|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
165-475 |
3.02e-149 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 432.42 E-value: 3.02e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 165 EKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIR-SNLEPLFESYITNLRRQLEVLVSDQARLQAERNHLQ 243
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 244 DVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLYMEEIQLLQSHISETSVIVKMD 323
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 324 NSRDLNLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRA 403
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119617029 404 KLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLREYQELMNAKLGLDIEIATYRRLLEGEESR 475
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
16-161 |
4.97e-48 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 164.83 E-value: 4.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 16 NFSSCSAMTPqNLNRFRANSVSCWSGPGFRGL------GSFGSRSVITFG---SYSPRIAAVGSRPIhCGVRFGAGCGMG 86
Cdd:pfam16208 1 GFSSCSAVVP-SRSRRSYSSVSSSRRGGGGGGggggggGGFGSRSLYNLGgskSISISVAGGGSRPG-SGFGFGGGGGGG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119617029 87 F--GDGRGVGLGPRADSCVGLGFGAGSGIGYGFGGPGFGYRVGGVGVPAAPS-ITAVTVNKSLLTPLNLEIDPNAQRV 161
Cdd:pfam16208 79 FggGFGGGGGGGFGGGGGFGGGFGGGGYGGGGFGGGGFGGRGGFGGPPCPPGgIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
151-407 |
8.04e-16 |
|
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: 80.83 E-value: 8.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 151 NLEIDPNAQRVKKDEKE-QIKTLNNKFASFIDKVRFLEQQNKLLETKwsfLQEQKcirsNLEPLFESYITNLRRQLEVLV 229
Cdd:TIGR04523 353 NSESENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQE----KLNQQKDEQIKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 230 SDQARLQAERN----------------------------HLQDVLEGFKKKYEEEvvcRANAEN---EFVALKKDVDAAF 278
Cdd:TIGR04523 426 KEIERLKETIIknnseikdltnqdsvkeliiknldntreSLETQLKVLSRSINKI---KQNLEQkqkELKSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 279 MNKSDLEANVDTLTQEIDFLKtlymEEIQLLQSHI----SETSVIVKMDNSRDLNLDgiiaevKAQYEEVARRSRADAEA 354
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLK----EKIEKLESEKkekeSKISDLEDELNKDDFELK------KENLEKEIDEKNKEIEE 572
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 119617029 355 WYQT------KYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEA 407
Cdd:TIGR04523 573 LKQTqkslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
200-478 |
9.74e-12 |
|
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: 68.17 E-value: 9.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 200 LQEQKCIRSNLEpLFESYITNLRRQLEvlvsdqaRLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFm 279
Cdd:TIGR02169 176 LEELEEVEENIE-RLDLIIDEKRQQLE-------RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 280 nkSDLEANVDTLTQEIDFLKtLYMEEIQLLQSHISETsvIVKMDNSRDLNLDGIIAEVKAQYEEvARRSRADAEawyqtk 359
Cdd:TIGR02169 247 --ASLEEELEKLTEEISELE-KRLEEIEQLLEELNKK--IKDLGEEEQLRVKEKIGELEAEIAS-LERSIAEKE------ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 360 yEEMQVTAGQhcdnLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAE----------QQGEATLSDAKCKLAD 429
Cdd:TIGR02169 315 -RELEDAEER----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlraelEEVDKEFAETRDELKD 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 119617029 430 LECALQQAKQDMARQLREYQELMNAKLGLDIEIATYRRLLEGEESRLCE 478
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
261-556 |
1.16e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 63.70 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 261 ANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLktlyMEEIQLLQSHISETSVivKMDNSRDlNLDGIIAEVKAQ 340
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQA--EIDKLQA-EIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 341 YEEVARRSRADAEAWYQTKYEEMQVTAG------QHCDNLRNI----RNEINELTRLIQRL---KAEIEHAKAQRAKLEA 407
Cdd:COG3883 85 REELGERARALYRSGGSVSYLDVLLGSEsfsdflDRLSALSKIadadADLLEELKADKAELeakKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 408 AVAEAEQQGEATLSDAKCKLADL---ECALQQAKQDMARQLREYQELMNAKLGLDIEIATYRRLLEGEESRLCEGVGPVN 484
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLsaeEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119617029 485 ISVSSSRGGLVCGPEPLVAGSTLSRGGVTFSGSSSVCATSGVLASCGPSLGGARVAPATGDLLSTGTRSGSM 556
Cdd:COG3883 245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSG 316
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-451 |
3.11e-10 |
|
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: 63.54 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 169 IKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYITNLRRQLEVL-------VSDQARLQAERNH 241
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqlEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 242 LQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLY---MEEIQLLQSHISETSV 318
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 319 IVKMDNSRDLNLDGIIAEVKAQ---YEEVARRSRADAEAWYQtKYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEI 395
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEieeLEELIEELESELEALLN-ERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119617029 396 EHAKAQRAKLEAAVAEAEQQ-----------GEATLSDAKCKLADLECALQQAKQDMARQLREYQEL 451
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-476 |
1.17e-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: 58.14 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 162 KKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLqeqkcirsnleplfESYITNLRRQLEVLvsdQARLQAERNH 241
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEEL--------------RLEVSELEEEIEEL---QKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 242 LQDvLEGFKKKYEEEvvcRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKtlymEEIQLLQSHISETSVIVK 321
Cdd:TIGR02168 297 ISR-LEQQKQILRER---LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK----EELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 322 MDNSRdlnldgiIAEVKAQYEEvARRSRADAEAwyqtkyeemqvtagqhcdNLRNIRNEINELTRLIQRLKAEIEHAKAQ 401
Cdd:TIGR02168 369 ELESR-------LEELEEQLET-LRSKVAQLEL------------------QIASLNNEIERLEARLERLEDRRERLQQE 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119617029 402 RAKLEAAVAEAE-QQGEATLSDAKCKLADLECALQQAKQDMARQLREYQELMNAKLGLDIEIATYRRLLEGEESRL 476
Cdd:TIGR02168 423 IEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-474 |
1.22e-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: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 152 LEIDpNAQRVKKDEKEQIKTLNNKFASfidkvrfLEQQNKLLETKWSFLQEQKcIRSNLEplfesyITNLRRQLEVLVSD 231
Cdd:COG1196 232 LKLR-ELEAELEELEAELEELEAELEE-------LEAELAELEAELEELRLEL-EELELE------LEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 232 QARLQAERNHLQDvlegfkkkyeeevvcranaenefvalkkdvdaafmNKSDLEANVDTLTQEIDFLKtlymEEIQLLQS 311
Cdd:COG1196 297 LARLEQDIARLEE-----------------------------------RRRELEERLEELEEELAELE----EELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 312 HISETSVIVKMDNSRDLNLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQhcdnlRNIRNEINELTRLIQRL 391
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-----AELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 392 KAEIEHAKAQRAKLEAAVAEAEQ---QGEATLSDAKCKLADLECALQQAKQDMARQLREYQELMNAKLGLDIEIATYRRL 468
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
....*.
