|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
13-345 |
0e+00 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 694.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 13 DNVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDS-SNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEG 91
Cdd:cd01371 1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 92 YNGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEV 171
Cdd:cd01371 81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 172 KERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDL 251
Cdd:cd01371 161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 252 AGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDE 331
Cdd:cd01371 241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
|
330
....*....|....
gi 46852174 332 TISTLRYANRAKNI 345
Cdd:cd01371 321 TLSTLRYANRAKNI 334
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
20-345 |
1.81e-178 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 511.35 E-value: 1.81e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 20 RCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAY 99
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 100 GQTGTGKTFTMEGvraIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQT--QRLEVKERPDV 177
Cdd:pfam00225 81 GQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKnkRKLRIREDPKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 178 GVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAGSERQ 257
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSERA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 258 AKTG-ATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTL 336
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317
|
....*....
gi 46852174 337 RYANRAKNI 345
Cdd:pfam00225 318 RFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
14-352 |
6.26e-171 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 492.47 E-value: 6.26e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYN 93
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 94 GTIFAYGQTGTGKTFTMEGvraIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQtQRLEVKE 173
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSS-KKLEIRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 174 RPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGiDGNMHVRMGKLHLVDLAG 253
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN-SSSGSGKASKLNLVDLAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 254 SERQAKTGATGQRLKEATKINLSLSTLGNVISALVD-GKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDET 332
Cdd:smart00129 236 SERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEET 315
|
330 340
....*....|....*....|
gi 46852174 333 ISTLRYANRAKNIKNKARIN 352
Cdd:smart00129 316 LSTLRFASRAKEIKNKPIVN 335
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
14-343 |
3.18e-162 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 469.81 E-value: 3.18e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 14 NVKVVVRCRPLNEREKSMCyKQAVSVDEMRgTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYN 93
Cdd:cd00106 1 NVRVAVRVRPLNGREARSA-KSVISVDGGK-SVVLDPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 94 GTIFAYGQTGTGKTFTMEGVRaiPELRGIIPNSFAHIFGHI-AKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVK 172
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPD--PEQRGIIPRALEDIFERIdKRKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 173 ERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGnMHVRMGKLHLVDLA 252
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSG-ESVTSSKLNLVDLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 253 GSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDET 332
Cdd:cd00106 236 GSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEET 315
|
330
....*....|.
gi 46852174 333 ISTLRYANRAK 343
Cdd:cd00106 316 LSTLRFASRAK 326
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
15-346 |
7.39e-134 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 397.86 E-value: 7.39e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 15 VKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVhktdssnEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNG 94
Cdd:cd01372 3 VRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTV-------GTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 95 TIFAYGQTGTGKTFTMEGVRAIPEL---RGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGK--DQTQRL 169
Cdd:cd01372 76 TVLAYGQTGSGKTYTMGTAYTAEEDeeqVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPetDKKPTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 170 EVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIE-------CSEKGIDGNMHVR 242
Cdd:cd01372 156 SIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEqtkkngpIAPMSADDKNSTF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 243 MGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDG--KSTHVPYRNSKLTRLLQDSLGGNSKTMMCA 320
Cdd:cd01372 236 TSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDEskKGAHVPYRDSKLTRLLQDSLGGNSHTLMIA 315
|
330 340
....*....|....*....|....*.
gi 46852174 321 NIGPADYNYDETISTLRYANRAKNIK 346
Cdd:cd01372 316 CVSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
14-354 |
1.15e-132 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 395.16 E-value: 1.15e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITV-HKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGY 92
Cdd:cd01364 3 NIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 93 NGTIFAYGQTGTGKTFTMEGVRAI--------PELRGIIPNSFAHIFGHIAkaEGDTRFLVRVSYLEIYNEEVRDLLG-- 162
Cdd:cd01364 83 NCTIFAYGQTGTGKTYTMEGDRSPneeytwelDPLAGIIPRTLHQLFEKLE--DNGTEYSVKVSYLEIYNEELFDLLSps 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 163 KDQTQRLEVKERPDV--GVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMH 240
Cdd:cd01364 161 SDVSERLRMFDDPRNkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 241 VRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDgKSTHVPYRNSKLTRLLQDSLGGNSKTMMCA 320
Cdd:cd01364 241 VKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-RAPHVPYRESKLTRLLQDSLGGRTKTSIIA 319
|
330 340 350
....*....|....*....|....*....|....
gi 46852174 321 NIGPADYNYDETISTLRYANRAKNIKNKARINED 354
Cdd:cd01364 320 TISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
13-345 |
6.32e-132 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 392.08 E-value: 6.32e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 13 DNVKVVVRCRPLNEREKSMCYKQAVSVDEMRgTITVhktdSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGY 92
Cdd:cd01369 2 CNIKVVCRFRPLNELEVLQGSKSIVKFDPED-TVVI----ATSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 93 NGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTqRLEVK 172
Cdd:cd01369 77 NGTIFAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKT-NLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 173 ERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIEcSEKGIDGNmhVRMGKLHLVDLA 252
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVK-QENVETEK--KKSGKLYLVDLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 253 GSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDET 332
Cdd:cd01369 233 GSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESET 312
|
330
....*....|...
gi 46852174 333 ISTLRYANRAKNI 345
Cdd:cd01369 313 LSTLRFGQRAKTI 325
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
14-347 |
1.01e-131 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 391.96 E-value: 1.01e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNeppKTFTFDTVFGPESKQLDVYNLTArPIIDSVLEGYN 93
Cdd:cd01366 3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIELTSIGAKQ---KEFSFDKVFDPEASQEDVFEEVS-PLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 94 GTIFAYGQTGTGKTFTMEGVraiPELRGIIPNSFAHIFgHIAK--AEGDTRFLVRVSYLEIYNEEVRDLL--GKDQTQRL 169
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGP---PESPGIIPRALQELF-NTIKelKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 170 EVKERPDVG-VYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIEcsekGID-GNMHVRMGKLH 247
Cdd:cd01366 155 EIRHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIS----GRNlQTGEISVGKLN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 248 LVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKStHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADY 327
Cdd:cd01366 231 LVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS-HIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAES 309
|
330 340
....*....|....*....|
gi 46852174 328 NYDETISTLRYANRAKNIKN 347
Cdd:cd01366 310 NLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
13-352 |
6.65e-130 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 388.25 E-value: 6.65e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 13 DNVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSN-----EPPKTFTFDTVF----GPESK---QLDVYNLT 80
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNnkatrEVPKSFSFDYSYwshdSEDPNyasQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 81 ARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGvraIPELRGIIPNSFAHIFGHIAKAEGD-TRFLVRVSYLEIYNEEVRD 159
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMG---TQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 160 LLGKD---QTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIecSEKGID 236
Cdd:cd01365 158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVL--TQKRHD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 237 ---GNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVD-------GKSTHVPYRNSKLTRLL 306
Cdd:cd01365 236 aetNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVLTWLL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 46852174 307 QDSLGGNSKTMMCANIGPADYNYDETISTLRYANRAKNIKNKARIN 352
Cdd:cd01365 316 KENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
14-345 |
3.75e-125 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 374.75 E-value: 3.75e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEmrGTITVHKTDSSNeppktFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYN 93
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEIDN--DTIYLVEPPSTS-----FTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 94 GTIFAYGQTGTGKTFTMEGVRAIPelrGIIPNSFAHIFGHIAKAEgDTRFLVRVSYLEIYNEEVRDLLGKdQTQRLEVKE 173
Cdd:cd01374 74 GTIFAYGQTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQDTP-DREFLLRVSYLEIYNEKINDLLSP-TSQNLKIRD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 174 RPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAG 253
Cdd:cd01374 149 DVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTVRVSTLNLIDLAG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 254 SERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGK-STHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDET 332
Cdd:cd01374 229 SERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKvGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEET 308
|
330
....*....|...
gi 46852174 333 ISTLRYANRAKNI 345
Cdd:cd01374 309 LNTLKFASRAKKI 321
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
13-354 |
1.48e-119 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 361.44 E-value: 1.48e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 13 DNVKVVVRCRPLNEREKSMCYKQAVSVdEMRGTITVHktdssNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGY 92
Cdd:cd01373 1 DAVKVFVRIRPPAEREGDGEYGQCLKK-LSSDTLVLH-----SKPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 93 NGTIFAYGQTGTGKTFTM-----EGVRAIPELRGIIPNSFAHIFGHI----AKAEGDTRFLVRVSYLEIYNEEVRDLLgk 163
Cdd:cd01373 75 NGTIFAYGQTGSGKTYTMwgpseSDNESPHGLRGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 164 DQTQR-LEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGiDGNMHVR 242
Cdd:cd01373 153 DPASRnLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKK-ACFVNIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 243 MGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVD---GKSTHVPYRNSKLTRLLQDSLGGNSKTMMC 319
Cdd:cd01373 232 TSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAII 311
|
330 340 350
....*....|....*....|....*....|....*
gi 46852174 320 ANIGPADYNYDETISTLRYANRAKNIKNKARINED 354
Cdd:cd01373 312 ANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
14-345 |
4.72e-115 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 349.72 E-value: 4.72e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 14 NVKVVVRCRPLNEREKSMCYKQAVSV-----------DEMRGTITVHKTDSSNEP----PKTFTFDTVFGPESKQLDVYN 78
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfdpkDEEDGFFHGGSNNRDRRKrrnkELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 79 LTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAIPelrGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVR 158
Cdd:cd01370 81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 159 DLLGKdQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGN 238
Cdd:cd01370 158 DLLNP-SSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 239 MHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDG--KSTHVPYRNSKLTRLLQDSLGGNSKT 316
Cdd:cd01370 237 QQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPgkKNKHIPYRDSKLTRLLKDSLGGNCRT 316
|
330 340
....*....|....*....|....*....
