|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
165-475 |
4.29e-148 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 429.73 E-value: 4.29e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 165 EKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIR-SNLEPLFESYITNLRRQLEVLVSDQARLQAERNHLQ 243
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 244 DVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLYMEEIQLLQSHISETSVIVKMD 323
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 324 NSRDLNLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRA 403
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15431316 404 KLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLEGEESR 475
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
16-161 |
4.77e-48 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 164.83 E-value: 4.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 16 NFSSCSAMTPqNLNRFRANSVSCWSGPGFRGL------GSFGSRSVITFG---SYSPRIAAVGSRPIhCGVRFGAGCGMG 86
Cdd:pfam16208 1 GFSSCSAVVP-SRSRRSYSSVSSSRRGGGGGGggggggGGFGSRSLYNLGgskSISISVAGGGSRPG-SGFGFGGGGGGG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15431316 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 15431316 151 NLEIDPNAQRVKKDEKE-QIKTLNNKFASFIDKVRFLEQQNKLLETKwsfLQEQKcirsNLEPLFESYITNLRRQLEVLV 229
Cdd:TIGR04523 353 NSESENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQE----KLNQQKDEQIKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 230 SDQARLQAERN----------------------------HLQDVLEGFKKKYEEEvvcRANAEN---EFVALKKDVDAAF 278
Cdd:TIGR04523 426 KEIERLKETIIknnseikdltnqdsvkeliiknldntreSLETQLKVLSRSINKI---KQNLEQkqkELKSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 279 MNKSDLEANVDTLTQEIDFLKtlymEEIQLLQSHI----SETSVIVKMDNSRDLNLDgiiaevKAQYEEVARRSRADAEA 354
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLK----EKIEKLESEKkekeSKISDLEDELNKDDFELK------KENLEKEIDEKNKEIEE 572
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15431316 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 |
4.57e-11 |
|
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: 66.24 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 200 LQEQKCIRSNLEpLFESYITNLRRQLEvlvsdqaRLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFm 279
Cdd:TIGR02169 176 LEELEEVEENIE-RLDLIIDEKRQQLE-------RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 280 nkSDLEANVDTLTQEIDFLKtLYMEEIQLLQSHISETsvIVKMDNSRDLNLDGIIAEVKAQYEEvARRSRADAEawyqtk 359
Cdd:TIGR02169 247 --ASLEEELEKLTEEISELE-KRLEEIEQLLEELNKK--IKDLGEEEQLRVKEKIGELEAEIAS-LERSIAEKE------ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 360 yEEMQVTAGQhcdnLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAE----------QQGEATLSDAKCKLAD 429
Cdd:TIGR02169 315 -RELEDAEER----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlraelEEVDKEFAETRDELKD 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15431316 430 LECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLEGEESRLCE 478
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
261-556 |
1.60e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 63.31 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 261 ANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLktlyMEEIQLLQSHISETSVivKMDNSRDlNLDGIIAEVKAQ 340
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQA--EIDKLQA-EIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 341 YEEVARRSRADAEAWYQTKYEEMQVTAG------QHCDNLRNI----RNEINELTRLIQRL---KAEIEHAKAQRAKLEA 407
Cdd:COG3883 85 REELGERARALYRSGGSVSYLDVLLGSEsfsdflDRLSALSKIadadADLLEELKADKAELeakKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 408 AVAEAEQQGEATLSDAKCKLADL---ECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLEGEESRLCEGVGPVN 484
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLsaeEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15431316 485 ISVSSSRGGLVCGPEPLVAGSTLSRGGVTFSGSSSVCATSGVLASCGPSLGGARVAPATGDLLSTGTRSGSM 556
Cdd:COG3883 245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSG 316
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-443 |
4.65e-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: 62.77 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 169 IKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYITNLRRQLEVL-------VSDQARLQAERNH 241
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqlEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 242 LQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLY---MEEIQLLQSHISETSV 318
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 319 IVKMDNSRDLNLDGIIAEVKAQ---YEEVARRSRADAEAWYQtKYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEI 395
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEieeLEELIEELESELEALLN-ERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15431316 396 EHAKAQRAKLEAAVAEAEQQ-----------GEATLSDAKCKLADLECALQQAKQDMAR 443
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-446 |
1.60e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 144 KSLLTPLNLEIDPNAQRVKKDE--KEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKcirSNLEPLFESyITNL 221
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKEE-IEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 222 RRQLEVLVSDQARLQAERNHLQDVLEGFKKKYE--EEVVCRANA----ENEFVALKKdvdaaFMNKSDLEANvdtltqEI 295