gi 119617029 469 LEGEES 474
Cdd:COG1196 493 LLLLLE 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-438 |
2.97e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 144 KSLLTPLNLEIDPNAQRVKKDE--KEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKcirSNLEPLFESyITNL 221
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKEE-IEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 222 RRQLEVLVSDQARLQAERNHLQDVLEGFKKKYE--EEVVCRANA----ENEFVALKKdvdaaFMNKSDLEANvdtltqEI 295
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKElkekAEEYIKLSE-----FYEEYLDELR------EI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 296 DFLKTLYMEEIQLLQSHISETSvivkMDNSRDLNLDGIIAEVKAQYEEVARRSRAdaeawyqtkYEEmqvtAGQHCDNLR 375
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERHEL---------YEE----AKAKKEELE 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119617029 376 NIRNEINELTrlIQRLKAEIEhaKAQRAKLEaaVAEAEQQGEATLSDAKCKLADLECALQQAK 438
Cdd:PRK03918 376 RLKKRLTGLT--PEKLEKELE--ELEKAKEE--IEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-476 |
4.12e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 221 LRRQLEVLvSDQARlQAERnhlqdvlegfKKKYEEEvvcranaenefvALKKDVDAAFMNKSDLEANVDTLTQEIDFLKt 300
Cdd:COG1196 198 LERQLEPL-ERQAE-KAER----------YRELKEE------------LKELEAELLLLKLRELEAELEELEAELEELE- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 301 lymEEIQLLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGqhcdnLRNIRNE 380
Cdd:COG1196 253 ---AELEELEAELAE--------------LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD-----IARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 381 INELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQG---EATLSDAKCKLADLECALQQAKQDMARQLREYQELMNAKLG 457
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELeeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250
....*....|....*....
gi 119617029 458 LDIEIATYRRLLEGEESRL 476
Cdd:COG1196 391 ALRAAAELAAQLEELEEAE 409
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
190-487 |
4.90e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 190 NKLLEtkwSFLQEQkcIRSNLEPLfESYITNLRRQLEVLvsdQARLQAernhLQDVLEGFKKKyeeevvcranaeNEFVA 269
Cdd:COG3206 155 NALAE---AYLEQN--LELRREEA-RKALEFLEEQLPEL---RKELEE----AEAALEEFRQK------------NGLVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 270 LKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLYmeeiQLLQSHISETSvivkmDNSRDLNLDGIIAEVKAQYEEVARRsR 349
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARL----AALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-L 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 350 ADAEAWYQTKYEEMQVTAGQhcdnLRNIRNEIN-ELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGeatlsdakckla 428
Cdd:COG3206 280 AELSARYTPNHPDVIALRAQ----IAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARL------------ 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119617029 429 dlecalqqakQDMARQLREYQELMNaklglDIEIA--TYRRLLEG-EESRLCEGVGPVNISV 487
Cdd:COG3206 344 ----------AELPELEAELRRLER-----EVEVAreLYESLLQRlEEARLAEALTVGNVRV 390
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
336-431 |
1.94e-07 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 50.33 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 336 EVKAQYEEVARRSRAD----AEAW--YQTKYE-EMQvtagQHCD---NLRNIRNEINELTRLIQRLKAEIEHAKAQRAKL 405
Cdd:pfam07926 15 EEAADAEAQLQKLQEDlekqAEIAreAQQNYErELV----LHAEdikALQALREELNELKAEIAELKAEAESAKAELEES 90
|
90 100
....*....|....*....|....*.
gi 119617029 406 EAAVAEAEQQGEATLSDAKCKLADLE 431
Cdd:pfam07926 91 EESWEEQKKELEKELSELEKRIEDLN 116
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
163-476 |
3.36e-07 |
|
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: 53.49 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 163 KDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYITNLRRQLEVLVSDQARLQAERNHL 242
Cdd:TIGR04523 92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 243 QDVLEGFKK---KYEEEVvcrANAENEFVAL--------KKDVDAAFMNK--SDLEANVDTLTQEIDFLKtlymEEIQLL 309
Cdd:TIGR04523 172 ENELNLLEKeklNIQKNI---DKIKNKLLKLelllsnlkKKIQKNKSLESqiSELKKQNNQLKDNIEKKQ----QEINEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 310 QSHISET-----SVIVKMDNSRD----------------LNLDGIIAEVKAQYEEVARRSRADaeaWYQTKYEEMQvtag 368
Cdd:TIGR04523 245 TTEISNTqtqlnQLKDEQNKIKKqlsekqkeleqnnkkiKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELK---- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 369 QHCDNLRNIRNE-------INELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLEcALQQAKQDM 441
Cdd:TIGR04523 318 NQEKKLEEIQNQisqnnkiISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDL 396
|
330 340 350
....*....|....*....|....*....|....*...