gi 46852174 317 MMCANIGPADYNYDETISTLRYANRAKNI 345
Cdd:cd01370 317 VMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
14-539 |
4.54e-93 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 300.12 E-value: 4.54e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSS-----NEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSV 88
Cdd:COG5059 6 NSPLKSRLSSRNEKSVSDIKSTIRIIPGELGERLINTSKKShvsleKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 89 LEGYNGTIFAYGQTGTGKTFTMEGvraIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDqTQR 168
Cdd:COG5059 86 LLGYNCTVFAYGQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPN-EES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 169 LEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIE--CSEKGIDGNmhvrmGKL 246
Cdd:COG5059 162 LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELAskNKVSGTSET-----SKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 247 HLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVD-GKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPA 325
Cdd:COG5059 237 SLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 326 DYNYDETISTLRYANRAKNIKNKARINEdpkdalLRQFQKEIEELKKKLEE-GEEISGSdisgseedddeegevgedgek 404
Cdd:COG5059 317 SNSFEETINTLKFASRAKSIKNKIQVNS------SSDSSREIEEIKFDLSEdRSEIEIL--------------------- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 405 rkkrrgkkkVSPDKMIEMQAKIDEERKALET---KLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEklSALEKKVIV 481
Cdd:COG5059 370 ---------VFREQSQLSQSSLSGIFAYMQSlkkETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYK--STLQFLRIE 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 46852174 482 GGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQerLDIEEKYTSLQEEA 539
Cdd:COG5059 439 IDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSD--RVESEKASKLRSSA 494
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
15-343 |
5.03e-90 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 284.47 E-value: 5.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 15 VKVVVRCRPLNEREKSMCY----KQAVSV----DEMRGTITVHKTDSSneppktFTFDTVFGPESKQLdVYNLTARPIID 86
Cdd:cd01375 2 VQAFVRVRPTDDFAHEMIKygedGKSISIhlkkDLRRGVVNNQQEDWS------FKFDGVLHNASQEL-VYETVAKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 87 SVLEGYNGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKaEGDTRFLVRVSYLEIYNEEVRDLLGK--- 163
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEE-RPTKAYTVHVSYLEIYNEQLYDLLSTlpy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 164 --DQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIEcSEKGIDGNMHV 241
Cdd:cd01375 154 vgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLE-AHSRTLSSEKY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 242 RMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCAN 321
Cdd:cd01375 233 ITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVAN 312
|
330 340
....*....|....*....|..
gi 46852174 322 IGPADYNYDETISTLRYANRAK 343
Cdd:cd01375 313 IYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
14-343 |
5.26e-82 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 262.82 E-value: 5.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 14 NVKVVVRCRPLNEREKSMCYKQAVSV-DEMrgTITVHKTDSSNEPPKtFTFDTVFGPESKQLDVYNLTARPIIDSVLEGY 92
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGiDSC--SVELADPRNHGETLK-YQFDAFYGEESTQEDIYAREVQPIVPHLLEGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 93 NGTIFAYGQTGTGKTFTMEGvraIPELRGIIPNSFAHIFGHIAKAEGDTRFLvrVSYLEIYNEEVRDLL-GKDqtQRLEV 171
Cdd:cd01376 78 NATVFAYGSTGAGKTFTMLG---SPEQPGLMPLTVMDLLQMTRKEAWALSFT--MSYLEIYQEKILDLLePAS--KELVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 172 KERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIdgNMHVRMGKLHLVDL 251
Cdd:cd01376 151 REDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLA--PFRQRTGKLNLIDL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 252 AGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKStHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDE 331
Cdd:cd01376 229 AGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQD 307
|
330
....*....|..
gi 46852174 332 TISTLRYANRAK 343
Cdd:cd01376 308 TLSTLNFAARSR 319
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
13-343 |
8.44e-81 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 260.40 E-value: 8.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 13 DNVKVVVRCRPLNEREK----SMCYK----QAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPI 84
Cdd:cd01368 1 DPVKVYLRVRPLSKDELesedEGCIEvinsTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 85 IDSVLEGYNGTIFAYGQTGTGKTFTMEGVraiPELRGIIPNSFAHIFGHIAKaegdtrFLVRVSYLEIYNEEVRDLL--- 161
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGS---PGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLeps 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 162 GKDQTQR---LEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGN 238
Cdd:cd01368 152 PSSPTKKrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 239 M-----HVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISAL----VDGKSTHVPYRNSKLTRLLQDS 309
Cdd:cd01368 232 VdqdkdQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrenqLQGTNKMVPFRDSKLTHLFQNY 311
|
330 340 350
....*....|....*....|....*....|....
gi 46852174 310 LGGNSKTMMCANIGPADYNYDETISTLRYANRAK 343
Cdd:cd01368 312 FDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
15-371 |
2.31e-80 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 279.13 E-value: 2.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 15 VKVVVRCRPLNEREKSMCYKQAVSVDEMrgtitvhktdSSNEppKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNG 94
Cdd:PLN03188 100 VKVIVRMKPLNKGEEGEMIVQKMSNDSL----------TING--QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 95 TIFAYGQTGTGKTFTMEG-VRAIPE------LRGIIPNSFAHIFGHIAK-----AEGDTRFLVRVSYLEIYNEEVRDLLg 162
Cdd:PLN03188 168 SVFAYGQTGSGKTYTMWGpANGLLEehlsgdQQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLL- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 163 kDQTQR-LEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGI-DGNMH 240
Cdd:PLN03188 247 -DPSQKnLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVaDGLSS 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 241 VRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVD----GKSTHVPYRNSKLTRLLQDSLGGNSKT 316
Cdd:PLN03188 326 FKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46852174 317 MMCANIGPADYNYDETISTLRYANRAKNIKNKARINEDPKD------ALLRQFQKEIEELK 371
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDdvnflrEVIRQLRDELQRVK 466
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
14-343 |
2.08e-79 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 256.45 E-value: 2.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEmRGTITVHKTDSSNEPPK-----TFTFDTVFGPESKQLDVYNLTARPIIDSV 88
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPS-KLTLIVHEPKLKVDLTKyienhTFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 89 LEGYNGTIFAYGQTGTGKTFTMEGVRAIPELR-GIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLgkDQTQ 167
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGDFSGQEESkGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL--NRKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 168 RLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIecsEKGIDGNMHvrmGKLH 247
Cdd:cd01367 158 RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL---RDRGTNKLH---GKLS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 248 LVDLAGSERQAKT-GATGQRLKEATKINLSLSTLGNVISALVDGKStHVPYRNSKLTRLLQDSL-GGNSKTMMCANIGPA 325
Cdd:cd01367 232 FVDLAGSERGADTsSADRQTRMEGAEINKSLLALKECIRALGQNKA-HIPFRGSKLTQVLKDSFiGENSKTCMIATISPG 310
|
330
....*....|....*...
gi 46852174 326 DYNYDETISTLRYANRAK 343
Cdd:cd01367 311 ASSCEHTLNTLRYADRVK 328
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
17-286 |
6.87e-28 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 110.51 E-value: 6.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 17 VVVRCRPLNEREKsmcykqavsvdemrgtitvhktdssNEPPKTFTFDTVFGPESKQLDVYNLtARPIIDSVLEGYNG-T 95
Cdd:cd01363 1 VLVRVNPFKELPI-------------------------YRDSKIIVFYRGFRRSESQPHVFAI-ADPAYQSMLDGYNNqS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 96 IFAYGQTGTGKTFTMEgvraipelrGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNeEVRDllgkdqtqrlevkerp 175
Cdd:cd01363 55 IFAYGESGAGKTETMK---------GVIPYLASVAFNGINKGETEGWVYLTEITVTLED-QILQ---------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 176 dvgvyikdlsayvvnnaddmdrIMTLGHKNRsVGATNMNEHSSRSHAIFTItiecsekgidgnmhvrmgklhLVDLAGSE 255
Cdd:cd01363 109 ----------------------ANPILEAFG-NAKTTRNENSSRFGKFIEI---------------------LLDIAGFE 144
|
250 260 270
....*....|....*....|....*....|.
