|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03562 |
PRK03562 |
glutathione-regulated potassium-efflux system protein KefC; Provisional |
578-1098 |
1.12e-122 |
|
glutathione-regulated potassium-efflux system protein KefC; Provisional
Pssm-ID: 235131 [Multi-domain] Cd Length: 621 Bit Score: 391.66 E-value: 1.12e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 578 ASVIFVPLFQKIPGGSpVLGYLAAGILIGPYGLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSAQ 657
Cdd:PRK03562 16 AAVLIVPIAVRLGLGS-VLGYLIAGCIIGPWGLRLVTDVESILHFAEFGVVLMLFVIGLELDPQRLWKLRRSIFGGGALQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 658 VLVTAAVIGLIThYVAGQAGPAAIVIGNGLALSSTAVVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLISPN 737
Cdd:PRK03562 95 MVACGGLLGLFC-MLLGLRWQVALLIGLGLALSSTAIAMQAMNERNLMVTQMGRSAFAILLFQDIAAIPLVAMIPLLAAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 738 SSKGGIGfqaiaeALGLAAIKAAVAITGIIAGGRLLLRPIYKQIAENRNAEIFSANTLLVILGTSLLTARAGLSMALGAF 817
Cdd:PRK03562 174 GASTTLG------AFALSALKVAGALALVVLGGRYVTRPALRFVARSGLREVFTAVALFLVFGFGLLMEEVGLSMALGAF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 818 LAGLLLAETEFSLQVESDIAPYRGLLLGLFFMTVGMSIDPKLLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISIISAV 897
Cdd:PRK03562 248 LAGVLLASSEYRHALESDIEPFKGLLLGLFFIAVGMSIDFGTLLENPLRILILLLGFLAIKIAMLWLLARPLGVPRKQRR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 898 RVGLLLAPGGEFAFVAFGEAVNQGIMTPQLSSLLFLVVGISMALTP-WLAAGGQLIASRFElqdvrsLLPVESETDDLQG 976
Cdd:PRK03562 328 WFAVLLGQGGEFAFVVFGAAQMANVLEPEWAKLLTLAVALSMAATPlLLVLLDRLEQSRTE------EAREADEIDEQQP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 977 HIIICGFGRIGQIIAQLLSERLIPFVALDVSSDRVAIGRSLDLPVYFGDAGSREVLHKIGADRACAAAIALDTPGANYRC 1056
Cdd:PRK03562 402 RVIIAGFGRFGQIVGRLLLSSGVKMTVLDHDPDHIETLRKFGMKVFYGDATRMDLLESAGAAKAEVLINAIDDPQTSLQL 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 240255705 1057 VWALSKYFPNVKTFVRAHDVDHGLNLEKAGATAVVPETLEPS 1098
Cdd:PRK03562 482 VELVKEHFPHLQIIARARDVDHYIRLRQAGVEKPERETFEGA 523
|
|
| PRK03659 |
PRK03659 |
glutathione-regulated potassium-efflux system protein KefB; Provisional |
578-1073 |
3.72e-107 |
|
glutathione-regulated potassium-efflux system protein KefB; Provisional
Pssm-ID: 179625 [Multi-domain] Cd Length: 601 Bit Score: 349.33 E-value: 3.72e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 578 ASVIFVPLFQKIPGGSpVLGYLAAGILIGPYGLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSAQ 657
Cdd:PRK03659 16 AAVVAVPLAQRLGIGA-VLGYLLAGIAIGPWGLGFISDVDEILHFSELGVVFLMFIIGLELNPSKLWQLRRSIFGVGAAQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 658 VLVTAAVIGLIThYVAGQAGPAAIVIGNGLALSSTAVVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLISPN 737
Cdd:PRK03659 95 VLLSAAVLAGLL-MLTDFSWQAAVVGGIGLAMSSTAMALQLMREKGMNRSESGQLGFSVLLFQDLAVIPALALVPLLAGS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 738 SSKGGIGFQAIAEALGLAaikaavaitGIIAGGRLLLRPIYKQIAENRNAEIFSANTLLVILGTSLLTARAGLSMALGAF 817
Cdd:PRK03659 174 ADEHFDWMKIGMKVLAFA---------GMLIGGRYLLRPLFRFIAASGVREVFTAAALLLVLGSALFMDALGLSMALGTF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 818 LAGLLLAETEFSLQVESDIAPYRGLLLGLFFMTVGMSIDPKLLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISIISAV 897
Cdd:PRK03659 245 IAGVLLAESEYRHELEIAIEPFKGLLLGLFFISVGMALNLGVLYTHLLWVLISVVVLVAVKGLVLYLLARLYGLRSSERM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 898 RVGLLLAPGGEFAFVAFGEAVNQGIMTPQLSSLLFLVVGISMALTPWLAAG-GQLIASRFELQDVRSLLPvesETDDLQG 976
Cdd:PRK03659 325 QFAGVLSQGGEFAFVLFSAASSQRLLQGDQMALLLVVVTLSMMTTPLLMKLiDKWLARRLNGPEEEDEKP---WVEDDKP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 977 HIIICGFGRIGQIIAQLLSERLIPFVALDVSSDRVAIGRSLDLPVYFGDAGSREVLHKIGADRACAAAIALDTPGANYRC 1056
Cdd:PRK03659 402 QVIIVGFGRFGQVIGRLLMANKMRITVLERDISAVNLMRKYGYKVYYGDATQLELLRAAGAEKAEAIVITCNEPEDTMKI 481
|
490
....*....|....*..
gi 240255705 1057 VWALSKYFPNVKTFVRA 1073
Cdd:PRK03659 482 VELCQQHFPHLHILARA 498
|
|
| KefB |
COG0475 |
Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism]; ... |
578-957 |
8.79e-100 |
|
Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism];
Pssm-ID: 440243 [Multi-domain] Cd Length: 384 Bit Score: 321.71 E-value: 8.79e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 578 ASVIFVPLFQKIpGGSPVLGYLAAGILIGPYGLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSAQ 657
Cdd:COG0475 15 AAVLAGLLARRL-GLPSVLGYILAGILLGPSGLGLIEDSEALELLAELGVVLLLFLIGLELDLKRLRKMGRRALGIGLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 658 VLVTAAVIGLIThYVAGQAGPAAIVIGNGLALSSTAVVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLISPN 737
Cdd:COG0475 94 VLLPFLLGFLLA-LLLGLSLAAALFLGAALAATSTAIVLKVLKELGLLKTPLGQLILGVALFDDIAAILLLALVPALAGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 738 SSkggigfqaIAEALGLAAIKAAVAITGIIAGGRLLLRPIYKQIAENRNAEIFSANTLLVILGTSLLTARAGLSMALGAF 817
Cdd:COG0475 173 GS--------VAGSLLLALLKALLFLALLLLVGRYLLRRLFRLVARTRSRELFLLFALLLVLLAAALAELLGLSAALGAF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 818 LAGLLLAETEFSLQVESDIAPYRGLLLGLFFMTVGMSIDPKLLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISIISAV 897
Cdd:COG0475 245 LAGLVLAESEYRHELEEKIEPFGDLFLPLFFVSVGLSLDLSALLSNPLLALLLVLAAIVGKLLGAYLAARLFGLSRREAL 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 898 RVGLLLAPGGEFAFVAFGEAVNQGIMTPQLSSLLFLVVGISMALTPWLAAGGQLIASRFE 957
Cdd:COG0475 325 RIGLLLAPRGEFALVLASLGLSAGLISPELFAALVLVVLLTTLLTPLLLRLALRLAERAK 384
|
|
| RosB |
COG4651 |
Predicted Kef-type K+ transport protein, K+/H+ antiporter domain [Inorganic ion transport and ... |
593-1132 |
5.26e-92 |
|
Predicted Kef-type K+ transport protein, K+/H+ antiporter domain [Inorganic ion transport and metabolism];
Pssm-ID: 443689 [Multi-domain] Cd Length: 564 Bit Score: 306.90 E-value: 5.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 593 SPVLGYLAAGILIGPYGLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSAQVLVTAAVIGLITHYV 672
Cdd:COG4651 30 PPIVGYLLAGVLIGPFTPGLVADVELIEQLAEIGVILLLFGVGLEFSLKDLLAVRKIALPGALLQIALTTLLGFGIALLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 673 aGQAGPAAIVIGNGLALSSTAVVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLIspnsskgGIGFQAIAEAL 752
Cdd:COG4651 110 -GWSLGESLVFGLALSLSSTVVLLKLLEDRGELDTLHGRIAVGWLIVQDLAVVLMLVLLPAL-------AGGGGGLLGTL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 753 GLAAIKAAVAITGIIAGGRLLLRPIYKQIAENRNAEIFsanTLLVI---LGTSLLTARAGLSMALGAFLAGLLLAETEFS 829
Cdd:COG4651 182 GLTLLKVALFVALMLVVGRRVIPWLLHRVARTRSRELF---LLAVLaicLGVAYLAALFGLSFALGAFLAGMVLAESEYS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 830 LQVESDIAPYRGLLLGLFFMTVGMSIDPKLLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISIISAVRVGLLLAPGGEF 909
