|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
163-473 |
4.07e-147 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 427.03 E-value: 4.07e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 163 EKEQIKTLNNKFTSFIDKVRFLEQQNKLLETKWSFLQEQKCIR-SNLEPLFESYITNLRRQLEVLVSDQARLQAERNHLQ 241
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 242 DVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLYMEEIQLLQSHISETSVIVKMD 321
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 322 NSRDLNLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRA 401
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42760016 402 KLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLEGEESR 473
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
14-159 |
8.10e-48 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 164.44 E-value: 8.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 14 NFSSCSAMTPqNLNRFRANSVSCWSGPGFRGL------GSFGSRSVITFG---SYSPRIAAVGSRPVhCGVRFGAGCGMG 84
Cdd:pfam16208 1 GFSSCSAVVP-SRSRRSYSSVSSSRRGGGGGGggggggGGFGSRSLYNLGgskSISISVAGGGSRPG-SGFGFGGGGGGG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42760016 85 F--GDGRGVGLGPRADSCVGLGFGAGSGIGYGFGGPGFGYRVGGVGVPAAPS-ITAVTVNKSLLTPLNLEIDPNAQRV 159
Cdd:pfam16208 79 FggGFGGGGGGGFGGGGGFGGGFGGGGYGGGGFGGGGFGGRGGFGGPPCPPGgIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-405 |
1.48e-15 |
|
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: 80.06 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 149 NLEIDPNAQRVKKDEKE-QIKTLNNKFTSFIDKVRFLEQQNKLLETKwsfLQEQKcirsNLEPLFESYITNLRRQLEVLV 227
Cdd:TIGR04523 353 NSESENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQE----KLNQQKDEQIKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 228 SDQARLQAERN----------------------------HLQDVLEGFKKKYEEEvvcRANAEN---EFVALKKDVDAAF 276
Cdd:TIGR04523 426 KEIERLKETIIknnseikdltnqdsvkeliiknldntreSLETQLKVLSRSINKI---KQNLEQkqkELKSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 277 MNKSDLEANVDTLTQEIDFLKtlymEEIQLLQSHI----SETSVIVKMDNSRDLNLDgiiaevKAQYEEVARRSRADAEA 352
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLK----EKIEKLESEKkekeSKISDLEDELNKDDFELK------KENLEKEIDEKNKEIEE 572
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 42760016 353 WYQT------KYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEA 405
Cdd:TIGR04523 573 LKQTqkslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-476 |
4.13e-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: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 198 LQEQKCIRSNLEpLFESYITNLRRQLEvlvsdqaRLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFm 277
Cdd:TIGR02169 176 LEELEEVEENIE-RLDLIIDEKRQQLE-------RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 278 nkSDLEANVDTLTQEIDFLKtLYMEEIQLLQSHISETsvIVKMDNSRDLNLDGIIAEVKAQYEEvARRSRADAEawyqtk 357
Cdd:TIGR02169 247 --ASLEEELEKLTEEISELE-KRLEEIEQLLEELNKK--IKDLGEEEQLRVKEKIGELEAEIAS-LERSIAEKE------ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 358 yEEMQVTAGQhcdnLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAE----------QQGEATLSDAKCKLAD 427
Cdd:TIGR02169 315 -RELEDAEER----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlraelEEVDKEFAETRDELKD 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 42760016 428 LECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLEGEESRLCE 476
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
259-554 |
7.96e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.08 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 259 ANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLktlyMEEIQLLQSHISETSVivKMDNSRDlNLDGIIAEVKAQ 338
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQA--EIDKLQA-EIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 339 YEEVARRSRADAEAWYQTKYEEMQVTAG------QHCDNLRNI----RNEINELTRLIQRL---KAEIEHAKAQRAKLEA 405
Cdd:COG3883 85 REELGERARALYRSGGSVSYLDVLLGSEsfsdflDRLSALSKIadadADLLEELKADKAELeakKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 406 AVAEAEQQGEATLSDAKCKLADL---ECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLEGEESRLCEGVGPVN 482
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLsaeEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42760016 483 ISVSSSRGGLVCGPEPLVAGSTLSRGGVTFSGSSSVCATSGVLASCGPSLGGARVAPATGDLLGTGTRSGSM 554
Cdd:COG3883 245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSG 316
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
167-441 |
1.06e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 167 IKTLNNKFTSFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYITNLRRQLEVL-------VSDQARLQAERNH 239
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqlEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 240 LQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLY---MEEIQLLQSHISETSV 316
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 317 IVKMDNSRDLNLDGIIAEVKAQ---YEEVARRSRADAEAWYQtKYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEI 393
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEieeLEELIEELESELEALLN-ERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 42760016 394 EHAKAQRAKLEAAVAEAEQQ-----------GEATLSDAKCKLADLECALQQAKQDMAR 441
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-444 |
1.03e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 142 KSLLTPLNLEIDPNAQRVKKDE--KEQIKTLNNKFTSFIDKVRFLEQQNKLLETKWSFLQEQKcirSNLEPLFESyITNL 219
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKEE-IEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 220 RRQLEVLVSDQARLQAERNHLQDVLEGFKKKYE--EEVVCRANA----ENEFVALKKdvdaaFMNKSDLEANvdtltqEI 293
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKElkekAEEYIKLSE-----FYEEYLDELR------EI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 294 DFLKTLYMEEIQLLQSHISETSvivkMDNSRDLNLDGIIAEVKAQYEEVARRSRAdaeawyqtkYEEmqvtAGQHCDNLR 373
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERHEL---------YEE----AKAKKEELE 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42760016 374 NIRNEINELTrlIQRLKAEIEhaKAQRAKLEaaVAEAEQQGEATLSDAKCKLADLECALQQAKQdmARQLC 444
Cdd:PRK03918 376 RLKKRLTGLT--PEKLEKELE--ELEKAKEE--IEEEISKITARIGELKKEIKELKKAIEELKK--AKGKC 438
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-474 |
1.38e-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: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 157 QRVKKDEKE-QIKTLNNKFTSFIDKVRFLEQQNKLLETKWSFLQEQKcirSNLEPLFE---SYITNLRRQLEVLvsdQAR 232
Cdd:TIGR02168 216 KELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAEL---QELEEKLEelrLEVSELEEEIEEL---QKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 233 LQAERNHLQDvLEGFKKKYEEEvvcRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKtlymEEIQLLQSHIS 312
Cdd:TIGR02168 290 LYALANEISR-LEQQKQILRER---LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK----EELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 313 ETSVIVKMDNSRdlnldgiIAEVKAQYEEvARRSRADAEAwyqtkyeemqvtagqhcdNLRNIRNEINELTRLIQRLKAE 392
Cdd:TIGR02168 362 ELEAELEELESR-------LEELEEQLET-LRSKVAQLEL------------------QIASLNNEIERLEARLERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 393 IEHAKAQRAKLEAAVAEAE-QQGEATLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLEGEE 471
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
...