gi 46852174 256 RqaktgatgqrlkeatkINLSLSTLGNVISA 286
Cdd:cd01363 145 I----------------INESLNTLMNVLRA 159
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
14-161 |
7.21e-21 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 89.20 E-value: 7.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 14 NVKVVVRCRPLNEREKSMCYkqavsvdeMRGTITVHKTDSSNeppKTFTFDTVFGPESKQLDVYNLTaRPIIDSVLEGYN 93
Cdd:pfam16796 21 NIRVFARVRPELLSEAQIDY--------PDETSSDGKIGSKN---KSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYN 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852174 94 GTIFAYGQTGTGKTFTMegvraipelrgiIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLL 161
Cdd:pfam16796 89 VCIFAYGQTGSGSNDGM------------IPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
424-588 |
2.38e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 424 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVggvdLLAKAEEQEKLLEESNME 503
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR----LEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 504 LEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKkvwtmlmAAKSEMADLQQEHQREIEGLLENIRQLSR 583
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL-------EAEAELAEAEEELEELAEELLEALRAAAE 397
|
....*
gi 46852174 584 ELRLQ 588
Cdd:COG1196 398 LAAQL 402
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
421-585 |
3.63e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 421 EMQAKIDEERKA---LETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIvggvDLLAKAEEQEKLL 497
Cdd:COG1196 278 ELELELEEAQAEeyeLLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE----ELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 498 EESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKvwtmLMAAKSEMADLQQEHQREIEGLLEN 577
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE----LEEAEEALLERLERLEEELEELEEA 429
|
....*...
gi 46852174 578 IRQLSREL 585
Cdd:COG1196 430 LAELEEEE 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
423-585 |
9.22e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 9.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 423 QAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNM 502
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 503 E---LEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQ---QEHQREIEGLLE 576
Cdd:COG1196 398 LaaqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLellAELLEEAALLEA 477
|
....*....
gi 46852174 577 NIRQLSREL 585
Cdd:COG1196 478 ALAELLEEL 486
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
336-584 |
2.09e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 336 LRYANRAKNIKNKARINEDPKDALLRQFQ--KEIEELKK--KLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGK 411
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEekKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 412 KKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKaraELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAE 491
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 492 EQEKLLEESNMELEERRKRAEQLRRELEE-KEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQRE 570
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEaKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
250
....*....|....
gi 46852174 571 IEGLLENIRQLSRE 584
Cdd:PTZ00121 1752 DEEEKKKIAHLKKE 1765
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
428-585 |
3.03e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 428 EERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEESNMELEER 507
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----EDLRAELEEVDKEFAETRDELKDY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 508 RKRAEQLRRELEE--KEQERL-------------------DIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQE 566
Cdd:TIGR02169 391 REKLEKLKREINElkRELDRLqeelqrlseeladlnaaiaGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
170 180
....*....|....*....|..
gi 46852174 567 HQR---EIEGLLENIRQLSREL 585
Cdd:TIGR02169 471 LYDlkeEYDRVEKELSKLQREL 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
434-589 |
4.06e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 434 ETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDL--------LAKAEEQEKLLEESNMELE 505
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 506 ERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSE---------------------MADLQ 564
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelralleerfaaalgdavERELR 768
|
170 180
....*....|....*....|....*
gi 46852174 565 QEHQREIEGLLENIRQLSRELRLQM 589
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAM 793
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
424-585 |
9.06e-09 |
|
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: 56.47 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 424 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEE--SN 501
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNvrNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 502 MELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQL 581
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
....
gi 46852174 582 SREL 585
Cdd:COG1579 169 AAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
418-588 |
9.72e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 418 KMIEMQAKIDEERKALETKLDMEEEERNKARAELE--KREKDLLKAQQEHQSLLEKLSALEKKvivggvdlLAKAEEQEK 495
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEelREELEKLEKLLQLLPLYQELEALEAE--------LAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 496 LLEESNMELEERRKRAEQLRRELEEKEQErldIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLL 575
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|...
gi 46852174 576 ENIRQLSRELRLQ 588
Cdd:COG4717 227 EELEQLENELEAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
421-570 |
1.93e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 421 EMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEES 500
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 501 NmELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVwtmLMAAKSEMADLQQEHQRE 570
Cdd:COG1196 424 E-ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE---AALLEAALAELLEELAEA 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-586 |
2.86e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 340 NRAKNIKN-KARINEdpKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDK 418
Cdd:TIGR02168 674 ERRREIEElEEKIEE--LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 419 MIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKV------------------- 479
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerlesler 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 480 -----IVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLM 554
Cdd:TIGR02168 832 riaatERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250 260 270
....*....|....*....|....*....|....*
gi 46852174 555 AAKSEMADLQQEH---QREIEGLLENIRQLSRELR 586
Cdd:TIGR02168 912 ELRRELEELREKLaqlELRLEGLEVRIDNLQERLS 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
428-585 |
6.12e-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: 56.22 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 428 EERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGV-----------------DLLAKA 490
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErlanlerqleeleaqleELESKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 491 EEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKK---LKKVWTMLMAAKSEMADLQQEH 567
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERL 412
|
170
....*....|....*...
gi 46852174 568 QREIEGLLENIRQLSREL 585
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKL 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
424-583 |
7.92e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 424 AKIDEERKAL-----ETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLE 498
Cdd:COG4913 272 AELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 499 EsnmELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENI 578
Cdd:COG4913 352 R---ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
....*
gi 46852174 579 RQLSR 583
Cdd:COG4913 429 ASLER 433
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
421-539 |
7.95e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.55 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 421 EMQAKIDEERKALETKldmEEEERNKARAELEKREKDLLKAQQEHQsLLEKLSALEKKvivggvdlLAKAEEQEKLLEES 500
Cdd:PRK12704 48 KKEAEAIKKEALLEAK---EEIHKLRNEFEKELRERRNELQKLEKR-LLQKEENLDRK--------LELLEKREEELEKK 115
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 46852174 501 NMELEERRKRAEQLRRELEEKEQERLDIEEKYTSL-QEEA 539
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQLQELERISGLtAEEA 155
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
343-580 |
1.39e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.98 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 343 KNIKNKARINEDPKDALLRQFQKEIEELKK---KLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDKM 419
Cdd:pfam02463 194 ELKLQELKLKEQAKKALEYYQLKEKLELEEeylLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 420 IEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVggvdllaKAEEQEKLLEE 499
Cdd:pfam02463 274 NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE-------EIEELEKELKE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 500 SNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEmADLQQEHQREIEGLLENIR 579
Cdd:pfam02463 347 LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE-AQLLLELARQLEDLLKEEK 425
|
.
gi 46852174 580 Q 580
Cdd:pfam02463 426 K 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
337-574 |
2.47e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 337 RYANRAKNIKNKARINEDPKDAllRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSP 416
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKK-------VIVGGVDLLAK 489
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKkaeedknMALRKAEEAKK 1588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 490 AEEQeKLLEESNMELEERRKRAEQLRRELEE--------KEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMA 561
Cdd:PTZ00121 1589 AEEA-RIEEVMKLYEEEKKMKAEEAKKAEEAkikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
250
....*....|...
gi 46852174 562 DLQQEHQREIEGL 574
Cdd:PTZ00121 1668 KKAEEDKKKAEEA 1680
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
426-586 |
4.29e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 426 IDEERKALETKldmeEEERNKARAELEKREKDLLKAqqehqsllEKLSALEKKVivggVDLLAKAEEQEKLLEESNMELE 505
Cdd:PRK02224 470 IEEDRERVEEL----EAELEDLEEEVEEVEERLERA--------EDLVEAEDRI----ERLEERREDLEELIAERRETIE 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 506 ERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLqqEHQREIEGLLENIRQLSREL 585
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIERL 611
|
.
gi 46852174 586 R 586
Cdd:PRK02224 612 R 612
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
418-586 |
4.53e-07 |
|
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: 53.53 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 418 KMIEMQAKIDEERKALEtKLdmeEEERNKA------RAELEKREKDLLKAQQEhqSLLEKLSALEKKVivggvdllakaE 491
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLE-RL---RREREKAeryqalLKEKREYEGYELLKEKE--ALERQKEAIERQL-----------A 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 492 EQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDI-EEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQR- 569
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKl 327
|
170
....*....|....*....
gi 46852174 570 --EIEGLLENIRQLSRELR 586
Cdd:TIGR02169 328 eaEIDKLLAEIEELEREIE 346
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
336-548 |
4.62e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 336 LRYANRAKNIKnKARINEDPKDALLRQFQKEiEELKKKLEE---GEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKK 412
Cdd:PTZ00121 1580 LRKAEEAKKAE-EARIEEVMKLYEEEKKMKA-EEAKKAEEAkikAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 413 KVSPDKMIEMQAKIDEERKALETKldMEEEERNKARAELEKREKDLLKAQQehqslLEKLSALEKKvivgGVDLLAKAEE 492
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAK--KAEEDEKKAAEALKKEAEEAKKAEE-----LKKKEAEEKK----KAEELKKAEE 1726
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46852174 493 QEKL-LEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKK 548
Cdd:PTZ00121 1727 ENKIkAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
448-616 |
6.24e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 448 RAELEKREKDLLKAQ-QEHQSLLEKLSALEKKvivggvdlLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQE-- 524
Cdd:COG4717 48 LERLEKEADELFKPQgRKPELNLKELKELEEE--------LKEAEEKEEEYAELQEELEELEEELEELEAELEELREEle 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 525 RLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQqEHQREIEGLLENIRQLSRELRLQMLIIDNFIPRDYQEMI 604
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170
....*....|..
