|
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 578810113 13 DNVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDS-SNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEG 91
Cdd:cd01371 1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 92 YNGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEV 171
Cdd:cd01371 81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 172 KERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDL 251
Cdd:cd01371 161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 252 AGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDE 331
Cdd:cd01371 241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
|
330
....*....|....
gi 578810113 332 TISTLRYANRAKNI 345
Cdd:cd01371 321 TLSTLRYANRAKNI 334
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
20-345 |
2.22e-178 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 511.73 E-value: 2.22e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 20 RCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAY 99
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 100 GQTGTGKTFTMEGvraIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQT--QRLEVKERPDV 177
Cdd:pfam00225 81 GQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKnkRKLRIREDPKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 178 GVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAGSERQ 257
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSERA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 258 AKTG-ATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTL 336
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317
|
....*....
gi 578810113 337 RYANRAKNI 345
Cdd:pfam00225 318 RFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
14-352 |
1.29e-170 |
|
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: 1.29e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYN 93
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 94 GTIFAYGQTGTGKTFTMEGvraIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQtQRLEVKE 173
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSS-KKLEIRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 174 RPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGiDGNMHVRMGKLHLVDLAG 253
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN-SSSGSGKASKLNLVDLAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 254 SERQAKTGATGQRLKEATKINLSLSTLGNVISALVD-GKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDET 332
Cdd:smart00129 236 SERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEET 315
|
330 340
....*....|....*....|
gi 578810113 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 |
5.49e-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: 470.20 E-value: 5.49e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 14 NVKVVVRCRPLNEREKSMCyKQAVSVDEMRgTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYN 93
Cdd:cd00106 1 NVRVAVRVRPLNGREARSA-KSVISVDGGK-SVVLDPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 94 GTIFAYGQTGTGKTFTMEGVRaiPELRGIIPNSFAHIFGHI-AKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVK 172
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPD--PEQRGIIPRALEDIFERIdKRKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 173 ERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGnMHVRMGKLHLVDLA 252
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSG-ESVTSSKLNLVDLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 253 GSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDET 332
Cdd:cd00106 236 GSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEET 315
|
330
....*....|.
gi 578810113 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 |
9.40e-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: 398.24 E-value: 9.40e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 15 VKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVhktdssnEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNG 94
Cdd:cd01372 3 VRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTV-------GTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 95 TIFAYGQTGTGKTFTMEGVRAIPEL---RGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGK--DQTQRL 169
Cdd:cd01372 76 TVLAYGQTGSGKTYTMGTAYTAEEDeeqVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPetDKKPTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 170 EVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIE-------CSEKGIDGNMHVR 242
Cdd:cd01372 156 SIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEqtkkngpIAPMSADDKNSTF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 243 MGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDG--KSTHVPYRNSKLTRLLQDSLGGNSKTMMCA 320
Cdd:cd01372 236 TSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDEskKGAHVPYRDSKLTRLLQDSLGGNSHTLMIA 315
|
330 340
....*....|....*....|....*.
gi 578810113 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 |
1.52e-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: 395.54 E-value: 1.52e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITV-HKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGY 92
Cdd:cd01364 3 NIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 93 NGTIFAYGQTGTGKTFTMEGVRAI--------PELRGIIPNSFAHIFGHIAkaEGDTRFLVRVSYLEIYNEEVRDLLG-- 162
Cdd:cd01364 83 NCTIFAYGQTGTGKTYTMEGDRSPneeytwelDPLAGIIPRTLHQLFEKLE--DNGTEYSVKVSYLEIYNEELFDLLSps 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 163 KDQTQRLEVKERPDV--GVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMH 240
Cdd:cd01364 161 SDVSERLRMFDDPRNkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 241 VRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDgKSTHVPYRNSKLTRLLQDSLGGNSKTMMCA 320
Cdd:cd01364 241 VKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-RAPHVPYRESKLTRLLQDSLGGRTKTSIIA 319
|
330 340 350
....*....|....*....|....*....|....
gi 578810113 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 |
1.31e-131 |
|
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: 1.31e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 13 DNVKVVVRCRPLNEREKSMCYKQAVSVDEMRgTITVhktdSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGY 92
Cdd:cd01369 2 CNIKVVCRFRPLNELEVLQGSKSIVKFDPED-TVVI----ATSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 93 NGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTqRLEVK 172
Cdd:cd01369 77 NGTIFAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKT-NLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 173 ERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIEcSEKGIDGNmhVRMGKLHLVDLA 252
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVK-QENVETEK--KKSGKLYLVDLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 253 GSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDET 332
Cdd:cd01369 233 GSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESET 312
|
330
....*....|...
gi 578810113 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 |
1.83e-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: 1.83e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNeppKTFTFDTVFGPESKQLDVYNLTArPIIDSVLEGYN 93
Cdd:cd01366 3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIELTSIGAKQ---KEFSFDKVFDPEASQEDVFEEVS-PLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 94 GTIFAYGQTGTGKTFTMEGVraiPELRGIIPNSFAHIFgHIAK--AEGDTRFLVRVSYLEIYNEEVRDLL--GKDQTQRL 169
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGP---PESPGIIPRALQELF-NTIKelKEKGWSYTIKASMLEIYNETIRDLLapGNAPQKKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 170 EVKERPDVG-VYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIEcsekGID-GNMHVRMGKLH 247
Cdd:cd01366 155 EIRHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIS----GRNlQTGEISVGKLN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 248 LVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKStHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADY 327
Cdd:cd01366 231 LVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS-HIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAES 309
|
330 340
....*....|....*....|
gi 578810113 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 |
1.52e-129 |
|
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: 1.52e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 13 DNVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSN-----EPPKTFTFDTVF----GPESK---QLDVYNLT 80
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNnkatrEVPKSFSFDYSYwshdSEDPNyasQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 81 ARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGvraIPELRGIIPNSFAHIFGHIAKAEGD-TRFLVRVSYLEIYNEEVRD 159
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMG---TQEQPGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 160 LLGKD---QTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIecSEKGID 236
Cdd:cd01365 158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVL--TQKRHD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 237 ---GNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVD-------GKSTHVPYRNSKLTRLL 306
Cdd:cd01365 236 aetNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVLTWLL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578810113 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 |
6.16e-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: 6.16e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEmrGTITVHKTDSSNeppktFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYN 93
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEIDN--DTIYLVEPPSTS-----FTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 94 GTIFAYGQTGTGKTFTMEGVRAIPelrGIIPNSFAHIFGHIAKAEgDTRFLVRVSYLEIYNEEVRDLLGKdQTQRLEVKE 173
Cdd:cd01374 74 GTIFAYGQTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQDTP-DREFLLRVSYLEIYNEKINDLLSP-TSQNLKIRD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 174 RPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAG 253
Cdd:cd01374 149 DVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTVRVSTLNLIDLAG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 254 SERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGK-STHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDET 332
Cdd:cd01374 229 SERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKvGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEET 308
|
330
....*....|...
gi 578810113 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 |
3.53e-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: 361.06 E-value: 3.53e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 13 DNVKVVVRCRPLNEREKSMCYKQAVSVdEMRGTITVHktdssNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGY 92
Cdd:cd01373 1 DAVKVFVRIRPPAEREGDGEYGQCLKK-LSSDTLVLH-----SKPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 93 NGTIFAYGQTGTGKTFTM-----EGVRAIPELRGIIPNSFAHIFGHI----AKAEGDTRFLVRVSYLEIYNEEVRDLLgk 163
Cdd:cd01373 75 NGTIFAYGQTGSGKTYTMwgpseSDNESPHGLRGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 164 DQTQR-LEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGiDGNMHVR 242
Cdd:cd01373 153 DPASRnLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKK-ACFVNIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 243 MGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVD---GKSTHVPYRNSKLTRLLQDSLGGNSKTMMC 319
Cdd:cd01373 232 TSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAII 311
|
330 340 350
....*....|....*....|....*....|....*
gi 578810113 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 |
7.86e-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: 7.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 14 NVKVVVRCRPLNEREKSMCYKQAVSV-----------DEMRGTITVHKTDSSNEP----PKTFTFDTVFGPESKQLDVYN 78
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfdpkDEEDGFFHGGSNNRDRRKrrnkELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 79 LTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAIPelrGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVR 158
Cdd:cd01370 81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 159 DLLGKdQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGN 238
Cdd:cd01370 158 DLLNP-SSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 239 MHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDG--KSTHVPYRNSKLTRLLQDSLGGNSKT 316
Cdd:cd01370 237 QQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPgkKNKHIPYRDSKLTRLLKDSLGGNCRT 316
|
330 340
....*....|....*....|....*....
