|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
173-483 |
1.51e-147 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 428.57 E-value: 1.51e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 173 EKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCAR-SNLEPLFDNYITNLRRQLDVLSSDQARLQAERNHLQ 251
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 252 DILEGFKKKYEEEVVFRANAENEFVALKKDVDAAFLNKSDLEANVDTLIQETEFLKALYHEEIEMLQSHISETSVIVKMD 331
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 332 NSRDLNLDGIIAEVKAQYEEVARRSRADVESWYQTKYEEMRVTAGQHCDNLRSTRDEINELTRLIQRLKAEIEHTKAQCA 411
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940882 412 KLEAAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMARQLREYQELMNVKLALDIEIVTYRRLLEGEEIR 483
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
16-169 |
2.27e-37 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 135.94 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 16 SFSSCSAMAPqHLNRFRSSSVSCRSGPGFRGL------GGFGSRSVINFG---SSSPRIAVGCSRPVrCGVGFGAGSGMA 86
Cdd:pfam16208 1 GFSSCSAVVP-SRSRRSYSSVSSSRRGGGGGGggggggGGFGSRSLYNLGgskSISISVAGGGSRPG-SGFGFGGGGGGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 87 FGSGDG----LGFRASSgvglgfgaggCPSYGFGGPGFGGPGFGGPGFGYRiGGIGGPSAP--AITAVTVNQSLLTPLNL 160
Cdd:pfam16208 79 FGGGFGggggGGFGGGG----------GFGGGFGGGGYGGGGFGGGGFGGR-GGFGGPPCPpgGIQEVTVNQSLLQPLNL 147
|
....*....
gi 341940882 161 EIDPNAQRV 169
Cdd:pfam16208 148 EIDPEIQRV 156
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
159-415 |
1.33e-11 |
|
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: 67.35 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 159 NLEIDPNAQRVKRDEKE-QIKTLNNKFASFIDKVRFLEQQNKLLETKwsfLQEQKcarsNLEPLFDNYITNLRRQLDVLS 237
Cdd:TIGR04523 353 NSESENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQE----KLNQQKDEQIKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 238 SDQARLQAERN----------------------------HLQDILEGFKKKYEEEvvfRANAEN---EFVALKKDVDAAF 286
Cdd:TIGR04523 426 KEIERLKETIIknnseikdltnqdsvkeliiknldntreSLETQLKVLSRSINKI---KQNLEQkqkELKSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 287 LNKSDLEANVDTLIQETEFLKalyhEEIEMLQSHI----SETSVIVKMDNSRDLNLDgiiaevKAQYEEVARRSRADVES 362
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLK----EKIEKLESEKkekeSKISDLEDELNKDDFELK------KENLEKEIDEKNKEIEE 572
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 341940882 363 WYQT------KYEEMRVTAGQHCDNLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEA 415
Cdd:TIGR04523 573 LKQTqkslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-465 |
4.39e-11 |
|
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: 66.23 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 163 DPNAQRVKRDEKeqIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCARSNLEPLFDNYITNLRRQLDVL------ 236
Cdd:TIGR02168 667 KTNSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveq 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 237 -SSDQARLQAERNHLQDILEGFKKKYEEEVVFRANAENEFVALKKDVDAAFLNKSDLEANVDTLIQETEFLKALYH---E 312
Cdd:TIGR02168 745 lEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAnlrE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 313 EIEMLQSHISETSVIVKMDNSRDLNLDGIIAEVKAQ---YEEVARRSRADVESWYQtKYEEMRVTAGQHCDNLRSTRDEI 389
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieeLEELIEELESELEALLN-ERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 390 NELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQ-----------GEAALNDAKCKLADLEGALQQAKQDMARQLREYQE 458
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
....*..
