|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
197-512 |
6.64e-146 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 425.10 E-value: 6.64e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 197 QEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQGTSSISgtnNLEPLFENHINYLRSYLDNILGERGRLDSEL 276
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS---RLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 277 KNMEDLVEDFKKKYEDEINKRTAAENEFVTLKKDVDSAYMNKVELQAKVDALIDEIDFLRTLYDAELSQMQSHISDTSVV 356
Cdd:pfam00038 78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 357 LSMDNNRSLDLDSIIAEVRAQYEDIAQRSKAEAEALYQTKLGELQTTAGRHGDDLRNTKSEIIELNRMIQRLRAEIEGVK 436
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109148552 437 KQNANLQTAIAEAEQHGEMALKDANAKLQELQAALQQAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGEEYR 512
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
170-194 |
1.06e-12 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 66.22 E-value: 1.06e-12
10 20
....*....|....*....|....*
gi 109148552 170 IQEVTINQSLLQPLNVEIDPQIGQV 194
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
196-494 |
4.77e-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: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 196 AQEREQ-IKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQGTSSISGTNNLEPLF---ENHINYLRSYLDNILGERGR 271
Cdd:TIGR02168 672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 272 LDSELKNMEDLVEDFKKKYEDEINKRTAAENEFVTLKKDVDSAYMNKVELQAKVDALIDEIDFLRTLYDA---ELSQMQS 348
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlreRLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 349 HISDTSVVLSMDNNRSLDLDSIIAEVRAQYEDI----------------AQRSKAEAEALYQTKLGELQTTAGRHGDDLR 412
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELeelieeleseleallnERASLEEALALLRSELEELSEELRELESKRS 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 413 NTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEaeqHGEMALKDANAKLQELQAALQQAKDDLARLLRDYQELMNVK 492
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE---EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVN 988
|
..
gi 109148552 493 LA 494
Cdd:TIGR02168 989 LA 990
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-507 |
8.95e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 273 DSELKNMEDLVEDFKKKYEDEINKRTAAENEFVTLKKDVDSAYMNKVELQAKVDALIDEIDFLRTLYDAELSQMQShisd 352
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ---- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 353 tsvvlsmdnnRSLDLDSIIAEVRAQYEDIAQRSKAEAEALyqTKLGELQTTAGRHGDDLRNTKSEIIELNRMIQRLRAEI 432
Cdd:TIGR02168 752 ----------LSKELTELEAEIEELEERLEEAEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109148552 433 EGVKKQNANLQTAIAEAEQHGEMA---LKDANAKLQELQAALQQAKDDLARLLRDYQELMNVKLALDVEIATYRKLLE 507
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
367-504 |
1.20e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 367 LDSIIAEVRAQYEDIAQRSKAEAEALYQTKL--GELQTTAGRHGDDLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQT 444
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109148552 445 AIAEAEQHGEMALKDAN---AKLQELQAALQQAKDDLARLLRDYQELMNVKLALDVEIATYRK 504
Cdd:TIGR02168 324 QLEELESKLDELAEELAeleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
340-480 |
3.55e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.58 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 340 DAELSQMQSHISDTSVVLSMDNNRSLDLDSIIAEVRAQYEDiAQRSKAEAEALYQTKLGELQTTAGRHGD---DLRNTKS 416
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109148552 417 EIIELNRMIQRLRAEIEGVKKQNANLQTAIAEAEQHGemalKDANAKL----QELQAALQQAKDDLAR 480
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIadlgRRLNVALAQRVQELNR 194
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
186-510 |
1.31e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 186 EIDPQ-IGQVKAQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQGTSSISGT-------NNLEPLFENHINY 257
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTtlgeeksNHIINHYNEKKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 258 LRSYLDNILGERGRLDSE---LKNMEDLVEDFK-KKYEDEINKRTAAENEfvtLKKDVDSAYMNKvELQAKVDALIDEID 333
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEiNKSINEYNKIESARAD---LEDIKIKINELK-DKHDKYEEIKNRYK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 334 FL--------RTLYDAELSQMQSHISDTSVVLSMDNNRSL-DLDSIIAEVRAQYEDIaqrskaeaEALYQTKLGELQTTA 404
Cdd:PRK01156 557 SLkledldskRTSWLNALAVISLIDIETNRSRSNEIKKQLnDLESRLQEIEIGFPDD--------KSYIDKSIREIENEA 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 405 grhgDDLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQtAIAEAEQHGEMALKDANAKLQELQAALQQAKDDLARLLRD 484
Cdd:PRK01156 629 ----NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEST 703
|
330 340
....*....|....*....|....*.