gi 119617029 442 ARQLREYQELMNAKlglDIEIATY---RRLLEGEESRL 476
Cdd:TIGR04523 397 ESKIQNQEKLNQQK---DEQIKKLqqeKELLEKEIERL 431
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
221-447 |
6.92e-07 |
|
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: 51.69 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 221 LRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEevvcranAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKT 300
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 301 LYMEEIQLLQ--SHISETSVIVKMDNSRDLNLDGIIaevkaqYEEVARRSRADAEAWYQTKYEEMQVTAgqhcdNLRNIR 378
Cdd:COG4942 105 ELAELLRALYrlGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARREQAEELRADLAELAALRA-----ELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119617029 379 NEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLRE 447
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
374-454 |
1.17e-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: 50.92 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 374 LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQ---GEATLSDAKCKLADLECALQQAKQDMARQLREYQE 450
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
....
gi 119617029 451 LMNA 454
Cdd:COG4942 109 LLRA 112
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-451 |
1.60e-06 |
|
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: 51.22 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 221 LRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEevvcranAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKt 300
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGE-------IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK- 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 301 lymEEIQLLQSHISE-TSVIVKM-----DNSRDLN---LDGIIAEVKAQYEEVARRSRADAEAwyQTKYEEMQVTAGQHC 371
Cdd:TIGR02169 758 ---SELKELEARIEElEEDLHKLeealnDLEARLShsrIPEIQAELSKLEEEVSRIEARLREI--EQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 372 DNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQgEATLSDakcKLADLECALQQAKQDMARQLREYQEL 451
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-LRDLES---RLGDLKKERDELEAQLRELERKIEEL 908
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-443 |
2.47e-06 |
|
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: 50.84 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 158 AQRVKKDEKEQIKTLNNKFASfidKVRFLEQQNKLLETKWSflQEQKCIRSNLEPLfESYITNLRRQLEVLVSDQ----- 232
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGE--EEQLRVKEKIGEL-EAEIASLERSIAEKERELedaee 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 233 --ARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKtlymEEIQLLQ 310
Cdd:TIGR02169 323 rlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR----EKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 311 SHIsetsvivkmdNSRDLNLDGIIAEVKAQYEEVARrSRADAEAwyqtkyeemqvtagqhcdnlrnIRNEINELTRLIQR 390
Cdd:TIGR02169 399 REI----------NELKRELDRLQEELQRLSEELAD-LNAAIAG----------------------IEAKINELEEEKED 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 119617029 391 LKAEIEHAKAQRAKLEAAVAEAEQQgeatLSDAKCKLADLECALQQAKQDMAR 443
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQE----LYDLKEEYDRVEKELSKLQRELAE 494
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
153-476 |
3.37e-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: 50.02 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 153 EIDPNAQRVKKDEKEqIKTLNNKFASFIDKVRFLEQ------------QNKLLETKWSFLQEQKCIrSNLEP------LF 214
Cdd:TIGR04523 139 NIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENelnllekeklniQKNIDKIKNKLLKLELLL-SNLKKkiqknkSL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 215 ESYITNLRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAfmNK--SDLEANVDTLT 292
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN--NKkiKELEKQLNQLK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 293 QEI---------DFLKTLYME------EIQLLQSHISETsvivkmdnsrdlnlDGIIAEVKAQYEEVaRRSRADAEAWYQ 357
Cdd:TIGR04523 295 SEIsdlnnqkeqDWNKELKSElknqekKLEEIQNQISQN--------------NKIISQLNEQISQL-KKELTNSESENS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 358 TKYEEMQvtagQHCDNLRNIRNE-------INELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGE----------ATL 420
Cdd:TIGR04523 360 EKQRELE----EKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllekeierlkETI 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 119617029 421 SDAKCKLADLEcalqqaKQDMARQLrEYQELMNAKLGLDIEIATYRRLLEGEESRL 476
Cdd:TIGR04523 436 IKNNSEIKDLT------NQDSVKEL-IIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
157-452 |
4.73e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 157 NAQRVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKW---------SFLQEQKCIRSNLEP----------LFESY 217
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallALLGLGGSLLSLILTiagvlflvlgLLALL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 218 ITNLRRQLEVLVSDQARLQ--AERNHLQDV-LEGFKKKYEeevVCRANAENEFVALKKDVDAAFmnksDLEANVDTLTQE 294
Cdd:COG4717 290 FLLLAREKASLGKEAEELQalPALEELEEEeLEELLAALG---LPPDLSPEELLELLDRIEELQ----ELLREAEELEEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 295 IDfLKTLYMEEIQLLQShisetsviVKMDNSRDLNLdgiIAEVKAQYEEVARRsRADAEAWYQTKYEEMQVTAGQHcdNL 374
Cdd:COG4717 363 LQ-LEELEQEIAALLAE--------AGVEDEEELRA---ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DE 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119617029 375 RNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEatlsdakckLADLECALQQAKQDMARQLREYQELM 452
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------LAELLQELEELKAELRELAEEWAALK 496
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
163-489 |
6.16e-06 |
|
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: 49.35 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 163 KDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETK---WSFLQEQKCI--------RSNLEPLFESYITnLRRQLEVLVSD 231
Cdd:pfam05557 227 KEEVEDLKRKLEREEKYREEAATLELEKEKLEQElqsWVKLAQDTGLnlrspedlSRRIEQLQQREIV-LKEENSSLTSS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 232 QARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEfvalkkdvdaafmnKSDLEANVDTLTQEIDFLKtlymeeiQLLQS 311
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL--------------VRRLQRRVLLLTKERDGYR-------AILES 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 312 HISETSvivkMDNS------RDLNLDGIIAEVKAQYEEV-ARRSRADAEAwyqTKYEEMQVTAGQHCDNLR--------- 375
Cdd:pfam05557 365 YDKELT----MSNYspqlleRIEEAEDMTQKMQAHNEEMeAQLSVAEEEL---GGYKQQAQTLERELQALRqqesladps 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 376 NIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQ--QAKQDMARQLREyqelmn 453
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEayQQRKNQLEKLQA------ 511
|
330 340 350
....*....|....*....|....*....|....*.