gi 341940882 459 LMNVKLA 465
Cdd:TIGR02168 984 LGPVNLA 990
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
208-459 |
7.21e-09 |
|
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: 58.93 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 208 LQEQKCARSNLEpLFDNYITNLRRQLDvlssdqaRLQAERNHLQDILEGFKKKYEEEVVFRANAENEFVALKKDVDA--- 284
Cdd:TIGR02169 176 LEELEEVEENIE-RLDLIIDEKRQQLE-------RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERqla 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 285 ---AFLNKSD---------LEANVDTLIQETEFLKALYHEEIEMLQSHISET---------SVIVKMDNSRDL-----NL 338
Cdd:TIGR02169 248 sleEELEKLTeeiselekrLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeaeiaslerSIAEKERELEDAeerlaKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 339 DGIIAEVKAQYEEVARR---SRADVESW------YQTKYEEMRVTAGQHCDNLRSTRD--------------EINELTRL 395
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREieeERKRRDKLteeyaeLKEELEDLRAELEEVDKEFAETRDelkdyrekleklkrEINELKRE 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940882 396 IQRLKAEIEHTKAQCAKLEAAVAEAEQ---QGEAALNDAKCKLADLEGALQQAKQDMARQLREYQEL 459
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
265-591 |
8.97e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 8.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 265 VVFRANAENEFVALKKDVDAAFLNKSDLEANVDTLIQETEFLKALY---HEEIEMLQSHISETSVivkmdnsrdlNLDGI 341
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQA----------EIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 342 IAEVKAQYEEVARRSRADVESWYQTKYEEMRVTAG------QHCDNLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEA 415
Cdd:COG3883 78 EAEIEERREELGERARALYRSGGSVSYLDVLLGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 416 AVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMARQLREYQELMNVKLALDIEIVTYRRLLEGEEIRICEGVGPVNISV 495
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 496 SSSRGGVLCGPELVSGSSLSHNGGVTFSTSSSIRATGGVLASSSLRAGGDLLSSGSRGGSVLVGDACAPSIPCALPTEGG 575
Cdd:COG3883 238 AAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGG 317
|
330
....*....|....*.
gi 341940882 576 FSSCSGGRGNRSSSVR 591
Cdd:COG3883 318 GAGAVVGGASAGGGGG 333
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
155-470 |
5.47e-08 |
|
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: 55.80 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 155 LTPLNLEIDPNAQRVKRDE------KEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCARSNLEPLFDNYITN 228
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEvelnklEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 229 LRRQLDVLSSDQARLqaerNHLQDILEGFKKKYEEEVVFRANAENEFVALKKDVDaafLNKSDLEaNVDTLIQETE---- 304
Cdd:TIGR04523 185 IQKNIDKIKNKLLKL----ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE---KKQQEIN-EKTTEISNTQtqln 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 305 FLKALYHEEIEMLQSHISEtsviVKMDNSRDLNLDGIIAEVKAQYEEVARRSRAD----VESWYQTKYEEMRVTAGQhcd 380
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKE----LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwnkeLKSELKNQEKKLEEIQNQ--- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 381 nLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQGEAALNDAKCKLADLEgALQQAKQDMARQLREYQELM 460
Cdd:TIGR04523 330 -ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLN 407
|
330
....*....|
gi 341940882 461 NVKlalDIEI 470
Cdd:TIGR04523 408 QQK---DEQI 414
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
214-484 |
7.13e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 214 ARSNLEPLFDnyITN-LRRQLDVLSsDQARlQAERnhlqdilegfKKKYEEEvvfranaenefvALKKDVDAAFLNKSDL 292
Cdd:COG1196 184 TEENLERLED--ILGeLERQLEPLE-RQAE-KAER----------YRELKEE------------LKELEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 293 EANVDTLIQETEFLKAlyheEIEMLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEVARRSRADVESWYQTKYEEMR 372
Cdd:COG1196 238 EAELEELEAELEELEA----ELEELEAELAE--------------LEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 373 VTAGqhcdnLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQGEAA---LNDAKCKLADLEGALQQAKQDM 449
Cdd:COG1196 300 LEQD-----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAEL 374
|
250 260 270
....*....|....*....|....*....|....*
gi 341940882 450 ARQLREYQELMNVKLALDIEIVTYRRLLEGEEIRI 484
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
223-495 |
1.31e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 223 DNYIT-NLRRQLDVLSSDQARLQAERNHLQDILEGFKKKYEEevvFRAnaENEFVALKKDVDAAFLNKSDLEANVDTLIQ 301
Cdd:COG3206 159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE---FRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 302 ETEFLKALYheeiEMLQSHISETSvivkmDNSRDLNLDGIIAEVKAQYEEVARRsRADVESWYQTKYEEMRvtagqhcdn 381
Cdd:COG3206 234 ELAEAEARL----AALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-LAELSARYTPNHPDVI--------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 382 lrSTRDEINELTRLIQRLKAEIEhtkaqcAKLEAAVAEAEQQgEAALNDakcKLADLEGALQQakqdMARQLREYQELMN 461
Cdd:COG3206 295 --ALRAQIAALRAQLQQEAQRIL------ASLEAELEALQAR-EASLQA---QLAQLEARLAE----LPELEAELRRLER 358
|
250 260 270
....*....|....*....|....*....|....*..