gi 109148552 485 YQELMNVKLALDVEIATYRKLLEGEE 510
Cdd:PRK01156 704 IEILRTRINELSDRINDINETLESMK 729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-488 |
1.58e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 367 LDSIIAEVRAQYEDI-AQRSKAEAE-ALYQTKLGELQTTAGRHGDDLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQT 444
Cdd:COG1196 244 LEAELEELEAELEELeAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 109148552 445 AIAEAEQHGEMA---LKDANAKLQELQAALQQAKDDLARLLRDYQEL 488
Cdd:COG1196 324 ELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
271-479 |
2.44e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 271 RLDSELKNMEDLVEDFKKKYEDEINKRTAAE----------NEFVTLKKDVDSAYMNKVELQAKVDALIDEIDFLRTLYD 340
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADevleeheerrEELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 341 aELSQMQSHISDTSVVLSMDNN----RSLDLDSIIAEVRAQYEDI---AQRSKAEAEAL------YQTKLGELQTTAGRH 407
Cdd:PRK02224 290 -ELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAEELREEAAEL 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109148552 408 GDDLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEAEQHGEMALK---DANAKLQELQAALQQAKDDLA 479
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTARERVE 443
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
317-481 |
3.31e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.19 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 317 NKVELQAKVDALIDEI-----DFLR----------TLYDAELSQMQSHISDTSVVLSmDNNRSLDLDSIIAEVRAQYE-- 379
Cdd:COG1566 44 RVVTVAAKVSGRVTEVlvkegDRVKkgqvlarldpTDLQAALAQAEAQLAAAEAQLA-RLEAELGAEAEIAAAEAQLAaa 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 380 ----DIAQRSKAEAEALYQTKLGelqttagrhgddlrnTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEAEQhgem 455
Cdd:COG1566 123 qaqlDLAQRELERYQALYKKGAV---------------SQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEE---- 183
|
170 180
....*....|....*....|....*.
gi 109148552 456 aLKDANAKLQELQAALQQAKDDLARL 481
Cdd:COG1566 184 -LAAAQAQVAQAEAALAQAELNLART 208
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
284-507 |
4.05e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 284 EDFKKKYEDEINKRTAAENEFVTLKKDVDSAYMNKVELQAKVDALIDEIDFLRTLYDAELSQMQSHISDTSVVLSMDNNR 363
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 364 SLDLDSIIAEVRAQYEDIAQRSKAEAEAL-----YQTKLGELQTTAGRHGDDLRNTKSEIIELNRMIQRLRAEIEGVKKQ 438
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEeeleeAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109148552 439 NANLQTAIAEAEQHGEMALKDANAKLQELQAALQQAKDDLARLLRDYQELMNVKLALDVEIATYRKLLE 507
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
258-507 |
4.68e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 258 LRSYLDNILGERGRLDSELKNMEDLVEDFKKKyedeinkrtaaeNEFVTLKKDVDSAYMNKVELQAKVDALIDEIDFLRT 337
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 338 LYDAELSQMQSHISDTSVVLSmdnnrsldlDSIIAEVRAQYEDIaqrskaeaealyQTKLGELQTTAG-RHgddlrntkS 416
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ---------SPVIQQLRAQLAEL------------EAELAELSARYTpNH--------P 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 417 EIIELNRMIQRLRAEIEgvkkqnANLQTAIAEAEQhgemALKDANAKLQELQAALQQAKDDLARLLRDYQELMNVKLALD 496
Cdd:COG3206 292 DVIALRAQIAALRAQLQ------QEAQRILASLEA----ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
250
....*....|.
