEEAKKAEELKK 1709
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
141-580 |
8.62e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 141 LTVEDDGNSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIeEKEEAQSRVRQLEQDL-------L 213
Cdd:pfam05483 249 ITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKM-SLQRSMSTQKALEEDLqiatktiC 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 214 KITQKAVLKETELDCLRDKLQKVISERD----SLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTI 289
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEattcSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 290 AQYQEELHRLRTERDTHPAETGLKEQLRQAEEQL-------------------------QATRQQAAMLGSELR------ 338
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarekeihdleiqltaiktseEHYLKEVEDLKTELEkeklkn 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 339 -DASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEELKLR 417
Cdd:pfam05483 488 iELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 418 LNMAAEHYKEKYRE--------------CQRLRRQVTKLTQQQET--QQGDANRNDASTET-----------TLELHTPD 470
Cdd:pfam05483 568 LDKSEENARSIEYEvlkkekqmkilenkCNNLKKQIENKNKNIEElhQENKALKKKGSAENkqlnayeikvnKLELELAS 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 471 A----ETPSESYPAEI-------KTVARDVEKSRDEEGNEQEEEDEEEEECSLSVEAELACMEEKWREQCTINENLKL-- 537
Cdd:pfam05483 648 AkqkfEEIIDNYQKEIedkkiseEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSel 727
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 251765105 538 -LLANEEKRFKTQVAEKDREVSALRESLVVVTK--EKERLEKQYMR 580
Cdd:pfam05483 728 gLYKNKEQEQSSAKAALEIELSNIKAELLSLKKqlEIEKEEKEKLK 773
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-596 |
9.65e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 153 VRVEEVQQECKELQKALRllTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQ--KAVLKETELDCLR 230
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEE--KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElkKAAAAKKKADEAK 1424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 231 DKLQKViSERDSLQTQLKNERDERELYKSHVRSAELENTKLSAElQMLKAVELNREVTIAQYQEELHRLRTERDTHPAET 310
Cdd:PTZ00121 1425 KKAEEK-KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 311 GLKEQLRQAEEQLQatRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAhlaeaQEECRHAQDQldRMKNQTSQEM 390
Cdd:PTZ00121 1503 KKAAEAKKKADEAK--KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK-----AEELKKAEEK--KKAEEAKKAE 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 391 GRAGGGVGVASELEAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQQETQQGDANRNDASTETTLEL-HTP 469
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeELK 1653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 470 DAETPSESYPAEIKTVARDVEKSRDEEGNEQEEEDEEEEECSLSVEAELACMEEKWREQCTINENLKLLLANEEKRFKTQ 549
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 251765105 550 VAEKDREVSALR-ESLVVVTKEKERLEKQYMREGTTRSRRLEVREPVV 596
Cdd:PTZ00121 1734 EAKKEAEEDKKKaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
240-450 |
1.46e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 240 RDSLQTQLKNERDEreLYKSHVRSAELENTKLSAELQMLKAVELNREV------TIAQYQEELHRLRTERDTHPAETGLK 313
Cdd:COG4717 44 RAMLLERLEKEADE--LFKPQGRKPELNLKELKELEEELKEAEEKEEEyaelqeELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 314 EQLRQAEE---QLQATRQQAAMLGSELRDAsggrDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDrmkNQTSQEM 390
Cdd:COG4717 122 EKLLQLLPlyqELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEEL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 391 GRAGGGVGVASELEAELQKEVEELKlrlnmaaehykekyRECQRLRRQVTKLTQQQETQQ 450
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQ--------------EELEELEEELEQLENELEAAA 240
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
148-592 |
1.63e-05 |
|
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: 48.68 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 148 NSDILVRVEEVQQECKElqKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKET--- 224
Cdd:pfam12128 388 NNRDIAGIKDKLAKIRE--ARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELllq 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 225 ------ELDCLRDKLQKVISERDSLQ---TQLKNERDE--RELYKSHVRSAELENTKLSAELQ----------------- 276
Cdd:pfam12128 466 lenfdeRIERAREEQEAANAEVERLQselRQARKRRDQasEALRQASRRLEERQSALDELELQlfpqagtllhflrkeap 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 277 -------------MLKAVELNREVTIAQYQEELH----RLRTERDTHPAETGLKEQLR----QAEEQLQATRQQAAMLGS 335
Cdd:pfam12128 546 dweqsigkvispeLLHRTDLDPEVWDGSVGGELNlygvKLDLKRIDVPEWAASEEELRerldKAEEALQSAREKQAAAEE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 336 ELRDASGGRDRTMTELYRVRQEAEELRAHL----AEAQEECRHAQDQLDRMKNQTSQEMGragggvgvaseleaELQKEV 411
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALKNARLDLrrlfDEKQSEKDKKNKALAERKDSANERLN--------------SLEAQL 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 412 EELKLRLNMAAEHYKEKYRECQRLRRQVTK-LTQQQETQQGDANRNDASTETTLELHTPDAETpseSYPAEIKtvARDVE 490
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKQAYWQvVEGALDAQLALLKAAIAARRSGAKAELKALET---WYKRDLA--SLGVD 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 491 KSRDEEGNEQEEEDEEEEECSLSVEAELACMEEKWREQCTInenlklllanEEKRFKTQVAEKDREVSALRESLVVVTKE 570
Cdd:pfam12128 767 PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQ----------RRPRLATQLSNIERAISELQQQLARLIAD 836
|
490 500
....*....|....*....|..
gi 251765105 571 KERLEKQYMREGTTrSRRLEVR 592
Cdd:pfam12128 837 TKLRRAKLEMERKA-SEKQQVR 857
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
158-441 |
1.72e-05 |
|
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: 48.15 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 158 VQQECkELQKALRLLTQERDQLqEKQRQQNQELQKSLIEEkeeaQSRVRQLEQDLLKITQK--AVLKETEldclrdklqK 235
Cdd:pfam05622 165 MQRTL-QLEEELKKANALRGQL-ETYKRQVQELHGKLSEE----SKKADKLEFEYKKLEEKleALQKEKE---------R 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 236 VISERDSLQtqlknERDErELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTER------------ 303
Cdd:pfam05622 230 LIIERDTLR-----ETNE-ELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENkmlrlgqegsyr 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 304 -----------DTHPAETGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTelyrVRQEAEELRAHLAEAQEEC 372
Cdd:pfam05622 304 erltelqqlleDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSL----LKQKLEEHLEKLHEAQSEL 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251765105 373 RHAQDQLDRMKNQTSQEMGRAGGgvgvasELEAELQKEVEELKlrlnmAAEhykEKYRECQRLRRQVTK 441
Cdd:pfam05622 380 QKKKEQIEELEPKQDSNLAQKID------ELQEALRKKDEDMK-----AME---ERYKKYVEKAKSVIK 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-487 |
1.79e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 201 AQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQKVISERDSLQTQLKnerderelykshvrsaelentKLSAELQmlka 280
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---------------------ALQAEID---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 281 vELNREvtIAQYQEELHRLRTErdthpaetgLKEQLRQAEEQLQATRQQAAMLGSE-----------LRDASGGRDRTMT 349
Cdd:COG3883 69 -KLQAE--IAEAEAEIEERREE---------LGERARALYRSGGSVSYLDVLLGSEsfsdfldrlsaLSKIADADADLLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 350 ELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMgragggvgvaseleAELQKEVEELKLRLNMAAEHYKEKY 429
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ--------------AEQEALLAQLSAEEAAAEAQLAELE 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 251765105 430 RECQRLRRQVTKLTQQQETQQGDANRNDASTETTLELHTPDAETPSESYPAEIKTVAR 487
Cdd:COG3883 203 AELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
278-472 |
1.96e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 278 LKAVELNREVTIAQYQEELHRLRTERDTHPAETGLKEQLRQAEEQLQATRQQA-------------------------AM 332
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELeaeleelrleleeleleleeaqaeeYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 333 LGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKEVE 412
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 413 ELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQQETQQGDANRNDASTETTLELHTPDAE 472
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-593 |
2.00e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 231 DKLQKVISE-RDSLQTqLKNERDERELYKshvrsaelentKLSAELQMLKAVELNREVTIAqyQEELHRLRTERDTHPAE 309
Cdd:TIGR02169 187 ERLDLIIDEkRQQLER-LRREREKAERYQ-----------ALLKEKREYEGYELLKEKEAL--ERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 310 -TGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGrdrtmtELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQ 388
Cdd:TIGR02169 253 lEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 389 emgRAGGGVGVASELEaELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLtqqqetqqgdanrnDASTETTLELHT 468
Cdd:TIGR02169 327 ---LEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV--------------DKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 469 pDAETPSESYPAEIKTVARDVEKSRDEEGNEQEEEDEeeeecslsVEAELACMEEKWREQCTINENLKLLLANEEKRFKT 548
Cdd:TIGR02169 389 -DYREKLEKLKREINELKRELDRLQEELQRLSEELAD--------LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 251765105 549 QVAEK---DREVSALRESLVVVTKEKERLEKQYMR-EGTTRSRRLEVRE 593
Cdd:TIGR02169 460 LAADLskyEQELYDLKEEYDRVEKELSKLQRELAEaEAQARASEERVRG 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-554 |
2.02e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 144 EDDGNSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQdllKITQKAVLKE 223
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE---AKKADEAKKK 1478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 224 TELDCLRDKLQKVISERDSLQTQLKNERDERElykshvRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHR---LR 300
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKK------KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKadeLK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 301 TERDTHPAETGLK-EQLRQAEEQlqatRQQAAMLGSELRDASGGRDRTMTELYrvrQEAEELRAHLAEAQEECRHAQDQL 379
Cdd:PTZ00121 1553 KAEELKKAEEKKKaEEAKKAEED----KNMALRKAEEAKKAEEARIEEVMKLY---EEEKKMKAEEAKKAEEAKIKAEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 380 DRMKNQTSQEMGRAGGGVGVASELEaELQKEVEELKLRLNMAAEHYKEKYRECQRLRR--QVTKLTQQQETQQGDANRND 457
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKaeEDEKKAAEALKKEAEEAKKA 1704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 458 ASTETTLELHTPDAE---TPSESYPAEIKTVARDVEKSRDEEGNEQEEEDEEEEECSLSVEAELACMEEKWREQCTINEN 534
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEelkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
410 420
....*....|....*....|
gi 251765105 535 LKllLANEEKRFKTQVAEKD 554
Cdd:PTZ00121 1785 LD--EEDEKRRMEVDKKIKD 1802
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-323 |
2.03e-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: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEK------QRQQN--------QELQKSLIEEKEEAQSRVRQLEQDLLKITQKA 219
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREEldeleaQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 220 VLKETELDCLRDKLQKVISERDSLQTQLKNERDERElykshVRSAELEN--TKLSAELQMLKAVELNrevtiaqYQEELH 297
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAE-----AALRDLRRelRELEAEIASLERRKSN-------IPARLL 443
|
170 180
....*....|....*....|....*.