gi 341940882 462 vklalDIEIV--TYRRLLEG-EEIRICEGVGPVNISV 495
Cdd:COG3206 359 -----EVEVAreLYESLLQRlEEARLAEALTVGNVRV 390
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-478 |
1.82e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 226 ITNLRRQLDVLSSDQARLQAERNHLQDILEGFKKKYEEEVVFRANAENEFVALKKDVDAAFLNKSDLEANvdtliqetef 305
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---------- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 306 lKALYHEEIEMLQSHISETSVIVKMDNSRDLNLDGIIAEVKAQYEEVARRS---RADVESwYQTKYEEMRVTAGQHCDNL 382
Cdd:TIGR02168 304 -KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELeslEAELEE-LEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 383 RSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQG--------EAALNDAKCKLADLEGALQQAKQDMARQLR 454
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkkleEAELKELQAELEELEEELEELQEELERLEE 461
|
250 260
....*....|....*....|....
gi 341940882 455 EYQELMNVKLALDIEIVTYRRLLE 478
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELA 485
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
167-463 |
2.19e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 167 QRVKRDEkEQIKTLNNKFASfidKVRFLEQQNKLLETKWSFLQEQKCARSNLEPLFDNyitnlRRQLDVLSSDqarLQAE 246
Cdd:pfam05483 370 QRLEKNE-DQLKIITMELQK---KSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE-----KKQFEKIAEE---LKGK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 247 RNHLQDILEGFKKK---YEEEVVFRANAENEFVA----LKKDVDAAFLNKSDLEANVDTLIQETeflKALYHEEIEM--- 316
Cdd:pfam05483 438 EQELIFLLQAREKEihdLEIQLTAIKTSEEHYLKevedLKTELEKEKLKNIELTAHCDKLLLEN---KELTQEASDMtle 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 317 LQSH--------ISETSVIVKMDN--SRDLNL----DGIIAEVKAQYEEV------ARRSRADVESWYQTKYEEMRVTAG 376
Cdd:pfam05483 515 LKKHqediinckKQEERMLKQIENleEKEMNLrdelESVREEFIQKGDEVkckldkSEENARSIEYEVLKKEKQMKILEN 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 377 QhCDNLRStrdEINELTRLIQRLKAEIEHTKAQcakleaAVAEAEQqgeaaLNDAKCKLADLEGALQQAKQDMARQLREY 456
Cdd:pfam05483 595 K-CNNLKK---QIENKNKNIEELHQENKALKKK------GSAENKQ-----LNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
....*..
gi 341940882 457 QELMNVK 463
Cdd:pfam05483 660 QKEIEDK 666
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
206-459 |
3.24e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 206 SFLQEQKCARSNLEPLFDNyITNLRRQLDVLSSDQARLQAERNHLQDILEGFKKKYEEEVVFRANAENEFVALKKDVDAA 285
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQE-LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 286 FLNKSDLEANVDTLIQEteflkaLYHEEIEMLQSHISETSVIVKmdnsrdlNLDGIIAEVKAQYEEVARRsRADVESWYQ 365
Cdd:TIGR02169 771 EEDLHKLEEALNDLEAR------LSHSRIPEIQAELSKLEEEVS-------RIEARLREIEQKLNRLTLE-KEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 366 TKYEEMRvtagqhcdnlrSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQgeaalndakckLADLEGALQQA 445
Cdd:TIGR02169 837 ELQEQRI-----------DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR-----------LGDLKKERDEL 894
|
250
....*....|....
gi 341940882 446 KQDMARQLREYQEL 459
Cdd:TIGR02169 895 EAQLRELERKIEEL 908
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
223-589 |
1.12e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 223 DNYITNLRRQLDVLSSDQARLQAERNHLQDILEGFKKKYEEevvfranAENEFVALKKDVDAAflnksdleanvdtliqe 302
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEIDKL----------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 303 teflkalyHEEIEMLQshisetsvivkmdnsrdlnldgiiAEVKAQYEEVARRSRADVESWYQTKYEEMRVTAgqhcDNL 382
Cdd:COG3883 71 --------QAEIAEAE------------------------AEIEERREELGERARALYRSGGSVSYLDVLLGS----ESF 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 383 RSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQgeaaLNDAKCKLADLEGALQQAKQDMARQLREYQELMNV 462
Cdd:COG3883 115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK----LAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 463 KLALDIEIVTYRRLLEGEEIRICEGVGPVNISVSSSRGGVLCGPELVSGSSLSHNGGVTFSTSSSIRATGGVLASSSLRA 542
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 341940882 543 GGDLLSSGSRGGSVLVGDACAPSIPCALPTEGGFSSCSGGRGNRSSS 589
Cdd:COG3883 271 AAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGG 317
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
344-439 |
1.17e-05 |
|
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: 44.94 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 344 EVKAQYEEVARRSRADVES----W--YQTKYE-EMRvtagQHCD---NLRSTRDEINELTRLIQRLKAEIEHTKAQCAKL 413
Cdd:pfam07926 15 EEAADAEAQLQKLQEDLEKqaeiAreAQQNYErELV----LHAEdikALQALREELNELKAEIAELKAEAESAKAELEES 90
|
90 100
....*....|....*....|....*.