Cdd:COG4651 259 HQAAAELLPLRDAFAVLFFVSVGMLFDPSFLLENPLPVLALLLIVLIGKPLIAFLIVLALGYPLRTALLVGLSLAQIGEF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 910 AFVAFGEAVNQGIMTPQLSSLLFLVVGISMALTPWLAAGGQLIASRFE-LQDVRSLL--PVESETDDLQGHIIICGFGRI 986
Cdd:COG4651 339 SFILAALGLSLGLLSEEAYQLILAVAILTIALSPYLIALADPLYARLErRPPLAARLerDRPEESDLVVHVVVVGGGGGG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 987 GQIIAQLLSERLIPFVALDVSSDRVAIGRSLDLPVYFGDAGSREVLHKIGADRACAAAIALDTPGANYRCVWALSKYFPN 1066
Cdd:COG4651 419 GGLALRLLLRGIVVVVVVDNVEEVVRARRRGGIAGGGGAAADLELLAALLAAAAIAVVAIPAAAAALLLIAAARRALPLL 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255705 1067 VKTFVRAHDVDHGLNLEKAGATAVVPETLEPSLQLAAAVLAQAKLPTSEIATTINEFRSRHLSELA 1132
Cdd:COG4651 499 IIIARAARRAEEEELLLAGAVEVVVEEEEEAAEAALLLLLLLLLLRALAERAILRAARRRLRAERA 564
|
|
| 2a37 |
TIGR00932 |
transporter, monovalent cation:proton antiporter-2 (CPA2) family; [Transport and binding ... |
578-856 |
3.12e-89 |
|
transporter, monovalent cation:proton antiporter-2 (CPA2) family; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273348 [Multi-domain] Cd Length: 273 Bit Score: 288.78 E-value: 3.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 578 ASVIFVPLFQKIPGGsPVLGYLAAGILIGPYGLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSAQ 657
Cdd:TIGR00932 3 AAVLAVPLSRRLGIP-SVLGYLLAGVLIGPSGLGLISNVEGVNHLAEFGVILLMFLIGLELDLERLWKLRKAAFGVGVLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 658 VLVTAAVIGLITHYVAGQAGPAAIVIGNGLALSSTAVVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLISPn 737
Cdd:TIGR00932 82 VLVPGVLLGLLLGHLLGLALGAAVVIGIILALSSTAVVVQVLKERGLLKTPFGQTVLGILLFQDIAVVPLLALLPLLAT- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 738 sskggiGFQAIAEALGLAAIKAAVAITGIIAGGRLLLRPIYKQIAENRNAEIFSANTLLVILGTSLLTARAGLSMALGAF 817
Cdd:TIGR00932 161 ------SASTEHVALALLLLKVFLAFLLLVLLGRWLLRPVLRLTAELRPSELFTAGSLLLMFGSAYFADLLGLSMALGAF 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 240255705 818 LAGLLLAETEFSLQVESDIAPYRGLLLGLFFMTVGMSID 856
Cdd:TIGR00932 235 LAGVVLSESEYRHKLESDLEPIGGVLLPLFFISVGMSVD 273
|
|
| Na_H_Exchanger |
pfam00999 |
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH ... |
578-947 |
5.80e-50 |
|
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family.
Pssm-ID: 425982 [Multi-domain] Cd Length: 377 Bit Score: 181.68 E-value: 5.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 578 ASVIFVPLFQKIPGGSPVLGYLAAGILIGPYGLSIIRNV-HGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSA 656
Cdd:pfam00999 6 LLALLAPLLARRLKLPPIVGLIIAGILLGPSGLGLISEVdEDLEVLSNLGLPPLLFLAGLELDLRELRKNGGSILLLALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 657 QVLVTAAVIGLITHYVAGQAGP-AAIVIGNGLALSSTAVVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLIS 735
Cdd:pfam00999 86 GVLIPFVLIGLLLYLLGLGIPLlEALLFGAILSATSPVVVLAILKELGRVPERLGTLLLGESVLNDGVAVVLLAVLLALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 736 PnsskgGIGFQAIAEALGLAAIKAAVAITGIIAGGRLLLRPIYKQIAENRnaEIFSANTLLVILGTSLLTARAGLSMALG 815
Cdd:pfam00999 166 Q-----GVGGGSDLGWLLLIFLVVAVGGLLLGLLIGWLLRLITRFTDDDR--ELEVLLVLLLALLAALLAEALGVSGILG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 816 AFLAGLLLAETEFSLQVESDIAPYR-GLLLGLFFMTVGMSIDPK-LLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISI 893
Cdd:pfam00999 239 AFLAGLVLSEYPFANKLSEKLEPFGyGLFNPLFFVLVGLSLDLSsLLLSVWILVLLALVAILLGRFLGVFLLLRLLGLSL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 240255705 894 ISAVRVGLLLAPGGEFAFVAFGEAVNQGIMTPQLSSLLFLVVGISM-----ALTPWLAA 947
Cdd:pfam00999 319 REALIIGFGGLQRGAVSLALAAIGPLLGIIARELYPLLIVVVLFTVlvqgiTLKPLLFK 377
|
|
| Kch |
COG1226 |
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; |
852-1127 |
1.57e-47 |
|
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
Pssm-ID: 440839 [Multi-domain] Cd Length: 279 Bit Score: 171.45 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 852 GMSIDPKLLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISIISAVRVGLLLAPGGEFAFVAFGEAVNQGIMTPQLSSLL 931
Cdd:COG1226 1 LGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAALALAALLLLLLLAGGGGFFLLLLLAAAALLLLLLLAAALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 932 FLVVGISMALTPWLAAGGQLIASRFELQDVRSLLPVESETDDLQGHIIICGFGRIGQIIAQLLSERLIPFVALDVSSDRV 1011
Cdd:COG1226 81 LLLVLLLLLLLLLLLLLLALLLLLLALAAREEEAEAAEDAIDLEGHVIIAGFGRVGQIVARLLRAEGIPFVVIDLDPERV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 1012 AIGRSLDLPVYFGDAGSREVLHKIGADRACAAAIALDTPGANYRCVWALSKYFPNVKTFVRAHDVDHGLNLEKAGATAVV 1091
Cdd:COG1226 161 EELRRFGIKVYYGDATRPDVLEAAGIERARALVVAIDDPEAALRIVELARELNPDLKIIARARDREHAEELRQAGADEVV 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 240255705 1092 PETLEPSLQLAAAVLAQAKLPTSEIATTINEFRSRH 1127
Cdd:COG1226 241 RETFESALQLARHALEALGVPEEEAARAIQEFRRRD 276
|
|
| PRK10669 |
PRK10669 |
putative cation:proton antiport protein; Provisional |
593-1032 |
3.06e-42 |
|
putative cation:proton antiport protein; Provisional
Pssm-ID: 182633 [Multi-domain] Cd Length: 558 Bit Score: 163.73 E-value: 3.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 593 SPVLGYLAAGILIGPYGLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSAQVLVtAAVIGLITHYV 672
Cdd:PRK10669 31 SPLVGYLLAGVLAGPFTPGFVADTKLAPELAELGVILLMFGVGLHFSLKDLMAVKSIAIPGAIAQIAV-ATLLGMALSAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 673 AGQAGPAAIVIGNGLALSSTAVVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLISPNSSKGGIGFQAIAEAL 752
Cdd:PRK10669 110 LGWSLMTGIVFGLCLSTASTVVLLRALEERQLIDSQRGQIAIGWLIVEDLVMVLTLVLLPAVAGMMEQGDVGFATLAVDL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 753 GLAAIKAAVAITGIIAGGRLLLRPIYKQIAENRNAEIFSANTLLVILGTSLLTARA-GLSMALGAFLAGLLLAETEFSLQ 831
Cdd:PRK10669 190 GITIGKVIAFIAIMMLVGRRLVPWILARSAATGSRELFTLSVLALALGIAFGAVELfDVSFALGAFFAGMVLNESELSHR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 832 VESDIAPYRGLLLGLFFMTVGMSIDPKLLLaNFPL-IMGTLGLLLVGKTILVVIIGKLFGISIISAVRVGLLLAPGGEFA 910
Cdd:PRK10669 270 AAHDTLPLRDAFAVLFFVSVGMLFDPMILI-QQPLaVLATLAIIVFGKSLAAFFLVRLFGHSRRTALTIAASLAQIGEFA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 911 FVAFGEAVNQGIMTPQLSSLLFLVVGISMALTPWLAAGGQLIASRFELQDVRSLL-PVESETD---DLQGHIIICGFGRI 986
Cdd:PRK10669 349 FILAGLGMALNLLPQAGQNLVLAGAILSIMLNPVLFTLLERYLAKTETLEEQTLEeAIEEEKQipvDICNHALLVGYGRV 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 240255705 987 GQIIAQLLSERLIPFVALDVSSDRVAIGRSLDLPVYFGDAGSREVL 1032
Cdd:PRK10669 429 GSLLGEKLLAAGIPLVVIETSRTRVDELRERGIRAVLGNAANEEIM 474
|
|
| TrkA_N |
pfam02254 |
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
978-1091 |
1.05e-16 |
|
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.
Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 77.18 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 978 IIICGFGRIGQIIAQLLSERlIPFVALDVSSDRVAIGRSLDLPVYFGDAGSREVLHKIGADRACAAAIALDTPGANYRCV 1057
Cdd:pfam02254 1 IIIIGYGRVGRSLAEELSEG-GDVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILIV 79
|
90 100 110
....*....|....*....|....*....|....
gi 240255705 1058 WALSKYFPNVKTFVRAHDVDHGLNLEKAGATAVV 1091
Cdd:pfam02254 80 LLARELNPDKKIIARANDPEHAELLRRLGADHVI 113
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
883-1095 |
1.03e-14 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 76.26 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 883 VIIGKLFGISIISAVRVGLLLAPGGEFAFVAFGEAVNQGIMTPQLSSLLFLVVGISMALTPWLAAGGQLIASRFE--LQD 960
Cdd:COG0569 1 LLILLLLLVLLFAMGIEGLVLLDALYGLLITLTTVTTLGGGLLDPVTLVAAIFLIGVVIIPLGYTLITFGDAVLFggLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 961 VRSLLPVESETDDLQGHIIICGFGRIGQIIAQLLSERLIPFVALDVSSDRVAIGRSLDLPVYFGDAGSREVLHKIGADRA 1040
Cdd:COG0569 81 ALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 240255705 1041 CAAAIALDTPGANYRCVWALSKYFPnVKTFVRAHDVDHGLNLEKAGATAVV-PETL 1095
Cdd:COG0569 161 DAVIAATGDDEANILACLLAKELGV-PRIIARANDPEYADLLERLGADVVIsPERL 215
|
|
| NhaP |
COG0025 |
NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism]; |
578-946 |
2.27e-14 |
|
NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism];
Pssm-ID: 439796 [Multi-domain] Cd Length: 506 Bit Score: 77.31 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 578 ASVIFVPLFQKIPGgSPVLGYLAAGILIGPY-GLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSA 656
Cdd:COG0025 13 LGLLSQWLARRLKL-PAPLLLLLAGILLGPGlGLELDPELGDLEPLLELFLPPLLFEAALNLDLRELRRNGRPILRLAVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 657 QVLVTAAVIGLITHYVAGQAGPAAIVIGNGLALSSTAVVLQVLQE-----------RGEStsrhgratfsvlLFQD-LAV 724
Cdd:COG0025 92 GVLLTTLAVALAAHWLLGLPLAAALLLGAILAPTDPVAVSPILRRlgvpkrlrtilEGES------------LLNDaTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 725 VVLLILIPLISPnsskGGIGFQAIAEALGLAAIKAAVAitGIIAG---GRLLLRpiykqiAENRNAEIFSanTLLVILGT 801
Cdd:COG0025 160 VLFVLALAAALG----GGFSLGEALLDFLLAILGGILV--GLLLGwllGRLLRR------LPDPLLEILL--TLALPFLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 802 SLLTARAGLS--------------MALGAFLAGLLLAETEFSLQVESdiapyrgLLLGLFFMTVGMSIDPKLLLAN-FPL 866
Cdd:COG0025 226 YLLAEALHGSgvlavvvaglvlgnAGRRSLSPETRLQLLEFWETLEF-------LLNSLLFVLLGAQLPLILLGALgLGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 867 IMGTLGLLLVGKTILVVIIGKLFGISIisAVRVGLLLAPGGE-------FAFVAFGEAVNQGIMTPQLSSLLFLVVGISM 939
Cdd:COG0025 299 ILLVLLALLVVRPLWVFLSLALRGSRL--SWRERLFLSWGGPrgivslaLALSLPLHGGAGFPGRDLILALAFGVILLTL 376
|
410
....*....|.
gi 240255705 940 AL----TPWLA 946
Cdd:COG0025 377 VLqgltLPPLA 387
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
118-388 |
5.67e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 118 EGSDDREVTFSKEEKDTREQDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASAWNDVNQTLN 197
Cdd:PRK02224 305 DDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 198 VVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEA----EGYNTSEESEVRDGVKDKEEALLSAK----------- 262
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDElrerEAELEATLRTARERVEEAEALLEAGKcpecgqpvegs 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 263 ---ADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERA-QISALK----------------AEEDVANIMVLAE 322
Cdd:PRK02224 465 phvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdRIERLEerredleeliaerretIEEKRERAEELRE 544
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240255705 323 QAVAFELEATQRVNDAEIALQRAEKTLFGSQTQETTQGKV---LDGKNTIVgedEVLSEIVDVSHQAER 388
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELkerIESLERIR---TLLAAIADAEDEIER 610
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
121-347 |
8.87e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 8.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 121 DDREVTFSKEEKDTREQDSApsLEELRDLLNKATKELEVA-----SLNSTMFEEKAQRISEV--AIALKDEAASAWNDVN 193
Cdd:COG1196 249 EELEAELEELEAELAELEAE--LEELRLELEELELELEEAqaeeyELLAELARLEQDIARLEerRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 194 QTLNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEgynTSEESEVRDGVKDKEEALLSAKADIKECQENLA 273
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA---EAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240255705 274 SCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFELEATQRVNDAEIALQRAEK 347
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
130-349 |
2.49e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 130 EEKDTREQdsAPSLEELRDLLNKATKELEVAslnstmfEEKAQRISEVAiALKDEAASAWNDVNQtlnvvQEAVDEESVA 209
Cdd:COG4913 219 EEPDTFEA--ADALVEHFDDLERAHEALEDA-------REQIELLEPIR-ELAERYAAARERLAE-----LEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 210 KEAVQKATmALSLAEARLQVALESLEAEgyntseESEVRDGVKDKEEALLSAKADIKECQ-ENLASCEEQLRRLQVKKDE 288
Cdd:COG4913 284 WFAQRRLE-LLEAELEELRAELARLEAE------LERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255705 289 LQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFELEATQRVNDAEIALQRAEKTL 349
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-382 |
1.64e-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: 59.30 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 103 SVGDLVGNDRNLEFAEGSDDREVTfSKEEKDTREQDSAPSLEELRDLLNKATKELEVAslnSTMFEEKAQRIS--EVAIA 180
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEE-ELEELTAELQELEEKLEELRLEVSELEEEIEEL---QKELYALANEISrlEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 181 LKDEAAsawNDVNQTLNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEV-RDGVKDKEEALL 259
Cdd:TIGR02168 306 ILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 260 SAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRL-------NEAAERAQISAL------------KAEEDVANIMVL 320
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeieelLKKLEEAELKELqaeleeleeeleELQEELERLEEA 462
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240255705 321 AEQAVAFELEATQRVNDAEIALQRAEKTLFGSQTQET-----TQG--KVLDGKNTIVGEDEVLSEIVDV 382
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlegfSEGvkALLKNQSGLSGILGVLSELISV 531
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-365 |
1.70e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 122 DREVTFSKEEKDTREQDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASAWNDVNQTLNVVQE 201
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 202 AVDEESVAKEAVQKATMALSLAEARLQVALESLEAEgynTSEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRR 281
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 282 LQVKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFELEATQRVNDAEIALQRAEKTLFGSQTQETTQGK 361
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
....
gi 240255705 362 VLDG 365
Cdd:COG1196 471 EAAL 474
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
137-418 |
5.19e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 137 QDSAPSLEELRDLLNKATKELEVAslnstmfEEKAQRISEVAIALKDEAASAWNDVNQTLNVVQEAVDEESVAKEAVQka 216
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQA-------REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 217 tmALSLAEARLQVALESLEAEGYN-TSEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQV-----KKDELQ 290
Cdd:COG4372 105 --SLQEEAEELQEELEELQKERQDlEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 291 KEVDRLNEAAERAQISALKAEEDVANIMVLAEQavaFELEATQRVNDAEIALQRAEKTLFGSQTQETTQGKVLDGKNTIV 370
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRE---LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 240255705 371 GEDEVLSEIVDVSHQAERDLVVVGVSSDVGTQSYESDNENGKPTADFA 418
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-459 |
9.52e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 143 LEELRDLLNKATKELEVAslnsTMFEEKAQRISEVAIAL----KDEAASAWNDVNQTLNVVQEAVDEESVAKEAVQKATM 218
Cdd:TIGR02168 195 LNELERQLKSLERQAEKA----ERYKELKAELRELELALlvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 219 ALSLAEARLQVALESLEAEGYNTSEEsevrdgVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNE 298
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANE------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 299 AAERAQISALKAEEDVANimvlaEQAVAFELEatQRVNDAEIALQRAEKTLFGSQTQETTQgkvldgKNTIVGEDEVLSE 378
Cdd:TIGR02168 345 KLEELKEELESLEAELEE-----LEAELEELE--SRLEELEEQLETLRSKVAQLELQIASL------NNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 379 I---VDVSHQAERDLVVVGVSSDVGTQSYESDNEN-GKPTADFAKEAEGEAEKSKNVVLTKKQEVQKDLPRESSSHNGTK 454
Cdd:TIGR02168 412 LedrRERLQQEIEELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
....*
gi 240255705 455 TSLKK 459
Cdd:TIGR02168 492 DSLER 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-359 |
9.87e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 199 VQEAVDEESVAKEAVQKATMALSLAEARLQV--ALESLEAEGYNTSE-ESEVRDgVKDKEEALLSAKADIKECQENLASC 275
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASaEREIAE-LEAELERLDASSDDLAALEEQLEEL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 276 EEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFELEATQRVNDAEIALQRAEKTLFGSQTQ 355
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDA 777
|
....