gi 42760016 472 SRL 474
Cdd:TIGR02168 496 RLQ 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
188-461 |
5.84e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 188 NKLLEtkwSFLQEQkcIRSNLEPLfESYITNLRRQLEVLvsdQARLQAernhLQDVLEGFKKKyeeevvcranaeNEFVA 267
Cdd:COG3206 155 NALAE---AYLEQN--LELRREEA-RKALEFLEEQLPEL---RKELEE----AEAALEEFRQK------------NGLVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 268 LKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLYmeeiQLLQSHISETSvivkmDNSRDLNLDGIIAEVKAQYEEVARRsR 347
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARL----AALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-L 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 348 ADAEAWYQTKYEEMQVTAGQhcdnLRNIRNEIN-ELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGeATLSDAKCKLA 426
Cdd:COG3206 280 AELSARYTPNHPDVIALRAQ----IAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELR 354
|
250 260 270
....*....|....*....|....*....|....*
gi 42760016 427 DLecalqQAKQDMARQLceYQELMNAKLGLDIEIA 461
Cdd:COG3206 355 RL-----EREVEVAREL--YESLLQRLEEARLAEA 382
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
334-429 |
1.31e-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: 50.72 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 334 EVKAQYEEVARRSRAD----AEAW--YQTKYE-EMQvtagQHCD---NLRNIRNEINELTRLIQRLKAEIEHAKAQRAKL 403
Cdd:pfam07926 15 EEAADAEAQLQKLQEDlekqAEIAreAQQNYErELV----LHAEdikALQALREELNELKAEIAELKAEAESAKAELEES 90
|
90 100
....*....|....*....|....*.
gi 42760016 404 EAAVAEAEQQGEATLSDAKCKLADLE 429
Cdd:pfam07926 91 EESWEEQKKELEKELSELEKRIEDLN 116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
216-474 |
1.63e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 216 ITNLRRQLEVLVSDQARLQAERNHLQDvlegfkkkyeeevvcranaenefvalkkdvdaafmNKSDLEANVDTLTQEIDF 295
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEE-----------------------------------RRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 296 LKtlymEEIQLLQSHISETSVIVKMDNSRDLNLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQhcdnlRNI 375
Cdd:COG1196 328 LE----EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-----AEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 376 RNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSdakcKLADLECALQQAKQDMARQLCEYQELMNAKLG 455
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE----ALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250
....*....|....*....
gi 42760016 456 LDIEIATYRRLLEGEESRL 474
Cdd:COG1196 475 LEAALAELLEELAEAAARL 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
219-474 |
4.88e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 219 LRRQLEVLvSDQARlQAERnhlqdvlegfKKKYEEEvvcranaenefvALKKDVDAAFMNKSDLEANVDTLTQEIDFLKt 298
Cdd:COG1196 198 LERQLEPL-ERQAE-KAER----------YRELKEE------------LKELEAELLLLKLRELEAELEELEAELEELE- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 299 lymEEIQLLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGqhcdnLRNIRNE 378
Cdd:COG1196 253 ---AELEELEAELAE--------------LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD-----IARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 379 INELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQG---EATLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKLG 455
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELeeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250
....*....|....*....