gi 341940882 414 EAAVAEAEQQGEAALNDAKCKLADLE 439
Cdd:pfam07926 91 EESWEEQKKELEKELSELEKRIEDLN 116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
382-462 |
1.64e-05 |
|
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: 47.45 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 382 LRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQ---GEAALNDAKCKLADLEGALQQAKQDMARQLREYQE 458
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
....
gi 341940882 459 LMNV 462
Cdd:COG4942 109 LLRA 112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
292-478 |
2.95e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 292 LEANVDTLIQETEflKAL----YHEEIEMLQSHISeTSVIVKMDNSRDlNLDGIIAEVKAQYEEVARRSRAdveswYQTK 367
Cdd:TIGR02168 198 LERQLKSLERQAE--KAErykeLKAELRELELALL-VLRLEELREELE-ELQEELKEAEEELEELTAELQE-----LEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 368 YEEMRVTAGQHCDNLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAE---QQGEAALNDAKCKLADLEGALQQ 444
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEaqlEELESKLDELAEELAELEEKLEE 348
|
170 180 190
....*....|....*....|....*....|....
gi 341940882 445 AKQDMARQLREYQELMNVKLALDIEIVTYRRLLE 478
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
195-486 |
5.62e-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: 44.92 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 195 EQQNKLLEtkwsfLQEqkcarsnleplFDNYITNLRRQLdvlssdqARLQAERNHLQDILEGFKKKYEEevvfranAENE 274
Cdd:COG1579 4 EDLRALLD-----LQE-----------LDSELDRLEHRL-------KELPAELAELEDELAALEARLEA-------AKTE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 275 FVALKKDVDAAflnKSDLEAnVDTLIqeteflkalyhEEIEMLQSHISetsvivkmdNSRDLnlDGIIAEVkaqyeEVAR 354
Cdd:COG1579 54 LEDLEKEIKRL---ELEIEE-VEARI-----------KKYEEQLGNVR---------NNKEY--EALQKEI-----ESLK 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 355 RSRADVEswyqtkyeemrvtagqhcdnlrstrDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQGEAALNDAKCK 434
Cdd:COG1579 103 RRISDLE-------------------------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341940882 435 LADLEGALQQAKQDM-ARQLREYQELMNVK--LA-------------LDIEIVTYRRLLEGEEIRICE 486
Cdd:COG1579 158 LEELEAEREELAAKIpPELLALYERIRKRKngLAvvpveggacggcfMELPPQELNEIRAADEIVRCP 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-461 |
7.09e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 222 FDNyitnlRRQLDVLSSDQARLQAERNHLQDILEGFKKKYEEevvfranaenefVALKKDVDAAFLNKSDLEANVDTLiq 301
Cdd:COG4913 606 FDN-----RAKLAALEAELAELEEELAEAEERLEALEAELDA------------LQERREALQRLAEYSWDEIDVASA-- 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 302 eteflkalyHEEIEMLQSHISEtsvivkMDNSrdlnlDGIIAEVKAQYEEVARRsradveswyqtkyeemrvtagqhcdn 381
Cdd:COG4913 667 ---------EREIAELEAELER------LDAS-----SDDLAALEEQLEELEAE-------------------------- 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 382 LRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQGEAALN---DAKCKLADLEGALQQAKQDMARQLREYQE 458
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAALGDAVERELRENLEERIDALRA 780
|
...