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKElkekAEEYIKLSE-----FYEEYLDELR------EI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 296 DFLKTLYMEEIQLLQSHISETSvivkMDNSRDLNLDGIIAEVKAQYEEVARRSRAdaeawyqtkYEEmqvtAGQHCDNLR 375
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERHEL---------YEE----AKAKKEELE 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15431316 376 NIRNEINELTrlIQRLKAEIEhaKAQRAKLEaaVAEAEQQGEATLSDAKCKLADLECALQQAKQdmARQLC 446
Cdd:PRK03918 376 RLKKRLTGLT--PEKLEKELE--ELEKAKEE--IEEEISKITARIGELKKEIKELKKAIEELKK--AKGKC 438
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-476 |
2.09e-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: 57.37 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 162 KKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLqeqkcirsnleplfESYITNLRRQLEVLvsdQARLQAERNH 241
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEEL--------------RLEVSELEEEIEEL---QKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 242 LQDvLEGFKKKYEEEvvcRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKtlymEEIQLLQSHISETSVIVK 321
Cdd:TIGR02168 297 ISR-LEQQKQILRER---LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK----EELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 322 MDNSRdlnldgiIAEVKAQYEEvARRSRADAEAwyqtkyeemqvtagqhcdNLRNIRNEINELTRLIQRLKAEIEHAKAQ 401
Cdd:TIGR02168 369 ELESR-------LEELEEQLET-LRSKVAQLEL------------------QIASLNNEIERLEARLERLEDRRERLQQE 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15431316 402 RAKLEAAVAEAE-QQGEATLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLEGEESRL 476
Cdd:TIGR02168 423 IEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
190-463 |
6.98e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 190 NKLLEtkwSFLQEQkcIRSNLEPLfESYITNLRRQLEVLvsdQARLQAernhLQDVLEGFKKKyeeevvcranaeNEFVA 269
Cdd:COG3206 155 NALAE---AYLEQN--LELRREEA-RKALEFLEEQLPEL---RKELEE----AEAALEEFRQK------------NGLVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 270 LKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLYmeeiQLLQSHISETSvivkmDNSRDLNLDGIIAEVKAQYEEVARRsR 349
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARL----AALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-L 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 350 ADAEAWYQTKYEEMQVTAGQhcdnLRNIRNEIN-ELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGeATLSDAKCKLA 428
Cdd:COG3206 280 AELSARYTPNHPDVIALRAQ----IAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELR 354
|
250 260 270
....*....|....*....|....*....|....*
gi 15431316 429 DLecalqQAKQDMARQLceYQELMNAKLGLDIEIA 463
Cdd:COG3206 355 RL-----EREVEVAREL--YESLLQRLEEARLAEA 382
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-476 |
1.10e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 152 LEIDpNAQRVKKDEKEQIKTLNNKFASfidkvrfLEQQNKLLETKWSFLQEQKcIRSNLEplfesyITNLRRQLEVLVSD 231
Cdd:COG1196 232 LKLR-ELEAELEELEAELEELEAELEE-------LEAELAELEAELEELRLEL-EELELE------LEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 232 QARLQAERNHLQDvlegfkkkyeeevvcranaenefvalkkdvdaafmNKSDLEANVDTLTQEIDFLKtlymEEIQLLQS 311
Cdd:COG1196 297 LARLEQDIARLEE-----------------------------------RRRELEERLEELEEELAELE----EELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 312 HISETSVIVKMDNSRDLNLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQhcdnlRNIRNEINELTRLIQRL 391
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-----AELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 392 KAEIEHAKAQRAKLEAAVAEAEQQGEATLSdakcKLADLECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLEG 471
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEE----ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
....*
gi 15431316 472 EESRL 476
Cdd:COG1196 489 AAARL 493
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
336-431 |
1.62e-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: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 336 EVKAQYEEVARRSRAD----AEAW--YQTKYE-EMQvtagQHCD---NLRNIRNEINELTRLIQRLKAEIEHAKAQRAKL 405
Cdd:pfam07926 15 EEAADAEAQLQKLQEDlekqAEIAreAQQNYErELV----LHAEdikALQALREELNELKAEIAELKAEAESAKAELEES 90
|
90 100
....*....|....*....|....*.
gi 15431316 406 EAAVAEAEQQGEATLSDAKCKLADLE 431
Cdd:pfam07926 91 EESWEEQKKELEKELSELEKRIEDLN 116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-476 |
5.44e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 221 LRRQLEVLvSDQARlQAERnhlqdvlegfKKKYEEEvvcranaenefvALKKDVDAAFMNKSDLEANVDTLTQEIDFLKt 300
Cdd:COG1196 198 LERQLEPL-ERQAE-KAER----------YRELKEE------------LKELEAELLLLKLRELEAELEELEAELEELE- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 301 lymEEIQLLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGqhcdnLRNIRNE 380
Cdd:COG1196 253 ---AELEELEAELAE--------------LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD-----IARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 381 INELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQG---EATLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKLG 457
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELeeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250
....*....|....*....