gi 46852174 605 ENYVHWNEDIGE 616
Cdd:COG4717 199 EELEELQQRLAE 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
424-586 |
1.48e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 424 AKIDEERKALETKLDMEEEERNKARAE---LEKREKDLLKAQQEHQSLLEK-LSALEKKVIVGGVDLLAKAE-------- 491
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAElaeLEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEdfldavrr 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 492 ------------EQEKLLEESNMELEERRKRAEQLRRELEEKEQERldiEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSE 559
Cdd:COG4942 138 lqylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAELAAE 214
|
170 180
....*....|....*....|....*..
gi 46852174 560 MADLQQEhQREIEGLLENIRQLSRELR 586
Cdd:COG4942 215 LAELQQE-AEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
429-586 |
1.52e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 429 ERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVD----------------------L 486
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekigeleaeiaslersI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 487 LAKAEEQEKLLEESNMELEERRK---RAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADL 563
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKllaEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190
....*....|....*....|....*....|...
gi 46852174 564 QQ----------EHQREIEGLLENIRQLSRELR 586
Cdd:TIGR02169 391 REkleklkreinELKRELDRLQEELQRLSEELA 423
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
485-581 |
1.53e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 485 DLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEK-YTSLQEEAQGKTKKLKKVWTMLMAAKSEMADL 563
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKlLEEAEKEAQQAIKEAKKEADEIIKELRQLQKG 599
|
90
....*....|....*...
gi 46852174 564 QQEHQREIEgLLENIRQL 581
Cdd:PRK00409 600 GYASVKAHE-LIEARKRL 616
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
341-584 |
1.68e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 341 RAKNIKNKARINEDPKDALLR--QFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDK 418
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 419 MIEMQAKIDEERKALETKLDMEEEERNK---ARAELEKREKDLLKAQQEHQSLLEKLSALEKKvivgGVDLLAKAEEQEK 495
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKAdeaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK----KADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 496 LLEESNME---LEERRKRAEQLRRELEEKEQ--ERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQRE 570
Cdd:PTZ00121 1548 ADELKKAEelkKAEEKKKAEEAKKAEEDKNMalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
250
....*....|....
gi 46852174 571 IEGLLENIRQLSRE 584
Cdd:PTZ00121 1628 AEEEKKKVEQLKKK 1641
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
443-586 |
1.90e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 443 ERNKARAELEKREKDLLKAQQEHQSLLEKLSALEkkvivggvdllAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKE 522
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELE-----------AELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852174 523 QERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQR---EIEGLLENIRQLSRELR 586
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALL 368
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
424-585 |
3.54e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 424 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEESNME 503
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI----DKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 504 LEER---------------------------------RKRAEQLRRELEEKEQERLDIEEKytslQEEAQGKTKKLKKVW 550
Cdd:COG3883 88 LGERaralyrsggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAK----KAELEAKLAELEALK 163
|
170 180 190
....*....|....*....|....*....|....*
gi 46852174 551 TMLMAAKSEMADLQQEHQREIEGLLENIRQLSREL 585
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
417-553 |
4.06e-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: 50.44 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEMQAKIDEERKALET---KLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdLLAKAEEQ 493
Cdd:TIGR02168 365 AELEELESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL------EEAELKEL 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 494 EKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTML 553
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
417-580 |
4.37e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVI------------VGGV 484
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyrsggsVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 485 DLLAKAEEQEKLLEESNM-------------ELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWT 551
Cdd:COG3883 106 DVLLGSESFSDFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180
....*....|....*....|....*....
gi 46852174 552 MLMAAKSEMADLQQEHQREIEGLLENIRQ 580
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
417-554 |
5.98e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEmqAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDL-LAKAEEQEK 495
Cdd:COG2433 383 EELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELsEARSEERRE 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 46852174 496 LLEESnmELEERRKRAEQLRRELEEKEQERldieekytslqEEAQGKTKKLKKVWTMLM 554
Cdd:COG2433 461 IRKDR--EISRLDREIERLERELEEERERI-----------EELKRKLERLKELWKLEH 506
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
423-559 |
1.19e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 423 QAKIDEERKALETKLDMEE--EERNKARAELE---KREKDLLKAQQEHQSLLEKLSALEKKVivggvdllakAEEQEKLL 497
Cdd:COG4717 111 LEELREELEKLEKLLQLLPlyQELEALEAELAelpERLEELEERLEELRELEEELEELEAEL----------AELQEELE 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46852174 498 EESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSE 559
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
417-583 |
1.56e-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: 48.53 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSAL--EKKVIVGGV--------DL 486
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeELQRLSEELadlnaaiaGI 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 487 LAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEM---ADL 563
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrggRAV 512
|
170 180
....*....|....*....|
gi 46852174 564 QQEHQREIEGLLENIRQLSR 583
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQLGS 532
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
427-547 |
2.71e-05 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 44.60 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 427 DEERKALETKLDMEEEERNKARAELeKREKDLLKAQQEHQSLLEklsALEKKVIVggvdLLAKAEEQEKLLEESNMELEE 506
Cdd:pfam12718 34 EQEIKSLTHKNQQLEEEVEKLEEQL-KEAKEKAEESEKLKTNNE---NLTRKIQL----LEEELEESDKRLKETTEKLRE 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 46852174 507 RRKRAEQLRRELEEKEQERLDIEEKYtslqEEAQGKTKKLK 547
Cdd:pfam12718 106 TDVKAEHLERKVQALEQERDEWEKKY----EELEEKYKEAK 142
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
429-581 |
2.76e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 429 ERKaLETKLDMEEEERNKAR-----AELEKReKDLLKAQ----QEHQSLLEKLSALEKKVIVGGVD-LLAKAEEQEKLLE 498
Cdd:TIGR02168 172 ERR-KETERKLERTRENLDRledilNELERQ-LKSLERQaekaERYKELKAELRELELALLVLRLEeLREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 499 ESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENI 578
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
...
gi 46852174 579 RQL 581
Cdd:TIGR02168 330 SKL 332
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
489-568 |
2.87e-05 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 46.45 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 489 KAEEQEKLLEESNMELEERRKRAEQLrrELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVW----TMLMAAK--SEMAD 562
Cdd:pfam15991 26 KQEQEAKMEEERLRREREEREKEDRM--TLEETKEQILKLEKKLADLKEEKHQLFLQLKKVLhedeTRKRQLKeqSELFA 103
|
....*.
gi 46852174 563 LQQEHQ 568
Cdd:pfam15991 104 LQQAAA 109
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
416-579 |
2.88e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.44 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 416 PDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLL------------EKLSALEKKVIVGG 483
Cdd:pfam09731 228 LDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSnddlnsliahahREIDQLSKKLAELK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 484 VD--------LLAKAEEQEKLLEESNMELEE-RRKRAEQLRRELEEKEQE-RLDIEEKY-TSLQEEAQGKTKKLKKVwtm 552
Cdd:pfam09731 308 KReekhieraLEKQKEELDKLAEELSARLEEvRAADEAQLRLEFEREREEiRESYEEKLrTELERQAEAHEEHLKDV--- 384
|
170 180
....*....|....*....|....*..
gi 46852174 553 lmaAKSEMADLQQEHQREIEGLLENIR 579
Cdd:pfam09731 385 ---LVEQEIELQREFLQDIKEKVEEER 408
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
432-547 |
3.18e-05 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 44.21 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 432 ALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEESNMELEERRKRA 511
Cdd:pfam10473 28 NLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDL----VTLRSEKENLTKELQKKQERVSELESLN 103
|
90 100 110
....*....|....*....|....*....|....*.
gi 46852174 512 EQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLK 547
Cdd:pfam10473 104 SSLENLLEEKEQEKVQMKEESKTAVEMLQTQLKELN 139
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
428-593 |
3.43e-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: 47.37 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 428 EERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQ-----SLLEKLSALEKKVivggvdllakaEEQEKLLEESNM 502
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIenrldELSQELSDASRKI-----------GEIEKEIEQLEQ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 503 ELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKsemADLQQEHQREIEGLLENIRQLS 582
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKLEEEV 807
|
170
....*....|.
gi 46852174 583 RELRLQMLIID 593
Cdd:TIGR02169 808 SRIEARLREIE 818
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
428-588 |
3.81e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 428 EERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKvIVGGVDLLAKAEEQ----EKLLEESNME 503
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-LEALLNERASLEEAlallRSELEELSEE 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 504 LEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMaaksemaDLQQEHQREIEGLLENIRQLSR 583
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL-------EEAEALENKIEDDEEEARRRLK 975
|
....*
gi 46852174 584 ELRLQ 588
Cdd:TIGR02168 976 RLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
425-595 |
4.25e-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: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 425 KIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEESNMEL 504
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI----KSIEKEIENLNGKKEELEEEL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 505 EERRKRAEQLRRELEEKEQERLDIEEKYTSLQE-------EAQGKTKKLKKVWTMLMAAKSEMADLQQEHQRE------- 570
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERkieeleaQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeee 950
|
170 180 190
....*....|....*....|....*....|.