gi 341940882 459 LMN 461
Cdd:COG4913 781 RLN 783
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
223-481 |
1.43e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 223 DNYITNLRRQLDVLSS-DQARLQAERNHLQDiLEGFKKKYEEEVVFRANAENEFVALKKDVDAafLNKSDLEAnvdtliQ 301
Cdd:PRK01156 496 DEKIVDLKKRKEYLESeEINKSINEYNKIES-ARADLEDIKIKINELKDKHDKYEEIKNRYKS--LKLEDLDS------K 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 302 ETEFLKALYHE---EIEMLQSHISETSVIVKMDNSRdlnldgiIAEVKAQYEevarrsraDVESWYQTKYEEMRvtagQH 378
Cdd:PRK01156 567 RTSWLNALAVIsliDIETNRSRSNEIKKQLNDLESR-------LQEIEIGFP--------DDKSYIDKSIREIE----NE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 379 CDNLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEaAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMARQLREYQE 458
Cdd:PRK01156 628 ANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
250 260
....*....|....*....|...
gi 341940882 459 LMNVKLALDIEIVTYRRLLEGEE 481
Cdd:PRK01156 707 LRTRINELSDRINDINETLESMK 729
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
390-452 |
2.54e-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: 41.53 E-value: 2.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940882 390 NELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQ---GEAALNDAKCKLADLEGALQQAKQDMARQ 452
Cdd:pfam11559 55 ESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
165-484 |
2.84e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 165 NAQRVKRDEKEQIKTLNNKFASFIDKvrfLEQQNKLLETKwsfLQEQKCARSNLEplfdnyitNLRRQLDVLSSDQARLQ 244
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEE---LEELNEQLQAA---QAELAQAQEELE--------SLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 245 AERNHLQDILEGFKKKYEEEVVFRANAENEFVALKKDVDAaflnksdLEANVDTLIQETEFL-KALYHEEIEMLQSHISE 323
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES-------LQEELAALEQELQALsEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 324 TSVIVK-----MDNSRDLNLDGIIAEVKAQYEEVARRSRADVESWYQTKYEEMRVTAGQHcDNLRSTRDEINELTRLIQR 398
Cdd:COG4372 195 NAEKEEelaeaEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE-VILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 399 LKAEIEHTKAQCAKLEAAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMARQLREYQELMNVKLALDIEIVTYRRLLE 478
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
....*.
gi 341940882 479 GEEIRI 484
Cdd:COG4372 354 DVLELL 359
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
197-469 |
3.40e-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: 43.35 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 197 QNKL---LETKWSFLQEQKCARSNLEPLFDNYITN---LRRQLDVLSSDQARLQAERNHLQDILEGFKKKYEEEVVFRAN 270
Cdd:pfam07888 33 QNRLeecLQERAELLQAQEAANRQREKEKERYKRDreqWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 271 AENEFVALKKDVDAAFLNKSDLEANVDTLIQ-----ETEF------------LKALYHEEIEMLQSHISETSVIVKMDNS 333
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQrvlerETELermkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 334 RDLNLDGIIAEVKAQyeevARRSRADVESWYQTKYEEMRVTAG--QHCDNLRSTRDEINELTRLIQRLKAEIEHTKAQ-- 409
Cdd:pfam07888 193 EFQELRNSLAQRDTQ----VLQLQDTITTLTQKLTTAHRKEAEneALLEELRSLQERLNASERKVEGLGEELSSMAAQrd 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940882 410 --CAKLEAAVAEAEQ------QGEAALNDAKCKLA-DLEGALQQAKQDMARQLREYQELMNVKLALDIE 469
Cdd:pfam07888 269 rtQAELHQARLQAAQltlqlaDASLALREGRARWAqERETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
308-484 |
4.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 308 ALYHEEIEMLQSHISEtsvivkmdnsrdlnLDGIIAEVKAQYEEVARRSRA----DVESWYQTK---YEEMRVTAGQHCD 380
Cdd:COG4913 613 AALEAELAELEEELAE--------------AEERLEALEAELDALQERREAlqrlAEYSWDEIDvasAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 381 NLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMARQLRE-YQEL 459
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErFAAA 758
|
170 180 190
....*....|....*....|....*....|.
gi 341940882 460 M------NVKLALDIEIVTYRRLLEGEEIRI 484
Cdd:COG4913 759 LgdaverELRENLEERIDALRARLNRAEEEL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
232-475 |
5.02e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 232 QLDVLSSDQARLQAERNHLQDILEGFKKKYEEEVVFRANAENEFVALKKDVDAAFLNKSDLEANVDTLIQETEFLKALYH 311
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 312 EEIEMLQSHISetsVIVKMDNSRDLNLdgIIAevKAQYEEVARRSRadveswYQTKYEEMRvtagqhcdnlrstRDEINE 391
Cdd:COG4942 101 AQKEELAELLR---ALYRLGRQPPLAL--LLS--PEDFLDAVRRLQ------YLKYLAPAR-------------REQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 392 LTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQG---EAALNDAKCKLADLEGALQQAKQDMARQLREYQELMNVKLALDI 468
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERaalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*..