gi 251765105 298 RLRTErdthpaetgLKEQLRQAEEQL 323
Cdd:COG4913 444 ALRDA---------LAEALGLDEAEL 460
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
160-579 |
3.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 160 QECKELQKALRLLTQERDQLQEKQRQQNQ--ELQKSLIEEKEEAQSRVRQLEQ--DLLKITQKAVLKETELDCLRDKLQK 235
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEEleEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 236 V---ISERDSLQTQLKNERDERELYKSHVRSAELENT--------KLSAELQMLKAVELNREVTIAQYQEELHRLRTERD 304
Cdd:COG4717 151 LeerLEELRELEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 305 THPAETGLKEQLRQAEEQLQATRQQAAMLG-SELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQdqLDRMK 383
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLAlLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE--AEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 384 NQTSQEMGRAGGGVGVASELEAELQKEVEELkLRLNMAAEHYKEKYRECQRLRRQVtKLTQQQETQQGDANRNDASTETT 463
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEEL-LELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 464 LELHTPDAETpSESYPAEIKTVARDVEKSRDEEGNEQEEEDEEEEECSL-SVEAELACMEEKwREQC-----TINENLKL 537
Cdd:COG4717 387 LRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEELEEELeELEEELEELEEE-LEELreelaELEAELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 251765105 538 LLAN--------EEKRFKTQVAEKDREVSALRESLVVVTKEKERLEKQYM 579
Cdd:COG4717 465 LEEDgelaellqELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
138-410 |
3.35e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 138 EELLTVEDDGNSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQ-----------------NQELQKSLIEEK-- 198
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAEtelcaeaeemrarlaarKQELEEILHELEsr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 199 -EEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQKVISERDSLQTQLKNERDErelykshVRSAELENTKLSAELQM 277
Cdd:pfam01576 84 lEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEED-------ILLLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 278 LKAVELNREVTIAQYQEELHRLRTERDTHPAE-TGLKEQLRQAEEQLQATRQQAAMLGSELRDASggrdrtmTELYRVRQ 356
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKRKLEGESTDLQ-------EQIAELQA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 251765105 357 EAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKE 410
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESE 283
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-593 |
3.79e-05 |
|
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: 47.36 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 148 NSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELD 227
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 228 CLRDKLQKVISERDSLQTQLKNERDE----RELYKS---------------HVRS---AELENTkLSAELQM-------- 277
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFsegvKALLKNqsglsgilgvlseliSVDEgyeAAIEAA-LGGRLQAvvvenlna 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 278 -------LKAVELNR----EVTIAQYQEELHRLRTERDTHPAETGLKEQLRQAEEQLQA-------------TRQQAAML 333
Cdd:TIGR02168 558 akkaiafLKQNELGRvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvdDLDNALEL 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 334 GSELRDA-----------------SGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTS--------- 387
Cdd:TIGR02168 638 AKKLRPGyrivtldgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEeleeeleql 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 388 ----------------------QEMGRAGGGVGVASELEAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQ 445
Cdd:TIGR02168 718 rkeleelsrqisalrkdlarleAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 446 --QETQQGDANRNDASTETTLELHTPDAETPSESYPAEIKTVARDVEKSRDEEGNEQEEEDEEEEECSLSVEAELACMEE 523
Cdd:TIGR02168 798 lkALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 524 KWREQCTINENLKLLLANEEKrFKTQVAEKDREVSALRESLvvvTKEKERLEKQYMREGTTRSRRLEVRE 593
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEE-LSEELRELESKRSELRREL---EELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-390 |
4.56e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 166 QKALRLLTQERDQLQEKQRQQNQELQKslieekeeAQSRVRQLEQDLLKITQKAVLKETELDclrdkLQKVISERDSLQT 245
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEA--------LEAELDALQERREALQRLAEYSWDEID-----VASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 246 QLknerderelykshvrsAELENTklSAELQMLKAVELNREVTIAQYQEELHRLRTERdthpaeTGLKEQLRQAEEQLQA 325
Cdd:COG4913 676 EL----------------ERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEI------GRLEKELEQAEEELDE 731
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251765105 326 TRQQaamlgseLRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEM 390
Cdd:COG4913 732 LQDR-------LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
154-415 |
4.83e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQ--NQELQKSLIEEKEEAQSRVRQLEQDLLKITQK----AVLKETELD 227
Cdd:TIGR00606 201 KVQEHQMELKYLKQYKEKACEIRDQITSKEAQLesSREIVKSYENELDPLKNRLKEIEHNLSKIMKLdneiKALKSRKKQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 228 CLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQML--KAVELNREVTiaQYQEELHRLRTERDT 305
Cdd:TIGR00606 281 MEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLnkERRLLNQEKT--ELLVEQGRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 306 HpaetglKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQ--EAEELRAHLAEAQEECRHAQDQLDRMK 383
Cdd:TIGR00606 359 H------QEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQedEAKTAAQLCADLQSKERLKQEQADEIR 432
|
250 260 270
....*....|....*....|....*....|...
gi 251765105 384 NQTSqemgraggGVGVASELEAE-LQKEVEELK 415
Cdd:TIGR00606 433 DEKK--------GLGRTIELKKEiLEKKQEELK 457
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
155-367 |
4.90e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 155 VEEVQQECKELQKalrlLTQERDQLQEKQRQQNQELQKsLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQ 234
Cdd:COG1579 2 MPEDLRALLDLQE----LDSELDRLEHRLKELPAELAE-LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 235 KviserdsLQTQLKNERDERELykshvrsaelenTKLSAELQMLKAvelnrevTIAQYQEELHRLRTERDThpaetgLKE 314
Cdd:COG1579 77 K-------YEEQLGNVRNNKEY------------EALQKEIESLKR-------RISDLEDEILELMERIEE------LEE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 251765105 315 QLRQAEEQLQATRQQAAMLGSELRDAsggRDRTMTELYRVRQEAEELRAHLAE 367
Cdd:COG1579 125 ELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-448 |
9.27e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 149 SDILVRVEEVQQECKELQKAL--------------RLLTQE-RDQLQEKQRQqnqELqKSLIEEKEEAQSRVRQLEQDLL 213
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIeelkkakgkcpvcgRELTEEhRKELLEEYTA---EL-KRIEKELKEIEEKERKLRKELR 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 214 KItQKAVLKETELDCLRDKLQKVISERDSLQ--TQLKNERDERELYKSHVRSAELEntklsAELQMLKAvELNREvtiaq 291
Cdd:PRK03918 484 EL-EKVLKKESELIKLKELAEQLKELEEKLKkyNLEELEKKAEEYEKLKEKLIKLK-----GEIKSLKK-ELEKL----- 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 292 yqEELHRLRTErdthpaetgLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYR-------VRQEAEELRAH 364
Cdd:PRK03918 552 --EELKKKLAE---------LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNeylelkdAEKELEREEKE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 365 LAEAQEECRHAQDQLDRMKNqtsqemgragggvgvasELEaELQKEVEELKLRLNmaAEHYKEKYRECQRLRRQVTKLTQ 444
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEK-----------------RLE-ELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRA 680
|
....