gi 42760016 456 LDIEIATYRRLLEGEESRL 474
Cdd:COG1196 391 ALRAAAELAAQLEELEEAE 409
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
219-442 |
6.37e-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: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 219 LRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEevvcranAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKT 298
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 299 LYMEEIQLLQ--SHISETSVIVKMDNSRDLNLDGIIaevkaqYEEVARRSRADAEAWYQTKYEEMQVTAgqhcdNLRNIR 376
Cdd:COG4942 105 ELAELLRALYrlGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARREQAEELRADLAELAALRA-----ELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42760016 377 NEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQ 442
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
161-474 |
7.38e-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: 52.33 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 161 KDEKEQIKTLNNKFTSFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYITNLRRQLEVLVSDQARLQAERNHL 240
Cdd:TIGR04523 92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 241 QDVLEGFKK---KYEEEVvcrANAENEFVAL--------KKDVDAAFMNK--SDLEANVDTLTQEIDFLKtlymEEIQLL 307
Cdd:TIGR04523 172 ENELNLLEKeklNIQKNI---DKIKNKLLKLelllsnlkKKIQKNKSLESqiSELKKQNNQLKDNIEKKQ----QEINEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 308 QSHISET-----SVIVKMDNSRD----------------LNLDGIIAEVKAQYEEVARRSRADaeaWYQTKYEEMQvtag 366
Cdd:TIGR04523 245 TTEISNTqtqlnQLKDEQNKIKKqlsekqkeleqnnkkiKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELK---- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 367 QHCDNLRNIRNE-------INELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLEcALQQAKQDM 439
Cdd:TIGR04523 318 NQEKKLEEIQNQisqnnkiISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDL 396
|
330 340 350
....*....|....*....|....*....|....*...
gi 42760016 440 ARQLCEYQELMNAKlglDIEIATY---RRLLEGEESRL 474
Cdd:TIGR04523 397 ESKIQNQEKLNQQK---DEQIKKLqqeKELLEKEIERL 431
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
142-474 |
9.47e-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: 51.94 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 142 KSLLTPLNLEIDpnaqrvkkDEKEQIKTLNNKFTSFIDKVrfLEQQNKLLETKWSFLQEQKCIrSNLEP------LFESY 215
Cdd:TIGR04523 151 EKELEKLNNKYN--------DLKKQKEELENELNLLEKEK--LNIQKNIDKIKNKLLKLELLL-SNLKKkiqknkSLESQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 216 ITNLRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAfmNK--SDLEANVDTLTQEI 293
Cdd:TIGR04523 220 ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN--NKkiKELEKQLNQLKSEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 294 ---------DFLKTLYME------EIQLLQSHISETsvivkmdnsrdlnlDGIIAEVKAQYEEVaRRSRADAEAWYQTKY 358
Cdd:TIGR04523 298 sdlnnqkeqDWNKELKSElknqekKLEEIQNQISQN--------------NKIISQLNEQISQL-KKELTNSESENSEKQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 359 EEMQvtagQHCDNLRNIRNE-------INELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGE----------ATLSDA 421
Cdd:TIGR04523 363 RELE----EKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllekeierlkETIIKN 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 42760016 422 KCKLADLEcalqqaKQDMARQLcEYQELMNAKLGLDIEIATYRRLLEGEESRL 474
Cdd:TIGR04523 439 NSEIKDLT------NQDSVKEL-IIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
372-452 |
4.85e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 372 LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQ---GEATLSDAKCKLADLECALQQAKQDMARQLCEYQE 448
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
....
gi 42760016 449 LMNA 452
Cdd:COG4942 109 LLRA 112
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
156-441 |
5.49e-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: 49.68 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 156 AQRVKKDEKEQIKTLNNKFTSfidKVRFLEQQNKLLETKWSflQEQKCIRSNLEPLfESYITNLRRQLEVLVSDQ----- 230
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGE--EEQLRVKEKIGEL-EAEIASLERSIAEKERELedaee 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 231 --ARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKtlymEEIQLLQ 308
Cdd:TIGR02169 323 rlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR----EKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 309 SHIsetsvivkmdNSRDLNLDGIIAEVKAQYEEVARrSRADAEAwyqtkyeemqvtagqhcdnlrnIRNEINELTRLIQR 388
Cdd:TIGR02169 399 REI----------NELKRELDRLQEELQRLSEELAD-LNAAIAG----------------------IEAKINELEEEKED 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 42760016 389 LKAEIEHAKAQRAKLEAAVAEAEQQgeatLSDAKCKLADLECALQQAKQDMAR 441
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQE----LYDLKEEYDRVEKELSKLQRELAE 494
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
367-454 |
6.51e-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: 47.21 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 367 QHCDNLRNIRNEINELTR----LIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEatlsdakcklaDLECALQQAKQDMA-- 440
Cdd:pfam13851 5 NHEKAFNEIKNYYNDITRnnleLIKSLKEEIAELKKKEERNEKLMSEIQQENK-----------RLTEPLQKAQEEVEel 73
|
90
....*....|....*....
gi 42760016 441 -RQLCEY----QELMNAKL 454
Cdd:pfam13851 74 rKQLENYekdkQSLKNLKA 92
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
161-487 |
1.50e-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: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 161 KDEKEQIKTLNNKFTSFIDKVRFLEQQNKLLETK---WSFLQEQKCI--------RSNLEPLFESYITnLRRQLEVLVSD 229
Cdd:pfam05557 227 KEEVEDLKRKLEREEKYREEAATLELEKEKLEQElqsWVKLAQDTGLnlrspedlSRRIEQLQQREIV-LKEENSSLTSS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 230 QARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEfvalkkdvdaafmnKSDLEANVDTLTQEIDFLKtlymeeiQLLQS 309
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL--------------VRRLQRRVLLLTKERDGYR-------AILES 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 310 HISETSvivkMDNS------RDLNLDGIIAEVKAQYEEV-ARRSRADAEAwyqTKYEEMQVTAGQHCDNLR--------- 373
Cdd:pfam05557 365 YDKELT----MSNYspqlleRIEEAEDMTQKMQAHNEEMeAQLSVAEEEL---GGYKQQAQTLERELQALRqqesladps 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 374 NIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSdaKCKLADLEC-----ALQQAKQDMarqlceyqE 448
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPK--KTKVLHLSMnpaaeAYQQRKNQL--------E 507
|
330 340 350
....*....|....*....|....*....|....*....