gi 341940882 469 EIVTYRR 475
Cdd:COG4942 235 EAAAAAE 241
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
178-481 |
5.91e-04 |
|
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: 43.11 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 178 KTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCARSNLEpLFDNYITNLRRQLDVLSSDQARLQAERNHLQ------ 251
Cdd:TIGR00606 169 KALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELK-YLKQYKEKACEIRDQITSKEAQLESSREIVKsyenel 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 252 DILEGFKKKYEEEVVFRANAENEFVALKKDVDAAFLNKSDLEANVDTLIQET-EFLKALYHEEIEMLQSHISETSVIVKM 330
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTdEQLNDLYHNHQRTVREKERELVDCQRE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 331 -----DNSRDLNldgiiaEVKAQYE-EVARRS-RADVESWYQTKYEEMRVTAGQHC--DNLRSTRDEINELTRLIQRLKA 401
Cdd:TIGR00606 328 leklnKERRLLN------QEKTELLvEQGRLQlQADRHQEHIRARDSLIQSLATRLelDGFERGPFSERQIKNFHTLVIE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 402 EIEHTKAQCAKLEAAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMArqlREYQELMNVKLALDIEIVTYRRLLEGEE 481
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE---KKQEELKFVIKELQQLEGSSDRILELDQ 478
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
188-398 |
6.00e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 188 IDKVRFLEQQNKLLETKW-SFLQE----QKCARSNLEPLFDNyITNLRRQLDVLSSD--QARLQAERNHLQDILEGFKKK 260
Cdd:COG4717 304 AEELQALPALEELEEEELeELLAAlglpPDLSPEELLELLDR-IEELQELLREAEELeeELQLEELEQEIAALLAEAGVE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 261 YEEEVVFRANAENEFVALKKDVDAA--FLNKSDLEANVDTLIQETEFLKA----------LYHEEIEMLQSHISETSVIV 328
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELeeQLEELLGELEELLEALDEEELEEeleeleeeleELEEELEELREELAELEAEL 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 329 KmdnsrDLNLDGIIAEVKAQYEEVARRSRADVESWYQTKYeeMRVTAGQHCDNLRSTRdeineLTRLIQR 398
Cdd:COG4717 463 E-----QLEEDGELAELLQELEELKAELRELAEEWAALKL--ALELLEEAREEYREER-----LPPVLER 520
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-468 |
6.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 342 IAEVKAQYEEVARRsRADVESWYQTKYEEMRVTAGQHcdNLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAE 421
Cdd:COG4717 390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 341940882 422 QQGEaalndakckLADLEGALQQAKQDMARQLREYQELmnvKLALDI 468
Cdd:COG4717 467 EDGE---------LAELLQELEELKAELRELAEEWAAL---KLALEL 501
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
189-455 |
6.99e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 189 DKVRFLEQQNKLLETKWSFLQEQkcarsnLEpLFDNYITNLRRQLDVlssDQARLQAernhlqdilegfkkKYEEEVVFR 268
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ------IK-TYNKNIEEQRKKNGE---NIARKQN--------------KYDELVEEA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 269 ANAENEFVALKKDVDAAFLNKSDLEANVDTLIQETEFLKA---LYHEEIEMLQSH---------ISETsvivkmdnsrdl 336
Cdd:PHA02562 230 KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSkieQFQKVIKMYEKGgvcptctqqISEG------------ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 337 nlDGIIAEVKAQYEEvarrsradveswYQTKYEEMRvtagQHCDNLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAA 416
Cdd:PHA02562 298 --PDRITKIKDKLKE------------LQHSLEKLD----TAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK 359
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 341940882 417 V--AEAE-QQGEAALNDAKCKLADLEGALQQAKQDMARQLRE 455
Cdd:PHA02562 360 AkkVKAAiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
232-458 |
7.50e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 232 QLDVLSSDQARLQAERNHLQDILEGFKK--KYEEEVVFR-ANAENEFVALKKDVDAAFLNKSDLEANVDTLIQETEFLKA 308
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKfiKRTENIEELiKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 309 LyHEEIEMLQSHISETSVIVKMDNSRDLNLDGIIAEVKAQYEEVaRRSRADVES--WYQTKYEEMRvtagqhcDNLRSTR 386
Cdd:PRK03918 236 L-KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVKELKElkEKAEEYIKLS-------EFYEEYL 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940882 387 DEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQgEAALNDAKCKLADLEG---ALQQAKQDMARqLREYQE 458
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL-KKKLKELEKRLEELEErheLYEEAKAKKEE-LERLKK 379