gi 251765105 445 QQET 448
Cdd:PRK03918 681 ELEE 684
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
150-444 |
1.10e-04 |
|
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: 45.73 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 150 DILVRVEEVQQECKELQKALRLL---TQERDQLQEKQRQQNQELQKSLIEEKE------------------EAQSRVRQL 208
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQKreaQEEQLKKQQLLKQLRARIEELRAQEAVleetqerinrarkaaplaAHIKAVTQI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 209 EQDLLKITQKAVLKETELDCLRDKLQKVISERDSLQTQlknERDERELYKSHVRSAELENtklsaelqmlkaVELNREVT 288
Cdd:TIGR00618 306 EQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ---RRLLQTLHSQEIHIRDAHE------------VATSIREI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 289 IAQYQEELHRLRTERDTHPAETGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEA 368
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251765105 369 QEECRHAQDQLDRMKNQTSQEmgragggVGVASELEAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQ 444
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKER-------EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQD 519
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
153-451 |
1.26e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 153 VRVEEVQQECKELQK-----ALRLLTQERDQLQEKQRQQNQelqKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELD 227
Cdd:pfam05557 252 LEKEKLEQELQSWVKlaqdtGLNLRSPEDLSRRIEQLQQRE---IVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 228 CLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTiAQYQEELHRLRTERDTHP 307
Cdd:pfam05557 329 DLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMT-QKMQAHNEEMEAQLSVAE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 308 AE-TGLKEQLRQAEEQLQATRQQAamlgsELRDASggrdRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQT 386
Cdd:pfam05557 408 EElGGYKQQAQTLERELQALRQQE-----SLADPS----YSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG 478
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251765105 387 SQEMgragggvgvaseleaelqKEVEELKLRLNMAAEHYKEKY-------RECQRLRRQVTKLTQQQETQQG 451
Cdd:pfam05557 479 DYDP------------------KKTKVLHLSMNPAAEAYQQRKnqleklqAEIERLKRLLKKLEDDLEQVLR 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
154-331 |
1.31e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIE-EKEEAQSRVRQL--EQDLLKITQKAVLKETELDCLR 230
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 231 DKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDThpaet 310
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE----- 224
|
170 180
....*....|....*....|.
gi 251765105 311 gLKEQLRQAEEQLQATRQQAA 331
Cdd:COG4942 225 -LEALIARLEAEAAAAAERTP 244
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
163-427 |
1.32e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.80 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 163 KELQKALRLLTQERDQLQEKQRQQNQELQK------SLIEEKEEAQSRVRQLEQDLLKITQKAVLKETEldCLRDKLQKV 236
Cdd:pfam15905 76 KELEKEIRALVQERGEQDKRLQALEEELEKveaklnAAVREKTSLSASVASLEKQLLELTRVNELLKAK--FSEDGTQKK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 237 ISERDSLQTQLKNERDERElykshvRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDTHPAETglkEQL 316
Cdd:pfam15905 154 MSSLSMELMKLRNKLEAKM------KEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSET---EKL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 317 RQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEmgraggg 396
Cdd:pfam15905 225 LEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE------- 297
|
250 260 270
....*....|....*....|....*....|.
gi 251765105 397 vgvASELEAELQKEVEELKLRLNMAAEHYKE 427
Cdd:pfam15905 298 ---YEEKEQTLNAELEELKEKLTLEEQEHQK 325
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
155-446 |
1.33e-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: 45.49 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 155 VEEVQQECKelqkALRLLTQERDQLQEKQRQQNQELQK-----------SLIE----EKEEAQSRVRQLEQDLLKITQKA 219
Cdd:pfam15921 543 LRNVQTECE----ALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagaMQVEkaqlEKEINDRRLELQEFKILKDKKDA 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 220 VLKETE-----LDCLRDKLQKVISERDSLQTQLKNERDErelYKSHVRSAELENTKLSAELQMLKAVELNRevtiaqyQE 294
Cdd:pfam15921 619 KIRELEarvsdLELEKVKLVNAGSERLRAVKDIKQERDQ---LLNEVKTSRNELNSLSEDYEVLKRNFRNK-------SE 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 295 ELHRLRTErdthpaetgLKEQLRQAEEQLQATRQQ-AAMLGSE---LRDASGGRDRTMTElyrvRQEAEELRAH---LAE 367
Cdd:pfam15921 689 EMETTTNK---------LKMQLKSAQSELEQTRNTlKSMEGSDghaMKVAMGMQKQITAK----RGQIDALQSKiqfLEE 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 368 AQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVAS-ELEA------ELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVT 440
Cdd:pfam15921 756 AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAgELEVlrsqerRLKEKVANMEVALDKASLQFAECQDIIQRQEQESV 835
|
....*.
gi 251765105 441 KLTQQQ 446
Cdd:pfam15921 836 RLKLQH 841
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
129-431 |
1.52e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 129 QFRPATPTGEELLTVED---DGNSDIL-VRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQElqKSLIEEKEEAQSR 204
Cdd:pfam05483 353 EFEATTCSLEELLRTEQqrlEKNEDQLkIITMELQKKSSELEEMTKFKNNKEVELEELKKILAED--EKLLDEKKQFEKI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 205 VRQL---EQDLLKITQKAVLK----ETELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQ- 276
Cdd:pfam05483 431 AEELkgkEQELIFLLQAREKEihdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASd 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 277 MLKAVELNREVTIAQYQEELHRLRTERDTHPAETGLKEQLRQAEEQLqatRQQAAMLGSELrdasggrDRTMTELYRVRQ 356
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF---IQKGDEVKCKL-------DKSEENARSIEY 580
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251765105 357 EAEELRAHLAEAQEECRHAQDQLDRmKNQTSQEMGRAGGGVGVASELEAElQKEVEELKL-RLNMAAEHYKEKYRE 431
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIEN-KNKNIEELHQENKALKKKGSAENK-QLNAYEIKVnKLELELASAKQKFEE 654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
319-467 |
1.59e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 319 AEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAH---------LAEAQEECRHAQDQLDRMKNqtsqe 389
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDA----- 682
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251765105 390 mgragggvgVASELEaELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQQETQQGDANRNDASTETTLELH 467
Cdd:COG4913 683 ---------SSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-590 |
1.66e-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: 45.43 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQeKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVlkETELDCLRDKL 233
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLN-NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL--QAELEELEEEL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 234 QKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREvtiaQYQEELHRLRTERDTHPAETGLK 313
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE----GFSEGVKALLKNQSGLSGILGVL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 314 EQLRQAEEQLQA---------------TRQQAAMLGSE-LRDASGGRdRTMTELYRVR-QEAEELRAHLAEAQEECRHAQ 376
Cdd:TIGR02168 526 SELISVDEGYEAaieaalggrlqavvvENLNAAKKAIAfLKQNELGR-VTFLPLDSIKgTEIQGNDREILKNIEGFLGVA 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 377 DQLDRMKN-------------------QTSQEMGRAGGGVGVASELEAEL---------------------QKEVEELKL 416
Cdd:TIGR02168 605 KDLVKFDPklrkalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLvrpggvitggsaktnssilerRREIEELEE 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 417 RLNMAAEHYKEKYRECQRLRRQVTKLTQQQETqqgdanRNDASTETTLELHtpDAETPSESYPAEIKTVARDVEKSRDEE 496
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQ------LRKELEELSRQIS--ALRKDLARLEAEVEQLEERIAQLSKEL 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 497 GNEQEEEDEEEEECSLSVEAELACMEEKWREQCTINENLKLLLANEEkrfktQVAEKDREVSALRESLVVVTKEKERLEK 576
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRERLESLER 831
|
490
....*....|....