gi 42760016 449 LMNAklgldiEIATYRRLLEGEESRLcEGVGPVNISVSS 487
Cdd:pfam05557 508 KLQA------EIERLKRLLKKLEDDL-EQVLRLPETTST 539
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
155-446 |
2.61e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 155 NAQRVKKDEKEQIKTLNNKFTSFIDKVRFLEQQNKLLETKW---------SFLQEQKCIRSNLEP----------LFESY 215
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallALLGLGGSLLSLILTiagvlflvlgLLALL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 216 ITNLRRQLEVLVSDQARLQ--AERNHLQDV-LEGFKKKYEeevVCRANAENEFVALKKDVDAAFmnksDLEANVDTLTQE 292
Cdd:COG4717 290 FLLLAREKASLGKEAEELQalPALEELEEEeLEELLAALG---LPPDLSPEELLELLDRIEELQ----ELLREAEELEEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 293 IDfLKTLYMEEIQLLQShisetsviVKMDNSRDLNLdgiIAEVKAQYEEVARRsRADAEAWYQTKYEEMQVTAGQHcdNL 372
Cdd:COG4717 363 LQ-LEELEQEIAALLAE--------AGVEDEEELRA---ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DE 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42760016 373 RNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEatLSDAKCKLADLECALQQ-AKQDMARQLCEY 446
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRElAEEWAALKLALE 500
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
217-473 |
3.05e-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: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 217 TNLRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEidfl 296
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT---- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 297 KTLYMEEIQllqshisetSVIVKMDNSRDL--NL-------DGIIAEVK---AQYEEvaRRSRADAEAwyqTKYEEMQVT 364
Cdd:pfam01576 575 KNRLQQELD---------DLLVDLDHQRQLvsNLekkqkkfDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALS 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 365 AGQHCDNLRNIRNEINELTRLiqrLKAEIE---HAKAQRAK----LEAAVAEAEQQgeatLSDAKCKLADLECALQQAKq 437
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKnvheLERSKRALEQQ----VEEMKTQLEELEDELQATE- 712
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 42760016 438 dmarqlceyqelmNAKLGLDIEI----ATYRRLLE-----GEESR 473
Cdd:pfam01576 713 -------------DAKLRLEVNMqalkAQFERDLQardeqGEEKR 744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
332-454 |
3.54e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 332 IAEVKAQYEEVARRSRAdaeawYQTKYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAE 411
Cdd:COG4372 68 LEQARSELEQLEEELEE-----LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 42760016 412 QQgeatLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKL 454
Cdd:COG4372 143 SE----IAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-317 |
3.70e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 157 QRVKKDEKEQIKTLNNKFTSFIDKVRFLEQQ-----NKLLETKWSFLQEQKCIRSNLEPLFESYIT------NLRRQLEV 225
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEElaellKELEELGFESVEELEERLKELEPFYNEYLElkdaekELEREEKE 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 226 LVSDQARLQAERNHLQDV----------LEGFKKKYEEEVvcRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDF 295
Cdd:PRK03918 621 LKKLEEELDKAFEELAETekrleelrkeLEELEKKYSEEE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
170 180
....*....|....*....|....*...
gi 42760016 296 LK------TLYMEEIQLLQSHISETSVI 317
Cdd:PRK03918 699 LKeeleerEKAKKELEKLEKALERVEEL 726
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
132-442 |
5.55e-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: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 132 APSITAVTVNKSLLTPLNLEID---PNAQRVKKDEKEQ---IKTLNNKFTSFIDKVRFLEQQNKLLETKWSFLQEQKCIR 205
Cdd:TIGR00606 656 AMLAGATAVYSQFITQLTDENQsccPVCQRVFQTEAELqefISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 206 SNLEPLFESYITNLRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEEVVC--------RANAENEFVALKKDVDAAFM 277
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKDVERKIAQQAAKL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 278 NKSDLEANVDTLTQEidflKTLYMEEIQLLQSHISETSVIVKMDNSRDLNLDGIIAEVKA---QYEEVARRSRADAEawy 354
Cdd:TIGR00606 816 QGSDLDRTVQQVNQE----KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEE--- 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 355 QTkyeEMQVTAGQHCdnLRNIRNEINELTRLIQRLKAEIEhakaQRAKLEAAVAEAEQQGEATLSDAKCKL-------AD 427
Cdd:TIGR00606 889 QL---VELSTEVQSL--IREIKDAKEQDSPLETFLEKDQQ----EKEELISSKETSNKKAQDKVNDIKEKVknihgymKD 959
|
330
....*....|....*
gi 42760016 428 LECALQQAKQDMARQ 442
Cdd:TIGR00606 960 IENKIQDGKDDYLKQ 974
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
359-474 |
6.07e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 359 EEMQVTAGQHcDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEatLSDAKCKLADLECALQQAKQd 438
Cdd:COG4717 78 EELKEAEEKE-EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE--LEALEAELAELPERLEELEE- 153
|
90 100 110
....*....|....*....|....*....|....*.
gi 42760016 439 marQLCEYQELMNAKLGLDIEIATYRRLLEGEESRL 474
Cdd:COG4717 154 ---RLEELRELEEELEELEAELAELQEELEELLEQL 186
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
372-476 |
6.55e-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: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 372 LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQgeatLSDAKCKLADLECALQQAKQDMARqlceYQE-LM 450
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE----LEDLEKEIKRLELEIEEVEARIKK----YEEqLG 83
|
90 100 110
....*....|....*....|....*....|.