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
161-438 |
1.02e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 161 EIDPNAQRVKRDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEqkcarsnleplfdnyitNLRRQLDVLSSDQ 240
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGR-----------------TIELKKEILEKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 241 ARLQAERNHLQDILEGFKKKYE-EEVVFRANAEnefvalkkdvdaafLNKSDLEANVDTLIQETEFLKalyHEEIEMLQS 319
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDRILElDQELRKAERE--------------LSKAEKNSLTETLKKEVKSLQ---NEKADLDRK 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 320 HISETSVIVKMDNSRdlnldgiiaEVKAQYEEVARRSradveswyQTKYEEMRVTAGQHCDNLRSTRDEI---NELTRLI 396
Cdd:TIGR00606 517 LRKLDQEMEQLNHHT---------TTRTQMEMLTKDK--------MDKDEQIRKIKSRHSDELTSLLGYFpnkKQLEDWL 579
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 341940882 397 QRLKAEIEHTKAQCAKLEAAVAEAEQQGEAALNDAKCKLADL 438
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
243-458 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 243 LQAERNHLQDILEGFKKKYEEEVVFRANAENEFVALK---KDVDAAFLNksdLEANVDTLIQEteflKALYHEEIEMLQS 319
Cdd:pfam01576 94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEakiKKLEEDILL---LEDQNSKLSKE----RKLLEERISEFTS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 320 HISETSVIVKMDNSRDLNLDGIIA--EVKAQYEEvarRSRADVESWYqtkyeemrvtagqhcdnlRSTRDEINELTRLIQ 397
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEE---KGRQELEKAK------------------RKLEGESTDLQEQIA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940882 398 RLKAEIEHTKAQCAK----LEAAVAEAEQQGeAALNDAKCKLADLEGALQQAKQDMA--RQLREYQE 458
Cdd:pfam01576 226 ELQAQIAELRAQLAKkeeeLQAALARLEEET-AQKNNALKKIRELEAQISELQEDLEseRAARNKAE 291
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
155-447 |
1.66e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 155 LTPLNLEIDpNAQRVKRDEKEQIKTLNNKFASFIDKVrFLEQQNKLLETKWSFLQEQ-KCARSNLEPL------FDNYIT 227
Cdd:TIGR00606 593 LAKLNKELA-SLEQNKNHINNELESKEEQLSSYEDKL-FDVCGSQDEESDLERLKEEiEKSSKQRAMLagatavYSQFIT 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 228 NLRRQ-------LDVLSSDQARLQAERNHLQDILEGFKKKYEEevvfranAENEFVALKKDVDAaFLNKSDLEANVDTLI 300
Cdd:TIGR00606 671 QLTDEnqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKS-------TESELKKKEKRRDE-MLGLAPGRQSIIDLK 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 301 QET-----EFLKALyHEEIEMLQSHISET-----SVIVKMDNSRDLNLD-GIIAEVKAQYEEVARR-----SRADVESWY 364
Cdd:TIGR00606 743 EKEipelrNKLQKV-NRDIQRLKNDIEEQetllgTIMPEEESAKVCLTDvTIMERFQMELKDVERKiaqqaAKLQGSDLD 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 365 QTkYEEMRVTAGQHCDNLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEA---AVAEAEQQGEAALNDAKCKLADLEGA 441
Cdd:TIGR00606 822 RT-VQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQSL 900
|
....*.
gi 341940882 442 LQQAKQ 447
Cdd:TIGR00606 901 IREIKD 906
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
380-470 |
1.66e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 380 DNLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQ---GEAALNDAKCKLADLEGALQQAKQDMARQLREY 456
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90
....*....|....
gi 341940882 457 QELMNVKLALDIEI 470
Cdd:COG4372 125 QDLEQQRKQLEAQI 138
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
231-445 |
1.68e-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: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 231 RQLDVLSSDQARLQAERNHLQDILegfkkkyEEEVVFRANAENEFVAL-------KKD-------VDAAFLNKSDLEANV 296
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQL-------EEEEEAKRNVERQLSTLqaqlsdmKKKleedagtLEALEEGKKRLQREL 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 297 DTLIQETEfLKALYHEEIE----MLQSHISEtsVIVKMDNSRDL--NL-------DGIIAEVK---AQYEEvaRRSRADV 360
Cdd:pfam01576 555 EALTQQLE-EKAAAYDKLEktknRLQQELDD--LLVDLDHQRQLvsNLekkqkkfDQMLAEEKaisARYAE--ERDRAEA 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 361 ESwyqtKYEEMRVTAGQHcdNLRSTRDEINELTRLIQRLKAEIE---HTKAQCAK----LEAAVAEAEQQGEaalnDAKC 433
Cdd:pfam01576 630 EA----REKETRALSLAR--ALEEALEAKEELERTNKQLRAEMEdlvSSKDDVGKnvheLERSKRALEQQVE----EMKT 699
|
250
....*....|..