gi 109148552 497 VEIATYRKLLE 507
Cdd:COG3206 362 VARELYESLLQ 372
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
322-510 |
8.97e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 322 QAKVDALIDEIDFLRTLYDAELSQMQSHISDTSVVLSMDNNRSLDLDSIIAEVRAQYEDIAQRSKAEAEalyqtKLGELQ 401
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-----RRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 402 TTAGRhgddlrnTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEAEQhgemALKDANAKLQELQAALQQAKDDLARL 481
Cdd:COG1196 316 ERLEE-------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180
....*....|....*....|....*....
gi 109148552 482 LRDYQELMNVKLALDVEIATYRKLLEGEE 510
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
268-487 |
2.90e-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: 43.60 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 268 ERGRLDSELKNMEDLVEDFKKKYEDEINKRTAAENEFVTLKKDVDSAYMNKVELQAKVDALIDEIDFLRtlydAELSQMQ 347
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 348 SHISDTSVVLSMDNNRSLDL------DSIIAEVRAQY-EDIAQRSKAEAEALYQTKlgelqttagrhgDDLRNTKSEIIE 420
Cdd:COG4942 104 EELAELLRALYRLGRQPPLAlllspeDFLDAVRRLQYlKYLAPARREQAEELRADL------------AELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109148552 421 LNRMIQRLRAEIEGVKKQNANLQTAIAEAEQHGEMALKDANAKLQELQAALQQAKDDLARLLRDYQE 487
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
252-474 |
4.51e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 252 ENHINYLRSYLDNILGERGRLDSELKNMEDLVEDFKKKYEDEINKRTAAENEFVTLKKDVDsaymnkvELQAKVDALIDE 331
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 332 I-DFLRTLYdaelsQMQSHISDTSVVLSMDN-----NRSLDLDSIIAEVRAQYEDI--AQRSKAEAEALYQTKLGELQTT 403
Cdd:COG3883 88 LgERARALY-----RSGGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109148552 404 AGRHGDDLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEAEQhgEMALKDANAKLQELQAALQQA 474
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA--AAAAAAAAAAAAAAAAAAAAA 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-510 |
4.62e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 367 LDSIIAEVRAQYEDIA-QRSKAE------AEA------LYQTKLGELQTTAGRHGDDLRNTKSEIIELNRMIQRLRAEIE 433
Cdd:COG1196 191 LEDILGELERQLEPLErQAEKAEryrelkEELkeleaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 434 GVKKQNANLQTAIAEA---EQHGEMALKDANAKLQELQAALQQAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGEE 510
Cdd:COG1196 271 ELRLELEELELELEEAqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
366-509 |
5.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 366 DLDSIIAEVRAQYEDIAQRSKAEAEALYQT----KLGELQTTAGRHGD---DLRNTKSEIIELNRMIQRLRAEIEGVKKQ 438
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEYSwdeiDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109148552 439 NANLQTAIAEAEQhgemALKDANAKLQELQAALQQAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGE 509
Cdd:COG4913 708 LDELKGEIGRLEK----ELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
214-492 |
5.95e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 214 DKVRFLEQQNKVLETKWNLLQQQgtssISgtnnlepLFENHINYLRSYLDNILgergrldSELKNMEDLVEDFKKKYEDE 293
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ----IK-------TYNKNIEEQRKKNGENI-------ARKQNKYDELVEEAKTIKAE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 294 INKRTAAENEFVTLKKDVDSAY----MNKVELQAKVDALIDEIDFLRTlyDAELSQMQSHISDTsvvlsmdnnrsldlDS 369
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEG--------------PD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 370 IIAEVRAQYEDIaqrskaeaealyQTKLGELQTtagrHGDDLRNTKSEIIELNRMIQRLRAEIEgvkKQNANLQTAIAEA 449
Cdd:PHA02562 300 RITKIKDKLKEL------------QHSLEKLDT----AIDELEEIMDEFNEQSKKLLELKNKIS---TNKQSLITLVDKA 360
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 109148552 450 eqhgemalKDANAKLQELQAALQQAKDDLARLLRDYQELMNVK 492
Cdd:PHA02562 361 --------KKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTK 395
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
382-476 |
6.45e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 40.36 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 382 AQRSKAEAEALyQTKLGELQTTAGRHGDDLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEAEQHGEMALKDAN 461
Cdd:pfam10473 47 AENSKAEVETL-KAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESK 125
|
90
....*....|....*
gi 109148552 462 AKLQELQAALQQAKD 476
Cdd:pfam10473 126 TAVEMLQTQLKELNE 140
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
252-490 |
6.66e-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: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 252 ENHINYLRSYLDNILGERGRLDSELKNMEDLVEDFKKKYEDE----INKRTAAENEFVTLKKDVDSAYMNKVELQAKVDA 327
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEgyelLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 328 LIDEIDFLRtlydAELSQMQSHISDtsvvlsMDNNRSLDLDSIIAEVRAQYEDiAQRSKAEAEAlyqtklgELQTTAGRh 407
Cdd:TIGR02169 263 LEKRLEEIE----QLLEELNKKIKD------LGEEEQLRVKEKIGELEAEIAS-LERSIAEKER-------ELEDAEER- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 408 gddLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEAEQhgemALKDANAKLQELQAALQQAKDDLARL---LRD 484
Cdd:TIGR02169 324 ---LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE----ELEDLRAELEEVDKEFAETRDELKDYrekLEK 396
|
....*.