gi 578810113 317 MMCANIGPADYNYDETISTLRYANRAKNI 345
Cdd:cd01370 317 VMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
14-533 |
3.24e-92 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 298.58 E-value: 3.24e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSS-----NEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSV 88
Cdd:COG5059 6 NSPLKSRLSSRNEKSVSDIKSTIRIIPGELGERLINTSKKShvsleKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 89 LEGYNGTIFAYGQTGTGKTFTMEGvraIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDqTQR 168
Cdd:COG5059 86 LLGYNCTVFAYGQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPN-EES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 169 LEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIE--CSEKGIDGNmhvrmGKL 246
Cdd:COG5059 162 LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELAskNKVSGTSET-----SKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 247 HLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVD-GKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPA 325
Cdd:COG5059 237 SLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 326 DYNYDETISTLRYANRAKNIKNKARIN-----------------EDPKDALLRQF-------QKEIEELKKKLEEGEEIS 381
Cdd:COG5059 317 SNSFEETINTLKFASRAKSIKNKIQVNsssdssreieeikfdlsEDRSEIEILVFreqsqlsQSSLSGIFAYMQSLKKET 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 382 GSDISGSEEDDDEEGEVGEDGEKRKKRRGSSSSSSSDSTCSVIEKPLDKFLPNQAGKKKVSPDKMIEMQAKIDEERKALE 461
Cdd:COG5059 397 ETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPE 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578810113 462 TKLDMEEEERNKARAELEKREKDLLKAQ--QEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEE 533
Cdd:COG5059 477 ETSDRVESEKASKLRSSASTKLNLRSSRshSKFRDHLNGSNSSTKELSLNQVDLAGSERKVSQSVGELLRETQS 550
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
15-343 |
5.24e-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: 284.86 E-value: 5.24e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 15 VKVVVRCRPLNEREKSMCY----KQAVSV----DEMRGTITVHKTDSSneppktFTFDTVFGPESKQLdVYNLTARPIID 86
Cdd:cd01375 2 VQAFVRVRPTDDFAHEMIKygedGKSISIhlkkDLRRGVVNNQQEDWS------FKFDGVLHNASQEL-VYETVAKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 87 SVLEGYNGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKaEGDTRFLVRVSYLEIYNEEVRDLLGK--- 163
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEE-RPTKAYTVHVSYLEIYNEQLYDLLSTlpy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 164 --DQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIEcSEKGIDGNMHV 241
Cdd:cd01375 154 vgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLE-AHSRTLSSEKY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 242 RMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCAN 321
Cdd:cd01375 233 ITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVAN 312
|
330 340
....*....|....*....|..
gi 578810113 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 |
6.50e-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: 263.21 E-value: 6.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 14 NVKVVVRCRPLNEREKSMCYKQAVSV-DEMrgTITVHKTDSSNEPPKtFTFDTVFGPESKQLDVYNLTARPIIDSVLEGY 92
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGiDSC--SVELADPRNHGETLK-YQFDAFYGEESTQEDIYAREVQPIVPHLLEGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 93 NGTIFAYGQTGTGKTFTMEGvraIPELRGIIPNSFAHIFGHIAKAEGDTRFLvrVSYLEIYNEEVRDLL-GKDqtQRLEV 171
Cdd:cd01376 78 NATVFAYGSTGAGKTFTMLG---SPEQPGLMPLTVMDLLQMTRKEAWALSFT--MSYLEIYQEKILDLLePAS--KELVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 172 KERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIdgNMHVRMGKLHLVDL 251
Cdd:cd01376 151 REDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLA--PFRQRTGKLNLIDL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 252 AGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKStHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDE 331
Cdd:cd01376 229 AGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQD 307
|
330
....*....|..
gi 578810113 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 |
1.72e-80 |
|
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: 1.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 13 DNVKVVVRCRPLNEREK----SMCYK----QAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPI 84
Cdd:cd01368 1 DPVKVYLRVRPLSKDELesedEGCIEvinsTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 85 IDSVLEGYNGTIFAYGQTGTGKTFTMEGVraiPELRGIIPNSFAHIFGHIAKaegdtrFLVRVSYLEIYNEEVRDLL--- 161
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGS---PGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDLLeps 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 162 GKDQTQR---LEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGN 238
Cdd:cd01368 152 PSSPTKKrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 239 M-----HVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISAL----VDGKSTHVPYRNSKLTRLLQDS 309
Cdd:cd01368 232 VdqdkdQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrenqLQGTNKMVPFRDSKLTHLFQNY 311
|
330 340 350
....*....|....*....|....*....|....
gi 578810113 310 LGGNSKTMMCANIGPADYNYDETISTLRYANRAK 343
Cdd:cd01368 312 FDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
15-371 |
1.86e-80 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 279.90 E-value: 1.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 15 VKVVVRCRPLNEREKSMCYKQAVSVDEMrgtitvhktdSSNEppKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNG 94
Cdd:PLN03188 100 VKVIVRMKPLNKGEEGEMIVQKMSNDSL----------TING--QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 95 TIFAYGQTGTGKTFTMEG-VRAIPE------LRGIIPNSFAHIFGHIAK-----AEGDTRFLVRVSYLEIYNEEVRDLLg 162
Cdd:PLN03188 168 SVFAYGQTGSGKTYTMWGpANGLLEehlsgdQQGLTPRVFERLFARINEeqikhADRQLKYQCRCSFLEIYNEQITDLL- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 163 kDQTQR-LEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGI-DGNMH 240
Cdd:PLN03188 247 -DPSQKnLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVaDGLSS 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 241 VRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVD----GKSTHVPYRNSKLTRLLQDSLGGNSKT 316
Cdd:PLN03188 326 FKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578810113 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 |
3.47e-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: 3.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 14 NVKVVVRCRPLNEREKSMCYKQAVSVDEmRGTITVHKTDSSNEPPK-----TFTFDTVFGPESKQLDVYNLTARPIIDSV 88
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPS-KLTLIVHEPKLKVDLTKyienhTFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 89 LEGYNGTIFAYGQTGTGKTFTMEGVRAIPELR-GIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLgkDQTQ 167
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGDFSGQEESkGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL--NRKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 168 RLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIecsEKGIDGNMHvrmGKLH 247
Cdd:cd01367 158 RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL---RDRGTNKLH---GKLS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 248 LVDLAGSERQAKT-GATGQRLKEATKINLSLSTLGNVISALVDGKStHVPYRNSKLTRLLQDSL-GGNSKTMMCANIGPA 325
Cdd:cd01367 232 FVDLAGSERGADTsSADRQTRMEGAEINKSLLALKECIRALGQNKA-HIPFRGSKLTQVLKDSFiGENSKTCMIATISPG 310
|
330
....*....|....*...
gi 578810113 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 |
8.26e-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: 110.13 E-value: 8.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 17 VVVRCRPLNEREKsmcykqavsvdemrgtitvhktdssNEPPKTFTFDTVFGPESKQLDVYNLtARPIIDSVLEGYNG-T 95
Cdd:cd01363 1 VLVRVNPFKELPI-------------------------YRDSKIIVFYRGFRRSESQPHVFAI-ADPAYQSMLDGYNNqS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 96 IFAYGQTGTGKTFTMEgvraipelrGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNeEVRDllgkdqtqrlevkerp 175
Cdd:cd01363 55 IFAYGESGAGKTETMK---------GVIPYLASVAFNGINKGETEGWVYLTEITVTLED-QILQ---------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 176 dvgvyikdlsayvvnnaddmdrIMTLGHKNRsVGATNMNEHSSRSHAIFTItiecsekgidgnmhvrmgklhLVDLAGSE 255
Cdd:cd01363 109 ----------------------ANPILEAFG-NAKTTRNENSSRFGKFIEI---------------------LLDIAGFE 144
|
250 260 270
....*....|....*....|....*....|.
gi 578810113 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 |
7.15e-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: 7.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 14 NVKVVVRCRPLNEREKSMCYkqavsvdeMRGTITVHKTDSSNeppKTFTFDTVFGPESKQLDVYNLTaRPIIDSVLEGYN 93
Cdd:pfam16796 21 NIRVFARVRPELLSEAQIDY--------PDETSSDGKIGSKN---KSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYN 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578810113 94 GTIFAYGQTGTGKTFTMegvraipelrgiIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLL 161
Cdd:pfam16796 89 VCIFAYGQTGSGSNDGM------------IPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
451-615 |
1.55e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVggvdLLAKAEEQEKLLEESNME 530
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR----LEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 531 LEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKkvwtmlmAAKSEMADLQQEHQREIEGLLENIRQLSR 610
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL-------EAEAELAEAEEELEELAEELLEALRAAAE 397
|
....*
gi 578810113 611 ELRLQ 615
Cdd:COG1196 398 LAAQL 402
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
451-615 |
1.58e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDL---LAKAEEQEKLLEES 527
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaEAELAEAEEALLEA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 528 NMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQ 607
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
....*...
gi 578810113 608 LSRELRLQ 615
Cdd:COG1196 451 EAELEEEE 458
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
450-615 |
2.34e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 450 QAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNM 529
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 530 ELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLkkvwtmlmAAKSEMADLQQEHQREIEGLLENIRQLS 609
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE--------EALEEAAEEEAELEEEEEALLELLAELL 469
|
....*.