gi 341940882 434 KLADLEGALQQA 445
Cdd:pfam01576 700 QLEELEDELQAT 711
|
|
| BRE1 |
pfam08647 |
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ... |
412-478 |
2.84e-03 |
|
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.
Pssm-ID: 462547 [Multi-domain] Cd Length: 95 Bit Score: 37.18 E-value: 2.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940882 412 KLEAAVAEAEQQgeaaLNDAKCKLADLEGALQQAKQDMARQLREYQELMNVKLALDIEIVTYRRLLE 478
Cdd:pfam08647 7 KLEQAFEELSEQ----LDKKVKDLTILEEKKLRLEAEKAKADQKYFAAMRSKDALENENKKLNTLLS 69
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
387-452 |
4.89e-03 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 38.31 E-value: 4.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940882 387 DEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQGE---AALNDAKCKLADLEGALQQAKQDMARQ 452
Cdd:pfam05335 66 QELREAEAVVQEESASLQQSQANANAAQRAAQQAQQQLEaltAALKAAQANLENAEQVAAGAQQELAEK 134
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
243-449 |
5.39e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 38.86 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 243 LQAERNHLQDILEGFKKKYEEEVVFRANAENEFVALKKDVDaafLNKSDLEANVDTLIQETeflkalyhEEIEMLQSHIS 322
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQ---LLEEELERTEERLAEAL--------EKLEEAEKAAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 323 ETSVIVKMDNSRDLNLDGIIAEVKAQ--------------YEEVARR------------SRADV-ESWYQTKYEEMRVTA 375
Cdd:pfam00261 75 ESERGRKVLENRALKDEEKMEILEAQlkeakeiaeeadrkYEEVARKlvvvegdleraeERAELaESKIVELEEELKVVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 376 gqhcDNLRS---------TRDEINELT-RLIQ-RLKAEI---EHTKAQCAKLEAAVaeaeQQGEAALNDAKCKLADLEGA 441
Cdd:pfam00261 155 ----NNLKSleaseekasEREDKYEEQiRFLTeKLKEAEtraEFAERSVQKLEKEV----DRLEDELEAEKEKYKAISEE 226
|
....*...
gi 341940882 442 LQQAKQDM 449
Cdd:pfam00261 227 LDQTLAEL 234
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
390-464 |
5.41e-03 |
|
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: 38.35 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 390 NELTR----LIQRLKAEIEHTKAQCAKLEAAVAEAEQQGEaalndakcklaDLEGALQQAKQDMA---RQLREY----QE 458
Cdd:pfam13851 18 NDITRnnleLIKSLKEEIAELKKKEERNEKLMSEIQQENK-----------RLTEPLQKAQEEVEelrKQLENYekdkQS 86
|
....*.
gi 341940882 459 LMNVKL 464
Cdd:pfam13851 87 LKNLKA 92
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
380-468 |
5.54e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 37.42 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 380 DNLRSTRDEINELTRLIQRLKAEIEHTKAQCAK-LEAAVAEAEQQGEAALNDAKcklADLEGALQQAKQDMARQLRE-YQ 457
Cdd:cd06503 37 ESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiIEEARKEAEKIKEEILAEAK---EEAERILEQAKAEIEQEKEKaLA 113
|
90
....*....|...
gi 341940882 458 ELMN--VKLALDI 468
Cdd:cd06503 114 ELRKevADLAVEA 126
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
338-459 |
8.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940882 338 LDGIIAEVKAQYEEV-ARRSRAdveswyqtkyEEMRVTAGQHCDNLRSTR-----DEINELTRLIQRLKAEIEHTK---- 407
Cdd:COG4913 293 LEAELEELRAELARLeAELERL----------EARLDALREELDELEAQIrgnggDRLEQLEREIERLERELEERErrra 362
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 341940882 408 ---AQCAKLEAAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMARQLREYQEL 459
Cdd:COG4913 363 rleALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
|
| |