gi 15431316 458 LDIEIATYRRLLEGEESRL 476
Cdd:COG1196 391 ALRAAAELAAQLEELEEAE 409
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
221-444 |
6.45e-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: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 221 LRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEevvcranAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKT 300
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 301 LYMEEIQLLQ--SHISETSVIVKMDNSRDLNLDGIIaevkaqYEEVARRSRADAEAWYQTKYEEMQVTAgqhcdNLRNIR 378
Cdd:COG4942 105 ELAELLRALYrlGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARREQAEELRADLAELAALRA-----ELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15431316 379 NEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQ 444
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
163-476 |
1.80e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 163 KDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYITNLRRQLEVLVSDQARLQAERNHL 242
Cdd:TIGR04523 92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 243 QDVLEGFKK---KYEEEVvcrANAENEFVAL--------KKDVDAAFMNK--SDLEANVDTLTQEIDFLKtlymEEIQLL 309
Cdd:TIGR04523 172 ENELNLLEKeklNIQKNI---DKIKNKLLKLelllsnlkKKIQKNKSLESqiSELKKQNNQLKDNIEKKQ----QEINEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 310 QSHISET-----SVIVKMDNSRD----------------LNLDGIIAEVKAQYEEVARRSRADaeaWYQTKYEEMQvtag 368
Cdd:TIGR04523 245 TTEISNTqtqlnQLKDEQNKIKKqlsekqkeleqnnkkiKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELK---- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 369 QHCDNLRNIRNE-------INELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLEcALQQAKQDM 441
Cdd:TIGR04523 318 NQEKKLEEIQNQisqnnkiISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDL 396
|
330 340 350
....*....|....*....|....*....|....*...
gi 15431316 442 ARQLCEYQELMNAKlglDIEIATY---RRLLEGEESRL 476
Cdd:TIGR04523 397 ESKIQNQEKLNQQK---DEQIKKLqqeKELLEKEIERL 431
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-443 |
1.80e-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: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 158 AQRVKKDEKEQIKTLNNKFASfidKVRFLEQQNKLLETKWSflQEQKCIRSNLEPLfESYITNLRRQLEVLVSDQ----- 232
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGE--EEQLRVKEKIGEL-EAEIASLERSIAEKERELedaee 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 233 --ARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKtlymEEIQLLQ 310
Cdd:TIGR02169 323 rlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR----EKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 311 SHIsetsvivkmdNSRDLNLDGIIAEVKAQYEEVARrSRADAEAwyqtkyeemqvtagqhcdnlrnIRNEINELTRLIQR 390
Cdd:TIGR02169 399 REI----------NELKRELDRLQEELQRLSEELAD-LNAAIAG----------------------IEAKINELEEEKED 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 15431316 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 15431316 153 EIDPNAQRVKKDEKEqIKTLNNKFASFIDKVRFLEQ------------QNKLLETKWSFLQEQKCIrSNLEP------LF 214
Cdd:TIGR04523 139 NIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENelnllekeklniQKNIDKIKNKLLKLELLL-SNLKKkiqknkSL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 215 ESYITNLRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAfmNK--SDLEANVDTLT 292
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN--NKkiKELEKQLNQLK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 293 QEI---------DFLKTLYME------EIQLLQSHISETsvivkmdnsrdlnlDGIIAEVKAQYEEVaRRSRADAEAWYQ 357
Cdd:TIGR04523 295 SEIsdlnnqkeqDWNKELKSElknqekKLEEIQNQISQN--------------NKIISQLNEQISQL-KKELTNSESENS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 358 TKYEEMQvtagQHCDNLRNIRNE-------INELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGE----------ATL 420
Cdd:TIGR04523 360 EKQRELE----EKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllekeierlkETI 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15431316 421 SDAKCKLADLEcalqqaKQDMARQLcEYQELMNAKLGLDIEIATYRRLLEGEESRL 476
Cdd:TIGR04523 436 IKNNSEIKDLT------NQDSVKEL-IIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
374-454 |
4.87e-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: 48.99 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 374 LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQ---GEATLSDAKCKLADLECALQQAKQDMARQLCEYQE 450
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
....
gi 15431316 451 LMNA 454
Cdd:COG4942 109 LLRA 112
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
369-456 |
7.73e-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: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 369 QHCDNLRNIRNEINELTR----LIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEatlsdakcklaDLECALQQAKQDMA-- 442
Cdd:pfam13851 5 NHEKAFNEIKNYYNDITRnnleLIKSLKEEIAELKKKEERNEKLMSEIQQENK-----------RLTEPLQKAQEEVEel 73
|
90
....*....|....*....