gi 119617029 454 aklgldiEIATYRRLLEGEESRLcEGVGPVNISVSS 489
Cdd:pfam05557 512 -------EIERLKRLLKKLEDDL-EQVLRLPETTST 539
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-476 |
8.09e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 222 RRQLEVLVSDQARLQAERNHLQDVLEGFKKKyeeevvcRANAENEFVALKKDVDAAFMnksdlEANVDTLTQEIDFLKtl 301
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAE-------LDALQERREALQRLAEYSWD-----EIDVASAEREIAELE-- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 302 ymEEIQLLQShisetsvivkmdNSRDLnldgiiAEVKAQYEEvARRSRADAEAwyqtKYEEMQVTAGQHcdnlrniRNEI 381
Cdd:COG4913 675 --AELERLDA------------SSDDL------AALEEQLEE-LEAELEELEE----ELDELKGEIGRL-------EKEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 382 NELTRLIQRLKAEIEHA-----KAQRAKLEAAVAEA-----EQQGEATLSDakcKLADLECALQQAKQDMARQLREYQEL 451
Cdd:COG4913 723 EQAEEELDELQDRLEAAedlarLELRALLEERFAAAlgdavERELRENLEE---RIDALRARLNRAEEELERAMRAFNRE 799
|
250 260 270
....*....|....*....|....*....|
gi 119617029 452 -MNAKLGLDIEIAT---YRRLLEG-EESRL 476
Cdd:COG4913 800 wPAETADLDADLESlpeYLALLDRlEEDGL 829
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
369-456 |
9.31e-06 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 46.82 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 369 QHCDNLRNIRNEINELTR----LIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEatlsdakcklaDLECALQQAKQDMA-- 442
Cdd:pfam13851 5 NHEKAFNEIKNYYNDITRnnleLIKSLKEEIAELKKKEERNEKLMSEIQQENK-----------RLTEPLQKAQEEVEel 73
|
90
....*....|....*....
gi 119617029 443 -RQLREY----QELMNAKL 456
Cdd:pfam13851 74 rKQLENYekdkQSLKNLKA 92
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
224-458 |
9.39e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 224 QLEVLVsdqaRLQAERNHLqDVLEGFKKKYEEEVvcrANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLyM 303
Cdd:COG1579 5 DLRALL----DLQELDSEL-DRLEHRLKELPAEL---AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 304 EEIQLLQSHISetsvivkmdNSRDlnLDGIIAEVkaqyeEVARRSRADAEawyqtkyeemqvtagqhcdnlrnirNEINE 383
Cdd:COG1579 76 KKYEEQLGNVR---------NNKE--YEALQKEI-----ESLKRRISDLE-------------------------DEILE 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119617029 384 LTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDM-ARQLREYQELMNAKLGL 458
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPELLALYERIRKRKNGL 190
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
334-456 |
1.39e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 334 IAEVKAQYEEVARRSRAdaeawYQTKYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAE 413
Cdd:COG4372 68 LEQARSELEQLEEELEE-----LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 119617029 414 QQgeatLSDAKCKLADLECALQQAKQDMARQLREYQELMNAKL 456
Cdd:COG4372 143 SE----IAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
374-478 |
2.04e-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: 46.07 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 374 LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQgeatLSDAKCKLADLECALQQAKQDMAR---QL----- 445
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE----LEDLEKEIKRLELEIEEVEARIKKyeeQLgnvrn 87
|
90 100 110
....*....|....*....|....*....|....
gi 119617029 446 -REYQELMNaklgldiEIATYRRLLEGEESRLCE 478
Cdd:COG1579 88 nKEYEALQK-------EIESLKRRISDLEDEILE 114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
159-319 |
2.90e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 159 QRVKKDEKEQIKTLNNKFASFIDKVRFLEQQ-----NKLLETKWSFLQEQKCIRSNLEPLFESYIT------NLRRQLEV 227
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEElaellKELEELGFESVEELEERLKELEPFYNEYLElkdaekELEREEKE 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 228 LVSDQARLQAERNHLQDV----------LEGFKKKYEEEVvcRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDF 297
Cdd:PRK03918 621 LKKLEEELDKAFEELAETekrleelrkeLEELEKKYSEEE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
170 180
....*....|....*....|....*...