gi 578810113 610 RELRLQ 615
Cdd:COG1196 470 EEAALL 475
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
336-611 |
7.89e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 336 LRYANRAKNIKNKARINEDPKDAllrQFQKEIEELKK--KLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGSSS 413
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKA---DEAKKAEEAKKadEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 414 SSSSDSTCSVIEKPLDKflpnQAGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAqqehq 493
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIE----EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA----- 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 494 sllEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEE---------KEQERLDIEEKYTSLQE 564
Cdd:PTZ00121 1650 ---EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakkaeelkkKEAEEKKKAEELKKAEE 1726
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 578810113 565 EAQGKTKKLKKvwtmlmaaKSEMADLQQEHQREIEGLLENIRQLSRE 611
Cdd:PTZ00121 1727 ENKIKAEEAKK--------EAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
461-616 |
2.92e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 461 ETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDL--------LAKAEEQEKLLEESNMELE 532
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 533 ERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSE---------------------MADLQ 591
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelralleerfaaalgdavERELR 768
|
170 180
....*....|....*....|....*
gi 578810113 592 QEHQREIEGLLENIRQLSRELRLQM 616
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAM 793
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
445-615 |
6.00e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 445 KMIEMQAKIDEERKALETKLDMEEEERNKARAELE--KREKDLLKAQQEHQSLLEKLSALEKKvivggvdlLAKAEEQEK 522
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEelREELEKLEKLLQLLPLYQELEALEAE--------LAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 523 LLEESNMELEERRKRAEQLRRELEEKEQErldIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLL 602
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|...
gi 578810113 603 ENIRQLSRELRLQ 615
Cdd:COG4717 227 EELEQLENELEAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
451-612 |
6.12e-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: 57.24 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEE--SN 528
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNvrNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 529 MELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQL 608
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
....
gi 578810113 609 SREL 612
Cdd:COG1579 169 AAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
448-597 |
1.38e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 448 EMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEES 527
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 528 NmELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVwtmLMAAKSEMADLQQEHQRE 597
Cdd:COG1196 424 E-ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE---AALLEAALAELLEELAEA 489
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
364-601 |
3.05e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 364 QKEIEELKKKLEEGEEisgsdisgSEEDDDEEGEVGEDGEKRKKRRGSSSSSSSDSTCSVIEKPLDKFLPNQAGKKKVSP 443
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKK--------AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 444 DKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKL 523
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 524 LEESNMELEERRKRAEQLRRELEE--------KEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQ 595
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAkikaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
....*.
gi 578810113 596 REIEGL 601
Cdd:PTZ00121 1675 KKAEEA 1680
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
357-612 |
3.57e-08 |
|
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: 57.00 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 357 DALLRQFQKEIEELKKKLEE-GEEIS--GSDISGSEEDDDEEGEVGEDGEKRKKRRGSSSSSSSDSTCSVIEKPLDKFLp 433
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEElNKKIKdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 434 nqagKKKVSPDKMIEMQAKideERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKvivggvdl 513
Cdd:TIGR02169 336 ----AEIEELEREIEEERK---RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE-------- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 514 lakaeeqeklLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQE 593
Cdd:TIGR02169 401 ----------INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
250 260
....*....|....*....|..
gi 578810113 594 HQR---EIEGLLENIRQLSREL 612
Cdd:TIGR02169 471 LYDlkeEYDRVEKELSKLQREL 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
455-612 |
4.58e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 455 EERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGV-----------------DLLAKA 517
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErlanlerqleeleaqleELESKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 518 EEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKK---LKKVWTMLMAAKSEMADLQQEH 594
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERL 412
|
170
....*....|....*...
gi 578810113 595 QREIEGLLENIRQLSREL 612
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKL 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
451-610 |
6.13e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKAL-----ETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLE 525
Cdd:COG4913 272 AELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 526 EsnmELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENI 605
Cdd:COG4913 352 R---ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
....*
gi 578810113 606 RQLSR 610
Cdd:COG4913 429 ASLER 433
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
448-566 |
7.09e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.55 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 448 EMQAKIDEERKALETKldmEEEERNKARAELEKREKDLLKAQQEHQsLLEKLSALEKKvivggvdlLAKAEEQEKLLEES 527
Cdd:PRK12704 48 KKEAEAIKKEALLEAK---EEIHKLRNEFEKELRERRNELQKLEKR-LLQKEENLDRK--------LELLEKREEELEKK 115
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 578810113 528 NMELEERRKRAEQLRRELEEKEQERLDIEEKYTSL-QEEA 566
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQLQELERISGLtAEEA 155
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-613 |
8.04e-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: 55.83 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 340 NRAKNIKN-KARINEdpKDALLRQFQKEIEELKKKLEEGEEisgsDISGSEEDDDEEGEVGEDGEKRKKRRGSSSSSSSD 418
Cdd:TIGR02168 674 ERRREIEElEEKIEE--LEEKIAELEKALAELRKELEELEE----ELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 419 STCSviekpLDKFLPNQAGKKKVSPDKMIEMQAKIDE---ERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSL 495
Cdd:TIGR02168 748 RIAQ-----LSKELTELEAEIEELEERLEEAEEELAEaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 496 LEKLSALEKKVIVGG---VDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKK 572
Cdd:TIGR02168 823 RERLESLERRIAATErrlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 578810113 573 LKKVWTMLMAAKSEMADLQQEH---QREIEGLLENIRQLSRELR 613
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLaqlELRLEGLEVRIDNLQERLS 946
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
338-607 |
8.19e-08 |
|
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: 56.13 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 338 YANRAKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRgssSSSSS 417
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI---DLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 418 DSTCSVIEKPLDKFLPNQAGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLE 497
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 498 KLSALEKKVIVggvdllaKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVW 577
Cdd:pfam02463 325 KAEKELKKEKE-------EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270
....*....|....*....|....*....|
gi 578810113 578 TMLMAAKSEmADLQQEHQREIEGLLENIRQ 607
Cdd:pfam02463 398 ELKSEEEKE-AQLLLELARQLEDLLKEEKK 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
456-615 |
1.02e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 456 ERKAlETKLDMEEEERNKAR-----AELEKReKDLLKAQ----QEHQSLLEKLSALEKKVIVGGVDLL-AKAEEQEKLLE 525
Cdd:COG1196 172 ERKE-EAERKLEATEENLERledilGELERQ-LEPLERQaekaERYRELKEELKELEAELLLLKLRELeAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 526 ESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKvwtmLMAAKSEMADLQQEHQREIEGLLENI 605
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR----LEQDIARLEERRRELEERLEELEEEL 325
|
170
....*....|
gi 578810113 606 RQLSRELRLQ 615
Cdd:COG1196 326 AELEEELEEL 335
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
337-601 |
1.42e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 337 RYANRAKNIKNKARINEDPK--DALLRQFQKEIEELKKKLEEG----EEISGSDISGSEEDDDEEGEVGEDGEKRKKRRG 410
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEARKaeDAKKAEAVKKAEEAKKDAEEAkkaeEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 411 SSSSSSSDSTCSVIE--KPLDKFLPNQAGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAEL--EKREKDLL 486
Cdd:PTZ00121 1280 ADELKKAEEKKKADEakKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaeAEAAADEA 1359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 487 KAQQEHQSLLEKLSALEKKvivgGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEK---EQERLDIEEKYTSlq 563
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKK----KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkaDEAKKKAEEKKKA-- 1433
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 578810113 564 EEAQGKTKKLKKVWTMLMAA----KSEMADLQQEHQREIEGL 601
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAeeakKAEEAKKKAEEAKKADEA 1475
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
453-613 |
2.38e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 453 IDEERKALETKldmeEEERNKARAELEKREKDLLKAqqehqsllEKLSALEKKVivggVDLLAKAEEQEKLLEESNMELE 532
Cdd:PRK02224 470 IEEDRERVEEL----EAELEDLEEEVEEVEERLERA--------EDLVEAEDRI----ERLEERREDLEELIAERRETIE 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 533 ERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLqqEHQREIEGLLENIRQLSREL 612
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIERL 611
|
.
gi 578810113 613 R 613
Cdd:PRK02224 612 R 612
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
448-619 |
3.45e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 448 EMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEES 527
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL----QAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 528 NMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLEN-IR 606
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQaLD 186
|
170
....*....|...
gi 578810113 607 QLSRELRLQMLII 619
Cdd:COG4372 187 ELLKEANRNAEKE 199
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
475-643 |
3.99e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 475 RAELEKREKDLLKAQ-QEHQSLLEKLSALEKKvivggvdlLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQE-- 551
Cdd:COG4717 48 LERLEKEADELFKPQgRKPELNLKELKELEEE--------LKEAEEKEEEYAELQEELEELEEELEELEAELEELREEle 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 552 RLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQqEHQREIEGLLENIRQLSRELRLQMLIIDNFIPRDYQEMI 631
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170
....*....|..