gi 109148552 485 YQELMN 490
Cdd:TIGR02169 397 LKREIN 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
320-510 |
8.06e-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: 42.06 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 320 ELQAKVDALIDEIDFLRTLYDA---ELSQMQSHISDTSVVLSMDNNRSLDLDSIIAEVRAQyEDIAQRSKAEAEALYQTK 396
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQELAALEAELAELEKE-IAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 397 LGELQTTAGR-------HGDDLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEAEQHG---EMALKDANAKLQE 466
Cdd:COG4942 110 LRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERaelEALLAELEEERAA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 109148552 467 LQAALQQAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGEE 510
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-514 |
8.47e-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: 42.74 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 362 NRSLDLDSIIAEVRAQYEDIAQRSKAEAEAlyQTKLGELQTTAGRHGDDLRNTKSEIIELNRMIQRLRAEIEGVKKQNAN 441
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAEL--RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 442 LQTAIAEAEQHGE----------MALKDANAKLQELQAALQQAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGEEY 511
Cdd:TIGR02168 752 LSKELTELEAEIEeleerleeaeEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
...
gi 109148552 512 RMS 514
Cdd:TIGR02168 832 RIA 834
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
320-488 |
1.33e-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: 40.68 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 320 ELQAKVDALIDEIDFLRTlydaELSQMQSHISDTSVVLSmdnnrslDLDSIIAEVRAQYEDIAQRSKA-----EAEALyq 394
Cdd:COG1579 28 ELPAELAELEDELAALEA----RLEAAKTELEDLEKEIK-------RLELEIEEVEARIKKYEEQLGNvrnnkEYEAL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 395 tkLGELQTTAGRHGDdlrnTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEAEQHGEMALKDANAKLQELQAALQQA 474
Cdd:COG1579 95 --QKEIESLKRRISD----LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
170
....*....|....*
gi 109148552 475 KDDL-ARLLRDYQEL 488
Cdd:COG1579 169 AAKIpPELLALYERI 183
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
366-504 |
2.04e-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: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 366 DLDSIIAEVRAQYEDI-AQRSKAEAE-ALYQTKLGELQTTAGRHGDDLRNTKSEIIELNRMIQRLRA------------- 430
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkeyea 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109148552 431 ---EIEGVKKQNANLQTAIAEAeqhgEMALKDANAKLQELQAALQQAKDDLARLLRDYQELMNvklALDVEIATYRK 504
Cdd:COG1579 94 lqkEIESLKRRISDLEDEILEL----MERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEA 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
247-507 |
2.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 247 LEPLFENhINYLRSYLDNILGERGRLDSELKNMEDLVEDFKKKYEdEINKRTAAENEfvtLKKDVDsAYMNKVELQAKVD 326
Cdd:PRK03918 233 LEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 327 ALIDEIDFLRTLYDAELSQMQSHISDtsvvLSMDNNRSLDLDSIIAEVRAQYEDIAQRSKAEAEALyqTKLGELQTTAGR 406
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYEEAK--AKKEELERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 407 HGD--------DLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAE---------------AEQHGEMALKDANAK 463