gi 119617029 298 LK------TLYMEEIQLLQSHISETSVI 319
Cdd:PRK03918 699 LKeeleerEKAKKELEKLEKALERVEEL 726
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
160-451 |
4.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 160 RVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETkwsFLQEQKCIRSNLEPLFEsyITNLRRQLEVL----VSDQARL 235
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK---VLKKESELIKLKELAEQ--LKELEEKLKKYnleeLEKKAEE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 236 QAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLE--------ANVDTLTQEIDFLKTLYMEEIQ 307
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfESVEELEERLKELEPFYNEYLE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 308 LLQSHiSETSVIVKMDNSRDLNLDGI---IAEVKAQYEEVarRSRADAeawYQTKYEEmqvtagqhcDNLRNIRNEINEL 384
Cdd:PRK03918 607 LKDAE-KELEREEKELKKLEEELDKAfeeLAETEKRLEEL--RKELEE---LEKKYSE---------EEYEELREEYLEL 671
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119617029 385 TRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEaTLSDAKCKLADLECALQQAkQDMARQLREYQEL 451
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERV-EELREKVKKYKAL 736
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
219-475 |
4.21e-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: 46.71 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 219 TNLRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEidfl 298
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT---- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 299 KTLYMEEIQllqshisetSVIVKMDNSRDL--NL-------DGIIAEVK---AQYEEvaRRSRADAEAwyqTKYEEMQVT 366
Cdd:pfam01576 575 KNRLQQELD---------DLLVDLDHQRQLvsNLekkqkkfDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALS 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 367 AGQHCDNLRNIRNEINELTRLiqrLKAEIEHAKAQRAKLEAAVAEAEQQGEatlsdakckladlecALQQAKQDMARQLR 446
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQ---LRAEMEDLVSSKDDVGKNVHELERSKR---------------ALEQQVEEMKTQLE 702
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 119617029 447 ----EYQELMNAKLGLDIEI----ATYRRLLE-----GEESR 475
Cdd:pfam01576 703 eledELQATEDAKLRLEVNMqalkAQFERDLQardeqGEEKR 744
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
134-456 |
5.25e-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: 46.58 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 134 APSITAVTVNKSLLTPLNLEID---PNAQRVKKDEKEQ---IKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIR 207
Cdd:TIGR00606 656 AMLAGATAVYSQFITQLTDENQsccPVCQRVFQTEAELqefISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 208 SNLEPLFESYITNLRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEEVVC--------RANAENEFVALKKDVDAAFM 279
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKDVERKIAQQAAKL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 280 NKSDLEANVDTLTQEidflKTLYMEEIQLLQSHISETSVIVKMDNSRDLNLDGIIAEVKA---QYEEVARRSRADAEawy 356
Cdd:TIGR00606 816 QGSDLDRTVQQVNQE----KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEE--- 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 357 QTkyeEMQVTAGQHCdnLRNIRNEINELTRLIQRLKAEIEhakaQRAKLEAAVAEAEQQGEATLSDAKCKL-------AD 429
Cdd:TIGR00606 889 QL---VELSTEVQSL--IREIKDAKEQDSPLETFLEKDQQ----EKEELISSKETSNKKAQDKVNDIKEKVknihgymKD 959
|
330 340
....*....|....*....|....*..
gi 119617029 430 LECALQQAKQDMARQLREYQELMNAKL 456
Cdd:TIGR00606 960 IENKIQDGKDDYLKQKETELNTVNAQL 986
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-461 |
1.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 335 AEVKAQYEEvARRSRADAEAWYQTKyEEMQVTAGQHCDNLrnIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQ 414
Cdd:COG4913 255 EPIRELAER-YAAARERLAELEYLR-AALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 119617029 415 Q----GEATLSDAKCKLADLEcalqQAKQDMARQLREYQELMnAKLGLDIE 461
Cdd:COG4913 331 QirgnGGDRLEQLEREIERLE----RELEERERRRARLEALL-AALGLPLP 376
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-478 |
2.78e-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: 44.01 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 164 DEKEQIKTLN---NKFASFI----------DKVRF-LEQQNKLLETKWSFLQEQKCirsnlEPlfESYITNLRRQL---- 225
Cdd:pfam01576 170 EEEEKAKSLSklkNKHEAMIsdleerlkkeEKGRQeLEKAKRKLEGESTDLQEQIA-----EL--QAQIAELRAQLakke 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 226 EVLVSDQARLQAERNH----------LQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAfmnKSDLEANVDTLT--- 292
Cdd:pfam01576 243 EELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARNKAEKQRRDLGEELEAL---KTELEDTLDTTAaqq 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 293 -------QEIDFLKTLYMEEIQLLQSHISEtsviVKMDNSRDLNldgiiaEVKAQYEEvARRSRADAEAWYQTkyeemqv 365
Cdd:pfam01576 320 elrskreQEVTELKKALEEETRSHEAQLQE----MRQKHTQALE------ELTEQLEQ-AKRNKANLEKAKQA------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 366 tagqhcdnLRNIRNEINELTRLIQRLKAEIEH----AKAQRAKLEAAVAEAEQQ----------GEATLSDAKCKLADLE 431
Cdd:pfam01576 382 --------LESENAELQAELRTLQQAKQDSEHkrkkLEGQLQELQARLSESERQraelaeklskLQSELESVSSLLNEAE 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 119617029 432 CALQQAKQDMAR---QLREYQELMNAKLGLDIEIATYRRLLEGEESRLCE 478
Cdd:pfam01576 454 GKNIKLSKDVSSlesQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQE 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-478 |
2.88e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 378 RNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEA----------TLSDAKCKLADLECALQQAKQDMARQLRE 447
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlrkeleelsrQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110
....*....|....*....|....*....|.
gi 119617029 448 YQElmnaklgLDIEIATYRRLLEGEESRLCE 478
Cdd:TIGR02168 756 LTE-------LEAEIEELEERLEEAEEELAE 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
221-415 |
3.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 221 LRRQLEVLVSDQARLQAERNHLQDVLEGFKKkyeeevvcranaenefvalKKDVDAAFMNKSDLEANVDTLTQEIDFLKt 300
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEK-------------------LLQLLPLYQELEALEAELAELPERLEELE- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 301 lymEEIQLLQSHISEtsvivkmdnsrdlnldgiIAEVKAQYEEVARRSRADAEAWYQTKYEEMQvtagQHCDNLRNIRNE 380
Cdd:COG4717 153 ---ERLEELRELEEE------------------LEELEAELAELQEELEELLEQLSLATEEELQ----DLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*
gi 119617029 381 INELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQ 415
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
157-476 |
4.37e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 157 NAQRVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQkcirsnleplfesyITNLRRQLEVLVSDQARLQ 236
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--------------LESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 237 AERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAafmnksdLEANVDTLTQEIDFL-KTLYMEEIQLLQSHISE 315
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES-------LQEELAALEQELQALsEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 316 TSVIVK-----MDNSRDLNLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQHcDNLRNIRNEINELTRLIQR 390
Cdd:COG4372 195 NAEKEEelaeaEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE-VILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 391 LKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLREYQELMNAKLGLDIEIATYRRLLE 470
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
....*.