gi 578810113 632 ENYVHWNEDIGE 643
Cdd:COG4717 199 EELEELQQRLAE 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
431-618 |
4.57e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 431 FLPNQAGKKKVSPDKMIEMQAKIDEERKaletKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIvgg 510
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEK----ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 511 vDLLAKAEEQEKLLEESNMEL---------------------------------------EERRKRAEQLRRELEEKEQE 551
Cdd:COG4942 87 -ELEKEIAELRAELEAQKEELaellralyrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578810113 552 RLDIEEKYTSLQEEAQGKTKKLKKvwtmLMAAKSEMADLQQEHQREIEGLLENIRQLSR-ELRLQMLI 618
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAA----LEALKAERQKLLARLEKELAELAAELAELQQeAEELEALI 229
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
435-607 |
7.41e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 435 QAGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVI------- 507
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 508 -----VGGVDLLAKAEEQEKLLEESNM-------------ELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGK 569
Cdd:COG3883 97 rsggsVSYLDVLLGSESFSDFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 578810113 570 TKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQ 607
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
341-575 |
9.27e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 341 RAKNIKNKARINEDPKDALLR--QFQKEIEELKKKLEEgeeisgsdisgseeDDDEEGEVGEDGEKRKKRRGSSSSSSSD 418
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKaaAAKKKADEAKKKAEE--------------KKKADEAKKKAEEAKKADEAKKKAEEAK 1457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 419 STCSVIEKPLDKFLPNQAGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEER--NKARAELEKREKDLLKAQQEHQSLL 496
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKADEAKKAEEAKKAD 1537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 497 EKLSALEKKvivgGVDLLAKAEEQEKLLEESNMELEER--RKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLK 574
Cdd:PTZ00121 1538 EAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKaeEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
.
gi 578810113 575 K 575
Cdd:PTZ00121 1614 K 1614
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
336-575 |
9.83e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 336 LRYANRAKNIKNKARINEDPKDALLR-QFQKEIEElkKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGSSSS 414
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKaEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 415 SSSDSTCSVIEKPLDKFLPNQAGKKKVspdKMIEMQAKIDEERKALEtKLDMEEEERNKARAELEKREKDLLKAQQehqs 494
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKKEAEEAKKAEE---- 1706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 495 lLEKLSALEKKvivgGVDLLAKAEEQEKL-LEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKL 573
Cdd:PTZ00121 1707 -LKKKEAEEKK----KAEELKKAEEENKIkAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
..
gi 578810113 574 KK 575
Cdd:PTZ00121 1782 EE 1783
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
451-613 |
1.23e-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: 51.30 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDMEEEERNKARAE---LEKREKDLLKAQQEHQSLLEK-LSALEKKVIVGGVDLLAKAE-------- 518
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAElaeLEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEdfldavrr 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 519 ------------EQEKLLEESNMELEERRKRAEQLRRELEEKEQERldiEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSE 586
Cdd:COG4942 138 lqylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAELAAE 214
|
170 180
....*....|....*....|....*..
gi 578810113 587 MADLQQEhQREIEGLLENIRQLSRELR 613
Cdd:COG4942 215 LAELQQE-AEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
456-613 |
1.30e-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: 51.99 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 456 ERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVD----------------------L 513
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekigeleaeiaslersI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 514 LAKAEEQEKLLEESNMELEERRK---RAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADL 590
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKllaEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190
....*....|....*....|....*....|...
gi 578810113 591 QQ----------EHQREIEGLLENIRQLSRELR 613
Cdd:TIGR02169 391 REkleklkreinELKRELDRLQEELQRLSEELA 423
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
512-608 |
1.58e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 512 DLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEK-YTSLQEEAQGKTKKLKKVWTMLMAAKSEMADL 590
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKlLEEAEKEAQQAIKEAKKEADEIIKELRQLQKG 599
|
90
....*....|....*...
gi 578810113 591 QQEHQREIEgLLENIRQL 608
Cdd:PRK00409 600 GYASVKAHE-LIEARKRL 616
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
451-612 |
2.20e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEESNME 530
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI----DKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 531 LEER---------------------------------RKRAEQLRRELEEKEQERLDIEEKytslQEEAQGKTKKLKKVW 577
Cdd:COG3883 88 LGERaralyrsggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAK----KAELEAKLAELEALK 163
|
170 180 190
....*....|....*....|....*....|....*
gi 578810113 578 TMLMAAKSEMADLQQEHQREIEGLLENIRQLSREL 612
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
454-579 |
2.87e-06 |
|
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: 50.89 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 454 DEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVggvdllaKAEEQEKLLEEsnmELEE 533
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMI-------EEERKRKLLEK---EMEE 524
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578810113 534 RRKR--AEQLRRELEEKEQERLDIEEKyTSLQEEAQGKTKKLKKVWTM 579
Cdd:pfam17380 525 RQKAiyEEERRREAEEERRKQQEMEER-RRIQEQMRKATEERSRLEAM 571
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
444-608 |
3.08e-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: 50.83 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 444 DKMIEMQAKIDEERKALET---KLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdLLAKAEEQ 520
Cdd:TIGR02168 365 AELEELESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL------EEAELKEL 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 521 EKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMlmaaksemadlqqehQREIEG 600
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL---------------QENLEG 503
|
....*...
gi 578810113 601 LLENIRQL 608
Cdd:TIGR02168 504 FSEGVKAL 511
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
423-581 |
4.26e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.24 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 423 VIEKPLDKFLPNQAGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREkdllkaqqehqsllEKLSAL 502
Cdd:COG2433 381 ALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKD--------------ERIERL 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578810113 503 EKKVIvggvdlLAKAEEQEKLLEESnmELEERRKRAEQLRRELEEKEQERldieekytslqEEAQGKTKKLKKVWTMLM 581
Cdd:COG2433 447 ERELS------EARSEERREIRKDR--EISRLDREIERLERELEEERERI-----------EELKRKLERLKELWKLEH 506
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
424-606 |
4.89e-06 |
|
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: 49.76 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 424 IEKPLDKFLPNQAGKKKVS--PDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLL----- 496
Cdd:pfam09731 207 EEAAPPLLDAAPETPPKLPehLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSnddln 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 497 -------EKLSALEKKVIVGGVD--------LLAKAEEQEKLLEESNMELEE-RRKRAEQLRRELEEKEQE-RLDIEEKY 559
Cdd:pfam09731 287 sliahahREIDQLSKKLAELKKReekhieraLEKQKEELDKLAEELSARLEEvRAADEAQLRLEFEREREEiRESYEEKL 366
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578810113 560 -TSLQEEAQGKTKKLKKVwtmlmaAKSEMADLQQEHQREIEGLLENIR 606
Cdd:pfam09731 367 rTELERQAEAHEEHLKDV------LVEQEIELQREFLQDIKEKVEEER 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
450-586 |
7.57e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 450 QAKIDEERKALETKLDMEE--EERNKARAELE---KREKDLLKAQQEHQSLLEKLSALEKKVivggvdllakAEEQEKLL 524
Cdd:COG4717 111 LEELREELEKLEKLLQLLPlyQELEALEAELAelpERLEELEERLEELRELEEELEELEAEL----------AELQEELE 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578810113 525 EESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSE 586
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
437-610 |
8.99e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 437 GKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSAL--EKKVIVGGV--- 511
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeELQRLSEELadl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 512 -----DLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSE 586
Cdd:TIGR02169 426 naaiaGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
170 180
....*....|....*....|....*..
gi 578810113 587 M---ADLQQEHQREIEGLLENIRQLSR 610
Cdd:TIGR02169 506 VrggRAVEEVLKASIQGVHGTVAQLGS 532
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
340-617 |
1.60e-05 |
|
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: 48.43 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 340 NRAKNIKNKARINEDPKDaLLRQFQKEIEELKKKLEEGEEISGsdisgSEEDDDEEGEVGEDGEKRKKRRGSSSSSSSDS 419
Cdd:pfam02463 184 NLAELIIDLEELKLQELK-LKEQAKKALEYYQLKEKLELEEEY-----LLYLDYLKLNEERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 420 TCSVIEKPLDKFLPNQAGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKL 499
Cdd:pfam02463 258 QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 500 SALEKKVIVGGVDLLAKAEEQEKLLEESNmELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQE----EAQGKTKKLKK 575
Cdd:pfam02463 338 EELEKELKELEIKREAEEEEEEELEKLQE-KLEQLEEELLAKKKLESERLSSAAKLKEEELELKSeeekEAQLLLELARQ 416
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 578810113 576 VWTMLMAAKSEMADLQQEHQREIEGLLENIRQLSRELRLQML 617
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
454-574 |
1.81e-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: 44.99 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 454 DEERKALETKLDMEEEERNKARAELeKREKDLLKAQQEHQSLLEklsALEKKVIVggvdLLAKAEEQEKLLEESNMELEE 533
Cdd:pfam12718 34 EQEIKSLTHKNQQLEEEVEKLEEQL-KEAKEKAEESEKLKTNNE---NLTRKIQL----LEEELEESDKRLKETTEKLRE 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 578810113 534 RRKRAEQLRRELEEKEQERLDIEEKYtslqEEAQGKTKKLK 574
Cdd:pfam12718 106 TDVKAEHLERKVQALEQERDEWEKKY----EELEEKYKEAK 142
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
445-614 |
1.84e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 445 KMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvDLLAKAEEQ---- 520
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREE-----KELKKLEEEldka 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 521 EKLLEESNMELEERRKRAEQLRRELEEKEQERldIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEhqreieg 600
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE------- 702
|
170
....*....|....