Cdd:PRK03918 381 LTGltpeklekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEYTAE 460
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 109148552 464 LQELQAALQQAKDDLARLLRDYQELMNVkLALDVEIATYRKLLE 507
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKV-LKKESELIKLKELAE 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
300-504 |
2.45e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 300 AENEFVTLKKDVDSAYMNKVELQAKVDALIDEIDFLRTLYD---AELSQMQSHISDTSVvlsmdnnrslDLDSIIAEVRA 376
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqAELEALQAEIDKLQA----------EIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 377 QYEDIAQRSKAEAEALYQTKLGELQTTAGRHGDDLRNTKSeiieLNRMIQRLRAEIEGVKKQNANLQTAIAEAEQHGEMA 456
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 109148552 457 ---LKDANAKLQELQAALQQAKDDLARLLRDYQELMNVKLALDVEIATYRK 504
Cdd:COG3883 160 ealKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
367-504 |
3.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 367 LDSIIAEVRAQYEDIAQRSKA--EAEALYQTKLGELQTTAGRHGDDLRNTKSEiiELNRMIQRLRAEIEGVKKQNANLQT 444
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELRE 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 445 AIAEAEQHGEMALKDAnaKLQELQAALQQAKDDLARLLRDYQELMNVKLALDVEIATYRK 504
Cdd:COG4717 454 ELAELEAELEQLEEDG--ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
193-347 |
4.36e-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: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 193 QVKAQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQGTSSISGTNNLEPLFENHINYLRSYLDNILGERGRL 272
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 273 DselKNMEDLVEDFKKKYEDEINKRTAAENE-----------FVTLKKDVDSAYMNKVELQ-----AKVDALIDEIDFLR 336
Cdd:TIGR00606 961 E---NKIQDGKDDYLKQKETELNTVNAQLEEcekhqekinedMRLMRQDIDTQKIQERWLQdnltlRKRENELKEVEEEL 1037
|
170
....*....|.
gi 109148552 337 TLYDAELSQMQ 347
Cdd:TIGR00606 1038 KQHLKEMGQMQ 1048
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
268-481 |
5.06e-03 |
|
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: 40.21 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 268 ERGRLDSELKNMEDLVEDFKKKYEDEINKRTAAENEFvtlKKDVDSaymnkvELQAKVDALIDEIDFLRTLYDAELSQMQ 347
Cdd:pfam12128 683 RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY---WQVVEG------ALDAQLALLKAAIAARRSGAKAELKALE 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 348 SHISDTSVVLSMDNNRSLDLDSIIAEVRAQYEDIAQRsKAEAEALYQTklgeLQTTAGRHGDDLRNTKSEI-IELNRMIQ 426
Cdd:pfam12128 754 TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-RQEVLRYFDW----YQETWLQRRPRLATQLSNIeRAISELQQ 828
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 109148552 427 RLRAEIEGVKKQNANLqtaiaEAEQHgemALKDANAKLQELQAALQQAKDDLARL 481
Cdd:pfam12128 829 QLARLIADTKLRRAKL-----EMERK---ASEKQQVRLSENLRGLRCEMSKLATL 875
|
|
| Mce4_CUP1 |
pfam11887 |
Cholesterol uptake porter CUP1 of Mce4, putative; Mce4_CUP1 is a family of putative Mce4 ... |
419-481 |
5.19e-03 |
|
Cholesterol uptake porter CUP1 of Mce4, putative; Mce4_CUP1 is a family of putative Mce4 transporters of cholesterol. The domain is found associated with pfam02470. The full TCDB classification for this family in conjunction with PF02470 is TC:3.A.1.27.4.