gi 46852174 571 --IEGLLENIRQLSRELR----LQMLIIDNF 595
Cdd:TIGR02169 951 lsLEDVQAELQRVEEEIRalepVNMLAIQEY 981
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
421-584 |
4.74e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 421 EMQAK---IDEERKALETKLDMEEEERNK---------------ARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivg 482
Cdd:COG3096 445 AFRAKeqqATEEVLELEQKLSVADAARRQfekayelvckiagevERSQAWQTARELLRRYRSQQALAQRLQQLRAQL--- 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 483 gVDLLAKAEEQ---EKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQE----------EAQGKTKKLKKV 549
Cdd:COG3096 522 -AELEQRLRQQqnaERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrselrqqleQLRARIKELAAR 600
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46852174 550 WTMLMAAKSEMADLQ----------QEHQREIEGLLENIRQLSRE 584
Cdd:COG3096 601 APAWLAAQDALERLReqsgealadsQEVTAAMQQLLEREREATVE 645
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
424-586 |
5.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 424 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAK---AEEQEKLLEES 500
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaAALGDAVEREL 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 501 NMELEERRKRAEQLRRELEEK--------------EQERLDI--------EEKYTSLQE----EAQGKTKKLKKVWTmlm 554
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEleramrafnrewpaETADLDAdleslpeyLALLDRLEEdglpEYEERFKELLNENS--- 844
|
170 180 190
....*....|....*....|....*....|..
gi 46852174 555 aaKSEMADLQQEHQREIEGLLENIRQLSRELR 586
Cdd:COG4913 845 --IEFVADLLSKLRRAIREIKERIDPLNDSLK 874
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
438-588 |
7.39e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 438 DMEEEERNKARAELEKREKDLL----KAQQEHQSLLEKLSALEKkvivggVDLLAKAEEQEKLLEESNMELEERRKRAEQ 513
Cdd:COG4913 233 HFDDLERAHEALEDAREQIELLepirELAERYAAARERLAELEY------LRAALRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46852174 514 LRRELEEKEQERLDIEEKYTSLQEEAQG-KTKKLKkvwtmlmAAKSEMADLQQEhQREIEGLLENIRQLSRELRLQ 588
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGnGGDRLE-------QLEREIERLERE-LEERERRRARLEALLAALGLP 374
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
418-574 |
8.28e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 418 KMIEMQAKIDEERKALETKLDMEEEERN----KARAELEKREKDLLKAQQEHQSllEKLSALEKKvivGGVDLLAKAEEQ 493
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKadaaKKKAEEAKKAAEAAKAEAEAAA--DEAEAAEEK---AEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 494 EKlLEESNMELEERRKrAEQLRRELEE--KEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAA----KSEMADLQQEH 567
Cdd:PTZ00121 1378 KK-ADAAKKKAEEKKK-ADEAKKKAEEdkKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAeeakKADEAKKKAEE 1455
|
....*..
gi 46852174 568 QREIEGL 574
Cdd:PTZ00121 1456 AKKAEEA 1462
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
418-556 |
1.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 418 KMIEMQAKIDEERKALEtKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVggvDLLAKAEEQEKll 497
Cdd:COG4717 133 ELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---DLAEELEELQQ-- 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 46852174 498 eesnmELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEaqgktKKLKKVWTMLMAA 556
Cdd:COG4717 207 -----RLAELEEELEEAQEELEELEEELEQLENELEAAALE-----ERLKEARLLLLIA 255
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
424-678 |
1.02e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 424 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKkvivggvdllakaeEQEKLLEESNME 503
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN--------------ITVRLQDLTEKL 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 504 LEERRKRAEQLRRELEEKeQERLDIEEKYTSLQEEAQGKTKKLkkvwtmlMAAKSEMADLQQEHQREIEgllenirQLSR 583
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKL-QPEQDLQDVRLHLQQCSQELALKL-------TALHALQLTLTQERVREHA-------LSIR 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 584 ELRLQMLIIDNFIPRDYQEMIENYVHWNEDIGEWQLKcvaytgnnMRKQTPVPDKKEKDPFEVDLSHVY----LAYTEES 659
Cdd:TIGR00618 669 VLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL--------LRELETHIEEYDREFNEIENASSSlgsdLAAREDA 740
|
250
....*....|....*....
gi 46852174 660 LRQSLMKLERPRTSKGKAR 678
Cdd:TIGR00618 741 LNQSLKELMHQARTVLKAR 759
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
427-585 |
1.13e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 427 DEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALekkvivggvdLLAKAEEQEKLLE-------- 498
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL----------LAQRAAHEARIREleediktl 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 499 -----ESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQ--------- 564
Cdd:pfam07888 142 tqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtittltqk 221
|
170 180
....*....|....*....|....*
gi 46852174 565 ----QEHQREIEGLLENIRQLSREL 585
Cdd:pfam07888 222 lttaHRKEAENEALLEELRSLQERL 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
430-586 |
1.23e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 430 RKALETKLDMEEEERNKARAE-LEKREKDLLKAQQEHQSLLEKLSALEKKVIVG---GVDLLAKAEEQEKLLEESNMELE 505
Cdd:PRK04863 496 DVARELLRRLREQRHLAEQLQqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNlddEDELEQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 506 ERRKRAEQLRRELEEKEQERldieEKYTSLQEE---AQGKTKKLKKVW-------TMLMAAKSEMADLQQEHQREIEGLL 575
Cdd:PRK04863 576 EARERRMALRQQLEQLQARI----QRLAARAPAwlaAQDALARLREQSgeefedsQDVTEYMQQLLERERELTVERDELA 651
|
170
....*....|.
gi 46852174 576 ENIRQLSRELR 586
Cdd:PRK04863 652 ARKQALDEEIE 662
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
426-588 |
1.23e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 426 IDEERKALETKLDmeeeernKARAELE--KREKDLLKAQQEHQSLLEKLSALEKKVI---VGGVDLLAKAEEQEKLLEES 500
Cdd:COG3206 180 LEEQLPELRKELE-------EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAearAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 501 NMELEERRK--RAEQLRRELEEKEQERLDIEEKYTSLQEEAQgktkklkkvwtmlmAAKSEMADLQQEHQREIEGLLENI 578
Cdd:COG3206 253 PDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVI--------------ALRAQIAALRAQLQQEAQRILASL 318
|
170
....*....|
gi 46852174 579 RQLSRELRLQ 588
Cdd:COG3206 319 EAELEALQAR 328
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
417-592 |
1.32e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEMQAKIDEERKALETKLDMEEEERNKAR-AELEKREKdlLKAQQEHQSL-----LEKLSALEKKVIVGGVDLLAKA 490
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEAEKARqAEMDRQAA--IYAEQERMAMerereLERIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 491 EEQEKLLEESNMELEERRKRaEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKvwtMLMAAKSEMADLQQEHQRE 570
Cdd:pfam17380 372 MEISRMRELERLQMERQQKN-ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE---QEEARQREVRRLEEERARE 447
|
170 180
....*....|....*....|..
gi 46852174 571 ieglLENIRQLSRELRLQMLII 592
Cdd:pfam17380 448 ----MERVRLEEQERQQQVERL 465
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
430-584 |
1.41e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 430 RKALETKLDMEEEERN------KARAELEKREKdLLKAQQEhqsLLEKLSALEKKVivggVDLLAKAEEQEKLLEESNME 503
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrileeaKKEAEAIKKEA-LLEAKEE---IHKLRNEFEKEL----RERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 504 LEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWtmlmaakSEMADLQQEHQREIegLLENIRQLSR 583
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-------ERISGLTAEEAKEI--LLEKVEEEAR 168
|
.
gi 46852174 584 E 584
Cdd:PRK12704 169 H 169
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
464-594 |
1.50e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 464 EHQSLLEKLSALEKKvivggvdlLAKAEEQEKLLEEsnmELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKT 543
Cdd:COG1579 4 EDLRALLDLQELDSE--------LDRLEHRLKELPA---ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 46852174 544 KKLKKVWTMLMAAKS--EMADLqqehQREIEGLLENIRQLSRELRLQMLIIDN 594
Cdd:COG1579 73 ARIKKYEEQLGNVRNnkEYEAL----QKEIESLKRRISDLEDEILELMERIEE 121
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
421-538 |
1.54e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 421 EMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEES 500
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 46852174 501 nmELEERRKRAEQLRRELE----------EKEQERLD-IEEKYTSLQEE 538
Cdd:COG1196 764 --ELERELERLEREIEALGpvnllaieeyEELEERYDfLSEQREDLEEA 810
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
441-544 |
1.82e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.97 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 441 EEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVggvdLLAKAEEQEKL----------LEESNMELEERRKR 510
Cdd:pfam13851 32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEE----LRKQLENYEKDkqslknlkarLKVLEKELKDLKWE 107
|
90 100 110
....*....|....*....|....*....|....