gi 240255705 356 ETTQ 359
Cdd:COG4913 778 LRAR 781
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
123-441 |
8.34e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 123 REVTFSKEEKDTREQDSAPSLEELRDLLNKA--TKELEVASLNSTMFEEKAQRISEVAIALK--DEAASAWNDVNQTLNV 198
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAeeKKKADEAKKKAEEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEA 1436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 199 VQEAvDEESVAKEAVQKATMALSlAEARLQVALESLEA-EGYNTSEESEVRDGVKDKEEAL------LSAKADIKECQEN 271
Cdd:PTZ00121 1437 KKKA-EEAKKADEAKKKAEEAKK-AEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAkkkadeAKKAAEAKKKADE 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 272 LASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDV--ANIMVLAEQAVAFELEATQRVNDAEIALQ----RA 345
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeeaRI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 346 EKTLFGSQTQETTQGKVLDGKNTIVGEDEVLSEIVDVSHQAERDLVVVGVSSDVGTQSYESDNENGKPTADFAKEAEGEA 425
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
330
....*....|....*.
gi 240255705 426 EKSKNVvltKKQEVQK 441
Cdd:PTZ00121 1675 KKAEEA---KKAEEDE 1687
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-350 |
8.60e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 137 QDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALK---DEAASAWNDVNQTLNVVQEAVDEESVAKEAV 213
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRealDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 214 QKATMALSLAEARLQVALESLEAE--GYNTSEEsEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQK 291
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEieELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255705 292 EVDRLNEAAERAQISALKAEEDVANI--MVLAEQAVAFElEATQRVNDAEIALQRAEKTLF 350
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLqeRLSEEYSLTLE-EAEALENKIEDDEEEARRRLK 975
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
110-347 |
1.08e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 110 NDRNLEFAEGSDD-REVTFSKEEKDTREQDSAPSLEELRDLlNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASA 188
Cdd:PTZ00121 1150 DAKRVEIARKAEDaRKAEEARKAEDAKKAEAARKAEEVRKA-EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA 1228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 189 WNDVNQTLNVVQEAVDEESV-AKEAVQKATMALSLAEARLQVALESLE---------------AEGYNTSEESEVRDGVK 252
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEErNNEEIRKFEEARMAHFARRQAAIKAEEarkadelkkaeekkkADEAKKAEEKKKADEAK 1308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 253 DK-------EEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAv 325
Cdd:PTZ00121 1309 KKaeeakkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA- 1387
|
250 260
....*....|....*....|..
gi 240255705 326 afeleatQRVNDAEIALQRAEK 347
Cdd:PTZ00121 1388 -------EEKKKADEAKKKAEE 1402
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-299 |
1.94e-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: 52.37 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 112 RNLEFAEGSDDREVTFSKEEKDTREQD---SAPSLEELRDLLNKATKELEVASlnstmfEEKAQRISEVAiALKDEAASA 188
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDiesLAAEIEELEELIEELESELEALL------NERASLEEALA-LLRSELEEL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 189 WNDVNQTLNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEVRdgVKDKEEALLSAKADIKEC 268
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL--ENKIEDDEEEARRRLKRL 977
|
170 180 190
....*....|....*....|....*....|....*....
gi 240255705 269 QE--------NLASCEEqLRRLQVKKDELQKEVDRLNEA 299
Cdd:TIGR02168 978 ENkikelgpvNLAAIEE-YEELKERYDFLTAQKEDLTEA 1015
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
243-339 |
2.72e-06 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 47.61 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 243 EESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANimvLAE 322
Cdd:pfam20492 7 EKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ---LEA 83
|
90
....*....|....*..
gi 240255705 323 QAVAFELEATQRVNDAE 339
Cdd:pfam20492 84 ELAEAQEEIARLEEEVE 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
130-341 |
4.91e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 130 EEKDTREQDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASAWNDVNQTLNVVQEAVDEESVA 209
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 210 KEAVQkatmALSLAEARLQVALESLEAEgyntseesevRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDEL 289
Cdd:COG1196 406 EEAEE----ALLERLERLEEELEELEEA----------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 240255705 290 QKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFELEATQRVNDAEIA 341
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
117-454 |
5.33e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 117 AEGSDDREVTFSKEEKDTREQDSAPSLEELR--DLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASAwndvnq 194
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKkaDEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK------ 1565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 195 tlnvVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEVRDGVKDKEEALLSAKADIKECQENLAS 274
Cdd:PTZ00121 1566 ----AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 275 CEEQLRRL-QVKKDELQKEVdRLNEAAERAQISALKAEEdvanimvlaeqavAFELEATQRvNDAEIALQRAEKTLFGSQ 353
Cdd:PTZ00121 1642 EAEEKKKAeELKKAEEENKI-KAAEEAKKAEEDKKKAEE-------------AKKAEEDEK-KAAEALKKEAEEAKKAEE 1706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 354 TQETTQGKVLDGKNTIVGEDEVLSEIVDVSHQAERDlvvvgvssDVGTQSYESDNENGKPTADFAKEAEGEAE---KSKN 430
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED--------KKKAEEAKKDEEEKKKIAHLKKEEEKKAEeirKEKE 1778
|
330 340
....*....|....*....|....*
gi 240255705 431 VVLtkKQEV-QKDLPRESSSHNGTK 454
Cdd:PTZ00121 1779 AVI--EEELdEEDEKRRMEVDKKIK 1801
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
139-452 |
1.04e-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: 50.05 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 139 SAPS-LEELRDLLNKATKELEV----ASLNSTMFEEKAQRISEVAIALKD---EAASAWNDVNQTLNVVQEAVDEESVAK 210
Cdd:TIGR00606 706 LAPDkLKSTESELKKKEKRRDEmlglAPGRQSIIDLKEKEIPELRNKLQKvnrDIQRLKNDIEEQETLLGTIMPEEESAK 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 211 E------AVQKATMALSLAEARL-QVALESLEAEGYNTSEEseVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQ 283
Cdd:TIGR00606 786 VcltdvtIMERFQMELKDVERKIaQQAAKLQGSDLDRTVQQ--VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 284 VKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFELEATQRVNDAEIALQRAEKTLFGSQTQ-ETTQGKV 362
Cdd:TIGR00606 864 SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSnKKAQDKV 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 363 LDGK---NTIVGEDEVLSEIV-----DVSHQAERDLVVVGVSSDVGTQSYESDNEN-GKPTADFAKEAEGEAEKSKNVVL 433
Cdd:TIGR00606 944 NDIKekvKNIHGYMKDIENKIqdgkdDYLKQKETELNTVNAQLEECEKHQEKINEDmRLMRQDIDTQKIQERWLQDNLTL 1023
|
330
....*....|....*....
gi 240255705 434 TKKQEVQKDLPRESSSHNG 452
Cdd:TIGR00606 1024 RKRENELKEVEEELKQHLK 1042
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
129-346 |
1.52e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 129 KEEKD---------TREQDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASawndvnqtlnvV 199
Cdd:PRK02224 199 KEEKDlherlngleSELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRET-----------I 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 200 QEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEVRDGVKDKEEALlsaKADIKECQENLASCEEQL 279
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL---RDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255705 280 RRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVAN----IMVLAEQAVafelEATQRVNDAEIALQRAE 346
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDrreeIEELEEEIE----ELRERFGDAPVDLGNAE 411
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
123-441 |
1.74e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 123 REVTFSKEEKdtREQDSAPSLEELR--DLLNKATKELEVASLNSTmfEEKAQRISEvaiaLKDEAASAWNDVNQTLNVVQ 200
Cdd:PTZ00121 1268 RQAAIKAEEA--RKADELKKAEEKKkaDEAKKAEEKKKADEAKKK--AEEAKKADE----AKKKAEEAKKKADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 201 EAVDEESVAKEAVQKATMALSLAEarlqvalESLEAEGYNTSEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLR 280
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAE-------EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 281 RLQVKK--DELQK---EVDRLNEAAERAQiSALKAEEdvanIMVLAEQAVAFElEATQRVNDAEIAlQRAEKTLFGSQTQ 355
Cdd:PTZ00121 1413 AAAAKKkaDEAKKkaeEKKKADEAKKKAE-EAKKADE----AKKKAEEAKKAE-EAKKKAEEAKKA-DEAKKKAEEAKKA 1485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 356 ETTQGKVLDGKNtivgEDEVLSEIVDVSHQAERdlvvvGVSSDVGTQSYESDNENGKPTADFAKEAEgeaEKSKNVVLTK 435
Cdd:PTZ00121 1486 DEAKKKAEEAKK----KADEAKKAAEAKKKADE-----AKKAEEAKKADEAKKAEEAKKADEAKKAE---EKKKADELKK 1553
|
....*.