gi 251765105 577 QyMREGTTRSRRLE 590
Cdd:TIGR02168 832 R-IAATERRLEDLE 844
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
148-387 |
2.03e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.63 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 148 NSDILVRVEEVQQECKELQKALRLLTQE--RDQLQEKQRQQNQELQKSLIEEkEEAQSRVRQLEQDLLKITQKAVLKETE 225
Cdd:pfam05667 212 NAAELAAAQEWEEEWNSQGLASRLTPEEyrKRKRTKLLKRIAEQLRSAALAG-TEATSGASRSAQDLAELLSSFSGSSTT 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 226 LDCL--------RDKLQkVISERDSLQTQLKNERDERELYKSHvRSAELENTK-----LSAELQMLKAVELNREVTIAQY 292
Cdd:pfam05667 291 DTGLtkgsrfthTEKLQ-FTNEAPAATSSPPTKVETEEELQQQ-REEELEELQeqledLESSIQELEKEIKKLESSIKQV 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 293 QEELHRLRTERDTHPAETGLKEQ----LRQAEEQL-------QATRQQAAMLGS-----------ELRDASGGRDRTMTE 350
Cdd:pfam05667 369 EEELEELKEQNEELEKQYKVKKKtldlLPDAEENIaklqalvDASAQRLVELAGqwekhrvplieEYRALKEAKSNKEDE 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 251765105 351 LYRVRQEAEELRAHLAEAQEECR-------HAQDQLDRMKNQTS 387
Cdd:pfam05667 449 SQRKLEEIKELREKIKEVAEEAKqkeelykQLVAEYERLPKDVS 492
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
161-328 |
2.15e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 161 ECKELQKALRLLTQERDQLQEKQRQQNQELQKSLieekEEAQSRVRQLEQDLLKI----------TQKAVLKETELDCLR 230
Cdd:pfam15905 160 ELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNL----EHSKGKVAQLEEKLVSTekekieekseTEKLLEYITELSCVS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 231 DKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAEL-QMLKAVELNREVTIAQYQEELHRLRTERDThpae 309
Cdd:pfam15905 236 EQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLnEKCKLLESEKEELLREYEEKEQTLNAELEE---- 311
|
170
....*....|....*....
gi 251765105 310 tgLKEQLRQAEEQLQATRQ 328
Cdd:pfam15905 312 --LKEKLTLEEQEHQKLQQ 328
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
336-468 |
2.24e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 336 ELRDASGGRDRTMTELYRVRQEAEELRAHLAE----AQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKEV 411
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQEleaqQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLE 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 251765105 412 EELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQQETQQGDANRNDASTETTLELHT 468
Cdd:pfam09787 128 EELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQLTETLIQKQT 184
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
145-338 |
2.40e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 145 DDGNSDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLieekeeAQSRVRQLEQDLLKI-TQKAVLKE 223
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL------QSPVIQQLRAQLAELeAELAELSA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 224 TeldcLRDK---LQKVISERDSLQTQLKNERDERelykshVRSAELENTKLSAELQMLKA--VELNREV-TIAQYQEELH 297
Cdd:COG3206 285 R----YTPNhpdVIALRAQIAALRAQLQQEAQRI------LASLEAELEALQAREASLQAqlAQLEARLaELPELEAELR 354
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 251765105 298 RLRTERDThpaetgLKEQLRQAEEQLQATRQQAAMLGSELR 338
Cdd:COG3206 355 RLEREVEV------ARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-578 |
2.50e-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: 44.67 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 149 SDILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQEL------QKSLIEEKEEAQSRVRQLEQ-------DLLKI 215
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagieakINELEEEKEDKALEIKKQEWkleqlaaDLSKY 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 216 TQKAVLKETELDCLRDKLQKVISERDSLQTQLKNERDE-------RELYKSHVR------------------------SA 264
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrggravEEVLKASIQgvhgtvaqlgsvgeryataievaaGN 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 265 ELENTKLSAELQMLKAVELNREVT-----------IAQYQEELHRLRT-------------ERDTHPA------ETGLKE 314
Cdd:TIGR02169 548 RLNNVVVEDDAVAKEAIELLKRRKagratflplnkMRDERRDLSILSEdgvigfavdlvefDPKYEPAfkyvfgDTLVVE 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 315 QLRQAEEQLQATRQqaAMLGSELRDASGgrdrTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAG 394
Cdd:TIGR02169 628 DIEAARRLMGKYRM--VTLEGELFEKSG----AMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIE 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 395 GGVGVASELEAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQQETQQGDANRNDAS-TETTLELHTPDAE- 472
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARiEELEEDLHKLEEAl 781
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 473 -----TPSESYPAEIKTVARDVEKSRDEEGNEQEEEDEEEEECSLSVEAELACMEEKWREQCTINENLKLLLANEE---- 543
Cdd:TIGR02169 782 ndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlng 861
|
490 500 510
....*....|....*....|....*....|....*..
gi 251765105 544 --KRFKTQVAEKDREVSALRESLVVVTKEKERLEKQY 578
Cdd:TIGR02169 862 kkEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
156-353 |
2.56e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 156 EEVQQE----CKELQKALRLLTQERDQLQEKQRQQNQEL-----QKSLIEEKEEAQSRVRQL-EQDLLKITQkavlketE 225
Cdd:pfam09787 50 EELRQErdllREEIQKLRGQIQQLRTELQELEAQQQEEAessreQLQELEEQLATERSARREaEAELERLQE-------E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 226 LDCLRDKLQKvisERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVelnrEVTIAQYQEELHRLRTERDT 305
Cdd:pfam09787 123 LRYLEEELRR---SKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQL----TETLIQKQTMLEALSTEKNS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 251765105 306 hpaetgLKEQLRQAEEQL----QATRQQAAMLGSELRDASGGRDRTMTELYR 353
Cdd:pfam09787 196 ------LVLQLERMEQQIkelqGEGSNGTSINMEGISDGEGTRLRNVPGLFS 241
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
138-577 |
2.64e-04 |
|
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: 44.58 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 138 EELLTVEDDGNSDILVRVEEVQQEC---KELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLK 214
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEekeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 215 ITQKAVLKETELDCLRDKLQKVISERDSL-QTQLKNERDERELYKSHVRSAELENTKLS-AELQMLKAVELNREVTIA-- 290
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELeKLQEKLEQLEEELLAKKKLESERLSSAAKlKEEELELKSEEEKEAQLLle 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 291 ---QYQEELHRLRTERDTHPAETGLKEQLRQAEEQLQATRQ--QAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHL 365
Cdd:pfam02463 413 larQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELekQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 366 AEAQE-------------------------------------------------------------------ECRHAQDQ 378
Cdd:pfam02463 493 QKLEErsqkeskarsglkvllalikdgvggriisahgrlgdlgvavenykvaistavivevsatadeveerqKLVRALTE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 379 LDRMKNQTSQEMGRAGGGVGVASELE-----AELQKEVEELKLRLNMAAEHYKEKYRECQ----RLRRQVTKLTQQQETQ 449
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKSIAVLEidpilNLAQLDKATLEADEDDKRAKVVEGILKDTeltkLKESAKAKESGLRKGV 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 450 QGDANRNDASTETTLELHTPDAETPSESYPAEIKTVARDVEKSRDEEGNEQEEEDEEEEECSLSVEAELACMEEKWREQC 529
Cdd:pfam02463 653 SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD 732
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 251765105 530 TINENLKLLLANEEKRFKTQVAEKDREVSALRESLVVVTKEKERLEKQ 577
Cdd:pfam02463 733 KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
264-418 |
3.35e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.57 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 264 AELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDTHPAETGLKEQLRQAEEQLQATRQQA-AMLGSELRDASG 342
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAqAQLAQAQIDLAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 343 GRDrTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRM---KNQTSQEMGRAGGGVGVASELE-AELQKEVEELKLRL 418
Cdd:pfam00529 129 RRV-LAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIyvqITQSAAENQAEVRSELSGAQLQiAEAEAELKLAKLDL 207
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
744-770 |
3.80e-04 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 38.39 E-value: 3.80e-04
10 20
....*....|....*....|....*..
gi 251765105 744 RVCPVCSEQFPLDCQQQLYEKHVHTHF 770
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
156-264 |
3.88e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 156 EEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQ--KSLIEEKEEAQsrvRQLEQDLLKITQKAVLKETEldclrDKL 233
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELValEGLAAELEEKQ---QELEAQLEQLQEKAAETSQE-----RKQ 216
|
90 100 110
....*....|....*....|....*....|.