gi 578810113 601 lLENIRQLSRELRL 614
Cdd:PRK03918 703 -LEEREKAKKELEK 715
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
456-608 |
2.00e-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: 48.13 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 456 ERKaLETKLDMEEEERNKAR-----AELEKReKDLLKAQ----QEHQSLLEKLSALEKKVIVGGVD-LLAKAEEQEKLLE 525
Cdd:TIGR02168 172 ERR-KETERKLERTRENLDRledilNELERQ-LKSLERQaekaERYKELKAELRELELALLVLRLEeLREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 526 ESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENI 605
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
...
gi 578810113 606 RQL 608
Cdd:TIGR02168 330 SKL 332
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
459-574 |
2.21e-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: 44.98 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 459 ALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEESNMELEERRKRA 538
Cdd:pfam10473 28 NLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDL----VTLRSEKENLTKELQKKQERVSELESLN 103
|
90 100 110
....*....|....*....|....*....|....*.
gi 578810113 539 EQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLK 574
Cdd:pfam10473 104 SSLENLLEEKEQEKVQMKEESKTAVEMLQTQLKELN 139
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
445-613 |
2.84e-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: 47.76 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 445 KMIEMQAKidEERKALETKLDMEE--EERNKARAELEKREKDLLKAQ--------------------QEHQSLLEKLSAL 502
Cdd:TIGR02169 146 DFISMSPV--ERRKIIDEIAGVAEfdRKKEKALEELEEVEENIERLDliidekrqqlerlrrerekaERYQALLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 503 EKKVIVGGV-DLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKK--------L 573
Cdd:TIGR02169 224 EGYELLKEKeALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigeleaeI 303
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578810113 574 KKVWTMLMAAKSEMADLQQEHQR---EIEGLLENIRQLSRELR 613
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKleaEIDKLLAEIEELEREIE 346
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
516-595 |
3.00e-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: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 516 KAEEQEKLLEESNMELEERRKRAEQLrrELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVW----TMLMAAK--SEMAD 589
Cdd:pfam15991 26 KQEQEAKMEEERLRREREEREKEDRM--TLEETKEQILKLEKKLADLKEEKHQLFLQLKKVLhedeTRKRQLKeqSELFA 103
|
....*.
gi 578810113 590 LQQEHQ 595
Cdd:pfam15991 104 LQQAAA 109
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
435-612 |
3.03e-05 |
|
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: 47.20 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 435 QAGKKKVSPDKMIEMQAK--IDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALekkvivggvd 512
Cdd:pfam07888 51 EAANRQREKEKERYKRDReqWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL---------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 513 LLAKAEEQEKLLE-------------ESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTM 579
Cdd:pfam07888 121 LAQRAAHEARIREleediktltqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNS 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578810113 580 LMAAKSEMADLQ-------------QEHQREIEGLLENIRQLSREL 612
Cdd:pfam07888 201 LAQRDTQVLQLQdtittltqklttaHRKEAENEALLEELRSLQERL 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
455-620 |
3.06e-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: 47.76 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 455 EERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQ-----SLLEKLSALEKKVivggvdllakaEEQEKLLEESNM 529
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIenrldELSQELSDASRKI-----------GEIEKEIEQLEQ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 530 ELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKsemADLQQEHQREIEGLLENIRQLS 609
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKLEEEV 807
|
170
....*....|.
gi 578810113 610 RELRLQMLIID 620
Cdd:TIGR02169 808 SRIEARLREIE 818
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
455-615 |
3.20e-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: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 455 EERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKvIVGGVDLLAKAEEQ----EKLLEESNME 530
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-LEALLNERASLEEAlallRSELEELSEE 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 531 LEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMaaksemaDLQQEHQREIEGLLENIRQLSR 610
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL-------EEAEALENKIEDDEEEARRRLK 975
|
....*
gi 578810113 611 ELRLQ 615
Cdd:TIGR02168 976 RLENK 980
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
448-611 |
3.30e-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: 47.64 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 448 EMQAK---IDEERKALETKLDMEEEERNK---------------ARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivg 509
Cdd:COG3096 445 AFRAKeqqATEEVLELEQKLSVADAARRQfekayelvckiagevERSQAWQTARELLRRYRSQQALAQRLQQLRAQL--- 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 510 gVDLLAKAEEQ---EKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQE----------EAQGKTKKLKKV 576
Cdd:COG3096 522 -AELEQRLRQQqnaERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrselrqqleQLRARIKELAAR 600
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578810113 577 WTMLMAAKSEMADLQ----------QEHQREIEGLLENIRQLSRE 611
Cdd:COG3096 601 APAWLAAQDALERLReqsgealadsQEVTAAMQQLLEREREATVE 645
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
452-622 |
3.85e-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: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 452 KIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEESNMEL 531
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI----KSIEKEIENLNGKKEELEEEL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 532 EERRKRAEQLRRELEEKEQERLDIEEKYTSLQE-------EAQGKTKKLKKVWTMLMAAKSEMADLQQEHQRE------- 597
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERkieeleaQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeee 950
|
170 180 190
....*....|....*....|....*....|.
gi 578810113 598 --IEGLLENIRQLSRELR----LQMLIIDNF 622
Cdd:TIGR02169 951 lsLEDVQAELQRVEEEIRalepVNMLAIQEY 981
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
451-613 |
4.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAK---AEEQEKLLEES 527
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaAALGDAVEREL 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 528 NMELEERRKRAEQLRRELEEK--------------EQERLDI--------EEKYTSLQE----EAQGKTKKLKKVWTmlm 581
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEleramrafnrewpaETADLDAdleslpeyLALLDRLEEdglpEYEERFKELLNENS--- 844
|
170 180 190
....*....|....*....|....*....|..
gi 578810113 582 aaKSEMADLQQEHQREIEGLLENIRQLSRELR 613
Cdd:COG4913 845 --IEFVADLLSKLRRAIREIKERIDPLNDSLK 874
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
424-633 |
4.98e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 424 IEKPLDKfLPNQAGKKKVSPDKMIEMqakideERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALE 503
Cdd:PRK05771 55 LSEALDK-LRSYLPKLNPLREEKKKV------SVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 504 K-----------------KVIVGGVDlLAKAEEQEKLLEESNMELEER------------RKRAEQLRRELEEKEQERLD 554
Cdd:PRK05771 128 PwgnfdldlslllgfkyvSVFVGTVP-EDKLEELKLESDVENVEYISTdkgyvyvvvvvlKELSDEVEEELKKLGFERLE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 555 IEEKYTsLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREI---EGLLENIRQ----LSRELRLQML-IIDNFIPRD 626
Cdd:PRK05771 207 LEEEGT-PSELIREIKEELEEIEKERESLLEELKELAKKYLEELlalYEYLEIELEraeaLSKFLKTDKTfAIEGWVPED 285
|
....*..
gi 578810113 627 YQEMIEN 633
Cdd:PRK05771 286 RVKKLKE 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
465-615 |
5.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 465 DMEEEERNKARAELEKREKDLL----KAQQEHQSLLEKLSALEKkvivggVDLLAKAEEQEKLLEESNMELEERRKRAEQ 540
Cdd:COG4913 233 HFDDLERAHEALEDAREQIELLepirELAERYAAARERLAELEY------LRAALRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578810113 541 LRRELEEKEQERLDIEEKYTSLQEEAQG-KTKKLKkvwtmlmAAKSEMADLQQEhQREIEGLLENIRQLSRELRLQ 615
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGnGGDRLE-------QLEREIERLERE-LEERERRRARLEALLAALGLP 374
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
445-583 |
6.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 445 KMIEMQAKIDEERKALEtKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVggvDLLAKAEEQEKll 524
Cdd:COG4717 133 ELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---DLAEELEELQQ-- 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 578810113 525 eesnmELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEaqgktKKLKKVWTMLMAA 583
Cdd:COG4717 207 -----RLAELEEELEEAQEELEELEEELEQLENELEAAALE-----ERLKEARLLLLIA 255
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
451-705 |
6.60e-05 |
|
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: 46.50 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKkvivggvdllakaeEQEKLLEESNME 530
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN--------------ITVRLQDLTEKL 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 531 LEERRKRAEQLRRELEEKeQERLDIEEKYTSLQEEAQGKTKKLkkvwtmlMAAKSEMADLQQEHQREIEgllenirQLSR 610
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKL-QPEQDLQDVRLHLQQCSQELALKL-------TALHALQLTLTQERVREHA-------LSIR 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 611 ELRLQMLIIDNFIPRDYQEMIENYVHWNEDIGEWQLKcvaytgnnMRKQTPVPDKKEKDPFEVDLSHVY----LAYTEES 686
Cdd:TIGR00618 669 VLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL--------LRELETHIEEYDREFNEIENASSSlgsdLAAREDA 740
|
250
....*....|....*....