gi 119617029 471 GEESRL 476
Cdd:COG4372 354 DVLELL 359
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
153-473 |
4.47e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 153 EIDPNAQRVKKDE-KEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQ-KCI-------RSNLEPLFESYITNLRR 223
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsVCPvcgttlgEEKSNHIINHYNEKKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 224 ------QLEVLVSDqarLQAERNHLQDVLEGFKKKYEEEVVcraNAENEFVALKKDVDAaFMNK-SDLEANVDTLTQEID 296
Cdd:PRK01156 481 leekirEIEIEVKD---IDEKIVDLKKRKEYLESEEINKSI---NEYNKIESARADLED-IKIKiNELKDKHDKYEEIKN 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 297 FLKTLYMEEI-QLLQSHISETSVIVKMDNSrdlNLDGIIAEVKAQYEEVARRSR------ADAEAWYQTKYEEMQvtagQ 369
Cdd:PRK01156 554 RYKSLKLEDLdSKRTSWLNALAVISLIDIE---TNRSRSNEIKKQLNDLESRLQeieigfPDDKSYIDKSIREIE----N 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 370 HCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEaAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLREYQ 449
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
330 340
....*....|....*....|....
gi 119617029 450 ELMNAKLGLDIEIATYRRLLEGEE 473
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMK 729
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
159-452 |
6.29e-04 |
|
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: 42.57 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 159 QRVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYItnlrRQLEvlvsDQARLQAE 238
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARI----RELE----EDIKTLTQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 239 RNHLQDV-LEGFKKKYEEEVVCRANAENEFVALKKDVDAAfmnksdlEANVDTLTQEIDFLKTLYME---EIQLLQSHIS 314
Cdd:pfam07888 144 RVLERETeLERMKERAKKAGAQRKEEEAERKQLQAKLQQT-------EEELRSLSKEFQELRNSLAQrdtQVLQLQDTIT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 315 ETSVIVKMDNSRDLNLDGIIAEVKAQYEE------------------VARRSRADAEAwYQTKYEEMQVTA--------- 367
Cdd:pfam07888 217 TLTQKLTTAHRKEAENEALLEELRSLQERlnaserkveglgeelssmAAQRDRTQAEL-HQARLQAAQLTLqladaslal 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 368 -------GQHCDNLRNI----RNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQ 436
Cdd:pfam07888 296 regrarwAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV 375
|
330
....*....|....*.
gi 119617029 437 AKQDMARQLREYQELM 452
Cdd:pfam07888 376 AQKEKEQLQAEKQELL 391
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
223-451 |
6.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 223 RQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEevvcRANAENEFVALKKdvdaafmNKSDLEANVDTLTQEIDFLKTLy 302
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEA-------ELEELREELEKLEKLLQLLPLY- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 303 mEEIQLLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEvaRRSRADAEAWYQTKYEEMQVTAGQHCDNLRN-IRNEI 381
Cdd:COG4717 132 -QELEALEAELAE--------------LPERLEELEERLEE--LRELEEELEELEAELAELQEELEELLEQLSLaTEEEL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 382 NELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSdakckladlecalQQAKQDMARQLREYQEL 451
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-------------ELEAAALEERLKEARLL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
334-476 |
6.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 334 IAEVKAQYEEVarRSRADAEAWYQTKYEEMQvTAGQHCDNLRN----IRNEINELTRLIQ--RLKAEIEHAKAQRAKLEA 407
Cdd:COG4717 70 LKELKELEEEL--KEAEEKEEEYAELQEELE-ELEEELEELEAeleeLREELEKLEKLLQllPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 408 AVAEAEQQgEATLSDAKCKLADLECALQQAKQDMARQLR---------------EYQELMNAKLGLDIEIATYRRLLEGE 472
Cdd:COG4717 147 RLEELEER-LEELRELEEELEELEAELAELQEELEELLEqlslateeelqdlaeELEELQQRLAELEEELEEAQEELEEL 225
|
....
gi 119617029 473 ESRL 476
Cdd:COG4717 226 EEEL 229
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
334-442 |
7.84e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 334 IAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQhcdnlrniRNEINELTRLIQRLKAEIEHAKAQ-------RAKLE 406
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQR--------QLEIAEREREIELQEKEAEREEAEleadvrkPAEAE 317
|
90 100 110
....*....|....*....|....*....|....*.
gi 119617029 407 AAVAEAEQQGEATLSDAKCKladlecALQQAKQDMA 442
Cdd:COG2268 318 KQAAEAEAEAEAEAIRAKGL------AEAEGKRALA 347
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
232-461 |
8.01e-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: 42.47 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 232 QARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDV----------DAAF----MNKSDLEANVDTLTQEIDF 297
Cdd:pfam01576 63 RARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIqdleeqldeeEAARqklqLEKVTTEAKIKKLEEDILL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 298 L----------KTLYMEEIQLLQSHISETSVIVKMDNSRDLNLDGIIA--EVKAQYEEvarRSRADAEAWYqtkyeemqv 365
Cdd:pfam01576 143 LedqnsklskeRKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEE---KGRQELEKAK--------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 366 tagqhcdnlRNIRNEINELTRLIQRLKAEIEHAKAQRAK----LEAAVAEAEQQGeATLSDAKCKLADLECALQQAKQDM 441
Cdd:pfam01576 211 ---------RKLEGESTDLQEQIAELQAQIAELRAQLAKkeeeLQAALARLEEET-AQKNNALKKIRELEAQISELQEDL 280
|
250 260
....*....|....*....|..