gi 251765105 234 QKVISERDSLQTQLKNERDERELYKSHVRSA 264
Cdd:PRK11448 217 KRKEITDQAAKRLELSEEETRILIDQQLRKA 247
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
154-438 |
3.91e-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: 44.06 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQnQELQKSLIEEKEEAQSRVRQLEQDllkITQKAVLKETELDCLRDKL 233
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLI-ASRQEERQETSAELNQLLRTLDDQ---WKEKRDELNGELSAADAAV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 234 QKVISERDSLQTQLKNERDER-ELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQ--EELHRLRTERDTHPAET 310
Cdd:pfam12128 318 AKDRSELEALEDQHGAFLDADiETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNrrRSKIKEQNNRDIAGIKD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 311 GLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTE---LYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTS 387
Cdd:pfam12128 398 KLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEeeyRLKSRLGELKLRLNQATATPELLLQLENFDERIERAR 477
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 251765105 388 QEMGRAGGGVGVASELEAELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQ 438
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ 528
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
719-742 |
4.09e-04 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 37.94 E-value: 4.09e-04
10 20
....*....|....*....|....
gi 251765105 719 CPLCEVIFPPHFEQSSFERHVESH 742
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
746-769 |
4.09e-04 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 37.94 E-value: 4.09e-04
10 20
....*....|....*....|....
gi 251765105 746 CPVCSEQFPLDCQQQLYEKHVHTH 769
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
154-431 |
4.17e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQ-KAVLKE-----TELD 227
Cdd:COG3096 844 RRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEaQAFIQQhgkalAQLE 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 228 CLRDKLQKVISERDSLQTQLKNERDERELYKshvrsaelentklsAELQMLKAVELNREVTiaQYQEELHRLRTERDTHP 307
Cdd:COG3096 924 PLVAVLQSDPEQFEQLQADYLQAKEQQRRLK--------------QQIFALSEVVQRRPHF--SYEDAVGLLGENSDLNE 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 308 AetgLKEQLRQAE-------EQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECrhAQDQLD 380
Cdd:COG3096 988 K---LRARLEQAEearrearEQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEER--ARIRRD 1062
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 251765105 381 RMKNQTSQemgraggGVGVASELEAELQ---KEVEELKLRLNMAAEHYKEKYRE 431
Cdd:COG3096 1063 ELHEELSQ-------NRSRRSQLEKQLTrceAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
138-371 |
4.87e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 138 EELLTVEDDGNSDILV--RVEEVQQECKELQKALRLL-----TQER--DQLQEKQRQQNQELQKSLIEEKEEAQSRVRQL 208
Cdd:PHA02562 157 EDLLDISVLSEMDKLNkdKIRELNQQIQTLDMKIDHIqqqikTYNKniEEQRKKNGENIARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 209 EQ---DLLKItqkavlkETELDCLRDKLQKVISERDSLQTQLKNERDERELYKSH------VRSAELENTKLSAELQmlK 279
Cdd:PHA02562 237 EEltdELLNL-------VMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptcTQQISEGPDRITKIKD--K 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 280 AVELNREVT-----IAQYQEELHRLRTERDThpaETGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRV 354
Cdd:PHA02562 308 LKELQHSLEkldtaIDELEEIMDEFNEQSKK---LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKL 384
|
250
....*....|....*..
gi 251765105 355 RQEAEELRAHLAEAQEE 371
Cdd:PHA02562 385 QDELDKIVKTKSELVKE 401
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
156-325 |
4.89e-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: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 156 EEVQQECKELQKALRLL---TQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQ-KAVLKETE--LDCL 229
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIeqkLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEElEEELEELEaaLRDL 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 230 RDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAvelnrevTIAQYQEELHRLRTERDTHPAE 309
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE-------ELSEIEDPKGEDEEIPEEELSL 953
|
170
....*....|....*.
gi 251765105 310 TGLKEQLRQAEEQLQA 325
Cdd:TIGR02169 954 EDVQAELQRVEEEIRA 969
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
178-388 |
5.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 178 QLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQKVISERDSLQTQLKNerDERELY 257
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 258 KSHVRSAELENTKLSAELQ-MLKAVELNREVTiAQYQEELHRLRTERDthpAETGLKEQLRQAEEQLQATRQQAAMLGSE 336
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSdFLDRLSALSKIA-DADADLLEELKADKA---ELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 251765105 337 LRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQ 388
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
135-331 |
5.78e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 135 PTGEELLTVEDDGNS-DILVRVEEVQQECKELQKALrlltqerDQLQEKQRQQNQELQKSLIEEKEEAQSR-----VRQL 208
Cdd:PRK11281 54 LEAEDKLVQQDLEQTlALLDKIDRQKEETEQLKQQL-------AQAPAKLRQAQAELEALKDDNDEETRETlstlsLRQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 209 EQDLLKItqkavlketeLDCLRDkLQKVISERDS----LQTQLknERDERELYKSHVRSAELEN---------------- 268
Cdd:PRK11281 127 ESRLAQT----------LDQLQN-AQNDLAEYNSqlvsLQTQP--ERAQAALYANSQRLQQIRNllkggkvggkalrpsq 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251765105 269 -TKLSAELQMLKA-VELNREV--------TIAQYQEELHRLRTERDTHPAETgLKE-----QLRQAEEQL-QATRQQAA 331
Cdd:PRK11281 194 rVLLQAEQALLNAqNDLQRKSlegntqlqDLLQKQRDYLTARIQRLEHQLQL-LQEainskRLTLSEKTVqEAQSQDEA 271
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
174-450 |
6.85e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 174 QERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQKVISERDS-------LQTQ 246
Cdd:pfam01576 193 EERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNalkkireLEAQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 247 LKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEelhrLRTERDTHPAE--TGLKEQLRQAEEQLQ 324
Cdd:pfam01576 273 ISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE----LRSKREQEVTElkKALEEETRSHEAQLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 325 ATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELE 404
Cdd:pfam01576 349 EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQR 428
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 251765105 405 AELQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQ-QETQQ 450
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQE 475
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
156-219 |
7.41e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 7.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251765105 156 EEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKA 219
Cdd:PRK09510 90 EELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEA 153
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
225-494 |
7.54e-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: 43.13 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 225 ELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKavelnrevtiaQYQEELhrlrterd 304
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE-----------QEEEKL-------- 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 305 thpaetglKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAE----------------- 367
Cdd:TIGR02169 736 --------KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsripeiqaelskleeev 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 368 -----------------------AQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAEL---QKEVEELKLRLnma 421
Cdd:TIGR02169 808 sriearlreieqklnrltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeelEAALRDLESRL--- 884
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251765105 422 aEHYKEKYRECQRLRRQVTKLTQQQETQQGDANRNDASTETTL-----ELHTPDAETPSESYPAEIKTVARDVEKSRD 494
Cdd:TIGR02169 885 -GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLealeeELSEIEDPKGEDEEIPEEELSLEDVQAELQ 961
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
224-442 |
7.60e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 224 TELDCLRDKLQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAvELNREVTIAQYQEELHRLRTER 303
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK-EVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 304 DTHPAetGLKEQLRQAEEQLQATRQQAamlgSELRDasggRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMK 383
Cdd:PRK03918 251 EGSKR--KLEEKIRELEERIEELKKEI----EELEE----KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 251765105 384 NQTSQEMGRAGGGVGVASELEaELQKEVEELKLRLnmaaEHYKEKYRECQRLRRQVTKL 442
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLE-ELKKKLKELEKRL----EELEERHELYEEAKAKKEEL 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-455 |
7.87e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQ---QNQELQKSL------------IEEKEEAQSRVRQLEQDLLKITQK 218
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIREleeRIEELKKEIeeleekvkelkeLKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 219 AVLKETELDCLRDKLQKVISERDSLQTQLKN--------ERDERELYKSH-----VRSAELENTKLSAELQMLKAVELNR 285
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEElkkklkelEKRLEELEERHelyeeAKAKKEELERLKKRLTGLTPEKLEK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 286 EVTIA-----QYQEELHRLRTERDTHPAEtglKEQLRQAEEQLQATRQQAAMLGSELRDASGGR--DRTMTELYRVRQEA 358
Cdd:PRK03918 392 ELEELekakeEIEEEISKITARIGELKKE---IKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 359 EELRAHLAEAQEECRHAQDQLDRMKNQTSQEmgragggvgvaseleaELQKEVEELKLRLN-MAAEHYKEKYRECQRLRR 437
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKLK----------------ELAEQLKELEEKLKkYNLEELEKKAEEYEKLKE 532
|
330
....*....|....*...