gi 15431316 443 -RQLCEY----QELMNAKL 456
Cdd:pfam13851 74 rKQLENYekdkQSLKNLKA 92
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
157-448 |
1.78e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 157 NAQRVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKW---------SFLQEQKCIRSNLEP----------LFESY 217
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallALLGLGGSLLSLILTiagvlflvlgLLALL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 218 ITNLRRQLEVLVSDQARLQ--AERNHLQDV-LEGFKKKYEeevVCRANAENEFVALKKDVDAAFmnksDLEANVDTLTQE 294
Cdd:COG4717 290 FLLLAREKASLGKEAEELQalPALEELEEEeLEELLAALG---LPPDLSPEELLELLDRIEELQ----ELLREAEELEEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 295 IDfLKTLYMEEIQLLQShisetsviVKMDNSRDLNLdgiIAEVKAQYEEVARRsRADAEAWYQTKYEEMQVTAGQHcdNL 374
Cdd:COG4717 363 LQ-LEELEQEIAALLAE--------AGVEDEEELRA---ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DE 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15431316 375 RNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEatLSDAKCKLADLECALQQ-AKQDMARQLCEY 448
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRElAEEWAALKLALE 500
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
163-489 |
1.93e-05 |
|
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: 47.81 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 163 KDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETK---WSFLQEQKCI--------RSNLEPLFESYITnLRRQLEVLVSD 231
Cdd:pfam05557 227 KEEVEDLKRKLEREEKYREEAATLELEKEKLEQElqsWVKLAQDTGLnlrspedlSRRIEQLQQREIV-LKEENSSLTSS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 232 QARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEfvalkkdvdaafmnKSDLEANVDTLTQEIDFLKtlymeeiQLLQS 311
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL--------------VRRLQRRVLLLTKERDGYR-------AILES 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 312 HISETSvivkMDNS------RDLNLDGIIAEVKAQYEEV-ARRSRADAEAwyqTKYEEMQVTAGQHCDNLR--------- 375
Cdd:pfam05557 365 YDKELT----MSNYspqlleRIEEAEDMTQKMQAHNEEMeAQLSVAEEEL---GGYKQQAQTLERELQALRqqesladps 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 376 NIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSdaKCKLADLEC-----ALQQAKQDMarqlceyqE 450
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPK--KTKVLHLSMnpaaeAYQQRKNQL--------E 507
|
330 340 350
....*....|....*....|....*....|....*....
gi 15431316 451 LMNAklgldiEIATYRRLLEGEESRLcEGVGPVNISVSS 489
Cdd:pfam05557 508 KLQA------EIERLKRLLKKLEDDL-EQVLRLPETTST 539
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
159-319 |
2.49e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 159 QRVKKDEKEQIKTLNNKFASFIDKVRFLEQQ-----NKLLETKWSFLQEQKCIRSNLEPLFESYIT------NLRRQLEV 227
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEElaellKELEELGFESVEELEERLKELEPFYNEYLElkdaekELEREEKE 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 228 LVSDQARLQAERNHLQDV----------LEGFKKKYEEEVvcRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDF 297
Cdd:PRK03918 621 LKKLEEELDKAFEELAETekrleelrkeLEELEKKYSEEE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
170 180
....*....|....*....|....*...
gi 15431316 298 LK------TLYMEEIQLLQSHISETSVI 319
Cdd:PRK03918 699 LKeeleerEKAKKELEKLEKALERVEEL 726
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
219-475 |
3.46e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 219 TNLRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEidfl 298
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT---- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 299 KTLYMEEIQllqshisetSVIVKMDNSRDL--NL-------DGIIAEVK---AQYEEvaRRSRADAEAwyqTKYEEMQVT 366
Cdd:pfam01576 575 KNRLQQELD---------DLLVDLDHQRQLvsNLekkqkkfDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALS 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 367 AGQHCDNLRNIRNEINELTRLiqrLKAEIE---HAKAQRAK----LEAAVAEAEQQgeatLSDAKCKLADLECALQQAKq 439
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKnvheLERSKRALEQQ----VEEMKTQLEELEDELQATE- 712
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15431316 440 dmarqlceyqelmNAKLGLDIEI----ATYRRLLE-----GEESR 475
Cdd:pfam01576 713 -------------DAKLRLEVNMqalkAQFERDLQardeqGEEKR 744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
334-456 |
3.78e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 334 IAEVKAQYEEVARRSRAdaeawYQTKYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAE 413
Cdd:COG4372 68 LEQARSELEQLEEELEE-----LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15431316 414 QQgeatLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKL 456
Cdd:COG4372 143 SE----IAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
361-476 |
6.43e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 361 EEMQVTAGQHcDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEatLSDAKCKLADLECALQQAKQd 440
Cdd:COG4717 78 EELKEAEEKE-EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE--LEALEAELAELPERLEELEE- 153
|
90 100 110
....*....|....*....|....*....|....*.
gi 15431316 441 marQLCEYQELMNAKLGLDIEIATYRRLLEGEESRL 476
Cdd:COG4717 154 ---RLEELRELEEELEELEAELAELQEELEELLEQL 186
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
134-444 |
6.73e-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: 46.19 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 134 APSITAVTVNKSLLTPLNLEID---PNAQRVKKDEKEQ---IKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIR 207
Cdd:TIGR00606 656 AMLAGATAVYSQFITQLTDENQsccPVCQRVFQTEAELqefISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 208 SNLEPLFESYITNLRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEEVVC--------RANAENEFVALKKDVDAAFM 279
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKDVERKIAQQAAKL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 280 NKSDLEANVDTLTQEidflKTLYMEEIQLLQSHISETSVIVKMDNSRDLNLDGIIAEVKA---QYEEVARRSRADAEawy 356
Cdd:TIGR00606 816 QGSDLDRTVQQVNQE----KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEE--- 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 357 QTkyeEMQVTAGQHCdnLRNIRNEINELTRLIQRLKAEIEhakaQRAKLEAAVAEAEQQGEATLSDAKCKL-------AD 429
Cdd:TIGR00606 889 QL---VELSTEVQSL--IREIKDAKEQDSPLETFLEKDQQ----EKEELISSKETSNKKAQDKVNDIKEKVknihgymKD 959
|
330
....*....|....*
gi 15431316 430 LECALQQAKQDMARQ 444
Cdd:TIGR00606 960 IENKIQDGKDDYLKQ 974
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
374-478 |
6.95e-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: 44.53 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 374 LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQgeatLSDAKCKLADLECALQQAKQDMARqlceYQE-LM 452
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE----LEDLEKEIKRLELEIEEVEARIKK----YEEqLG 83
|
90 100 110
....*....|....*....|....*....|.