gi 578810113 687 LRQSLMKLERPRTSKGKAR 705
Cdd:TIGR00618 741 LNQSLKELMHQARTVLKAR 759
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
453-615 |
7.40e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 453 IDEERKALETKLDmeeeernKARAELE--KREKDLLKAQQEHQSLLEKLSALEKKVI---VGGVDLLAKAEEQEKLLEES 527
Cdd:COG3206 180 LEEQLPELRKELE-------EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAearAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 528 NMELEERRK--RAEQLRRELEEKEQERLDIEEKYTSLQEEAQgktkklkkvwtmlmAAKSEMADLQQEHQREIEGLLENI 605
Cdd:COG3206 253 PDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVI--------------ALRAQIAALRAQLQQEAQRILASL 318
|
170
....*....|
gi 578810113 606 RQLSRELRLQ 615
Cdd:COG3206 319 EAELEALQAR 328
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
457-613 |
8.83e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 457 RKALETKLDMEEEERNKARAE-LEKREKDLLKAQQEHQSLLEKLSALEKKVIVG---GVDLLAKAEEQEKLLEESNMELE 532
Cdd:PRK04863 496 DVARELLRRLREQRHLAEQLQqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNlddEDELEQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 533 ERRKRAEQLRRELEEKEQERldieEKYTSLQEE---AQGKTKKLKKVW-------TMLMAAKSEMADLQQEHQREIEGLL 602
Cdd:PRK04863 576 EARERRMALRQQLEQLQARI----QRLAARAPAwlaAQDALARLREQSgeefedsQDVTEYMQQLLERERELTVERDELA 651
|
170
....*....|.
gi 578810113 603 ENIRQLSRELR 613
Cdd:PRK04863 652 ARKQALDEEIE 662
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
360-574 |
9.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 360 LRQFQKEIEELKKKLEEGEEISGSdISGSEEDDDEEGEVGEDGEKRKKRRGSSSSSSSDSTCSVIEKPLDKFLpnqagKK 439
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKK-LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL-----EL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 440 KVSPDKMIEMQakidEERKALETKLDMEEEERNKARAELEKREKDLLKAQQ-----EHQSLLEKLSALEKkvivggvdLL 514
Cdd:PRK03918 608 KDAEKELEREE----KELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSR--------EL 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578810113 515 AKAEEQEKLLEESnmeLEERRKRAEQLRRELEEKEQERLDIE--EKYTSLQEEAQGKTKKLK 574
Cdd:PRK03918 676 AGLRAELEELEKR---REEIKKTLEKLKEELEEREKAKKELEklEKALERVEELREKVKKYK 734
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
450-612 |
9.32e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 450 QAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKvivggvdllakaeeqeklLEESNM 529
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE------------------LEQARS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 530 ELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWT---MLMAAKSEMADLQQEHQREIEGLLENIR 606
Cdd:COG4372 74 ELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
....*.
gi 578810113 607 QLSREL 612
Cdd:COG4372 154 ELEEQL 159
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
444-619 |
1.01e-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: 45.88 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 444 DKMIEMQAKIDEERKALETKLDMEEEERNKAR-AELEKREKdlLKAQQEHQSL-----LEKLSALEKKVIVGGVDLLAKA 517
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEAEKARqAEMDRQAA--IYAEQERMAMerereLERIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 518 EEQEKLLEESNMELEERRKRaEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKvwtMLMAAKSEMADLQQEHQRE 597
Cdd:pfam17380 372 MEISRMRELERLQMERQQKN-ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE---QEEARQREVRRLEEERARE 447
|
170 180
....*....|....*....|..
gi 578810113 598 ieglLENIRQLSRELRLQMLII 619
Cdd:pfam17380 448 ----MERVRLEEQERQQQVERL 465
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
491-621 |
1.06e-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: 44.53 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 491 EHQSLLEKLSALEKKvivggvdlLAKAEEQEKLLEEsnmELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKT 570
Cdd:COG1579 4 EDLRALLDLQELDSE--------LDRLEHRLKELPA---ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578810113 571 KKLKKVWTMLMAAKS--EMADLqqehQREIEGLLENIRQLSRELRLQMLIIDN 621
Cdd:COG1579 73 ARIKKYEEQLGNVRNnkEYEAL----QKEIESLKRRISDLEDEILELMERIEE 121
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
448-565 |
1.14e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 448 EMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEES 527
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578810113 528 nmELEERRKRAEQLRRELE----------EKEQERLD-IEEKYTSLQEE 565
Cdd:COG1196 764 --ELERELERLEREIEALGpvnllaieeyEELEERYDfLSEQREDLEEA 810
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
328-616 |
1.22e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 328 NYDETISTLRYAnraknIKNKARINE---DPKDALLRQFQKEIEELKKKLEEGEEiSGSDISGSEEDDDEEGEVGEDGEK 404
Cdd:pfam10174 433 NTDTALTTLEEA-----LSEKERIIErlkEQREREDRERLEELESLKKENKDLKE-KVSALQPELTEKESSLIDLKEHAS 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 405 RKKRRGSSSSSSSDSTCSVIEKPLDKFLPNQAGKKKVSPDKMIE-MQAKIDEERKALETKLDMEEEERNKARAELEKREK 483
Cdd:pfam10174 507 SLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVrTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLG 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 484 DLLKAQQEHQSLLEKLSALEKKVivggvdLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKytsLQ 563
Cdd:pfam10174 587 ILREVENEKNDKDKKIAELESLT------LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL---QL 657
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 578810113 564 EEAQGKTKKLKKVwtmLMAAKSEMADLQQEHQrEIEGLLENIRQLSR---ELRLQM 616
Cdd:pfam10174 658 EELMGALEKTRQE---LDATKARLSSTQQSLA-EKDGHLTNLRAERRkqlEEILEM 709
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
445-610 |
1.39e-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: 45.34 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 445 KMIEMQAKIDEERKALETKLDMEEEERNKARAE-LEKREKDLLKAQQEHQSLLEKLSALEK---------KVIVGGVDLL 514
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQvLEKELKHLREALQQTQQSHAYLTQKREaqeeqlkkqQLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 515 AKAEEQEKLLEESNMELEERRKrAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKS---EMADLQ 591
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARK-AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSieeQRRLLQ 348
|
170
....*....|....*....
gi 578810113 592 QEHQREIEGLLENIRQLSR 610
Cdd:TIGR00618 349 TLHSQEIHIRDAHEVATSI 367
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
455-597 |
1.42e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 455 EERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKL--SALEKKVIVGGVDLLAKAEEQEKLLEESNMELE 532
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEELE 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578810113 533 ERRKRAEQLRRELEEKEQERL--DIEEKYTSLQEEAQGKTKKlkkvWTMLMAAKSEMADLQQEHQRE 597
Cdd:COG4717 450 ELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEE----WAALKLALELLEEAREEYREE 512
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
444-573 |
1.47e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 444 DKMIEMQAKIDEERKALETKLDmEEEERNKARAE-LEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEK 522
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNELQ-KLEKRLLQKEEnLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 578810113 523 LLEE-SNMELEERRKR-AEQLRRELEEKEQERL-DIEEKYtslQEEAQGKTKKL 573
Cdd:PRK12704 143 ELERiSGLTAEEAKEIlLEKVEEEARHEAAVLIkEIEEEA---KEEADKKAKEI 193
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
476-609 |
1.59e-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: 45.33 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 476 AELEKRekdlLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQER--- 552
Cdd:COG3096 522 AELEQR----LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIkel 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578810113 553 -------LDIEEKYTSLQEE-------AQGKTKKLKKVWTMLMAAKSEMADLQQEHQReiegLLENIRQLS 609
Cdd:COG3096 598 aarapawLAAQDALERLREQsgealadSQEVTAAMQQLLEREREATVERDELAARKQA----LESQIERLS 664
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
468-571 |
1.75e-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: 43.36 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 468 EEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVggvdLLAKAEEQEKL----------LEESNMELEERRKR 537
Cdd:pfam13851 32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEE----LRKQLENYEKDkqslknlkarLKVLEKELKDLKWE 107
|
90 100 110
....*....|....*....|....*....|....
gi 578810113 538 AEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTK 571
Cdd:pfam13851 108 HEVLEQRFEKVERERDELYDKFEAAIQDVQQKTG 141
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-619 |
2.06e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 358 ALLRQFQKEIEELKKKLEEGEEI----SGSDISGSEEDDDEEGEVGEDGEKRKKRRGSSSSSSSDSTCSVIEKPLDKFLP 433
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIeeliKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 434 NQAGKKKVSPDKMIEMQAKIDEERKALEtkldmEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKkvivggvdL 513
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIE-----ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK--------R 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 514 LAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEqERLDIEEKYTSLQEEAQGKTKKLKKVwtmlmaaKSEMADLQQE 593
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERL-------KKRLTGLTPE 387
|
250 260
....*....|....*....|....*.