gi 251765105 438 QVTKLTQQQETQQGDANR 455
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEK 550
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
154-449 |
8.51e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKslieeKEEAQsrvRQLEQDLLKITQKavlkETELDCLRDKL 233
Cdd:COG3096 383 RLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQA-----LEKAR---ALCGLPDLTPENA----EDYLAAFRAKE 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 234 QKVISERDSLQTQLknerderelykshvRSAELENTKLSAELQMLKAV--ELNREVTIAQYQEELHRLRTERDTHPAETG 311
Cdd:COG3096 451 QQATEEVLELEQKL--------------SVADAARRQFEKAYELVCKIagEVERSQAWQTARELLRRYRSQQALAQRLQQ 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 312 LKEQLRQAEeQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMG 391
Cdd:COG3096 517 LRAQLAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251765105 392 RAGGGVGVASELEAELQKEVEELKLRLN-----MAA-EHYKEKYRECQRLRRQVTKLTQQQETQ 449
Cdd:COG3096 596 ELAARAPAWLAAQDALERLREQSGEALAdsqevTAAmQQLLEREREATVERDELAARKQALESQ 659
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
154-254 |
1.03e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEK-------QRQQNqELQKSLIEEKEEAQSRVRQ---LEQDLLKITQKAVLKE 223
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEImdefneqSKKLL-ELKNKISTNKQSLITLVDKakkVKAAIEELQAEFVDNA 378
|
90 100 110
....*....|....*....|....*....|.
gi 251765105 224 TELDCLRDKLQKVISERdslqTQLKNERDER 254
Cdd:PHA02562 379 EELAKLQDELDKIVKTK----SELVKEKYHR 405
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
269-448 |
1.05e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 269 TKLSAELQMLKAVELNREVTIAQYQEELHRLRTERdthpAETGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTM 348
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG----SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 349 TELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEELKLRL------NMAA 422
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIealgpvNLLA 786
|
170 180
....*....|....*....|....*.
gi 251765105 423 EhykekyRECQRLRRQVTKLTQQQET 448
Cdd:COG1196 787 I------EEYEELEERYDFLSEQRED 806
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
178-450 |
1.09e-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: 42.42 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 178 QLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDlLKITQKAVLKETELDCLRDKLQKvisERDSLQTQLKNERDERELY 257
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEA-EKARQAEMDRQAAIYAEQERMAM---ERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 258 KSHVRSAELENTKlsaeLQMLKAVELNREVTIAQYQEELHRLRTERDTHPAETGLKEQLRQAEEQLQATRQQAAMLgsEL 337
Cdd:pfam17380 364 RIRQEEIAMEISR----MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR--EV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 338 RDASGGRDRtmtELYRVRQEAEElRAHLAEA--QEECRHAQDQLDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEELK 415
Cdd:pfam17380 438 RRLEEERAR---EMERVRLEEQE-RQQQVERlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEER 513
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 251765105 416 LRLNMAAE--------HYKEKYRECQRLRRQVTKLTQQQETQQ 450
Cdd:pfam17380 514 KRKLLEKEmeerqkaiYEEERRREAEEERRKQQEMEERRRIQE 556
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
240-454 |
1.11e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 240 RDSLQTQLK--NERDERELYKSHVrSAELENTKL---SAELQMLKAVELNREV-----TIAQYQEELHRLRTERDTHPAE 309
Cdd:PRK11281 38 EADVQAQLDalNKQKLLEAEDKLV-QQDLEQTLAlldKIDRQKEETEQLKQQLaqapaKLRQAQAELEALKDDNDEETRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 310 TGLKEQLRQAEEQLQATRQQAAMLGSELRDASG-------GRDRTMTELYRVRQEAEELRAHLA---EAQEECRHAQ-DQ 378
Cdd:PRK11281 117 TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSqlvslqtQPERAQAALYANSQRLQQIRNLLKggkVGGKALRPSQrVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 379 LDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEELKLRLNmAAEHYKEKYREC---QRL---RRQVTKLTQQQETQQGD 452
Cdd:PRK11281 197 LQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQ-RLEHQLQLLQEAinsKRLtlsEKTVQEAQSQDEAARIQ 275
|
..
gi 251765105 453 AN 454
Cdd:PRK11281 276 AN 277
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
157-248 |
1.31e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 157 EVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDcLRDKLQKV 236
Cdd:PRK00409 531 ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGY-ASVKAHEL 609
|
90
....*....|..
gi 251765105 237 ISERDSLQTQLK 248
Cdd:PRK00409 610 IEARKRLNKANE 621
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
153-388 |
1.60e-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: 42.03 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 153 VRVEEVQQECKELQKaLRLLTQERDQLQEKQRQQNQELQKSLIEEKEeaqsrvRQLEQDLLKITQKAVLKETElDCLRDK 232
Cdd:pfam17380 365 IRQEEIAMEISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEE------RQRKIQQQKVEMEQIRAEQE-EARQRE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 233 LQKVISERDSLQTQLKNERDERELYKSHVRSAELENTKlsaelqmlKAVELNREVTIAQYQEELHRLRTERDTHPAETGL 312
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKR--------KKLELEKEKRDRKRAEEQRRKILEKELEERKQAM 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 313 KEQLRQAE--EQLQATRQQAAMLGSELRDASGGR--DRTMTELYRVRQE---AEELRAHLaEAQEECRHAQDQLDRMKNQ 385
Cdd:pfam17380 509 IEEERKRKllEKEMEERQKAIYEEERRREAEEERrkQQEMEERRRIQEQmrkATEERSRL-EAMEREREMMRQIVESEKA 587
|
...
gi 251765105 386 TSQ 388
Cdd:pfam17380 588 RAE 590
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
744-771 |
1.81e-03 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 2 (CALCOCO2) and similar proteins; CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. It acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. It may play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion. CALCOCO2 contains a C2H2-type zinc binding domain.
Pssm-ID: 412014 Cd Length: 27 Bit Score: 36.27 E-value: 1.81e-03
10 20
....*....|....*....|....*...
gi 251765105 744 RVCPVCSEQFPlDCQQQLYEKHVHTHFD 771
Cdd:cd21968 1 FECPICSKIFE-ATSKQEFEDHVFCHSL 27
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
198-598 |
1.83e-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: 42.03 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 198 KEEAQSRVRQL-EQDLLKITQKAVLKETELDCLRDKLQKVISERDSLQTQLK----NERDERELYKSHVrsAELENTkls 272
Cdd:pfam15921 251 KSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiqeQARNQNSMYMRQL--SDLEST--- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 273 aelqmlkavelnrevtiaqyqeeLHRLRTErdthpaetgLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELY 352
Cdd:pfam15921 326 -----------------------VSQLRSE---------LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 353 RVRQEAEELRAHLAEAQEECRHAQDQLDRMKNQTSQEmgragggvgvaSELEAELQKEVEELKLRLNMAAEHYKEKYREC 432
Cdd:pfam15921 374 NLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGN-----------SITIDHLRRELDDRNMEVQRLEALLKAMKSEC 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 433 Q-RLRRQVTKLTQQQETQQGDANRNdASTETTLELHTPDAETPSESypaeiKTVARDVEKSRDEEGNEQEEEDEEEEECS 511
Cdd:pfam15921 443 QgQMERQMAAIQGKNESLEKVSSLT-AQLESTKEMLRKVVEELTAK-----KMTLESSERTVSDLTASLQEKERAIEATN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 512 LSVEAELACMEEKWRE-QCTINENLKLLLANEE-KRFKTQVAEKDREVSALRESLVVVTK--------------EKERLE 575
Cdd:pfam15921 517 AEITKLRSRVDLKLQElQHLKNEGDHLRNVQTEcEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvEKAQLE 596
|
410 420
....*....|....*....|...
gi 251765105 576 KQymregtTRSRRLEVREPVVLR 598
Cdd:pfam15921 597 KE------INDRRLELQEFKILK 613
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
141-390 |
1.89e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.90 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 141 LTVEDDGNSDILVRVEEVQQECKEL------QKALRLLTQE-RDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDll 213
Cdd:pfam13779 477 LRIEDGDLSDAERRLRAAQERLSEAlergasDEEIAKLMQElREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTQQ-- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 214 kitqkavlketELDCLRDKLQKVISE--RDSLQTQLKNERDERElyksHVRSAELENTKLSAELQMLKAveLNREVTIAQ 291
Cdd:pfam13779 555 -----------DLQRMLDRIEELARSgrRAEAQQMLSQLQQMLE----NLQAGQPQQQQQQGQSEMQQA--MDELGDLLR 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 292 YQEELhrlrteRDthpaetglkEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEE 371
Cdd:pfam13779 618 EQQQL------LD---------ETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQA 682
|
250 260
....*....|....*....|
gi 251765105 372 CRHA-QDQLDRMKNQTSQEM 390
Cdd:pfam13779 683 LRRRlEELQDELKELGGKEP 702
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
298-427 |
2.12e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 298 RLRTERDTHPAEtglkeqLRQAEEQLQATRQQAAMLGSELRDASggrdrtmtelyrvRQEAEELRAHLAEAQEEcrhaqd 377
Cdd:COG0542 401 RVRMEIDSKPEE------LDELERRLEQLEIEKEALKKEQDEAS-------------FERLAELRDELAELEEE------ 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 251765105 378 qLDRMKNQTSQEMGRAGGGVGVASELEA------ELQKEVEELKLRLNMAAEHYKE 427
Cdd:COG0542 456 -LEALKARWEAEKELIEEIQELKEELEQrygkipELEKELAELEEELAELAPLLRE 510
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
154-239 |
2.17e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.82 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQnqeLQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKeteldcLRDKL 233
Cdd:COG2825 55 RQAELQKLEKELQALQEKLQKEAATLSEEERQK---KERELQKKQQELQRKQQEAQQDLQKRQQELLQP------ILEKI 125
|
....*.