gi 15431316 453 NAK-----LGLDIEIATYRRLLEGEESRLCE 478
Cdd:COG1579 84 NVRnnkeyEALQKEIESLKRRISDLEDEILE 114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
160-434 |
8.11e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 160 RVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETkwsFLQEQKCIRSNLEPLFEsyITNLRRQLEVL----VSDQARL 235
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK---VLKKESELIKLKELAEQ--LKELEEKLKKYnleeLEKKAEE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 236 QAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLE--------ANVDTLTQEIDFLKTLYMEEIQ 307
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfESVEELEERLKELEPFYNEYLE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 308 LLQSHiSETSVIVKMDNSRDLNLDGI---IAEVKAQYEEVarRSRADAeawYQTKYEEmqvtagqhcDNLRNIRNEINEL 384
Cdd:PRK03918 607 LKDAE-KELEREEKELKKLEEELDKAfeeLAETEKRLEEL--RKELEE---LEKKYSE---------EEYEELREEYLEL 671
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15431316 385 TRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEaTLSDAKCKLADLECAL 434
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKAL 720
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-476 |
8.42e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 222 RRQLEVLVSDQARLQAERNHLQDVLEGFKKKyeeevvcRANAENEFVALKKDVDAAFMnksdlEANVDTLTQEIDFLKtl 301
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAE-------LDALQERREALQRLAEYSWD-----EIDVASAEREIAELE-- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 302 ymEEIQLLQShisetsvivkmdNSRDLnldgiiAEVKAQYEEvARRSRADAEAwyqtKYEEMQVTAGQHcdnlrniRNEI 381
Cdd:COG4913 675 --AELERLDA------------SSDDL------AALEEQLEE-LEAELEELEE----ELDELKGEIGRL-------EKEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 382 NELTRLIQRLKAEIEHA-----KAQRAKLEAAVAEA-----EQQGEATLSDakcKLADLECALQQAKQDMARQLCEYQEL 451
Cdd:COG4913 723 EQAEEELDELQDRLEAAedlarLELRALLEERFAAAlgdavERELRENLEE---RIDALRARLNRAEEELERAMRAFNRE 799
|
250 260 270
....*....|....*....|....*....|
gi 15431316 452 -MNAKLGLDIEIAT---YRRLLEG-EESRL 476
Cdd:COG4913 800 wPAETADLDADLESlpeYLALLDRlEEDGL 829
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
187-411 |
1.43e-04 |
|
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: 43.76 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 187 EQQNKLLEtkwsfLQEqkcIRSNLEPLfESYITNLRRQLEVLVSDQARLQAERNHLQDVLEGFK---KKYEEEV-VCRAN 262
Cdd:COG1579 4 EDLRALLD-----LQE---LDSELDRL-EHRLKELPAELAELEDELAALEARLEAAKTELEDLEkeiKRLELEIeEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 263 AENefvaLKKDVDAAFMNKsDLEAnvdtLTQEIDFLKtlymEEIQLLQSHIsetsvivkmdnsrdLNLDGIIAEVKAQYE 342
Cdd:COG1579 75 IKK----YEEQLGNVRNNK-EYEA----LQKEIESLK----RRISDLEDEI--------------LELMERIEELEEELA 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15431316 343 EVarrsradaeawyQTKYEEMQvtagqhcdnlRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAE 411
Cdd:COG1579 128 EL------------EAELAELE----------AELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
159-415 |
2.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 159 QRVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEqkcirsnleplfesyitnLRRQLEVLVSDQARLQAE 238
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE------------------LQEELEELEEELEELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 239 RNHLQDVLEGFKKkyeeevvcranaenefvalKKDVDAAFMNKSDLEANVDTLTQEIDFLKtlymEEIQLLQSHISEtsv 318
Cdd:COG4717 111 LEELREELEKLEK-------------------LLQLLPLYQELEALEAELAELPERLEELE----ERLEELRELEEE--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 319 ivkmdnsrdlnldgiIAEVKAQYEEVARRSRADAEAWYQTKYEEMQvtagQHCDNLRNIRNEINELTRLIQRLKAEIEHA 398
Cdd:COG4717 165 ---------------LEELEAELAELQEELEELLEQLSLATEEELQ----DLAEELEELQQRLAELEEELEEAQEELEEL 225
|
250
....*....|....*..