gi 119617029 442 A--RQLREYQELMNAKLGLDIE 461
Cdd:pfam01576 281 EseRAARNKAEKQRRDLGEELE 302
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-396 |
8.10e-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: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 151 NLEIDPNAQRVKKDEKE-QIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYITNLRRQLEVLV 229
Cdd:TIGR02168 793 QLKEELKALREALDELRaELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 230 SDQARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLYMEEIQLL 309
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 310 QSHISETSVIVKMDNSR----------------DLNLDGIiaevkAQYEEVARRsradaeawyqtkYEEMqvtAGQHCD- 372
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEarrrlkrlenkikelgPVNLAAI-----EEYEELKER------------YDFL---TAQKEDl 1012
|
250 260
....*....|....*....|....*....
gi 119617029 373 -----NLRNIRNEINELTRliQRLKAEIE 396
Cdd:TIGR02168 1013 teakeTLEEAIEEIDREAR--ERFKDTFD 1039
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
382-444 |
1.18e-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: 39.61 E-value: 1.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119617029 382 NELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQ---GEATLSDAKCKLADLECALQQAKQDMARQ 444
Cdd:pfam11559 55 ESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-470 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 284 LEANVDTLTQEIDFLKtlymEEIQLLQSHISETSVIVKmdnsrDLNLDgiIAEVKAQYEEVARRsradaeawyQTKYEEM 363
Cdd:COG1579 22 LEHRLKELPAELAELE----DELAALEARLEAAKTELE-----DLEKE--IKRLELEIEEVEAR---------IKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 364 QvtaGQHCDN--LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDM 441
Cdd:COG1579 82 L---GNVRNNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170 180
....*....|....*....|....*....
gi 119617029 442 ARQLREYQELMnAKLGLDIeIATYRRLLE 470
Cdd:COG1579 159 EELEAEREELA-AKIPPEL-LALYERIRK 185
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
335-439 |
1.46e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.96 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 335 AEVKAQYEEvARRSRADAEAwYQTKYEEMqvtagqhcdnLRNIRNE----INELTRLIQRLKAEI-EHAKAQRAKL-EAA 408
Cdd:cd06503 33 EKIAESLEE-AEKAKEEAEE-LLAEYEEK----------LAEARAEaqeiIEEARKEAEKIKEEIlAEAKEEAERIlEQA 100
|
90 100 110
....*....|....*....|....*....|.
gi 119617029 409 VAEAEQQGEATLSDAKCKLADLecALQQAKQ 439
Cdd:cd06503 101 KAEIEQEKEKALAELRKEVADL--AVEAAEK 129
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
181-470 |
1.56e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 181 DKVRFLEQQNKLLEtkwsflqeqkcIRSNLEPLfESYITNLRRQLEVLVSDQARLQAERNHLQDVLEGFKK-------KY 253
Cdd:PRK04778 96 DKFRFRKAKHEINE-----------IESLLDLI-EEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKsllanrfSF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 254 -------EEEVvcrANAE---NEFVALKK--DVDAAFMNKSDLEANVDTLTQEIDFLKTLYME-------EIQLLQS--- 311
Cdd:PRK04778 164 gpaldelEKQL---ENLEeefSQFVELTEsgDYVEAREILDQLEEELAALEQIMEEIPELLKElqtelpdQLQELKAgyr 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 312 -------HISETSV---IVKMDNSRDLNLDGI----IAEVKAQYEEVARRsradaeawYQTKYEEMQ--VTAGQHCD-NL 374
Cdd:PRK04778 241 elveegyHLDHLDIekeIQDLKEQIDENLALLeeldLDEAEEKNEEIQER--------IDQLYDILEreVKARKYVEkNS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 375 RNIRNEINELTRLIQRLKAEIEHAK-----------------AQRAKLEAAVAEAEQQ---GEATLSDAKCKLADLECAL 434
Cdd:PRK04778 313 DTLPDFLEHAKEQNKELKEEIDRVKqsytlneselesvrqleKQLESLEKQYDEITERiaeQEIAYSELQEELEEILKQL 392
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 119617029 435 -----QQAK-QDMARQLREYQELMNAKLG-LDIEIATYRRLLE 470
Cdd:PRK04778 393 eeiekEQEKlSEMLQGLRKDELEAREKLErYRNKLHEIKRYLE 435
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
380-475 |
1.66e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 380 EINELTRL--------------IQRLKAEIEHAKAQRAKLEAAVAEAEQQGeatlSDAKCKLADLECALQQAKQDMARQL 445
Cdd:PRK09039 61 QIAELADLlslerqgnqdlqdsVANLRASLSAAEAERSRLQALLAELAGAG----AAAEGRAGELAQELDSEKQVSARAL 136
|
90 100 110
....*....|....*....|....*....|.