gi 42760016 451 NAK-----LGLDIEIATYRRLLEGEESRLCE 476
Cdd:COG1579 84 NVRnnkeyEALQKEIESLKRRISDLEDEILE 114
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
220-474 |
8.38e-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: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 220 RRQLEVLVSDQARLQAERNHLQDVLEGFKKKyeeevvcRANAENEFVALKKDVDAAFMnksdlEANVDTLTQEIDFLKtl 299
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAE-------LDALQERREALQRLAEYSWD-----EIDVASAEREIAELE-- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 300 ymEEIQLLQShisetsvivkmdNSRDLnldgiiAEVKAQYEEvARRSRADAEAwyqtKYEEMQVTAGQHcdnlrniRNEI 379
Cdd:COG4913 675 --AELERLDA------------SSDDL------AALEEQLEE-LEAELEELEE----ELDELKGEIGRL-------EKEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 380 NELTRLIQRLKAEIEHA-----KAQRAKLEAAVAEA-----EQQGEATLSDakcKLADLECALQQAKQDMARQLCEYQEL 449
Cdd:COG4913 723 EQAEEELDELQDRLEAAedlarLELRALLEERFAAAlgdavERELRENLEE---RIDALRARLNRAEEELERAMRAFNRE 799
|
250 260 270
....*....|....*....|....*....|
gi 42760016 450 -MNAKLGLDIEIAT---YRRLLEG-EESRL 474
Cdd:COG4913 800 wPAETADLDADLESlpeYLALLDRlEEDGL 829
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
185-409 |
1.27e-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: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 185 EQQNKLLEtkwsfLQEqkcIRSNLEPLfESYITNLRRQLEVLVSDQARLQAERNHLQDVLEGFK---KKYEEEV-VCRAN 260
Cdd:COG1579 4 EDLRALLD-----LQE---LDSELDRL-EHRLKELPAELAELEDELAALEARLEAAKTELEDLEkeiKRLELEIeEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 261 AENefvaLKKDVDAAFMNKsDLEAnvdtLTQEIDFLKtlymEEIQLLQSHIsetsvivkmdnsrdLNLDGIIAEVKAQYE 340
Cdd:COG1579 75 IKK----YEEQLGNVRNNK-EYEA----LQKEIESLK----RRISDLEDEI--------------LELMERIEELEEELA 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42760016 341 EVarrsradaeawyQTKYEEMQvtagqhcdnlRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAE 409
Cdd:COG1579 128 EL------------EAELAELE----------AELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
157-413 |
1.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 157 QRVKKDEKEQIKTLNNKFTSFIDKVRFLEQQNKLLETKWSFLQEqkcirsnleplfesyitnLRRQLEVLVSDQARLQAE 236
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE------------------LQEELEELEEELEELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 237 RNHLQDVLEGFKKkyeeevvcranaenefvalKKDVDAAFMNKSDLEANVDTLTQEIDFLKtlymEEIQLLQSHISEtsv 316
Cdd:COG4717 111 LEELREELEKLEK-------------------LLQLLPLYQELEALEAELAELPERLEELE----ERLEELRELEEE--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 317 ivkmdnsrdlnldgiIAEVKAQYEEVARRSRADAEAWYQTKYEEMQvtagQHCDNLRNIRNEINELTRLIQRLKAEIEHA 396
Cdd:COG4717 165 ---------------LEELEAELAELQEELEELLEQLSLATEEELQ----DLAEELEELQQRLAELEEELEEAQEELEEL 225
|
250
....*....|....*..
gi 42760016 397 KAQRAKLEAAVAEAEQQ 413
Cdd:COG4717 226 EEELEQLENELEAAALE 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
158-432 |
2.05e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 158 RVKKDEKEQIKTLNNKFTSFIDKVRFLEQQNKLLETkwsFLQEQKCIRSNLEPLFEsyITNLRRQLEVL----VSDQARL 233
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK---VLKKESELIKLKELAEQ--LKELEEKLKKYnleeLEKKAEE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 234 QAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLE--------ANVDTLTQEIDFLKTLYMEEIQ 305
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfESVEELEERLKELEPFYNEYLE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 306 LLQSHiSETSVIVKMDNSRDLNLDGI---IAEVKAQYEEVarRSRADAeawYQTKYEEmqvtagqhcDNLRNIRNEINEL 382
Cdd:PRK03918 607 LKDAE-KELEREEKELKKLEEELDKAfeeLAETEKRLEEL--RKELEE---LEKKYSE---------EEYEELREEYLEL 671
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 42760016 383 TRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEaTLSDAKCKLADLECAL 432
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKAL 720
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
221-471 |
3.75e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 221 RQLEVLVSDqarLQAERNHLQDVLEGFKKKYEEEVVcraNAENEFVALKKDVDAaFMNK-SDLEANVDTLTQEIDFLKTL 299
Cdd:PRK01156 486 REIEIEVKD---IDEKIVDLKKRKEYLESEEINKSI---NEYNKIESARADLED-IKIKiNELKDKHDKYEEIKNRYKSL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 300 YMEEI-QLLQSHISETSVIVKMDNSrdlNLDGIIAEVKAQYEEVARRSR------ADAEAWYQTKYEEMQvtagQHCDNL 372
Cdd:PRK01156 559 KLEDLdSKRTSWLNALAVISLIDIE---TNRSRSNEIKKQLNDLESRLQeieigfPDDKSYIDKSIREIE----NEANNL 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 373 RNIRNEINELTRLIQRLKAEIEHAKAQRAKLEaAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLCEYQELMNA 452
Cdd:PRK01156 632 NNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTR 710
|
250
....*....|....*....