gi 46852174 511 AEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTK 544
Cdd:pfam13851 108 HEVLEQRFEKVERERDELYDKFEAAIQDVQQKTG 141
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
428-570 |
1.91e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 428 EERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKL--SALEKKVIVGGVDLLAKAEEQEKLLEESNMELE 505
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEELE 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852174 506 ERRKRAEQLRRELEEKEQERL--DIEEKYTSLQEEAQGKTKKlkkvWTMLMAAKSEMADLQQEHQRE 570
Cdd:COG4717 450 ELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEE----WAALKLALELLEEAREEYREE 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
428-547 |
2.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 428 EERKALETKLDMEEEERNKARAELEKREKDLLKAQQ-----EHQSLLEKLSALEKkvivggvdLLAKAEEQEKLLEESnm 502
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSR--------ELAGLRAELEELEKR-- 688
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 46852174 503 eLEERRKRAEQLRRELEEKEQERLDIE--EKYTSLQEEAQGKTKKLK 547
Cdd:PRK03918 689 -REEIKKTLEKLKEELEEREKAKKELEklEKALERVEELREKVKKYK 734
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
423-585 |
2.11e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 423 QAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKvivggvdllakaeeqeklLEESNM 502
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE------------------LEQARS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 503 ELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWT---MLMAAKSEMADLQQEHQREIEGLLENIR 579
Cdd:COG4372 74 ELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
....*.
gi 46852174 580 QLSREL 585
Cdd:COG4372 154 ELEEQL 159
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
449-582 |
2.17e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 449 AELEKRekdlLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQER--- 525
Cdd:COG3096 522 AELEQR----LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIkel 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46852174 526 -------LDIEEKYTSLQEE-------AQGKTKKLKKVWTMLMAAKSEMADLQQEHQReiegLLENIRQLS 582
Cdd:COG3096 598 aarapawLAAQDALERLREQsgealadSQEVTAAMQQLLEREREATVERDELAARKQA----LESQIERLS 664
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
436-590 |
2.68e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.25 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 436 KLDMEEEERNKARAELEKR--EKDLLKAQQ-EHQSLLEKLSALEKKVivggvdllAKAEEQEKLLEESNMELEERrkrAE 512
Cdd:pfam05667 305 KLQFTNEAPAATSSPPTKVetEEELQQQREeELEELQEQLEDLESSI--------QELEKEIKKLESSIKQVEEE---LE 373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852174 513 QLRRELEEKEQErLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREiegLLENIRQLSRELRLQML 590
Cdd:pfam05667 374 ELKEQNEELEKQ-YKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVP---LIEEYRALKEAKSNKED 447
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
438-586 |
2.70e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 438 DMEEEERNKaraELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdllakaeeqeKLLEESNMELEerrkraeqlrRE 517
Cdd:COG2433 384 ELIEKELPE---EEPEAEREKEHEERELTEEEEEIRRLEEQV---------------ERLEAEVEELE----------AE 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46852174 518 LEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVwTMLmaaKSEMADLqqehQREIEGLLENIRQLSRELR 586
Cdd:COG2433 436 LEEKDERIERLERELSEARSEERREIRKDREI-SRL---DREIERL----ERELEEERERIEELKRKLE 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
434-585 |
4.15e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 434 ETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGG----------VDLLAKAEEQEKLLEESNME 503
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcaeaeemrARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 504 LEERRKRAEQLRRELEEKEQERLDIEEKYTslQEEAQGKTKKLKKVWTMLMAAKSE-----MADLQQEHQREIEGLLENI 578
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLD--EEEAARQKLQLEKVTTEAKIKKLEedillLEDQNSKLSKERKLLEERI 161
|
....*..
gi 46852174 579 RQLSREL 585
Cdd:pfam01576 162 SEFTSNL 168
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
357-587 |
4.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 357 DALLRQFQKEIEELKKKLEEGEEISGsdisgseeDDDEEGEVGEDGEKRKKRRGKKKVSPDKMIEMQAKIDEERKALETK 436
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVK--------ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 437 LDmEEEERNKARAELEKREKDLLKaqqEHQSLLEKLSALEK-KVIVGGVDLLaKAEEQEKLLEESNMELEERRKRAEQLR 515
Cdd:PRK03918 330 IK-ELEEKEERLEELKKKLKELEK---RLEELEERHELYEEaKAKKEELERL-KKRLTGLTPEKLEKELEELEKAKEEIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 516 RELEEKEQERLDIEEKYTSLQ------EEAQGK--------------------TKKLKKVWTMLMAAKSEMADLQQEhQR 569
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKkaieelKKAKGKcpvcgrelteehrkelleeyTAELKRIEKELKEIEEKERKLRKE-LR 483
|
250
....*....|....*...
gi 46852174 570 EIEGLLENIRQLSRELRL 587
Cdd:PRK03918 484 ELEKVLKKESELIKLKEL 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
423-523 |
4.27e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 423 QAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKvivggvdlLAKAEEQEKLLEESNM 502
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE--------AALLEAALAELLEELA 487
|
90 100
....*....|....*....|.
gi 46852174 503 ELEERRKRAEQLRRELEEKEQ 523
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLE 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
331-592 |
4.98e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 331 ETISTLRYANRAKNIKNKARINEdpKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGekrkkrrg 410
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINE--ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLE-------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 411 kkkvspDKMIEMQAKIDEERKALEtkldmEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKkvivggvdLLAKA 490
Cdd:PRK03918 259 ------EKIRELEERIEELKKEIE-----ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK--------RLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 491 EEQEKLLEESNMELEERRKRAEQLRRELEEKEqERLDIEEKYTSLQEEAQGKTKKLKKVwtmlmaaKSEMADLQQEhqrE 570
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERL-------KKRLTGLTPE---K 388
|
250 260
....*....|....*....|..
gi 46852174 571 IEGLLENIRQLSRELRLQMLII 592
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKI 410
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
463-579 |
5.63e-04 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 42.67 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 463 QEHQSLLEKLSALEKKVIvggvDLLAKAEEQEKLLEESNMELEER---RKRAEQLRRELEEKEQERLDIEEKYTSLQEEA 539
Cdd:pfam07767 195 EDHQELLQKAVEAEKKRL----KEEEKLERVLEKIAESAATAEAReekRKTKAQRNKEKRRKEEEREAKEEKALKKKLAQ 270
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 46852174 540 QGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIR 579
Cdd:pfam07767 271 LERLKEIAKEIAEKEKEREEKAEARKREKRKKKKEEKKLR 310
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
423-538 |
5.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 423 QAKIDEERKALETKLDMEEEERNKARA--------ELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQE 494
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 46852174 495 KLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEE 538
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
425-578 |
5.99e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 425 KIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdllAKAEEQEKLLEESNMEL 504
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV--------KDLTKKISSLKEKIEKL 529
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852174 505 EERRKRAEQLRRELeEKEQERLDIEEKYTSLQEEAQGKTK---KLKKVWTMLMAAKSEMADLQQEHQREIEGLLENI 578
Cdd:TIGR04523 530 ESEKKEKESKISDL-EDELNKDDFELKKENLEKEIDEKNKeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
424-541 |
6.59e-04 |
|
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: 43.13 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 424 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKV-----IVGGVDLLAKAEEQEKLLE 498
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKgedeeIPEEELSLEDVQAELQRVE 964
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 46852174 499 ESNMELEERRKRAEQlrrELEEKEQERLDIEEKYTSLQEEAQG 541
Cdd:TIGR02169 965 EEIRALEPVNMLAIQ---EYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
339-584 |
6.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 339 ANRAKNIKNKARINEDPKDAllrQFQKEIEELKKKLEE----GEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKV 414
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKA---EEKKKADEAKKKAEEdkkkADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 415 SPDkmiEMQAKIDEERKALETKLDMEEE---ERNKARAELEKREKDLLKAQQEHQSLLEKL--SALEKKvivgGVDLLAK 489
Cdd:PTZ00121 1445 KAD---EAKKKAEEAKKAEEAKKKAEEAkkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAkkAAEAKK----KADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 490 AEEQEKLLEesnMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMA-DLQQEHQ 568
Cdd:PTZ00121 1518 AEEAKKADE---AKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARI 1594
|
250
....*....|....*.
gi 46852174 569 REIEGLLENIRQLSRE 584
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAE 1610
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
341-538 |
7.32e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 341 RAKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDKMI 420
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 421 EMQAKIDEERKaLETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVD---LLAKAEEQEKLL 497
Cdd:pfam02463 884 LKDELESKEEK-EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEkekEENNKEEEEERN 962
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46852174 498 EESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEE 538
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
417-535 |
7.51e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdllAKAEEQEKL 496
Cdd:smart00787 179 DRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKI--------EDLTNKKSE 250
|
90 100 110
....*....|....*....|....*....|....*....