gi 240255705 436 KQEVQK 441
Cdd:PTZ00121 1554 AEELKK 1559
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
129-305 |
1.81e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 129 KEEKDTREQdsapsLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALkdEAASAWNDVNQTLNVVQEAVDEESV 208
Cdd:COG4717 81 KEAEEKEEE-----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 209 AKEAVQKATMALSLAEARLQVALESLEAEGYNTSEEsevrdgvkdKEEALLSAKADIKECQENLASCEEQLRRLQVKKDE 288
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLA---------TEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*..
gi 240255705 289 LQKEVDRLNEAAERAQI 305
Cdd:COG4717 225 LEEELEQLENELEAAAL 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
130-456 |
2.41e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 130 EEKDTREQDSAPSL---EELRDLLNKATKE-LEVASLNSTMFEEKAQRISEVAIalKDEAASAWNDVNQTLNVVQEAVDE 205
Cdd:PTZ00121 1567 EEAKKAEEDKNMALrkaEEAKKAEEARIEEvMKLYEEEKKMKAEEAKKAEEAKI--KAEELKKAEEEKKKVEQLKKKEAE 1644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 206 ESVAKEAVQKATmalslAEARLQVALESLEAEgyntsEEsevrdgvKDKEEALLSAKADIKECQENLASCEEQLRRL-QV 284
Cdd:PTZ00121 1645 EKKKAEELKKAE-----EENKIKAAEEAKKAE-----ED-------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeEL 1707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 285 KKDElQKEVDRLNEAAERAQISALKaeedvanimvlAEQAVAFELEATQRVNDAEIALQRAEKTLFGSQTQETTQGKVLD 364
Cdd:PTZ00121 1708 KKKE-AEEKKKAEELKKAEEENKIK-----------AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 365 GKNTIVgEDEVLSEIVDVSHQAERDLVVVGVSSDVGTQSyesdNENGKPTADFAKEAEGEAEK----SKNVVLTKKQEVQ 440
Cdd:PTZ00121 1776 EKEAVI-EEELDEEDEKRRMEVDKKIKDIFDNFANIIEG----GKEGNLVINDSKEMEDSAIKevadSKNMQLEEADAFE 1850
|
330
....*....|....*...
gi 240255705 441 KDLPRES--SSHNGTKTS 456
Cdd:PTZ00121 1851 KHKFNKNneNGEDGNKEA 1868
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
144-387 |
2.66e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 48.49 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 144 EELRDLLNK--ATKELE--VASLNSTMFEEKAQRISEVAIALKDEAASAWNDvNQTLNVVQEAVDE-----ESVaKEAVQ 214
Cdd:pfam05701 233 EELQRLNQQllSAKDLKskLETASALLLDLKAELAAYMESKLKEEADGEGNE-KKTSTSIQAALASakkelEEV-KANIE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 215 KATmalslAEAR-LQVALESLEAEgynTSEESEVRDGVKDKEE----ALLSAKADIKECQENLASCEEQLRRLQVKKDEL 289
Cdd:pfam05701 311 KAK-----DEVNcLRVAAASLRSE---LEKEKAELASLRQREGmasiAVSSLEAELNRTKSEIALVQAKEKEAREKMVEL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 290 QKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVA------FELEATQRVNDAEIALQR----AEKTLFGSQTQETTQ 359
Cdd:pfam05701 383 PKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAaastveSRLEAVLKEIEAAKASEKlalaAIKALQESESSAEST 462
|
250 260 270
....*....|....*....|....*....|.
gi 240255705 360 GKVlDGKNTI---VGEDEVLSEIVdvsHQAE 387
Cdd:pfam05701 463 NQE-DSPRGVtlsLEEYYELSKRA---HEAE 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
122-390 |
8.30e-05 |
|
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: 46.98 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 122 DREVT-FSKEEKDTREQDSA--PSLEELRDLLNKATKELEvaSLNSTMfEEKAQRISEVAIALKDEAASAWNDVNQTLNV 198
Cdd:TIGR02169 222 EYEGYeLLKEKEALERQKEAieRQLASLEEELEKLTEEIS--ELEKRL-EEIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 199 VQ----EAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEVRDGVKD------KEEALLSAKA----- 263
Cdd:TIGR02169 299 LEaeiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEeyaelkEELEDLRAELeevdk 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 264 DIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANImvlaEQAVAfELEATQRVNDAEIALQ 343
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAKIN-ELEEEKEDKALEIKKQ 453
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 240255705 344 RAE-KTLfgSQTQETTQGKVLDGKNTIvgeDEVLSEIvdvsHQAERDL 390
Cdd:TIGR02169 454 EWKlEQL--AADLSKYEQELYDLKEEY---DRVEKEL----SKLQREL 492
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
144-349 |
1.13e-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: 46.71 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 144 EELRDLLNKATKELEvASLNstmfEEKAQRISEVAIALKDEAasawndvnqTLNVVQEAVDEESVAKEAVQKATMALSLA 223
Cdd:pfam01576 741 EEKRRQLVKQVRELE-AELE----DERKQRAQAVAAKKKLEL---------DLKELEAQIDAANKGREEAVKQLKKLQAQ 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 224 EARLQVALESLEA---EGYNTSEESEVRdgvkdkeeaLLSAKADIKECQENLASCEEQLRRLQVKKDELQKEV------- 293
Cdd:pfam01576 807 MKDLQRELEEARAsrdEILAQSKESEKK---------LKNLEAELLQLQEDLAASERARRQAQQERDELADEIasgasgk 877
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240255705 294 DRLNEAAER--AQISALKAE--EDVANIMVLAEQ-------------AVAFELEATQRVNDAEIALQRAEKTL 349
Cdd:pfam01576 878 SALQDEKRRleARIAQLEEEleEEQSNTELLNDRlrkstlqveqlttELAAERSTSQKSESARQQLERQNKEL 950
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
198-346 |
1.40e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.43 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 198 VVQEAVDEESVAKEAVQKatMALSLAEARLQVA-----LESLEAEgyNTSEESEVRDGVKDKEEALLSAKADI-KECQEN 271
Cdd:COG1842 17 LLDKAEDPEKMLDQAIRD--MEEDLVEARQALAqvianQKRLERQ--LEELEAEAEKWEEKARLALEKGREDLaREALER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 272 LASCEEQLRRLQVKKDELQKEVDRLNEAAERAQ--ISALKAEEDvaniMVLAEQAVAfelEATQRVN---------DAEI 340
Cdd:COG1842 93 KAELEAQAEALEAQLAQLEEQVEKLKEALRQLEskLEELKAKKD----TLKARAKAA---KAQEKVNealsgidsdDATS 165
|
....*.
gi 240255705 341 ALQRAE 346
Cdd:COG1842 166 ALERME 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-349 |
1.40e-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: 46.20 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 155 KELEVASLNSTMFEEKAQRISEVAIALKDEAASAWNDVNQTLNVVQEAVDEESVAKEAVQKATMALSLAEARL-QVALES 233
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIaQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 234 LEAEGyntsEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEED 313
Cdd:TIGR02168 757 TELEA----EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 240255705 314 VA----NIMVLAEQAVAFELE---ATQRVNDAEIALQRAEKTL 349
Cdd:TIGR02168 833 IAaterRLEDLEEQIEELSEDiesLAAEIEELEELIEELESEL 875
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
130-332 |
1.61e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 130 EEKDTREQDSAPSLEELRDLLNKatKELEVASL--NSTMFEEKAQRISEVAIALKDEAASAWNDVnQTLNVVQEAVDEES 207
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEE--KRERAEELreRAAELEAEAEEKREAAAEAEEEAEEAREEV-AELNSKLAELKERI 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 208 VAKEAVQKATMALSLAEARLQVALESLE--AEGYNTSEE--SEVRDGVKD-----KEEALLSAKADIKECQENLASCEEQ 278
Cdd:PRK02224 589 ESLERIRTLLAAIADAEDEIERLREKREalAELNDERRErlAEKRERKREleaefDEARIEEAREDKERAEEYLEQVEEK 668
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 240255705 279 LRRLQVKKDELQKEVDRLNEAAERaqISALKAEEDVANIMVLAEQAV---AFELEAT 332
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELEE--LEELRERREALENRVEALEALydeAEELESM 723
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
129-324 |
1.89e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 129 KEEKDTREQDSaPSLEELRDLLNKATKELEVASLNSTmfEEKA--QRISEVA--IALKDEAASAWNDVNQTLNVVQEAVD 204
Cdd:COG1340 98 RKELAELNKAG-GSIDKLRKEIERLEWRQQTEVLSPE--EEKElvEKIKELEkeLEKAKKALEKNEKLKELRAELKELRK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 205 EESVAKEAVQKatmalsLAEaRLQVALESLeaegyntSEESEVRDGVKDKEEALlsaKADIKECQENLASCEEQLRRLQV 284
Cdd:COG1340 175 EAEEIHKKIKE------LAE-EAQELHEEM-------IELYKEADELRKEADEL---HKEIVEAQEKADELHEEIIELQK 237
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 240255705 285 KKDELQKEVDRLneaaeRAQISALKAEEDVANIMVLAEQA 324
Cdd:COG1340 238 ELRELRKELKKL-----RKKQRALKREKEKEELEEKAEEI 272
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
214-388 |
1.97e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 214 QKATMALSLAEARLQVALESLEAEGYN----TSEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDEL 289
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEEleqlREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 290 QKEVDRLNEAAE--RAQISALKAEEDvanimVLAEQAVafELEATQRVNDAEIALQRAEKTLFGSQTQETTQG-KVLDGK 366
Cdd:COG4372 100 QEELESLQEEAEelQEELEELQKERQ-----DLEQQRK--QLEAQIAELQSEIAEREEELKELEEQLESLQEElAALEQE 172
|
170 180
....*....|....*....|..