gi 578810113 594 hqrEIEGLLENIRQLSRELRLQMLII 619
Cdd:PRK03918 388 ---KLEKELEELEKAKEEIEEEISKI 410
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
463-617 |
2.30e-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: 44.63 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 463 KLDMEEEERNKARAELEKR--EKDLLKAQQ-EHQSLLEKLSALEKKVivggvdllAKAEEQEKLLEESNMELEERrkrAE 539
Cdd:pfam05667 305 KLQFTNEAPAATSSPPTKVetEEELQQQREeELEELQEQLEDLESSI--------QELEKEIKKLESSIKQVEEE---LE 373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578810113 540 QLRRELEEKEQErLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREiegLLENIRQLSRELRLQML 617
Cdd:pfam05667 374 ELKEQNEELEKQ-YKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVP---LIEEYRALKEAKSNKED 447
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
459-618 |
2.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 459 ALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRA 538
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 539 ---------EQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKvwtmlMAAKSEMADLQQEHQReiegLLENIRQLS 609
Cdd:COG4717 419 eellealdeEELEEELEELEEELEELEEELEELREELAELEAELEQ-----LEEDGELAELLQELEE----LKAELRELA 489
|
....*....
gi 578810113 610 RELRLQMLI 618
Cdd:COG4717 490 EEWAALKLA 498
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
465-613 |
2.62e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 465 DMEEEERNKaraELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdllakaeeqeKLLEESNMELEerrkraeqlrRE 544
Cdd:COG2433 384 ELIEKELPE---EEPEAEREKEHEERELTEEEEEIRRLEEQV---------------ERLEAEVEELE----------AE 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578810113 545 LEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVwTMLmaaKSEMADLqqehQREIEGLLENIRQLSRELR 613
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 ... |
461-612 |
3.02e-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: 44.40 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 461 ETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGG----------VDLLAKAEEQEKLLEESNME 530
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcaeaeemrARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 531 LEERRKRAEQLRRELEEKEQERLDIEEKYTslQEEAQGKTKKLKKVWTMLMAAKSE-----MADLQQEHQREIEGLLENI 605
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLD--EEEAARQKLQLEKVTTEAKIKKLEedillLEDQNSKLSKERKLLEERI 161
|
....*..
gi 578810113 606 RQLSREL 612
Cdd:pfam01576 162 SEFTSNL 168
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
450-550 |
3.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 450 QAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKvivggvdlLAKAEEQEKLLEESNM 529
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE--------AALLEAALAELLEELA 487
|
90 100
....*....|....*....|.
gi 578810113 530 ELEERRKRAEQLRRELEEKEQ 550
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
331-565 |
5.05e-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: 43.42 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 331 ETISTLRYANRAKNIKNKariNEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRG 410
Cdd:pfam02463 770 SLKEKELAEEREKTEKLK---VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 411 SSSSSSSDSTCSVIEKPLDKFLPNQAGKKKVSPDKMIEMQAKIDEERKaLETKLDMEEEERNKARAELEKREKDLLKAQQ 490
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK-EKEEKKELEEESQKLNLLEEKENEIEERIKE 925
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578810113 491 EHQSLLEKLSALEKKVIVGGVD---LLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEE 565
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEkekEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
450-565 |
5.30e-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: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 450 QAKIDEERKALETKLDMEEEERNKARA--------ELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQE 521
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578810113 522 KLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEE 565
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
451-568 |
5.77e-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: 43.52 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKV-----IVGGVDLLAKAEEQEKLLE 525
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKgedeeIPEEELSLEDVQAELQRVE 964
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578810113 526 ESNMELEERRKRAEQlrrELEEKEQERLDIEEKYTSLQEEAQG 568
Cdd:TIGR02169 965 EEIRALEPVNMLAIQ---EYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
434-564 |
5.92e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 434 NQAGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREK--------------DLLKAQQEHQSLLEKL 499
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEeieelrerfgdapvDLGNAEDFLEELREER 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 500 SALEKKVIVGGVDL--LAKA-EEQEKLLEESNM--------------ELEERRKRAEQLRRELEEKEQERLDIEEKYTSL 562
Cdd:PRK02224 422 DELREREAELEATLrtARERvEEAEALLEAGKCpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
..
gi 578810113 563 QE 564
Cdd:PRK02224 502 ED 503
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
452-605 |
6.32e-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: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 452 KIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdllAKAEEQEKLLEESNMEL 531
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV--------KDLTKKISSLKEKIEKL 529
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578810113 532 EERRKRAEQLRRELeEKEQERLDIEEKYTSLQEEAQGKTK---KLKKVWTMLMAAKSEMADLQQEHQREIEGLLENI 605
Cdd:TIGR04523 530 ESEKKEKESKISDL-EDELNKDDFELKKENLEKEIDEKNKeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
444-562 |
6.64e-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: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 444 DKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdllAKAEEQEKL 523
Cdd:smart00787 179 DRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKI--------EDLTNKKSE 250
|
90 100 110
....*....|....*....|....*....|....*....
gi 578810113 524 LEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSL 562
Cdd:smart00787 251 LNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLTGW 289
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
490-606 |
7.26e-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: 42.28 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 490 QEHQSLLEKLSALEKKVIvggvDLLAKAEEQEKLLEESNMELEER---RKRAEQLRRELEEKEQERLDIEEKYTSLQEEA 566
Cdd:pfam07767 195 EDHQELLQKAVEAEKKRL----KEEEKLERVLEKIAESAATAEAReekRKTKAQRNKEKRRKEEEREAKEEKALKKKLAQ 270
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 578810113 567 QGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIR 606
Cdd:pfam07767 271 LERLKEIAKEIAEKEKEREEKAEARKREKRKKKKEEKKLR 310
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
448-611 |
1.03e-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: 41.79 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 448 EMQAKIDEERKALETKldMEEEERNKARAELEKREKDLLKA---------------QQEHQSLLEKLSALEKKVIvggvd 512
Cdd:cd16269 94 KLMEQLEEKKEEFCKQ--NEEASSKRCQALLQELSAPLEEKisqgsysvpggyqlyLEDREKLVEKYRQVPRKGV----- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 513 llaKAEE------------------QEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLK 574
Cdd:cd16269 167 ---KAEEvlqeflqskeaeaeailqADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLK 243
|
170 180 190
....*....|....*....|....*....|....*..
gi 578810113 575 KvwTMlmaaKSEMADLQQEHQREIEGLLENIRQLSRE 611
Cdd:cd16269 244 E--KM----EEERENLLKEQERALESKLKEQEALLEE 274
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
444-615 |
1.13e-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: 41.83 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 444 DKMIEMQAKIDEERKALETKLD--MEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEE-- 519
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDemMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQmd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 520 --QEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKK-LKKVWTMLMAAKSEMADLQQEHQR 596
Cdd:pfam13868 105 eiVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEyLKEKAEREEEREAEREEIEEEKER 184
|
170
....*....|....*....
gi 578810113 597 EIEGLLENIRQLSRELRLQ 615
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAER 203
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
448-613 |
1.16e-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: 42.52 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 448 EMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLL--- 524
Cdd:pfam12128 618 EKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLdkk 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 525 -----EESNMELEERRKRAEQLRRELEEKEQERLD-IEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREI 598
Cdd:pfam12128 698 hqawlEEQKEQKREARTEKQAYWQVVEGALDAQLAlLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI 777
|
170
....*....|....*...
gi 578810113 599 EGL---LENIRQLSRELR 613
Cdd:pfam12128 778 RTLerkIERIAVRRQEVL 795
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
451-608 |
1.20e-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: 41.59 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDMEEEERNKARAE--LEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESN 528
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTIKalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 529 -----MELEERRKRAEQLRRELEEKEQERLDieeKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQehqrEIEGLLE 603
Cdd:cd22656 174 gaiarKEIKDLQKELEKLNEEYAAKLKAKID---ELKALIADDEAKLAAALRLIADLTAADTDLDNLLA----LIGPAIP 246
|
....*
gi 578810113 604 NIRQL 608
Cdd:cd22656 247 ALEKL 251
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
457-608 |
1.39e-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: 41.54 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 457 RKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSL---LEKLSALEKKVIVGGVDLLAKAeeQEKLLEESnMELEE 533
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALeeeLRQLKQLEDELEDCDPTELDRA--KEKLKKLL-QEIMI 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578810113 534 RRKRAEQLRRELEEKEQerlDIEEKytslqeeaqgkTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQL 608
Cdd:smart00787 223 KVKKLEELEEELQELES---KIEDL-----------TNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLL 283
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
459-598 |
1.54e-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: 42.25 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 459 ALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSL-------LEKLSALEKKVIVGGVDLLAKAEEQEKLL-EESNME 530
Cdd:COG3096 988 KLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLkssrdakQQTLQELEQELEELGVQADAEAEERARIRrDELHEE 1067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 531 LEERRKRAEQL-------RRELEEKEQERLDIEEKYTSLQEEAQGKtkklKKVWTMLMA-----------AKSEMADLQQ 592
Cdd:COG3096 1068 LSQNRSRRSQLekqltrcEAEMDSLQKRLRKAERDYKQEREQVVQA----KAGWCAVLRlardndverrlHRRELAYLSA 1143
|
....*.
gi 578810113 593 EHQREI 598
Cdd:COG3096 1144 DELRSM 1149
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
444-551 |
1.54e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 444 DKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKL 523
Cdd:COG3883 132 ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
90 100
....*....|....*....|....*...