gi 119617029 446 REYqELMNAKL-GLDIEIATYRRLLEGEESR 475
Cdd:PRK09039 137 AQV-ELLNQQIaALRRQLAALEAALDASEKR 166
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
181-465 |
1.71e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 181 DKVRFLEQQNKLLETKWSFLQEQkcirsnleplFESYITNLRRQLEVLVSDQARLQAernhlqdvlegfkkKYEEEVVCR 260
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ----------IKTYNKNIEEQRKKNGENIARKQN--------------KYDELVEEA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 261 ANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKT---LYMEEIQLLQSH---------ISETsvivkmdnsrdl 328
Cdd:PHA02562 230 KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSkieQFQKVIKMYEKGgvcptctqqISEG------------ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 329 nlDGIIAEVKAQYEEvarrsradaeawYQTKYEEMQvtagQHCDNLRNIRNEINELTRLIQRLKAEIEhakAQRAKLEAA 408
Cdd:PHA02562 298 --PDRITKIKDKLKE------------LQHSLEKLD----TAIDELEEIMDEFNEQSKKLLELKNKIS---TNKQSLITL 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 119617029 409 VAEAeQQGEATLSDAKCKLADLECALQQAKQdmarqlrEYQELMNAKLGLDIEIATY 465
Cdd:PHA02562 357 VDKA-KKVKAAIEELQAEFVDNAEELAKLQD-------ELDKIVKTKSELVKEKYHR 405
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
160-344 |
1.89e-03 |
|
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: 41.16 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 160 RVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQ-EQKCIRSNLE-PLFESYITNLRRQLEVLVSDQARLQA 237
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKkENLEKEIDEKNKEIEELKQTQKSLKK 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 238 ERNHLQDVLegfkKKYEEevvcranaenEFVALKKDVdaafmnkSDLEANVDTLTQEIDFLKTLYmEEIQllqshisetS 317
Cdd:TIGR04523 583 KQEEKQELI----DQKEK----------EKKDLIKEI-------EEKEKKISSLEKELEKAKKEN-EKLS---------S 631
|
170 180
....*....|....*....|....*..
gi 119617029 318 VIVKMDNSrdlnLDGIIAEVKAQYEEV 344
Cdd:TIGR04523 632 IIKNIKSK----KNKLKQEVKQIKETI 654
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
373-455 |
1.91e-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: 38.72 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 373 NLRNIRNEINELTRLIQRLKAEiehAKAQRAKLEAAVAEAE------QQGEATLSDAKckLADLECALQQAKQDMARQLR 446
Cdd:smart00935 5 DVQKILQESPAGKAAQKQLEKE---FKKRQAELEKLEKELQklkeklQKDAATLSEAA--REKKEKELQKKVQEFQRKQQ 79
|
....*....
gi 119617029 447 EYQELMNAK 455
Cdd:smart00935 80 KLQQDLQKR 88
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
212-404 |
2.62e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 212 PLFESYITN-------LRRQLEvLVSDQARLQAE------RNHLqdvLEGFKKKYEEEVvcranaeNEFVALKKDVDAaF 278
Cdd:smart00787 99 PLFKEYFSAspdvkllMDKQFQ-LVKTFARLEAKkmwyewRMKL---LEGLKEGLDENL-------EGLKEDYKLLMK-E 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 279 MNKsdleanVDTLTQEIDFLKTLYMEEIQLLQSHISETSvivkmDNSRDLnLDGIIAEVKAQYEEVARRSRadaeawyqt 358
Cdd:smart00787 167 LEL------LNSIKPKLRDRKDALEEELRQLKQLEDELE-----DCDPTE-LDRAKEKLKKLLQEIMIKVK--------- 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 119617029 359 KYEEMQvtagqhcDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAK 404
Cdd:smart00787 226 KLEELE-------EELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
284-473 |
3.75e-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: 40.11 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 284 LEANVDTLTQEIDFLKTLYMEEIQLLQSHISETSVIVKMDNSRDLNLDGIIAEVKAQYEEVARRSRADAE-AWYQTKYEE 362
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 363 MQVTAGQHCDNL--------RNIRNEINELTRLIQR-------LKAEIEHAKAQRAKLEAAVAEAEQQGEA------TLS 421
Cdd:pfam05557 87 ALNKKLNEKESQladareviSCLKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLRQNlekqqsSLA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119617029 422 DAKCKLADLECALQQAKQDMA-------------------RQLRE----YQELMNAKLGLDIEIATYRRLLEGEE 473
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEivknskselaripelekelERLREhnkhLNENIENKLLLKEEVEDLKRKLEREE 241
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
372-444 |
7.34e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 37.03 E-value: 7.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119617029 372 DNLRNIRNEINELTRLIQRLKAEIEHAKAQRAK-LEAAVAEAEQQGEATLSDAKCKLADLecaLQQAKQDMARQ 444
Cdd:cd06503 37 ESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiIEEARKEAEKIKEEILAEAKEEAERI---LEQAKAEIEQE 107
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
374-439 |
7.76e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 36.76 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 374 LRNIRNEINELTRLIQRLKAEIEHAK------------AQRA----------KLEAAVAEAEQQGEATLSDAKCKLADLE 431
Cdd:COG3599 36 YERLIRENKELKEKLEELEEELEEYReleetlqktlvvAQETaeevkenaekEAELIIKEAELEAEKIIEEAQEKARKIV 115
|
....*...
gi 119617029 432 CALQQAKQ 439
Cdd:COG3599 116 REIEELKR 123
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
369-453 |
8.38e-03 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 37.89 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 369 QHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQ---GEATLSD---AKCKLADLECALQQAKQDMA 442
Cdd:pfam02321 91 QLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARyeaGLISLLDvlqAEVELLEARLELLNAEADLE 170
|
90
....*....|.
gi 119617029 443 RQLREYQELMN 453
Cdd:pfam02321 171 LALAQLEQLLG 181
|
|
| SynN |
smart00503 |
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ... |
372-453 |
8.89e-03 |
|
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p
Pssm-ID: 214699 [Multi-domain] Cd Length: 117 Bit Score: 36.55 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617029 372 DNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATlsdaKCKLADLE----------CALQQAKQDM 441
Cdd:smart00503 15 ANIQKISQNVAELQKLHEELLTPPDADKELREKLERLIDDIKRLAKEI----RAKLKELEkenlenrasgSASDRTRKAQ 90
|
90
....*....|...
gi 119617029 442 ARQL-REYQELMN 453
Cdd:smart00503 91 TEKLrKKFKEVMN 103
|
|
| |