gi 240255705 367 NTIVGEDEVLSEIVDVSHQAER 388
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANR 194
|
|
| DASH_Spc19 |
pfam08287 |
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ... |
220-296 |
3.24e-04 |
|
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle pole body and is important for spindle and kinetochore integrity during cell division.
Pssm-ID: 429900 [Multi-domain] Cd Length: 148 Bit Score: 42.23 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 220 LSLAE---ARLQVALESLEAegynTSEESEVR-----DGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQK 291
Cdd:pfam08287 68 LDKAEkslEKLERREETLKA----KLELNEGRlsnaeSSARDEEGSQESDEEVNSSEGDATNEELERLRALRQKKERLKY 143
|
....*
gi 240255705 292 EVDRL 296
Cdd:pfam08287 144 SLERL 148
|
|
| AbrB |
COG3180 |
Uncharacterized membrane protein AbrB, regulator of aidB expression [General function ... |
634-946 |
4.31e-04 |
|
Uncharacterized membrane protein AbrB, regulator of aidB expression [General function prediction only];
Pssm-ID: 442413 [Multi-domain] Cd Length: 352 Bit Score: 44.03 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 634 IGLELSVERLSSMKKY--VFGLGSAQVLVTAAVIGLITHYVAGQAGPAAI---VIGnglALSSTAVVlqvlqergeSTSR 708
Cdd:COG3180 70 IGSSFTPEVLAQLARWwpSLLLLTVLTLALSLLGGWLLRRLGGLDRATALlgsAPG---GLSEMVAL---------AEEY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 709 HGRATfSVLLFQDLAVVVLLILIPLIS----PNSSKGGIGFQAIAEALGLA--AIKAAVAITGIIAGGRLllrpiykqia 782
Cdd:COG3180 138 GADVR-LVALMQYLRVLLVVLLVPLVArllgGGGAGAAAALGPAAPPLSLLglLLLLALALAGGLLGRRL---------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 783 enrnaEIFSANTLLVILGTSLLTArAGLsmalgaflaglllaeTEFSLqvesdiaPyrGLLLGLFFMTVGMSI------- 855
Cdd:COG3180 207 -----RLPAGALLGPLLLSAALHL-TGL---------------VTAAL-------P--PWLLAAAQVLIGWSIglrftre 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 856 DPKLLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISIISAVrvgLLLAPGG--EFAFVAFGEAVNQG-IMTPQLSSLLF 932
Cdd:COG3180 257 TLRELLRLLPAALLSTLLLIALCALFAWLLALLTGLDLLTAL---LATAPGGldEMAIIALALGADVAfVTAHQLLRLLL 333
|
330
....*....|....
gi 240255705 933 LVVgismaLTPWLA 946
Cdd:COG3180 334 VLL-----LAPLLA 342
|
|
| AbrB |
pfam05145 |
Transition state regulatory protein AbrB; Bacillus subtilis respond to a multitude of ... |
595-946 |
4.63e-04 |
|
Transition state regulatory protein AbrB; Bacillus subtilis respond to a multitude of environmental stimuli by using transcription factors called transition state regulators (TSRs). They play an essential role in cell survival by regulating spore formation, competence, and biofilm development. AbrB is one of the most known TSRs, acting as a pleotropic regulator for over 60 different genes where it directly binds to their promoter or regulatory regions. Many other genes are indirectly controlled by AbrB since it is a regulator of other regulatory proteins, including ScoC, Abh, SinR and SigH. Hence, AbrB is considered a global regulatory protein controlling processes such as Bacillus subtilis growth and cell division as well as production of extracellular degradative enzymes, nitrogen utilization and amino acid metabolism, motility, synthesis of antibiotics and their resistant determinants, development of competence, transport systems, oxidative stress response, phosphate metabolism, cell surface components and sporulation. AbrB is a tetramer consisting of identical 94 residue monomers. Its DNA-binding function resides solely in the N-terminal domain (AbrBN) of 53 residues. Although it does not recognize a well-defined DNA base-pairing sequence, instead, it appears to target a very weak pseudo consensus nucleotide sequence, TGGNA-5bp-TGGNA, which allows it to be rather promiscuous in binding. The N-terminal domains of very similar sequences are present in two more Bacillus subtilis proteins, Abh and SpoVT. Mutagenesis studies suggest that the role of the C-terminal domain is in forming multimers.
Pssm-ID: 428334 [Multi-domain] Cd Length: 312 Bit Score: 43.69 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 595 VLGYLAAGILIGpygLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKY--VFGLGSAQVLVTAAVIGLITHYV 672
Cdd:pfam05145 2 LLGPMLAGIVAA---LALGAPLRVPRPLRNAGQAVLGVMIGLSFTPEVLAQLAAWwpSLLLLTVLTLLLSLLGGLLLRRW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 673 AGQAGPAAIvigngLALS----STAVVLqvlqergeSTSRHGRATFSVLLFQDLAVVVLLILIPLISPNSSKGGIGFQAI 748
Cdd:pfam05145 79 AGIDRTTAF-----LGSApggaSAMVAL--------AEERYGADVRLVALMQYLRVLLVVLLIPFVAALLGGAGAAALSA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 749 AEALGLAAIKAAVAITGIIAGGRLLLRPIYkqiaenrnaeIFSANTLLVILGTSLLTArAGLsmalgaflaglllaeTEF 828
Cdd:pfam05145 146 AALVLASWSWFLALLLALALLGALLGRRLR----------LPAAALLGPLLVGAALHL-TGL---------------LTI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 829 SLQVESDIAPYrgLLLGlffMTVGMSIDP---KLLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISIISAVrvgLLLAP 905
Cdd:pfam05145 200 ALPPWLLALAQ--LLIG---WSIGLRFTRetlRELARALPAALGSTLLLIALCAGLAWLLAWLTGVDFLTAY---LATAP 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 240255705 906 GG--EFAFVAFGEAVNQG-IMTPQLSSLLFLvvgisMALTPWLA 946
Cdd:pfam05145 272 GGldEMAIIALALGADVAfVTAHQLLRLLLV-----LLLAPPLA 310
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
131-318 |
5.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 131 EKDTRE---------QDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASAWNDVNqtLNVVQE 201
Cdd:COG4913 591 EKDDRRrirsryvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAER 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 202 AVDEESVAKEAVQKATMALSLAEARLQVALESLEAegyNTSEESEVRDGVKDKEEALLSAKADIKECQENLASCEE---- 277
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarl 745
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 240255705 278 ------QLRRLQVKKDELQKEV-DRLNEAAERAQISALKAEEDVANIM 318
Cdd:COG4913 746 elrallEERFAAALGDAVERELrENLEERIDALRARLNRAEEELERAM 793
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
194-349 |
6.36e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 194 QTLNVVQEAVDEESVAKEAVQKATMALSLAEARLqvalESLEAEGYNTSEESEVrdgvKDKEEALLSAKADIKECQENLA 273
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEEL----EELEAELEELREELEK----LEKLLQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 274 SCEEQLRRLQVKKD---ELQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFELE-ATQRVNDAEIALQRAEKTL 349
Cdd:COG4717 143 ELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEeLQQRLAELEEELEEAQEEL 222
|
|
| PLN03159 |
PLN03159 |
cation/H(+) antiporter 15; Provisional |
595-739 |
7.88e-04 |
|
cation/H(+) antiporter 15; Provisional
Pssm-ID: 215608 [Multi-domain] Cd Length: 832 Bit Score: 43.72 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 595 VLGYLAAGILIGPYGLSII----------RNVHGTKAIAEFGVVFLLFNIGLE--LSVERLSSMKKYVFGL-GSAQVLVT 661
Cdd:PLN03159 70 VISEILGGVILGPSVLGQSevfantifplRSVMVLETMANLGLLYFLFLVGVEmdISVIRRTGKKALAIAIaGMALPFCI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 662 AAVIGLITHYVAGQAGPAAIVIGNGLALSSTA--VVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLISPNSS 739
Cdd:PLN03159 150 GLAFSFIFHQVSRNVHQGTFILFLGVALSVTAfpVLARILAEIKLINTELGRIAMSAALVNDMCAWILLALAIALAENDS 229
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
133-360 |
9.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 133 DTREQDSAPSLEELRDLLNKATKELevASLNSTMfeekaqrisevaialkDEAASAWNDVNQTLNVVQEAVDEesvAKEA 212
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAEL--DALQAEL----------------EELNEEYNELQAELEALQAEIDK---LQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 213 VQKATMALSLAEARLQVALESLEAEGYNTSE-----ESE-----------VRDGVKDKEEALLSAKADIKECQENLASCE 276
Cdd:COG3883 74 IAEAEAEIEERREELGERARALYRSGGSVSYldvllGSEsfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 277 EQLRRLQVKKDELQKEVDRLNE--AAERAQISALKAEEDvanimvlAEQAVAFELEATQRVNDAEIALQRAEKTLFGSQT 354
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAqqAEQEALLAQLSAEEA-------AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
....*.