gi 15431316 399 KAQRAKLEAAVAEAEQQ 415
Cdd:COG4717 226 EEELEQLENELEAAALE 242
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
153-473 |
3.12e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 153 EIDPNAQRVKKDE-KEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQ-KCI-------RSNLEPLFESYITNLRR 223
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsVCPvcgttlgEEKSNHIINHYNEKKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 224 ------QLEVLVSDqarLQAERNHLQDVLEGFKKKYEEEVVcraNAENEFVALKKDVDAaFMNK-SDLEANVDTLTQEID 296
Cdd:PRK01156 481 leekirEIEIEVKD---IDEKIVDLKKRKEYLESEEINKSI---NEYNKIESARADLED-IKIKiNELKDKHDKYEEIKN 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 297 FLKTLYMEEI-QLLQSHISETSVIVKMDNSrdlNLDGIIAEVKAQYEEVARRSR------ADAEAWYQTKYEEMQvtagQ 369
Cdd:PRK01156 554 RYKSLKLEDLdSKRTSWLNALAVISLIDIE---TNRSRSNEIKKQLNDLESRLQeieigfPDDKSYIDKSIREIE----N 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 370 HCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEaAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLCEYQ 449
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
330 340
....*....|....*....|....
gi 15431316 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 |
5.53e-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: 42.96 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 159 QRVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYItnlrRQLEvlvsDQARLQAE 238
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARI----RELE----EDIKTLTQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 239 RNHLQDV-LEGFKKKYEEEVVCRANAENEFVALKKDVDAAfmnksdlEANVDTLTQEIDFLKTLYME---EIQLLQSHIS 314
Cdd:pfam07888 144 RVLERETeLERMKERAKKAGAQRKEEEAERKQLQAKLQQT-------EEELRSLSKEFQELRNSLAQrdtQVLQLQDTIT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 315 ETSVIVKMDNSRDLNLDGIIAEVKAQYEE------------------VARRSRADAEAwYQTKYEEMQVTA--------- 367
Cdd:pfam07888 217 TLTQKLTTAHRKEAENEALLEELRSLQERlnaserkveglgeelssmAAQRDRTQAEL-HQARLQAAQLTLqladaslal 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 368 -------GQHCDNLRNI----RNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQ 436
Cdd:pfam07888 296 regrarwAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV 375
|
330
....*....|....*.
gi 15431316 437 AKQDMARQLCEYQELM 452
Cdd:pfam07888 376 AQKEKEQLQAEKQELL 391
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-478 |
5.55e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 164 DEKEQIKTLN---NKFASFI----------DKVRF-LEQQNKLLETKWSFLQEQKCirsnlEPlfESYITNLRRQL---- 225
Cdd:pfam01576 170 EEEEKAKSLSklkNKHEAMIsdleerlkkeEKGRQeLEKAKRKLEGESTDLQEQIA-----EL--QAQIAELRAQLakke 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 226 EVLVSDQARLQAERNH----------LQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAfmnKSDLEANVDTLT--- 292
Cdd:pfam01576 243 EELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARNKAEKQRRDLGEELEAL---KTELEDTLDTTAaqq 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 293 -------QEIDFLKTLYMEEIQLLQSHISEtsviVKMDNSRDLNldgiiaEVKAQYEEvARRSRADAEAWYQTkyeemqv 365
Cdd:pfam01576 320 elrskreQEVTELKKALEEETRSHEAQLQE----MRQKHTQALE------ELTEQLEQ-AKRNKANLEKAKQA------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 366 tagqhcdnLRNIRNEINELTRLIQRLKAEIEH----AKAQRAKLEAAVAEAEQQ----------GEATLSDAKCKLADLE 431
Cdd:pfam01576 382 --------LESENAELQAELRTLQQAKQDSEHkrkkLEGQLQELQARLSESERQraelaeklskLQSELESVSSLLNEAE 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15431316 432 CALQQAKQDMAR---QLCEYQELMNAKLGLDIEIATYRRLLEGEESRLCE 478
Cdd:pfam01576 454 GKNIKLSKDVSSlesQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQE 503
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
223-439 |
5.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 223 RQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEevvcRANAENEFVALKKdvdaafmNKSDLEANVDTLTQEIDFLKTLy 302
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEA-------ELEELREELEKLEKLLQLLPLY- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 303 mEEIQLLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEvaRRSRADAEAWYQTKYEEMQVTAGQHCDNLRN-IRNEI 381
Cdd:COG4717 132 -QELEALEAELAE--------------LPERLEELEERLEE--LRELEEELEELEAELAELQEELEELLEQLSLaTEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15431316 382 NELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEAtLSDAKCKLADLECaLQQAKQ 439
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ-LENELEAAALEER-LKEARL 250
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
334-442 |
6.59e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 334 IAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQhcdnlrniRNEINELTRLIQRLKAEIEHAKAQ-------RAKLE 406
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQR--------QLEIAEREREIELQEKEAEREEAEleadvrkPAEAE 317
|
90 100 110
....*....|....*....|....*....|....*.