gi 42760016 453 KLGLDIEIATYRRLLEGEE 471
Cdd:PRK01156 711 INELSDRINDINETLESMK 729
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-476 |
5.12e-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: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 162 DEKEQIKTLN---NKFTSFI----------DKVRF-LEQQNKLLETKWSFLQEQKCirsnlEPlfESYITNLRRQL---- 223
Cdd:pfam01576 170 EEEEKAKSLSklkNKHEAMIsdleerlkkeEKGRQeLEKAKRKLEGESTDLQEQIA-----EL--QAQIAELRAQLakke 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 224 EVLVSDQARLQAERNH----------LQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAfmnKSDLEANVDTLT--- 290
Cdd:pfam01576 243 EELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARNKAEKQRRDLGEELEAL---KTELEDTLDTTAaqq 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 291 -------QEIDFLKTLYMEEIQLLQSHISEtsviVKMDNSRDLNldgiiaEVKAQYEEvARRSRADAEAWYQTkyeemqv 363
Cdd:pfam01576 320 elrskreQEVTELKKALEEETRSHEAQLQE----MRQKHTQALE------ELTEQLEQ-AKRNKANLEKAKQA------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 364 tagqhcdnLRNIRNEINELTRLIQRLKAEIEH----AKAQRAKLEAAVAEAEQQ----------GEATLSDAKCKLADLE 429
Cdd:pfam01576 382 --------LESENAELQAELRTLQQAKQDSEHkrkkLEGQLQELQARLSESERQraelaeklskLQSELESVSSLLNEAE 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 42760016 430 CALQQAKQDMAR---QLCEYQELMNAKLGLDIEIATYRRLLEGEESRLCE 476
Cdd:pfam01576 454 GKNIKLSKDVSSlesQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQE 503
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
221-437 |
5.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 221 RQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEevvcRANAENEFVALKKdvdaafmNKSDLEANVDTLTQEIDFLKTLy 300
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEA-------ELEELREELEKLEKLLQLLPLY- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 301 mEEIQLLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEvaRRSRADAEAWYQTKYEEMQVTAGQHCDNLRN-IRNEI 379
Cdd:COG4717 132 -QELEALEAELAE--------------LPERLEELEERLEE--LRELEEELEELEAELAELQEELEELLEQLSLaTEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 42760016 380 NELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEAtLSDAKCKLADLECaLQQAKQ 437
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ-LENELEAAALEER-LKEARL 250
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
332-440 |
6.29e-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: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 332 IAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQhcdnlrniRNEINELTRLIQRLKAEIEHAKAQ-------RAKLE 404
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQR--------QLEIAEREREIELQEKEAEREEAEleadvrkPAEAE 317
|
90 100 110
....*....|....*....|....*....|....*.
gi 42760016 405 AAVAEAEQQGEATLSDAKCKladlecALQQAKQDMA 440
Cdd:COG2268 318 KQAAEAEAEAEAEAIRAKGL------AEAEGKRALA 347
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
333-459 |
7.34e-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: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 333 AEVKAQYEEvARRSRADAEAWYQTKyEEMQVTAGQHCDNLrnIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQ 412
Cdd:COG4913 255 EPIRELAER-YAAARERLAELEYLR-AALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 42760016 413 Q----GEATLSDAKCKLADLEcalqQAKQDMARQLCEYQELMnAKLGLDIE 459
Cdd:COG4913 331 QirgnGGDRLEQLEREIERLE----RELEERERRRARLEALL-AALGLPLP 376
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
325-473 |
7.53e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 325 DLNLDGIIAEVKAQ--YEEVARRSRADAEAWYQTKYEEmqvtagqHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAK 402
Cdd:PHA02562 187 DMKIDHIQQQIKTYnkNIEEQRKKNGENIARKQNKYDE-------LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 403 LEAAVAEAEQQ--------------------------GEATLSDAKCKLADLECALQQAK---QDMARQLCEYQELMNAK 453
Cdd:PHA02562 260 LNTAAAKIKSKieqfqkvikmyekggvcptctqqiseGPDRITKIKDKLKELQHSLEKLDtaiDELEEIMDEFNEQSKKL 339
|
170 180
....*....|....*....|
gi 42760016 454 LGLDIEIATYRRLLEGEESR 473
Cdd:PHA02562 340 LELKNKISTNKQSLITLVDK 359
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
376-476 |
8.27e-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: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 376 RNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEA----------TLSDAKCKLADLECALQQAKQDMARQLCE 445
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlrkeleelsrQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110
....*....|....*....|....*....|.
gi 42760016 446 YQElmnaklgLDIEIATYRRLLEGEESRLCE 476
Cdd:TIGR02168 756 LTE-------LEAEIEELEERLEEAEEELAE 779
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
380-442 |
9.61e-04 |
|
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: 9.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42760016 380 NELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQ---GEATLSDAKCKLADLECALQQAKQDMARQ 442
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 ... |
333-437 |
9.69e-04 |
|
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: 39.73 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 333 AEVKAQYEEvARRSRADAEAwYQTKYEEMqvtagqhcdnLRNIRNE----INELTRLIQRLKAEI-EHAKAQRAKL-EAA 406
Cdd:cd06503 33 EKIAESLEE-AEKAKEEAEE-LLAEYEEK----------LAEARAEaqeiIEEARKEAEKIKEEIlAEAKEEAERIlEQA 100
|
90 100 110
....*....|....*....|....*....|.