gi 240255705 355 QETTQG 360
Cdd:COG3883 227 AAAAAA 232
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
128-405 |
1.04e-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: 43.24 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 128 SKEEKDTReqDSAPSLEELRdllnkatKELEvASLNSTMF--EEKAQRISEVAI---ALKDEAASAWNDV-------NQT 195
Cdd:pfam01576 288 NKAEKQRR--DLGEELEALK-------TELE-DTLDTTAAqqELRSKREQEVTElkkALEEETRSHEAQLqemrqkhTQA 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 196 LNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAegynTSEESEVRdgvKDKEEALLsakadiKECQENLASC 275
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ----AKQDSEHK---RKKLEGQL------QELQARLSES 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 276 EEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANI------------------MVLAEQAVAFELEAT---QR 334
Cdd:pfam01576 425 ERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqlqdtqellqeetrqkLNLSTRLRQLEDERNslqEQ 504
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255705 335 VNDAEIALQRAEKTLfgsqtqETTQGKVLDGKNTIVGEDEVLSEIVDVSHQAERDLVVVGVSSDVGTQSYE 405
Cdd:pfam01576 505 LEEEEEAKRNVERQL------STLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-344 |
1.11e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 171 AQRISEVAIALKDEAASAWNDVNQTLNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEVRDG 250
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 251 VKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFEL- 329
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELp 757
|
170 180
....*....|....*....|.
gi 240255705 330 ------EATQRVNDAEIALQR 344
Cdd:COG1196 758 eppdleELERELERLEREIEA 778
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
168-347 |
1.12e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 168 EEKAQRISEVAIALKDeaasawndvnqtlnvvQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAE--------GY 239
Cdd:COG2268 205 EAEAERETEIAIAQAN----------------REAEEAELEQEREIETARIAEAEAELAKKKAEERREAEtaraeaeaAY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 240 NTSEESEVRDGVKDKEEALLSAKADIKECQENLAscEEQLRRLQVKKDELQKEVDRLNEAAERAQISA-LKAEEDvanim 318
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEKEAERE--EAELEADVRKPAEAEKQAAEAEAEAEAEAIRAkGLAEAE----- 341
|
170 180
....*....|....*....|....*....
gi 240255705 319 vlAEQAVAfelEATQRVNDAEIALQRAEK 347
Cdd:COG2268 342 --GKRALA---EAWNKLGDAAILLMLIEK 365
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
131-374 |
1.33e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 131 EKDTREQDSAPSLEELRDL-LNKATKELEVASLNS-TMFEEKAQRISEVAIAL----KDEAASAWNDVNQTLNVVQEAVD 204
Cdd:COG4717 301 GKEAEELQALPALEELEEEeLEELLAALGLPPDLSpEELLELLDRIEELQELLreaeELEEELQLEELEQEIAALLAEAG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 205 EESVAkEAVQKATMALSL--AEARLQVALESLEAEGYNTSEESEVRDgvkdkEEALlsaKADIKECQENLASCEEQLRRL 282
Cdd:COG4717 381 VEDEE-ELRAALEQAEEYqeLKEELEELEEQLEELLGELEELLEALD-----EEEL---EEELEELEEELEELEEELEEL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 283 QVKKDELQKEVDRL---NEAAE-RAQISALKAE----EDVANIMVLAEQAVAFELEATQRVNDAEIaLQRAEKtLFGSQT 354
Cdd:COG4717 452 REELAELEAELEQLeedGELAElLQELEELKAElrelAEEWAALKLALELLEEAREEYREERLPPV-LERASE-YFSRLT 529
|
250 260
....*....|....*....|
gi 240255705 355 QETTQGKVLDGKNTIVGEDE 374
Cdd:COG4717 530 DGRYRLIRIDEDLSLKVDTE 549
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
129-315 |
1.63e-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: 41.55 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 129 KEEKDT---REQDSAPSLEELRDLLNKAtkELEVASLNS--TMFE---EKAQRISEVAIALKDEAASAWNDVNQTLNVVQ 200
Cdd:pfam00261 7 KEELDEaeeRLKEAMKKLEEAEKRAEKA--EAEVAALNRriQLLEeelERTEERLAEALEKLEEAEKAADESERGRKVLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 201 --EAVDEESVA------KEAVQKATMA----------LSLAEARLQVALESLE-AEGYNTSEESEVRDG---VKDKE--E 256
Cdd:pfam00261 85 nrALKDEEKMEileaqlKEAKEIAEEAdrkyeevarkLVVVEGDLERAEERAElAESKIVELEEELKVVgnnLKSLEasE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255705 257 ALLSAKAD-----IKECQENLASCEEQLRRLQVKKDELQKEVDRLNEA--AERAQISALKAEEDVA 315
Cdd:pfam00261 165 EKASEREDkyeeqIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDEleAEKEKYKAISEELDQT 230
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
144-315 |
1.79e-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: 41.45 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 144 EELRDLLNKATKELEVASLnstmfeekAQRISEVAIALKdEAASAWNDVNQTLNVVQEAVDEesvAKEAVQKATMALSLA 223
Cdd:COG1579 4 EDLRALLDLQELDSELDRL--------EHRLKELPAELA-ELEDELAALEARLEAAKTELED---LEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 224 EARLQVALESL-------EAEGYnTSEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRL 296
Cdd:COG1579 72 EARIKKYEEQLgnvrnnkEYEAL-QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170
....*....|....*....
gi 240255705 297 NEAAErAQISALKAEEDVA 315
Cdd:COG1579 151 LAELE-AELEELEAEREEL 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
130-323 |
1.87e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 130 EEKDTREQDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDE--------AASAWNDVNQTLNVVQE 201
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlSHSRIPEIQAELSKLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 202 AVDEESVAKEAVQKATMALSLAEARLQVALESLEAE-GYNTSEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLR 280
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 240255705 281 RLQVKKDELQKEV----DRLNEAAERAQISALKAEEDVANIMVLAEQ 323
Cdd:TIGR02169 886 DLKKERDELEAQLreleRKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
168-346 |
2.19e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 168 EEKAQRISEVAIALKDEAASA---WNDVNQTLNVVQEAVDEESVAKEAVQkatMALSLAEARLQVALESLEAEGyntsEE 244
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSrrqLAAEQYRLVEMARELAELNEAESDLE---QDYQAASDHLNLVQTALRQQE----KI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 245 SEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKE----VDRLNEAAERA-----QISAL-KAEE-- 312
Cdd:PRK04863 351 ERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyQQALDVQQTRAiqyqqAVQALeRAKQlc 430
|
170 180 190
....*....|....*....|....*....|....*....