gi 15431316 407 AAVAEAEQQGEATLSDAKCKladlecALQQAKQDMA 442
Cdd:COG2268 318 KQAAEAEAEAEAEAIRAKGL------AEAEGKRALA 347
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-396 |
6.83e-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: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 151 NLEIDPNAQRVKKDEKE-QIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYITNLRRQLEVLV 229
Cdd:TIGR02168 793 QLKEELKALREALDELRaELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 230 SDQARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLYMEEIQLL 309
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 310 QSHISETSVIVKMDNSR----------------DLNLDGIiaevkAQYEEVARRsradaeawyqtkYEEMqvtAGQHCD- 372
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEarrrlkrlenkikelgPVNLAAI-----EEYEELKER------------YDFL---TAQKEDl 1012
|
250 260
....*....|....*....|....*....
gi 15431316 373 -----NLRNIRNEINELTRliQRLKAEIE 396
Cdd:TIGR02168 1013 teakeTLEEAIEEIDREAR--ERFKDTFD 1039
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-461 |
7.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 335 AEVKAQYEEvARRSRADAEAWYQTKyEEMQVTAGQHCDNLrnIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQ 414
Cdd:COG4913 255 EPIRELAER-YAAARERLAELEYLR-AALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15431316 415 Q----GEATLSDAKCKLADLEcalqQAKQDMARQLCEYQELMnAKLGLDIE 461
Cdd:COG4913 331 QirgnGGDRLEQLEREIERLE----RELEERERRRARLEALL-AALGLPLP 376
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
327-475 |
7.56e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 327 DLNLDGIIAEVKAQ--YEEVARRSRADAEAWYQTKYEEmqvtagqHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAK 404
Cdd:PHA02562 187 DMKIDHIQQQIKTYnkNIEEQRKKNGENIARKQNKYDE-------LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 405 LEAAVAEAEQQ--------------------------GEATLSDAKCKLADLECALQQAK---QDMARQLCEYQELMNAK 455
Cdd:PHA02562 260 LNTAAAKIKSKieqfqkvikmyekggvcptctqqiseGPDRITKIKDKLKELQHSLEKLDtaiDELEEIMDEFNEQSKKL 339
|
170 180
....*....|....*....|
gi 15431316 456 LGLDIEIATYRRLLEGEESR 475
Cdd:PHA02562 340 LELKNKISTNKQSLITLVDK 359
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-478 |
8.82e-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: 42.35 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 378 RNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEA----------TLSDAKCKLADLECALQQAKQDMARQLCE 447
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlrkeleelsrQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110
....*....|....*....|....*....|.
gi 15431316 448 YQElmnaklgLDIEIATYRRLLEGEESRLCE 478
Cdd:TIGR02168 756 LTE-------LEAEIEELEERLEEAEEELAE 779
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
382-444 |
1.01e-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: 39.99 E-value: 1.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15431316 382 NELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQ---GEATLSDAKCKLADLECALQQAKQDMARQ 444
Cdd:pfam11559 55 ESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
335-439 |
1.21e-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: 39.34 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 335 AEVKAQYEEvARRSRADAEAwYQTKYEEMqvtagqhcdnLRNIRNE----INELTRLIQRLKAEI-EHAKAQRAKL-EAA 408
Cdd:cd06503 33 EKIAESLEE-AEKAKEEAEE-LLAEYEEK----------LAEARAEaqeiIEEARKEAEKIKEEIlAEAKEEAERIlEQA 100
|
90 100 110
....*....|....*....|....*....|.
gi 15431316 409 VAEAEQQGEATLSDAKCKLADLecALQQAKQ 439
Cdd:cd06503 101 KAEIEQEKEKALAELRKEVADL--AVEAAEK 129
|
|
| 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 15431316 181 DKVRFLEQQNKLLETKWSFLQEQkcirsnleplFESYITNLRRQLEVLVSDQARLQAernhlqdvlegfkkKYEEEVVCR 260
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ----------IKTYNKNIEEQRKKNGENIARKQN--------------KYDELVEEA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 261 ANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKT---LYMEEIQLLQSH---------ISETsvivkmdnsrdl 328
Cdd:PHA02562 230 KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSkieQFQKVIKMYEKGgvcptctqqISEG------------ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 329 nlDGIIAEVKAQYEEvarrsradaeawYQTKYEEMQvtagQHCDNLRNIRNEINELTRLIQRLKAEIEhakAQRAKLEAA 408
Cdd:PHA02562 298 --PDRITKIKDKLKE------------LQHSLEKLD----TAIDELEEIMDEFNEQSKKLLELKNKIS---TNKQSLITL 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15431316 409 VAEAeQQGEATLSDAKCKLADLECALQQAKQdmarqlcEYQELMNAKLGLDIEIATY 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 15431316 160 RVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQ-EQKCIRSNLE-PLFESYITNLRRQLEVLVSDQARLQA 237
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKkENLEKEIDEKNKEIEELKQTQKSLKK 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 238 ERNHLQDVLegfkKKYEEevvcranaenEFVALKKDVdaafmnkSDLEANVDTLTQEIDFLKTLYmEEIQllqshisetS 317
Cdd:TIGR04523 583 KQEEKQELI----DQKEK----------EKKDLIKEI-------EEKEKKISSLEKELEKAKKEN-EKLS---------S 631
|
170 180
....*....|....*....|....*..