gi 251765105 234 QKVISE 239
Cdd:COG2825 126 QKAIKE 131
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
312-461 |
2.18e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.51 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 312 LKEQLRQA-EEQLQATRQQAAMLGSELRDASGGRDRTMTE--LYRVRQEAEEL--RAHLAEAQEECRHAQDQLDRMKNQT 386
Cdd:pfam13779 514 LMQELREAlDDYMQALAEQAQQNPQDLQQPDDPNAQEMTQqdLQRMLDRIEELarSGRRAEAQQMLSQLQQMLENLQAGQ 593
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251765105 387 SQEMGRAGGGVGVAS--ELeAELQKEVEELKlrlnmaaehykekyRECQRLRRQVTKLTQQQETQQGDANRNDASTE 461
Cdd:pfam13779 594 PQQQQQQGQSEMQQAmdEL-GDLLREQQQLL--------------DETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQ 655
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
154-255 |
2.49e-03 |
|
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: 40.29 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQ-QNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDK 232
Cdd:COG1579 53 ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132
|
90 100
....*....|....*....|...
gi 251765105 233 LQKVISERDSLQTQLKNERDERE 255
Cdd:COG1579 133 LAELEAELEEKKAELDEELAELE 155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
295-452 |
2.77e-03 |
|
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: 40.29 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 295 ELHRLRTERDTHPAE-TGLKEQLRQAEEQLQATRQQAAMLGSELRdasggrdrtmtelyRVRQEAEELRAHLAEAQEecr 373
Cdd:COG1579 18 ELDRLEHRLKELPAElAELEDELAALEARLEAAKTELEDLEKEIK--------------RLELEIEEVEARIKKYEE--- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251765105 374 haqdqldRMKNQTSQEmgragggvgvasELEAeLQKEVEELKLRLNMAAEHYKEKYRECQRLRRQVTKLTQQQETQQGD 452
Cdd:COG1579 81 -------QLGNVRNNK------------EYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
167-451 |
2.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 167 KALRLLTQERDQLQEKQRQQNQELQKslIEEKEEAQSRVRQL----------EQDLLKITQKAVLKETELDCLRDKLQKV 236
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQK--LQRLHQAFSRFIGShlavafeadpEAELRQLNRRRVELERALADHESQEQQQ 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 237 ISERDSLQTQLKnerderELYKSHVRSAELENTKLSAELQMLKAvELNR----EVTIAQYQEELHRLRTERDTHPAETGL 312
Cdd:PRK04863 864 RSQLEQAKEGLS------ALNRLLPRLNLLADETLADRVEEIRE-QLDEaeeaKRFVQQHGNALAQLEPIVSVLQSDPEQ 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 313 KEQLRQAEEQLQATRQQAAMlgselrdasggRDRTMTELYRVR-----QEA-----------EELRAHLAEAQEECRHAQ 376
Cdd:PRK04863 937 FEQLKQDYQQAQQTQRDAKQ-----------QAFALTEVVQRRahfsyEDAaemlaknsdlnEKLRQRLEQAEQERTRAR 1005
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251765105 377 DQL----DRMkNQTSQEMGRAGGGVGVASELEAELQKEVEELKLRLNMAAEhykekyrecQRLRRQVTKLTQQQETQQG 451
Cdd:PRK04863 1006 EQLrqaqAQL-AQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAE---------ERARARRDELHARLSANRS 1074
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
744-770 |
3.09e-03 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 35.55 E-value: 3.09e-03
10 20
....*....|....*....|....*..
gi 251765105 744 RVCPVCSEQFPLDCQQQLYEKHVHTHF 770
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
138-256 |
3.42e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 138 EELLTVEDDGNSDILVRVEEVQQECKELQKALRlltQERDQLQEKQRQQNQELQK--SLIEEKEEAQSRVRQLEQDLLKI 215
Cdd:pfam09787 99 EEQLATERSARREAEAELERLQEELRYLEEELR---RSKATLQSRIKDREAEIEKlrNQLTSKSQSSSSQSELENRLHQL 175
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 251765105 216 TQKAVLKETELDCLRdklqkviSERDSLQTQLknERDEREL 256
Cdd:pfam09787 176 TETLIQKQTMLEALS-------TEKNSLVLQL--ERMEQQI 207
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
155-450 |
3.48e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 155 VEEVQQECKELQKALRLLTQERDQLQEKQR---QQNQELQKSLiEEKEEAQSRVRQLEQDLLKITQ-KAVLK-------- 222
Cdd:pfam05557 120 IQRAELELQSTNSELEELQERLDLLKAKASeaeQLRQNLEKQQ-SSLAEAEQRIKELEFEIQSQEQdSEIVKnskselar 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 223 ----ETELDCLRD---KLQKVISERDSLQTQ---LKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQ- 291
Cdd:pfam05557 199 ipelEKELERLREhnkHLNENIENKLLLKEEvedLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSp 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 292 --YQEELHRLRTERDTHPAE-TGLKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYR-------VRQEAEEL 361
Cdd:pfam05557 279 edLSRRIEQLQQREIVLKEEnSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlqrrvllLTKERDGY 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 362 RAHL-------------AEAQEECRHAQDQLDRMKN-------QTSQEMGRAGGGVGVASELEAELQ--KEVEELKLRlN 419
Cdd:pfam05557 359 RAILesydkeltmsnysPQLLERIEEAEDMTQKMQAhneemeaQLSVAEEELGGYKQQAQTLERELQalRQQESLADP-S 437
|
330 340 350
....*....|....*....|....*....|.
gi 251765105 420 MAAEHYKEKYRECQRLRRQVTKLTQQQETQQ 450
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELERQRLREQKNELE 468
|
|
| transpos_IS110 |
NF033542 |
IS110 family transposase; Proteins of this family are DEDD (Asp, Glu, Asp, Asp) type ... |
164-271 |
4.49e-03 |
|
IS110 family transposase; Proteins of this family are DEDD (Asp, Glu, Asp, Asp) type transposases, which are encoded by the IS110 family elements.
Pssm-ID: 468073 [Multi-domain] Cd Length: 345 Bit Score: 40.01 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 164 ELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEE-AQSRVRQLEQDLLKITQKAVLKETELdcLRDKLQKVISERDS 242
Cdd:NF033542 118 EEQQALRALHRRREQLVKERTALKNRLRGLLAEFGIAlPKAGLAALRRQLRAILEDLDNELPPL--ARELLRRLLERLLA 195
|
90 100
....*....|....*....|....*....
gi 251765105 243 LQTQLKneRDERELyKSHVRSAELENTKL 271
Cdd:NF033542 196 LEEQIK--EIEKEI-EALAREHPDAACQR 221
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
163-341 |
4.53e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 40.40 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 163 KELQKALRL-----LTQERDQLQEKQRQQNQELqkslieekeeAQSRVRQLEQDllkITQKA-VLKETELDCLRDKLQKV 236
Cdd:pfam05701 70 EELESTKRLieelkLNLERAQTEEAQAKQDSEL----------AKLRVEEMEQG---IADEAsVAAKAQLEVAKARHAAA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 237 ISERDSLQTQLKNERDERELYKSH------------VRSAELENT--KLSAELQMLK-AVELNREvtiAQYQEELHRLRT 301
Cdd:pfam05701 137 VAELKSVKEELESLRKEYASLVSErdiaikraeeavSASKEIEKTveELTIELIATKeSLESAHA---AHLEAEEHRIGA 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 251765105 302 ----ERDTHPAETglkeQLRQAEEQLQATRQQ---AAMLGSELRDAS 341
Cdd:pfam05701 214 alarEQDKLNWEK----ELKQAEEELQRLNQQllsAKDLKSKLETAS 256
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
154-416 |
5.00e-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: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDlLKITQKAVLKETELDCLRDKL 233
Cdd:pfam15921 343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQN-KRLWDRDTGNSITIDHLRREL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 234 QKVISERDSLQTQLKNERD------ERELYKSHVRSAELEN-TKLSAELQMLKavELNREVTIAQYQEELHRLRTERDTH 306
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSecqgqmERQMAAIQGKNESLEKvSSLTAQLESTK--EMLRKVVEELTAKKMTLESSERTVS 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 307 PAETGLKEQLRQAE---EQLQATRQQAAMLGSELRDASGGRDrtmtELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMK 383
Cdd:pfam15921 500 DLTASLQEKERAIEatnAEITKLRSRVDLKLQELQHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMT 575
|
250 260 270
....*....|....*....|....*....|....*.