gi 240255705 313 -----DVANIMVLAEQAVAFELEATQRVNDAEIALQRAE 346
Cdd:PRK04863 431 glpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ 469
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
115-323 |
2.60e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.51 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 115 EFAEGSDDREVTFSKEEKDTREQDSAPSLEELRDLLnkatKELEVASLNSTMFEEKAQRISEVAIALKDEAASAWNDVNQ 194
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALL----KKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 195 TLNVVQEAVDEesVAKEAVQKATmalslaeaRLQVALESLEaegyNTSEESEVRDGVKDKEEALLSAKADikecqENLAS 274
Cdd:cd00176 80 RLEELNQRWEE--LRELAEERRQ--------RLEEALDLQQ----FFRDADDLEQWLEEKEAALASEDLG-----KDLES 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 240255705 275 CEEQLRRLQVKKDELQKEVDRLNEAAERAQisALKAEEDVANIMVLAEQ 323
Cdd:cd00176 141 VEELLKKHKELEEELEAHEPRLKSLNELAE--ELLEEGHPDADEEIEEK 187
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
139-351 |
2.84e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.55 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 139 SAPSLEELrdlLNKATKELEVASLNstmfeEKAQRISEVAIALKDEAASawNDVNQTLNVVQEAVDEESVAKEAVQKATM 218
Cdd:pfam05701 350 AVSSLEAE---LNRTKSEIALVQAK-----EKEAREKMVELPKQLQQAA--QEAEEAKSLAQAAREELRKAKEEAEQAKA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 219 ALSLAEARLQVALESLEAegyntSEESEvrdgvkdkEEALLSAKAdikeCQENlasceEQLRRLQVKKD----------- 287
Cdd:pfam05701 420 AASTVESRLEAVLKEIEA-----AKASE--------KLALAAIKA----LQES-----ESSAESTNQEDsprgvtlslee 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240255705 288 --ELQKEVDRLNEAA-ER-----AQISALKaEEDVANIMVLAEQAvafeLEATQRVNDAEIALQRAEKTLFG 351
Cdd:pfam05701 478 yyELSKRAHEAEELAnKRvaeavSQIEEAK-ESELRSLEKLEEVN----REMEERKEALKIALEKAEKAKEG 544
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
225-349 |
3.05e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 225 ARLQVALESLEAEgyntseESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLrrLQVKK----DELQKEVDRLneaa 300
Cdd:COG1579 34 AELEDELAALEAR------LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL--GNVRNnkeyEALQKEIESL---- 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 240255705 301 eRAQISALkaEEDVANIMVLAEQAVAFELEATQRVNDAEIALQRAEKTL 349
Cdd:COG1579 102 -KRRISDL--EDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-346 |
3.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 124 EVTFSKEEKDTREQDSAPSLEELRDLLNKATKE-LEVASLNSTMFEEKAQRISEVAIALKDEAASAwNDVNQTLNVVQEA 202
Cdd:PRK03918 486 EKVLKKESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKK 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 203 VDE-----ESVAKEAVQKATMALSLAEARLQvALESLEAEgYNTSEESEVRdgVKDKEEALLSAKADIKECQENLASCEE 277
Cdd:PRK03918 565 LDEleeelAELLKELEELGFESVEELEERLK-ELEPFYNE-YLELKDAEKE--LEREEKELKKLEEELDKAFEELAETEK 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 278 QLRRLQVKKDELQKEVD-----RLNE---------AAERAQISALKA--EEDVANIMVLAEQAVAFElEATQRVNDAEIA 341
Cdd:PRK03918 641 RLEELRKELEELEKKYSeeeyeELREeylelsrelAGLRAELEELEKrrEEIKKTLEKLKEELEERE-KAKKELEKLEKA 719
|
....*
gi 240255705 342 LQRAE 346
Cdd:PRK03918 720 LERVE 724
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
143-440 |
3.64e-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: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 143 LEELRDLLNKATKELE--VASLNSTMFEEKAQRISEVAIALKDEAasawndvnqTLNVVQEAVDEESVAKEAVQKATMAL 220
Cdd:pfam01576 143 LEDQNSKLSKERKLLEerISEFTSNLAEEEEKAKSLSKLKNKHEA---------MISDLEERLKKEEKGRQELEKAKRKL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 221 --SLAEARLQVALESLEAEgyntseesEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNE 298
Cdd:pfam01576 214 egESTDLQEQIAELQAQIA--------ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 299 AAERA---------QISALKAE-EDvanimVLAEQAVAFELEAtQRvnDAEIA-LQRA---EKTLFGSQTQETTQgkvld 364
Cdd:pfam01576 286 ARNKAekqrrdlgeELEALKTElED-----TLDTTAAQQELRS-KR--EQEVTeLKKAleeETRSHEAQLQEMRQ----- 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255705 365 gKNTivgedEVLSEIVDVSHQAERdlvvVGVSSDVGTQSYESDNENGKPTADFAKEAEGEAEKSKnvvltKKQEVQ 440
Cdd:pfam01576 353 -KHT-----QALEELTEQLEQAKR----NKANLEKAKQALESENAELQAELRTLQQAKQDSEHKR-----KKLEGQ 413
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
108-359 |
4.74e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 108 VGNDRNLEFAEGSDDREVTFSKEEKDTREQDSAPSLEELRdllNKATKELEVASLNSTM---FEEKAQRISEVAIALKDE 184
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLG---ENAESSKRLNENANNLikqFENTKEKIAEYTKSIDIK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 185 AA-SAWNDVNQTLNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEVRDGVKD---------- 253
Cdd:COG5185 309 KAtESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEldsfkdties 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 254 -KEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVLA---------EQ 323
Cdd:COG5185 389 tKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAdeesqsrleEA 468
|
250 260 270
....*....|....*....|....*....|....*.
gi 240255705 324 AVAFELEATQRVNDAEIALQRAEKTLFGSQTQETTQ 359
Cdd:COG5185 469 YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKL 504
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
203-347 |
5.33e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 203 VDEESVAKEAVQKATMALSLAEARLQVAleslEAEgyntsEESEVRDGVKDKEEALLSAKADIKECQENLAsceEQLRRL 282
Cdd:COG2268 179 LEDENNYLDALGRRKIAEIIRDARIAEA----EAE-----RETEIAIAQANREAEEAELEQEREIETARIA---EAEAEL 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240255705 283 QVKKDELQKEvdrlneaAERAQISAlKAEEDVANIMvlAEQAVAFELEATQRvnDAEIALQRAEK 347
Cdd:COG2268 247 AKKKAEERRE-------AETARAEA-EAAYEIAEAN--AEREVQRQLEIAER--EREIELQEKEA 299
|
|
| PRK05326 |
PRK05326 |
potassium/proton antiporter; |
578-775 |
6.14e-03 |
|
potassium/proton antiporter;
Pssm-ID: 235410 [Multi-domain] Cd Length: 562 Bit Score: 40.57 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 578 ASVIFVPLFQKIpgGSPVL-GYLAAGILIGPYGLSIIR--NVHGTKAIAEFGVVFLLFNIGLElsvERLSSMKKYV---F 651
Cdd:PRK05326 17 LSILASRLSSRL--GIPSLlLFLAIGMLAGEDGLGGIQfdNYPLAYLVGNLALAVILFDGGLR---TRWSSFRPALgpaL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 652 GLGSAQVLVTAAVIGLITHYVAGQAGPAAIVIGNglALSST--AVVLQVLQERGESTSRHGRATfsvlL-----FQD-LA 723
Cdd:PRK05326 92 SLATLGVLITAGLTGLFAHWLLGLDWLEGLLLGA--IVGSTdaAAVFSLLRGKGLNLKERVAST----LeiesgSNDpMA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 240255705 724 VVVLLILIPLISPNSSKGGIGFqaiaeaLGLAAIKAAVAITGIIAGGRLLLR 775
Cdd:PRK05326 166 VFLTITLIELITGGETGLSWGF------LLLFLQQFGLGALIGLLGGWLLVQ 211
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
204-304 |
6.24e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.98 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 204 DEESVAKEAVQKAT-MALSLAEAR--LQVALESLEAEgyntseesevRDGVKDKEEALLSAKADIKECQENLAS----CE 276
Cdd:pfam20492 20 EETKKAQEELEESEeTAEELEEERrqAEEEAERLEQK----------RQEAEEEKERLEESAEMEAEEKEQLEAelaeAQ 89
|
90 100
....*....|....*....|....*...
gi 240255705 277 EQLRRLQVKKDELQKEVDRLNEAAERAQ 304
Cdd:pfam20492 90 EEIARLEEEVERKEEEARRLQEELEEAR 117
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
169-345 |
6.38e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.22 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 169 EKAQRISEvaiALKDEAASAWNDVNQTLnvvqeavdeesvAKEAVQKATMALSLAEARLQVALESLeaegyntseeSEVR 248
Cdd:COG3524 150 EDAQAIAE---ALLAESEELVNQLSERA------------REDAVRFAEEEVERAEERLRDAREAL----------LAFR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 249 DgvkdkEEALLSAKADIKECQENLASCEEQLRRLQVKKDEL--------------QKEVDRLNE--AAERAQISALKAEE 312
Cdd:COG3524 205 N-----RNGILDPEATAEALLQLIATLEGQLAELEAELAALrsylspnspqvrqlRRRIAALEKqiAAERARLTGASGGD 279
|
170 180 190
....*....|....*....|....*....|....
gi 240255705 313 DVANIMVLAEQAVAfELE-ATQRVNDAEIALQRA 345
Cdd:COG3524 280 SLASLLAEYERLEL-EREfAEKAYTSALAALEQA 312
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
174-374 |
9.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 174 ISEVAIALKDEAASAWNDVNQTLNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEaegyntseesEVRDGVKD 253
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ----------AAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 254 KEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNE--AAERAQISALKAEEDVANIMVLAEQAVAFELEA 331
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSeiAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 240255705 332 TQRVNDAEIALQRAEKTLFGSQTQETTQGKVLDGKNTIVGEDE 374
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-389 |
9.41e-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: 40.43 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 250 GVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEaaeraQISALKAEEDVANIMVLAEQAVAFEL 329
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE-----ELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255705 330 EatQRVNDAEIALQRAEKTLFGSQTQETTQGKVLDGKNTIVGEDEVlsEIVDVSHQAERD 389
Cdd:TIGR02168 739 E--AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA--EIEELEAQIEQL 794
|
|
| |