Pssm-ID: 432164 Cd Length: 222 Bit Score: 38.70 E-value: 5.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 419 IELNRMIQRLRAEIEGVK--KQNANLqTAIAEA-----EQHGEmALKDANAKLQELQAALQQAKDDLARL 481
Cdd:pfam11887 20 TELNTLFENLLPLLKAVDpaKLNATL-SAVAEAlrgrgERLGE-TLTDLNAYLDELNPRLPTLREDIRNL 87
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
252-460 |
5.21e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 252 ENHINYLRSYLDnilgERGRLDSELKNMEDL-VEDFKKKYEDEINKrtaAENEFVTLKKDVDsaymnkvELQAKVDALID 330
Cdd:PRK05771 56 SEALDKLRSYLP----KLNPLREEKKKVSVKsLEELIKDVEEELEK---IEKEIKELEEEIS-------ELENEIKELEQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 331 EIDFLRTL--YDAELSQMQSHiSDTSVVLSMDNNRSLDLDSIIAEVRAQYED----------IAQRSKAEAEALYQTKLG 398
Cdd:PRK05771 122 EIERLEPWgnFDLDLSLLLGF-KYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvVVVLKELSDEVEEELKKL 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 399 ELQ----TTAGRHGDDLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEA----EQHGEMALKDA 460
Cdd:PRK05771 201 GFErlelEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleieLERAEALSKFL 270
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
372-479 |
5.38e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 372 AEVRAQYEDIAQRSKAEAE-ALYQTKLGELQTTAgrhgDDLRNTKSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEA- 449
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEdKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEEt 114
|
90 100 110
....*....|....*....|....*....|.
gi 109148552 450 -EQHGEMALKDANAKLQELQAALQQAKDDLA 479
Cdd:PRK11281 115 rETLSTLSLRQLESRLAQTLDQLQNAQNDLA 145
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
199-489 |
5.89e-03 |
|
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: 39.49 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 199 REQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQgtssisgTNNLEPLFENHINYLRSYLDNI--LGERGRL-DSE 275
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE-------KDALLAQRAAHEARIRELEEDIktLTQRVLErETE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 276 LKNMEDLVEDF---KKKYEDE----INKRTAAENEFVTLKKDVDSAYMNKVELQAKVDALIDEIDFLRTLYD------AE 342
Cdd:pfam07888 152 LERMKERAKKAgaqRKEEEAErkqlQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahrkeAE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 343 LSQMQSHISDTSVVLSMDNNRSLDLDSIIAEVraqyedIAQRSKAEAEaLYQTKLGELQTT--------AGRHG------ 408
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVEGLGEELSSM------AAQRDRTQAE-LHQARLQAAQLTlqladaslALREGrarwaq 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 409 --DDLRNT----KSEIIELNRMIQRLRAEIEGVKKQNANLQTAIAEAEQHGEMALKDANAKLQELQAALQQAKDDLARLL 482
Cdd:pfam07888 305 erETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQ 384
|
....*..
gi 109148552 483 RDYQELM 489
Cdd:pfam07888 385 AEKQELL 391
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
425-486 |
5.98e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 37.68 E-value: 5.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109148552 425 IQRLRAEIEGVKKQNANLQTAIAEAEQhgemALKDANAKLQELQAALQQAKDDLARLLRDYQ 486
Cdd:pfam11559 68 IERLQSKIERLKTQLEDLERELALLQA----KERQLEKKLKTLEQKLKNEKEELQRLKNALQ 125
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
426-507 |
8.75e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 426 QRLRAEIEGVKKQNANLQTAIAEAEQHGEMA---LKDANAKLQELQAALQQAKDDLARLLRDYQELMNVKLALDVEIATY 502
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELsqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
....*
gi 109148552 503 RKLLE 507
Cdd:TIGR02169 757 KSELK 761
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
232-481 |
9.21e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 232 LLQQQGTSSISGTNNLEPLfENHINYLRSYLDNILGERGRLDSELKNMEDLVEDFKKKYEDEINKRTAAENEFVTLKKDV 311
Cdd:pfam01576 476 LLQEETRQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 312 DSAYMNKVELQAKVDALideidflrtlyDAELSQMQSHISDTSVVLsmDNNRSL---------DLDSIIAE---VRAQYE 379
Cdd:pfam01576 555 EALTQQLEEKAAAYDKL-----------EKTKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEekaISARYA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148552 380 DiaQRSKAEAEALyqtklgELQTTA---GRHGDDLRNTKSEIIELNRMiqrLRAEIEGVKKQNANLQTAIAEAEQHG--- 453
Cdd:pfam01576 622 E--ERDRAEAEAR------EKETRAlslARALEEALEAKEELERTNKQ---LRAEMEDLVSSKDDVGKNVHELERSKral 690
|
250 260
....*....|....*....|....*...
gi 109148552 454 EMALKDANAKLQELQAALQQAKDDLARL 481
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQATEDAKLRL 718
|
|
| |