gi 15431316 318 VIVKMDNSrdlnLDGIIAEVKAQYEEV 344
Cdd:TIGR04523 632 IIKNIKSK----KNKLKQEVKQIKETI 654
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
232-444 |
1.98e-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: 41.31 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 232 QARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDV----------DAAF----MNKSDLEANVDTLTQEIDF 297
Cdd:pfam01576 63 RARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIqdleeqldeeEAARqklqLEKVTTEAKIKKLEEDILL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 298 L----------KTLYMEEIQLLQSHISETSVIVKMDNSRDLNLDGIIA--EVKAQYEEvarRSRADAEAWYqtkyeemqv 365
Cdd:pfam01576 143 LedqnsklskeRKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEE---KGRQELEKAK--------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 366 tagqhcdnlRNIRNEINELTRLIQRLKAEIEHAKAQRAK----LEAAVAEAEQQGeATLSDAKCKLADLECALQQAKQDM 441
Cdd:pfam01576 211 ---------RKLEGESTDLQEQIAELQAQIAELRAQLAKkeeeLQAALARLEEET-AQKNNALKKIRELEAQISELQEDL 280
|
...
gi 15431316 442 ARQ 444
Cdd:pfam01576 281 ESE 283
|
|
| 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 15431316 212 PLFESYITN-------LRRQLEvLVSDQARLQAE------RNHLqdvLEGFKKKYEEEVvcranaeNEFVALKKDVDAaF 278
Cdd:smart00787 99 PLFKEYFSAspdvkllMDKQFQ-LVKTFARLEAKkmwyewRMKL---LEGLKEGLDENL-------EGLKEDYKLLMK-E 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 279 MNKsdleanVDTLTQEIDFLKTLYMEEIQLLQSHISETSvivkmDNSRDLnLDGIIAEVKAQYEEVARRSRadaeawyqt 358
Cdd:smart00787 167 LEL------LNSIKPKLRDRKDALEEELRQLKQLEDELE-----DCDPTE-LDRAKEKLKKLLQEIMIKVK--------- 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15431316 359 KYEEMQvtagqhcDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAK 404
Cdd:smart00787 226 KLEELE-------EELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
157-476 |
3.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 157 NAQRVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQkcirsnleplfesyITNLRRQLEVLVSDQARLQ 236
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--------------LESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 237 AERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAafmnksdLEANVDTLTQEIDFL-KTLYMEEIQLLQSHISE 315
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES-------LQEELAALEQELQALsEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 316 TSVIVK-----MDNSRDLNLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQHcDNLRNIRNEINELTRLIQR 390
Cdd:COG4372 195 NAEKEEelaeaEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE-VILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 391 LKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLE 470
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
....*.
gi 15431316 471 GEESRL 476
Cdd:COG4372 354 DVLELL 359
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
374-476 |
3.47e-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: 39.52 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 374 LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAE--------QQGEAtlSDAKcklaDLEcALQQ--AKQDMAR 443
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEarikkyeeQLGNV--RNNK----EYE-ALQKeiESLKRRI 105
|
90 100 110
....*....|....*....|....*....|....*
gi 15431316 444 QLCEYQ--ELMNAKLGLDIEIATYRRLLEGEESRL 476
Cdd:COG1579 106 SDLEDEilELMERIEELEEELAELEAELAELEAEL 140
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-443 |
4.42e-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: 39.14 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 284 LEANVDTLTQEIDFLKtlymEEIQLLQSHISETSVIVKmdnsrDLNLDgiIAEVKAQYEEVARRsradaeawyQTKYEEM 363
Cdd:COG1579 22 LEHRLKELPAELAELE----DELAALEARLEAAKTELE-----DLEKE--IKRLELEIEEVEAR---------IKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 364 QvtaGQHCDN--LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDM 441
Cdd:COG1579 82 L---GNVRNNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
..
gi 15431316 442 AR 443
Cdd:COG1579 159 EE 160
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
374-439 |
7.12e-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: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15431316 374 LRNIRNEINELTRLIQRLKAEIEHAK------------AQRA----------KLEAAVAEAEQQGEATLSDAKCKLADLE 431
Cdd:COG3599 36 YERLIRENKELKEKLEELEEELEEYReleetlqktlvvAQETaeevkenaekEAELIIKEAELEAEKIIEEAQEKARKIV 115
|
....*...
gi 15431316 432 CALQQAKQ 439
Cdd:COG3599 116 REIEELKR 123
|
|
| |