gi 42760016 407 VAEAEQQGEATLSDAKCKLADLecALQQAKQ 437
Cdd:cd06503 101 KAEIEQEKEKALAELRKEVADL--AVEAAEK 129
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
157-450 |
1.04e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 157 QRVKKDEKEQIKTLNNKFTSFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYItnlrRQLEvlvsDQARLQAE 236
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARI----RELE----EDIKTLTQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 237 RNHLQDV-LEGFKKKYEEEVVCRANAENEFVALKKDVDAAfmnksdlEANVDTLTQEIDFLKTLYME---EIQLLQSHIS 312
Cdd:pfam07888 144 RVLERETeLERMKERAKKAGAQRKEEEAERKQLQAKLQQT-------EEELRSLSKEFQELRNSLAQrdtQVLQLQDTIT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 313 ETSVIVKMDNSRDLNLDGIIAEVKAQYEE------------------VARRSRADAEAwYQTKYEEMQVTA--------- 365
Cdd:pfam07888 217 TLTQKLTTAHRKEAENEALLEELRSLQERlnaserkveglgeelssmAAQRDRTQAEL-HQARLQAAQLTLqladaslal 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 366 -------GQHCDNLRNI----RNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQ 434
Cdd:pfam07888 296 regrarwAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV 375
|
330
....*....|....*.
gi 42760016 435 AKQDMARQLCEYQELM 450
Cdd:pfam07888 376 AQKEKEQLQAEKQELL 391
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-394 |
1.05e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 149 NLEIDPNAQRVKKDEKE-QIKTLNNKFTSFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYITNLRRQLEVLV 227
Cdd:TIGR02168 793 QLKEELKALREALDELRaELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 228 SDQARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLYMEEIQLL 307
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 308 QSHISETSVIVKMDNSR----------------DLNLDGIiaevkAQYEEVARRsradaeawyqtkYEEMqvtAGQHCD- 370
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEarrrlkrlenkikelgPVNLAAI-----EEYEELKER------------YDFL---TAQKEDl 1012
|
250 260
....*....|....*....|....*....
gi 42760016 371 -----NLRNIRNEINELTRliQRLKAEIE 394
Cdd:TIGR02168 1013 teakeTLEEAIEEIDREAR--ERFKDTFD 1039
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
230-442 |
1.69e-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: 41.70 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 230 QARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDV----------DAAF----MNKSDLEANVDTLTQEIDF 295
Cdd:pfam01576 63 RARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIqdleeqldeeEAARqklqLEKVTTEAKIKKLEEDILL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 296 L----------KTLYMEEIQLLQSHISETSVIVKMDNSRDLNLDGIIA--EVKAQYEEvarRSRADAEAWYqtkyeemqv 363
Cdd:pfam01576 143 LedqnsklskeRKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEE---KGRQELEKAK--------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 364 tagqhcdnlRNIRNEINELTRLIQRLKAEIEHAKAQRAK----LEAAVAEAEQQGeATLSDAKCKLADLECALQQAKQDM 439
Cdd:pfam01576 211 ---------RKLEGESTDLQEQIAELQAQIAELRAQLAKkeeeLQAALARLEEET-AQKNNALKKIRELEAQISELQEDL 280
|
...
gi 42760016 440 ARQ 442
Cdd:pfam01576 281 ESE 283
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
179-463 |
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 42760016 179 DKVRFLEQQNKLLETKWSFLQEQkcirsnleplFESYITNLRRQLEVLVSDQARLQAernhlqdvlegfkkKYEEEVVCR 258
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ----------IKTYNKNIEEQRKKNGENIARKQN--------------KYDELVEEA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 259 ANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKT---LYMEEIQLLQSH---------ISETsvivkmdnsrdl 326
Cdd:PHA02562 230 KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSkieQFQKVIKMYEKGgvcptctqqISEG------------ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 327 nlDGIIAEVKAQYEEvarrsradaeawYQTKYEEMQvtagQHCDNLRNIRNEINELTRLIQRLKAEIEhakAQRAKLEAA 406
Cdd:PHA02562 298 --PDRITKIKDKLKE------------LQHSLEKLD----TAIDELEEIMDEFNEQSKKLLELKNKIS---TNKQSLITL 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 42760016 407 VAEAeQQGEATLSDAKCKLADLECALQQAKQdmarqlcEYQELMNAKLGLDIEIATY 463
Cdd:PHA02562 357 VDKA-KKVKAAIEELQAEFVDNAEELAKLQD-------ELDKIVKTKSELVKEKYHR 405
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
210-402 |
2.61e-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: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 210 PLFESYITN-------LRRQLEvLVSDQARLQAE------RNHLqdvLEGFKKKYEEEVvcranaeNEFVALKKDVDAaF 276
Cdd:smart00787 99 PLFKEYFSAspdvkllMDKQFQ-LVKTFARLEAKkmwyewRMKL---LEGLKEGLDENL-------EGLKEDYKLLMK-E 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 277 MNKsdleanVDTLTQEIDFLKTLYMEEIQLLQSHISETSvivkmDNSRDLnLDGIIAEVKAQYEEVARRSRadaeawyqt 356
Cdd:smart00787 167 LEL------LNSIKPKLRDRKDALEEELRQLKQLEDELE-----DCDPTE-LDRAKEKLKKLLQEIMIKVK--------- 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 42760016 357 KYEEMQvtagqhcDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAK 402
Cdd:smart00787 226 KLEELE-------EELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
372-474 |
3.10e-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: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 372 LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAE--------QQGEAtlSDAKcklaDLEcALQQ--AKQDMAR 441
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEarikkyeeQLGNV--RNNK----EYE-ALQKeiESLKRRI 105
|
90 100 110
....*....|....*....|....*....|....*
gi 42760016 442 QLCEYQ--ELMNAKLGLDIEIATYRRLLEGEESRL 474
Cdd:COG1579 106 SDLEDEilELMERIEELEEELAELEAELAELEAEL 140
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
282-441 |
4.06e-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: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 282 LEANVDTLTQEIDFLKtlymEEIQLLQSHISETSVIVKmdnsrDLNLDgiIAEVKAQYEEVARRsradaeawyQTKYEEM 361
Cdd:COG1579 22 LEHRLKELPAELAELE----DELAALEARLEAAKTELE-----DLEKE--IKRLELEIEEVEAR---------IKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 362 QvtaGQHCDN--LRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDM 439
Cdd:COG1579 82 L---GNVRNNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
..