gi 46852174 497 LEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSL 535
Cdd:smart00787 251 LNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLTGW 289
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
348-548 |
8.18e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 348 KARINEDPKDALLRQFQKEIEELKKKLEEG--------EEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDKM 419
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEArqrevrrlEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 420 IEMQAKIDEERKALetkLDMEEEERNKARAELEKREKDLLKAQQEHQSlleklsalekkvivggvdllAKAEEQEKLLEE 499
Cdd:pfam17380 483 KRDRKRAEEQRRKI---LEKELEERKQAMIEEERKRKLLEKEMEERQK--------------------AIYEEERRREAE 539
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46852174 500 ----SNMELEERRKRAEQLRRELEEKeqERLDIEEKYTSLQEEAQGKTKKLKK 548
Cdd:pfam17380 540 eerrKQQEMEERRRIQEQMRKATEER--SRLEAMEREREMMRQIVESEKARAE 590
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
421-584 |
1.26e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.41 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 421 EMQAKIDEERKALETKldMEEEERNKARAELEKREKDLLKA---------------QQEHQSLLEKLSALEKKVIvggvd 485
Cdd:cd16269 94 KLMEQLEEKKEEFCKQ--NEEASSKRCQALLQELSAPLEEKisqgsysvpggyqlyLEDREKLVEKYRQVPRKGV----- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 486 llaKAEE------------------QEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLK 547
Cdd:cd16269 167 ---KAEEvlqeflqskeaeaeailqADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLK 243
|
170 180 190
....*....|....*....|....*....|....*..
gi 46852174 548 KvwTMlmaaKSEMADLQQEHQREIEGLLENIRQLSRE 584
Cdd:cd16269 244 E--KM----EEERENLLKEQERALESKLKEQEALLEE 274
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
429-581 |
1.30e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 429 ERKALETKLDMEEEERNKARAELEKREKDLlkaqQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEESNMELEERR 508
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVL----EEHEERREELETLEAEI----EDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 509 KRAEQLRRELEE--KEQERLDIEEKYTSLQEEAqgktkklkkvwtmLMAAKSEMADL-------QQEHQREIEGLLENIR 579
Cdd:PRK02224 286 ERLEELEEERDDllAEAGLDDADAEAVEARREE-------------LEDRDEELRDRleecrvaAQAHNEEAESLREDAD 352
|
..
gi 46852174 580 QL 581
Cdd:PRK02224 353 DL 354
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
421-586 |
1.37e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 421 EMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLL--- 497
Cdd:pfam12128 618 EKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLdkk 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 498 -----EESNMELEERRKRAEQLRRELEEKEQERLD-IEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREI 571
Cdd:pfam12128 698 hqawlEEQKEQKREARTEKQAYWQVVEGALDAQLAlLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI 777
|
170
....*....|....*...
gi 46852174 572 EGL---LENIRQLSRELR 586
Cdd:pfam12128 778 RTLerkIERIAVRRQEVL 795
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
424-581 |
1.51e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 424 AKIDEERKALETKLDMEEEERNKARAE--LEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESN 501
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTIKalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 502 -----MELEERRKRAEQLRRELEEKEQERLDieeKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQehqrEIEGLLE 576
Cdd:cd22656 174 gaiarKEIKDLQKELEKLNEEYAAKLKAKID---ELKALIADDEAKLAAALRLIADLTAADTDLDNLLA----LIGPAIP 246
|
....*
gi 46852174 577 NIRQL 581
Cdd:cd22656 247 ALEKL 251
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
417-588 |
1.54e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEMQAKIDEERKALETKLD--MEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEE-- 492
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDemMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQmd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 493 --QEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKK-LKKVWTMLMAAKSEMADLQQEHQR 569
Cdd:pfam13868 105 eiVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEyLKEKAEREEEREAEREEIEEEKER 184
|
170
....*....|....*....
gi 46852174 570 EIEGLLENIRQLSRELRLQ 588
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAER 203
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
342-585 |
1.62e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 342 AKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDKMIE 421
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 422 MQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIvggvDLLAKAEEQEKLLEESN 501
Cdd:pfam02463 782 KTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL----ELKEEQKLEKLAEEELE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 502 MELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQL 581
Cdd:pfam02463 858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP 937
|
....
gi 46852174 582 SREL 585
Cdd:pfam02463 938 EELL 941
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
416-502 |
1.62e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.59 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 416 PDKMIEMQAK------------IDEERKALETKLDMEEEERN---KARAELEKREKDLLKAQQEHQSLLEKLSALEKKvi 480
Cdd:PRK05431 11 PEAVKEALAKrgfpldvdelleLDEERRELQTELEELQAERNalsKEIGQAKRKGEDAEALIAEVKELKEEIKALEAE-- 88
|
90 100
....*....|....*....|....
gi 46852174 481 vggvdlLAKAEEQ--EKLLEESNM 502
Cdd:PRK05431 89 ------LDELEAEleELLLRIPNL 106
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
430-581 |
1.84e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 430 RKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSL---LEKLSALEKKVIVGGVDLLAKAeeQEKLLEESnMELEE 506
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALeeeLRQLKQLEDELEDCDPTELDRA--KEKLKKLL-QEIMI 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46852174 507 RRKRAEQLRRELEEKEQerlDIEEKytslqeeaqgkTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQL 581
Cdd:smart00787 223 KVKKLEELEEELQELES---KIEDL-----------TNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLL 283
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
417-524 |
2.05e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKL 496
Cdd:COG3883 132 ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
90 100
....*....|....*....|....*...
gi 46852174 497 LEESNMELEERRKRAEQLRRELEEKEQE 524
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
432-571 |
2.08e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 432 ALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSL-------LEKLSALEKKVIVGGVDLLAKAEEQEKLL-EESNME 503
Cdd:COG3096 988 KLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLkssrdakQQTLQELEQELEELGVQADAEAEERARIRrDELHEE 1067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 504 LEERRKRAEQL-------RRELEEKEQERLDIEEKYTSLQEEAQGKtkklKKVWTMLMA-----------AKSEMADLQQ 565
Cdd:COG3096 1068 LSQNRSRRSQLekqltrcEAEMDSLQKRLRKAERDYKQEREQVVQA----KAGWCAVLRlardndverrlHRRELAYLSA 1143
|
....*.
gi 46852174 566 EHQREI 571
Cdd:COG3096 1144 DELRSM 1149
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
418-545 |
2.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 418 KMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKkvivggvdllakaeEQEKLL 497
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA--------------ERQKLL 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 46852174 498 EESNmeleerrKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKK 545
Cdd:COG4942 202 ARLE-------KELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3498 |
pfam12004 |
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ... |
440-538 |
3.67e-03 |
|
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.
Pssm-ID: 463427 [Multi-domain] Cd Length: 511 Bit Score: 40.51 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 440 EEEERNKARAELEKREKdllkAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRaeqLRRELE 519
Cdd:pfam12004 373 EESSGPESREELKQAEK----YEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEER---LRRQQE 445
|
90
....*....|....*....
gi 46852174 520 EKEQERLDIEEKYTSLQEE 538
Cdd:pfam12004 446 EKDSQMKSIISRLMAVEEE 464
|
|
| COG5493 |
COG5493 |
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ... |
422-524 |
4.01e-03 |
|
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];
Pssm-ID: 444244 [Multi-domain] Cd Length: 239 Bit Score: 39.58 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 422 MQAKIDEERKALETKLDMEEEERnKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdllAKAEEQEKLLEESN 501
Cdd:COG5493 1 MSLLKEELKRELLELLREDPEFR-YAVLGLLATKDGLEELLERLEKLEEQMRKWEEQL--------RKLEEEIKKLREQV 71
|
90 100
....*....|....*....|...
gi 46852174 502 MELEERRKRAEQLRRELEEKEQE 524
Cdd:COG5493 72 RKLEEDVKRLEEQERKLEEAMAE 94
|
|
| CENP-H |
pfam05837 |
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H ... |
456-553 |
4.03e-03 |
|
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H (CENP-H) sequences. Macromolecular centromere-kinetochore complex plays a critical role in sister chromatid separation, but its complete protein composition as well as its precise dynamic function during mitosis has not yet been clearly determined. CENP-H contains a coiled-coil structure and a nuclear localization signal. CENP-H is specifically and constitutively localized in kinetochores throughout the cell cycle. CENP-H may play a role in kinetochore organization and function throughout the cell cycle. This the C-terminus of the region, which is conserved from fungi to humans.