gi 251765105 384 NQTSQEMGRAGGGVGVASELEAELQK---EVEELKL 416
Cdd:pfam15921 576 QLVGQHGRTAGAMQVEKAQLEKEINDrrlELQEFKI 611
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
152-445 |
5.42e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 152 LVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRD 231
Cdd:TIGR00606 261 LSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 232 KLQKVISERDSLQTQlknerdeRELYKSHVRSAELENTKLSAELQMlkaVELNREVTIAQYQEELHRLRTERDTHPAETG 311
Cdd:TIGR00606 341 EKTELLVEQGRLQLQ-------ADRHQEHIRARDSLIQSLATRLEL---DGFERGPFSERQIKNFHTLVIERQEDEAKTA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 312 ------LKEQLRQAEEQLQATRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEELRA---HLAEAQEECRHAQDQLDRM 382
Cdd:TIGR00606 411 aqlcadLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssdRILELDQELRKAERELSKA 490
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251765105 383 KNQTSQEMGRAGGGVGVASELEAELQKEVEELKlrlNMAAEHYKEKYRECQRLRRQVTKLTQQ 445
Cdd:TIGR00606 491 EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQE---MEQLNHHTTTRTQMEMLTKDKMDKDEQ 550
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
746-769 |
5.89e-03 |
|
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the first one.
Pssm-ID: 412015 Cd Length: 24 Bit Score: 34.70 E-value: 5.89e-03
10 20
....*....|....*....|....
gi 251765105 746 CPVCSEQFPLDCQQQLYEKHVHTH 769
Cdd:cd21969 1 CPLCELVFPPNYDQSKFEQHVESH 24
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
154-384 |
6.45e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLqEKQRQQNQELQkSLIEEKEEAQSRVRQLEQDLLKITQKAVLKeTELDCLRDKL 233
Cdd:PRK04863 895 RVEEIREQLDEAEEAKRFVQQHGNAL-AQLEPIVSVLQ-SDPEQFEQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHF 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 234 -----QKVISE----RDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLrterd 304
Cdd:PRK04863 972 syedaAEMLAKnsdlNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL----- 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 305 THPAETGLKEQLRQAEEQLQAtrqqaamlgsELRDASGGRDRTMTELYRVRQEAEELRAHLAEAQEECRHAQDQLDRMKN 384
Cdd:PRK04863 1047 GVPADSGAEERARARRDELHA----------RLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-415 |
6.56e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 150 DILVRVEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQK--SLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELD 227
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKleKEVKELEELKEEIEELEKELESLEGSKRKLEEKIR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 228 CLRDKLQKVISERDSLQtqlKNERDERELYKShvrsaELENTKLSAELQMLKAVELNREVTIAQYQEELHRLrtERDTHP 307
Cdd:PRK03918 263 ELEERIEELKKEIEELE---EKVKELKELKEK-----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI--EERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 308 AETgLKEQLRQAEEQLQATRQQAAMLgselrdasGGRDRTMTELYRVRQEAEELRAHLA-EAQEECRHAQDQLDRMKNQT 386
Cdd:PRK03918 333 LEE-KEERLEELKKKLKELEKRLEEL--------EERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEI 403
|
250 260
....*....|....*....|....*....
gi 251765105 387 SQEMGRAGGGVGVASELEAELQKEVEELK 415
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
155-447 |
7.32e-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: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 155 VEEVQQECKELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKL- 233
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAl 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 234 -------------QKVISERDSLQTQLKNERDERELYKSHVRSAELENTKLSAELQMLKAVELNREVTIaQYQEELHRLR 300
Cdd:TIGR00618 666 sirvlpkellasrQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDL-AAREDALNQS 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 301 TERDTHPAETGLKEqlrQAEEQLQATRQQAA--MLGSELRDASGgrdrtmtELYRVRQEAEELRAHLAEAQEECRHAQDQ 378
Cdd:TIGR00618 745 LKELMHQARTVLKA---RTEAHFNNNEEVTAalQTGAELSHLAA-------EIQFFNRLREEDTHLLKTLEAEIGQEIPS 814
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251765105 379 LDRMKNQTSQEMGRAGGGVGVASELEAELQKEVEELKlrlnmaaEHYKEKYRECQRLRRQVTKLTQQQE 447
Cdd:TIGR00618 815 DEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL-------LKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
156-367 |
8.02e-03 |
|
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: 39.67 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 156 EEVQQECKELQKALRLLTQERdqlqekqrqqnqelqKSLIEEKEEAQSRVRQLE--QDLLKITQKAVLK-ETELDCLRDK 232
Cdd:pfam05622 10 DELAQRCHELDQQVSLLQEEK---------------NSLQQENKKLQERLDQLEsgDDSGTPGGKKYLLlQKQLEQLQEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 233 LQKVISERDSLqtQLKNERDERELYKSHVRSAELenTKLSAELQMLK---------AVELNR-EVTIAQYQEELHRLRTe 302
Cdd:pfam05622 75 NFRLETARDDY--RIKCEELEKEVLELQHRNEEL--TSLAEEAQALKdemdilresSDKVKKlEATVETYKKKLEDLGD- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251765105 303 rdthpaetgLKEQLRQAEEQLQATRQQAAMLGSELRDASGGrdRTMTELYrvRQEAEELRAHLAE 367
Cdd:pfam05622 150 ---------LRRQVKLLEERNAEYMQRTLQLEEELKKANAL--RGQLETY--KRQVQELHGKLSE 201
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
163-365 |
8.37e-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: 39.72 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 163 KELQKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDllKITQKAVLKETELDCLRDKLQKVISERDS 242
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE--RQQQVERLRQQEEERKRKKLELEKEKRDR 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 243 LQTQLKNERD-ERELYKSHVRSAELENTKLSAELQMlkavelnREVTIAQYQEELHRLRTERDTHPAETglkEQLRQAEE 321
Cdd:pfam17380 487 KRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEM-------EERQKAIYEEERRREAEEERRKQQEM---EERRRIQE 556
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 251765105 322 QLQATRQQAAMLGSELRDasggrdrtmTELYRVRQEAEELRAHL 365
Cdd:pfam17380 557 QMRKATEERSRLEAMERE---------REMMRQIVESEKARAEY 591
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
166-361 |
8.55e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 166 QKALRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKETELDCLRDKLQkviSERDSLQT 245
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELE---AQLEELEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 246 QLKNERDERelykshvrsaelenTKLSAELQMLKAvelnrevtiaQYQEELHRLRTERDTHPAETGLKEQLRQAEEQLQA 325
Cdd:COG3096 572 QAAEAVEQR--------------SELRQQLEQLRA----------RIKELAARAPAWLAAQDALERLREQSGEALADSQE 627
|
170 180 190
....*....|....*....|....*....|....*.
gi 251765105 326 TRQQAAMLGSELRDASGGRDRTMTELYRVRQEAEEL 361
Cdd:COG3096 628 VTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
154-345 |
8.72e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKAlRLLTQERDQLQEKQRQQNQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLK-ETELDCLRDK 232
Cdd:PRK09510 81 RKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKaEAEAKRAAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 233 LQKVISERDSLQTQLKNERDERELYKshvrSAELENTKLSAELQMLKAVELNREVTIAQYQEELHRLRTERDTHpAETGL 312
Cdd:PRK09510 160 AKKAAAEAKKKAEAEAAKKAAAEAKK----KAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAK-AAAEA 234
|
170 180 190
....*....|....*....|....*....|...
gi 251765105 313 KEQLRQAEEQLQATRQQAAMLGSELRDASGGRD 345
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLD 267
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
154-239 |
8.85e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 37.18 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251765105 154 RVEEVQQECKELQKALRLLTQERDQLQEKQRqqnQELQKSLIEEKEEAQSRVRQLEQDLLKITQKAVLKeteldcLRDKL 233
Cdd:smart00935 30 RQAELEKLEKELQKLKEKLQKDAATLSEAAR---EKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQK------ILDKI 100
|
....*.
gi 251765105 234 QKVISE 239
Cdd:smart00935 101 NKAIKE 106
|
|
| |