gi 42760016 440 AR 441
Cdd:COG1579 159 EE 160
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
155-474 |
4.93e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 155 NAQRVKKDEKEQIKTLNNKFTSFIDKVRFLEQQNKLLETKWSFLQEQkcirsnleplfesyITNLRRQLEVLVSDQARLQ 234
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--------------LESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 235 AERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAafmnksdLEANVDTLTQEIDFL-KTLYMEEIQLLQSHISE 313
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES-------LQEELAALEQELQALsEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 314 TSVIVK-----MDNSRDLNLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQHcDNLRNIRNEINELTRLIQR 388
Cdd:COG4372 195 NAEKEEelaeaEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE-VILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 389 LKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLE 468
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
....*.
gi 42760016 469 GEESRL 474
Cdd:COG4372 354 DVLELL 359
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
162-395 |
4.96e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.82 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 162 DEKEQIKTLN------NKFTSF------IDKVRFLEQQNKLLET-----KWSFLQEQKCIR---SNLEPLfESYITNLRR 221
Cdd:PRK04778 48 DELEKVKKLNltgqseEKFEEWrqkwdeIVTNSLPDIEEQLFEAeelndKFRFRKAKHEINeieSLLDLI-EEDIEQILE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 222 QLEVLVSDQARLQAERNHLQDVLEGFKK-------KY-------EEEVvcrANAE---NEFVALKK--DVDAAFMNKSDL 282
Cdd:PRK04778 127 ELQELLESEEKNREEVEQLKDLYRELRKsllanrfSFgpaldelEKQL---ENLEeefSQFVELTEsgDYVEAREILDQL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 283 EANVDTLTQEIDFLKTLYME-------EIQLLQS----------HISETSV---IVKMDNSRDLNLDGI----IAEVKAQ 338
Cdd:PRK04778 204 EEELAALEQIMEEIPELLKElqtelpdQLQELKAgyrelveegyHLDHLDIekeIQDLKEQIDENLALLeeldLDEAEEK 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 339 YEEVARRsradaeawYQTKYEEMQ--VTAGQHCD-NLRNIRNEINELTRLIQRLKAEIEH 395
Cdd:PRK04778 284 NEEIQER--------IDQLYDILEreVKARKYVEkNSDTLPDFLEHAKEQNKELKEEIDR 335
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
372-437 |
6.44e-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: 37.14 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 372 LRNIRNEINELTRLIQRLKAEIEHAK------------AQRA----------KLEAAVAEAEQQGEATLSDAKCKLADLE 429
Cdd:COG3599 36 YERLIRENKELKEKLEELEEELEEYReleetlqktlvvAQETaeevkenaekEAELIIKEAELEAEKIIEEAQEKARKIV 115
|
....*...
gi 42760016 430 CALQQAKQ 437
Cdd:COG3599 116 REIEELKR 123
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
213-437 |
7.98e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 38.55 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 213 ESYITNLRRQLEVLVSDQA----RLQAERNHLQDVLEGFKKKYEEEVVCRANAENefvaLKKDVDAAFMNKSDLEANVDT 288
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENahkiQIEILEKELSSLAQETEELQKKATQTLAKAQQ----VNAESERTLGHAKELAEAIKN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 289 LTQEIDFL--KTLYM--EEIQLLQSHISETSVIVK--MDNSRDLNLDGIIAEVKAQYEEvARRSRADAEAWYQTKYEEMQ 362
Cdd:pfam06008 94 LIDNIKEIneKVATLgeNDFALPSSDLSRMLAEAQrmLGEIRSRDFGTQLQNAEAELKA-AQDLLSRIQTWFQSPQEENK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42760016 363 VTA-------GQHCDNLRNIRNEINEL---TRLIQRLKAEIEHA--KAQRAKLEaaVAEAEQQGEATLSDAKCKLADLEC 430
Cdd:pfam06008 173 ALAnalrdslAEYEAKLSDLRELLREAaakTRDANRLNLANQANlrEFQRKKEE--VSEQKNQLEETLKTARDSLDAANL 250
|
....*..
gi 42760016 431 ALQQAKQ 437
Cdd:pfam06008 251 LLQEIDD 257
|
|
| |