Pssm-ID: 461756 [Multi-domain] Cd Length: 114 Bit Score: 37.56 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 456 KDLLKAQQEHQSLLEKLSALEKKVIVggvdllakaeeqeklLEESNMELeerrkrAEQLRRELEEKEQERLDIEEKytSL 535
Cdd:pfam05837 13 SAILKLSSELRELQEELTEVEKENLR---------------LKRKNREL------AAELLELAKEKESRREDPKLR--AQ 69
|
90
....*....|....*...
gi 46852174 536 QEEAQGKTKKLKKVWTML 553
Cdd:pfam05837 70 LEKLEAELKKSRRRWRVM 87
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
421-595 |
4.17e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 421 EMQAKIDEERKALETKlDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEES 500
Cdd:pfam15921 441 ECQGQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV----SDLTASLQEKERAIEAT 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 501 NMELEERRKRAEQLRRELEEKEQErldiEEKYTSLQEEAQG---KTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLEN 577
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQTECEAlklQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVE 591
|
170
....*....|....*...
gi 46852174 578 IRQLSRELRLQMLIIDNF 595
Cdd:pfam15921 592 KAQLEKEINDRRLELQEF 609
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
357-548 |
4.53e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 357 DALLRQFQKEIEELKKKLEEGE-EISGSDisgseedddeegevgedgekrkkrrgkkkvspDKMIEMQAKIDE---ERKA 432
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEdELAALE--------------------------------ARLEAAKTELEDlekEIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 433 LETKLDMEEEERNKARAELE--KREKDLLKAQQEHQSLLEKLSALEKKVIvggvDLLAKAEEQEKLLEESNMELEERRKR 510
Cdd:COG1579 64 LELEIEEVEARIKKYEEQLGnvRNNKEYEALQKEIESLKRRISDLEDEIL----ELMERIEELEEELAELEAELAELEAE 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 46852174 511 AEQLRRELEEKEQErldIEEKYTSLQEEAQGKTKKLKK 548
Cdd:COG1579 140 LEEKKAELDEELAE---LEAELEELEAEREELAAKIPP 174
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
431-540 |
4.57e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.10 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 431 KALETKldmEEEERNKARAELEKREKDLLKAQQEHQsLLEKLSALEKKvivggVDLLAKAEEQeklLEESNMELEERRKR 510
Cdd:pfam12072 54 ALLEAK---EEIHKLRAEAERELKERRNELQRQERR-LLQKEETLDRK-----DESLEKKEES---LEKKEKELEAQQQQ 121
|
90 100 110
....*....|....*....|....*....|.
gi 46852174 511 AEQLRRELEEKEQERLDIEEKYTSL-QEEAQ 540
Cdd:pfam12072 122 LEEKEEELEELIEEQRQELERISGLtSEEAK 152
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
351-529 |
4.65e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.24 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 351 INEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPD------KMIEMQA 424
Cdd:pfam02029 140 YQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEvksqngEEEVTKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 425 KIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSL-LEKLSALEKKVIVGGVDLLAKAEEQEKLLEESnme 503
Cdd:pfam02029 220 KVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEeFEKLRQKQQEAELELEELKKKREERRKLLEEE--- 296
|
170 180
....*....|....*....|....*...
gi 46852174 504 lEERRKRAEQLR--RELEEKEQERLDIE 529
Cdd:pfam02029 297 -EQRRKQEEAERklREEEEKRRMKEEIE 323
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
488-583 |
4.91e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 488 AKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEH 567
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90
....*....|....*.
gi 46852174 568 QREIEGLLENIRQLSR 583
Cdd:COG4942 100 EAQKEELAELLRALYR 115
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
418-566 |
5.10e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 418 KMIEMQAKIDEERKALETKLDME------------EEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvd 485
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALpellqspviqqlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 486 llakAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDI---EEKYTSLQEEAQGKTKKLkkvwtMLMAAKSEMAD 562
Cdd:COG3206 308 ----QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELY-----ESLLQRLEEAR 378
|
....
gi 46852174 563 LQQE 566
Cdd:COG3206 379 LAEA 382
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
417-572 |
5.26e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDL---LAKAEEQ 493
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkckLDKSEEN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 494 EKLLEESNMELEER-----------RKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMAD 562
Cdd:pfam05483 575 ARSIEYEVLKKEKQmkilenkcnnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE 654
|
170
....*....|
gi 46852174 563 LQQEHQREIE 572
Cdd:pfam05483 655 IIDNYQKEIE 664
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
486-591 |
5.34e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 38.71 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 486 LLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEqERLD-----IEEKYTSLQEeaqgKTKKLKKVWTMLMAAKSEM 560
Cdd:pfam12072 55 LLEAKEEIHKLRAEAERELKERRNELQRQERRLLQKE-ETLDrkdesLEKKEESLEK----KEKELEAQQQQLEEKEEEL 129
|
90 100 110
....*....|....*....|....*....|.
gi 46852174 561 ADLQQEHQREieglLENIRQLSRELRLQMLI 591
Cdd:pfam12072 130 EELIEEQRQE----LERISGLTSEEAKEILL 156
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
427-545 |
5.42e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 39.63 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 427 DEERKALETKLDMEEEERNKA-----RAELEKREKDLLKAQQEHQsllEKLSALEKKVIVGGVDLLAKAEEQEKL----L 497
Cdd:pfam15558 35 EELRRRDQKRQETLERERRLLlqqsqEQWQAEKEQRKARLGREER---RRADRREKQVIEKESRWREQAEDQENQrqekL 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 46852174 498 EESNMELEERRKRAEQLRRELEE-----KEQERLDIEEKytsLQEEAQGKTKK 545
Cdd:pfam15558 112 ERARQEAEQRKQCQEQRLKEKEEelqalREQNSLQLQER---LEEACHKRQLK 161
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
422-548 |
5.60e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.48 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 422 MQAKIDEER---KALETKLDME-EEERNKARAELEKREKDLLKAQQEhqslleklsalekkvivggvDLLAKAEEQEKLL 497
Cdd:cd16269 176 LQSKEAEAEailQADQALTEKEkEIEAERAKAEAAEQERKLLEEQQR--------------------ELEQKLEDQERSY 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 46852174 498 EESNMEL-----EERRKRAEQLRRELEEK--EQERLdieekytsLQEEAQGKTKKLKK 548
Cdd:cd16269 236 EEHLRQLkekmeEERENLLKEQERALESKlkEQEAL--------LEEGFKEQAELLQE 285
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
424-585 |
6.65e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 424 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvDLLAKAEEQEKLLEESNME 503
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-----TLLAAIADAEDEIERLREK 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 504 LEERRKRAEQLRRELEEKEQERLDIEEKY-----TSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEhQREIEGLLENI 578
Cdd:PRK02224 615 REALAELNDERRERLAEKRERKRELEAEFdeariEEAREDKERAEEYLEQVEEKLDELREERDDLQAE-IGAVENELEEL 693
|
....*..
gi 46852174 579 RQLSREL 585
Cdd:PRK02224 694 EELRERR 700
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
339-545 |
7.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 339 ANRAKNIKNKARINEDPKDALLRQ---FQKEIEELKKKLEegeeisgsdisgseedddeEGEVGEDGEKRKKRRGKKKVS 415
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKadaAKKKAEEKKKADE-------------------AKKKAEEDKKKADELKKAAAA 1416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 416 PDKMIEMQAKIDEERKALETKLDMEEE---ERNKARAELEKREKDLLKAQQEHQSLLE-KLSALEKKvivGGVDLLAKAE 491
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAkkaDEAKKKAEEAKKAEEAKKKAEEAKKADEaKKKAEEAK---KADEAKKKAE 1493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46852174 492 EQEKLLEESNmELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKK 545
Cdd:PTZ00121 1494 EAKKKADEAK-KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
418-585 |
7.66e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 38.47 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 418 KMIEMQAKIDEE---RKALETKlDMEEEERnkaraeLEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLlAKAEEQE 494
Cdd:pfam00261 65 KLEEAEKAADESergRKVLENR-ALKDEEK------MEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDL-ERAEERA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 495 KLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYtslQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGL 574
Cdd:pfam00261 137 ELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKY---EEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDEL 213
|
170
....*....|....
gi 46852174 575 L---ENIRQLSREL 585
Cdd:pfam00261 214 EaekEKYKAISEEL 227
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
423-548 |
8.35e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 423 QAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIvggvDLLAKAEEQEKLLEESNM 502
Cdd:PRK12705 51 EAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLE----EREKALSARELELEELEK 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 46852174 503 ELEERRKRAEQLRRElEEKEQ--ERLDIEekytsLQEEAQGKTKKLKK 548
Cdd:PRK12705 127 QLDNELYRVAGLTPE-QARKLllKLLDAE-----LEEEKAQRVKKIEE 168
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
417-546 |
8.98e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 39.29 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 417 DKMIEMQAKIDEERKALETkldMEEEER--NKARAELEKREKDLLKAQQEHQSLLEKLSALEKKvIVGGVDLLAKAEEQE 494
Cdd:pfam05622 304 ERLTELQQLLEDANRRKNE---LETQNRlaNQRILELQQQVEELQKALQEQGSKAEDSSLLKQK-LEEHLEKLHEAQSEL 379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 46852174 495 KLLEESNMELEER-----RKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKL 546
Cdd:pfam05622 380 QKKKEQIEELEPKqdsnlAQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTL 436
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
426-517 |
9.55e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 37.46 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852174 426 IDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIvggVDLLAKAEEQ-EKLLEESNMEL 504
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIA---EEAKAEAEAEaERIIAQAEAEI 105
|
90
....*....|....
gi 46852174 505 EERRKRA-EQLRRE 517
Cdd:COG0711 106 EQERAKAlAELRAE 119
|
|
| |