gi 578810113 524 LEESNMELEERRKRAEQLRRELEEKEQE 551
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
450-588 |
1.56e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.37 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 450 QAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIvggVDLLAKAEEQEKLLEEsnm 529
Cdd:TIGR02794 88 QARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK---EEAAKQAEEEAKAKAA--- 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 578810113 530 elEERRKRAEQLRRELEEKEQERLDIEEKytSLQEEAQGKTKKLKKVWTMLMAAKSEMA 588
Cdd:TIGR02794 162 --AEAKKKAEEAKKKAEAEAKAKAEAEAK--AKAEEAKAKAEAAKAKAAAEAAAKAEAE 216
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
443-529 |
1.61e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.59 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 443 PDKMIEMQAK------------IDEERKALETKLDMEEEERN---KARAELEKREKDLLKAQQEHQSLLEKLSALEKKvi 507
Cdd:PRK05431 11 PEAVKEALAKrgfpldvdelleLDEERRELQTELEELQAERNalsKEIGQAKRKGEDAEALIAEVKELKEEIKALEAE-- 88
|
90 100
....*....|....*....|....
gi 578810113 508 vggvdlLAKAEEQ--EKLLEESNM 529
Cdd:PRK05431 89 ------LDELEAEleELLLRIPNL 106
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
445-572 |
1.97e-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: 41.29 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 445 KMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKkvivggvdllakaeEQEKLL 524
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA--------------ERQKLL 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578810113 525 EESNmeleerrKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKK 572
Cdd:COG4942 202 ARLE-------KELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
515-618 |
2.54e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 515 AKAEEQEKLLE----------ESNMELEERRKRAEQLRRELEEKEqERLDIE-EKYTSLQEEAQGKTKKLKKVWTMLMAA 583
Cdd:PRK12704 51 AEAIKKEALLEakeeihklrnEFEKELRERRNELQKLEKRLLQKE-ENLDRKlELLEKREEELEKKEKELEQKQQELEKK 129
|
90 100 110
....*....|....*....|....*....|....*
gi 578810113 584 KSEMADLQQEHQREieglLENIRQLSRELRLQMLI 618
Cdd:PRK12704 130 EEELEELIEEQLQE----LERISGLTAEEAKEILL 160
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
434-575 |
2.98e-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: 40.25 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 434 NQAGKKKVSPDKMIE--MQAKIDEER---KALETKLDME-EEERNKARAELEKREKDLLKAQQEhqslleklsalekkvi 507
Cdd:cd16269 159 RQVPRKGVKAEEVLQefLQSKEAEAEailQADQALTEKEkEIEAERAKAEAAEQERKLLEEQQR---------------- 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578810113 508 vggvDLLAKAEEQEKLLEESNMEL-----EERRKRAEQLRRELEEK--EQERLdieekytsLQEEAQGKTKKLKK 575
Cdd:cd16269 223 ----ELEQKLEDQERSYEEHLRQLkekmeEERENLLKEQERALESKlkEQEAL--------LEEGFKEQAELLQE 285
|
|
| CENP-H |
pfam05837 |
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H ... |
483-580 |
3.19e-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: 37.95 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 483 KDLLKAQQEHQSLLEKLSALEKKVIVggvdllakaeeqeklLEESNMELeerrkrAEQLRRELEEKEQERLDIEEKytSL 562
Cdd:pfam05837 13 SAILKLSSELRELQEELTEVEKENLR---------------LKRKNREL------AAELLELAKEKESRREDPKLR--AQ 69
|
90
....*....|....*...
gi 578810113 563 QEEAQGKTKKLKKVWTML 580
Cdd:pfam05837 70 LEKLEAELKKSRRRWRVM 87
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
445-593 |
3.25e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 445 KMIEMQAKIDEERKALETKLDME------------EEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvd 512
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALpellqspviqqlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 513 llakAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDI---EEKYTSLQEEAQGKTKKLkkvwtMLMAAKSEMAD 589
Cdd:COG3206 308 ----QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELY-----ESLLQRLEEAR 378
|
....
gi 578810113 590 LQQE 593
Cdd:COG3206 379 LAEA 382
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
448-621 |
3.43e-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: 40.87 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 448 EMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKvivggvdlLAKAEEQEKLLEES 527
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAD--------LHKREKELSLEKEQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 528 NMELEERRK----RAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKlkkvwtmLMAA---KSEMADLQQEHQREIEG 600
Cdd:pfam15921 400 NKRLWDRDTgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMER-------QMAAiqgKNESLEKVSSLTAQLES 472
|
170 180
....*....|....*....|.
gi 578810113 601 LLENIRQLSRELRLQMLIIDN 621
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLES 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
448-622 |
3.58e-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: 40.87 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 448 EMQAKIDEERKALETKlDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggVDLLAKAEEQEKLLEES 527
Cdd:pfam15921 441 ECQGQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV----SDLTASLQEKERAIEAT 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 528 NMELEERRKRAEQLRRELEEKEQErldiEEKYTSLQEEAQG---KTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLEN 604
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQTECEAlklQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVE 591
|
170
....*....|....*...
gi 578810113 605 IRQLSRELRLQMLIIDNF 622
Cdd:pfam15921 592 KAQLEKEINDRRLELQEF 609
|
|
| COG5493 |
COG5493 |
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ... |
449-551 |
3.62e-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: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 449 MQAKIDEERKALETKLDMEEEERnKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdllAKAEEQEKLLEESN 528
Cdd:COG5493 1 MSLLKEELKRELLELLREDPEFR-YAVLGLLATKDGLEELLERLEKLEEQMRKWEEQL--------RKLEEEIKKLREQV 71
|
90 100
....*....|....*....|...
gi 578810113 529 MELEERRKRAEQLRRELEEKEQE 551
Cdd:COG5493 72 RKLEEDVKRLEEQERKLEEAMAE 94
|
|
| DUF3498 |
pfam12004 |
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ... |
467-565 |
3.64e-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: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 467 EEEERNKARAELEKREKdllkAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRaeqLRRELE 546
Cdd:pfam12004 373 EESSGPESREELKQAEK----YEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEER---LRRQQE 445
|
90
....*....|....*....
gi 578810113 547 EKEQERLDIEEKYTSLQEE 565
Cdd:pfam12004 446 EKDSQMKSIISRLMAVEEE 464
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
351-552 |
3.79e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.62 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 351 INEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKK---RRGSSSSSSSDSTCSVIEKP 427
Cdd:pfam02029 140 YQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVfldQKRGHPEVKSQNGEEEVTKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 428 LDKFLPNQAGKKKVSPDKMiemqakidEERKALETKLDMEEEERNkaRAELEKREkdllkAQQEHQSLLEKLSALEkkvi 507
Cdd:pfam02029 220 KVTTKRRQGGLSQSQEREE--------EAEVFLEAEQKLEELRRR--RQEKESEE-----FEKLRQKQQEAELELE---- 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578810113 508 vggvDLLAKAEEQEKLLEEsnmelEERRKRAEQLRRELEEKEQER 552
Cdd:pfam02029 281 ----ELKKKREERRKLLEE-----EEQRRKQEEAERKLREEEEKR 316
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
458-567 |
4.00e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.10 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 458 KALETKldmEEEERNKARAELEKREKDLLKAQQEHQsLLEKLSALEKKvivggVDLLAKAEEQeklLEESNMELEERRKR 537
Cdd:pfam12072 54 ALLEAK---EEIHKLRAEAERELKERRNELQRQERR-LLQKEETLDRK-----DESLEKKEES---LEKKEKELEAQQQQ 121
|
90 100 110
....*....|....*....|....*....|.
gi 578810113 538 AEQLRRELEEKEQERLDIEEKYTSL-QEEAQ 567
Cdd:pfam12072 122 LEEKEEELEELIEEQRQELERISGLtSEEAK 152
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
439-575 |
4.01e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 439 KKVSPDKMIEMQAKIDEERKALETKLDMEEE--ERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAK 516
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 578810113 517 AEEQEKLLEesnMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKK 575
Cdd:PTZ00121 1274 AEEARKADE---LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1329
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
444-611 |
4.26e-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: 40.48 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 444 DKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDL---LAKAEEQ 520
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkckLDKSEEN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 521 EKLLEESNMELEER-----------RKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMAD 589
Cdd:pfam05483 575 ARSIEYEVLKKEKQmkilenkcnnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE 654
|
170 180
....*....|....*....|..
gi 578810113 590 LQQEHQREIEgllenIRQLSRE 611
Cdd:pfam05483 655 IIDNYQKEIE-----DKKISEE 671
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
451-613 |
4.43e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvDLLAKAEEQEKLLEESNME 530
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-----TLLAAIADAEDEIERLREK 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 531 LEERRKRAEQLRRELEEKEQERLDIEEKY-----TSLQEEAQGKTKKLKKVWTMLMAAKSEMADLqqehQREIEGLLENI 605
Cdd:PRK02224 615 REALAELNDERRERLAEKRERKRELEAEFdeariEEAREDKERAEEYLEQVEEKLDELREERDDL----QAEIGAVENEL 690
|
....*...
gi 578810113 606 RQLsRELR 613
Cdd:PRK02224 691 EEL-EELR 697
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
361-612 |
4.61e-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: 40.34 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 361 RQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKrrgsssssssdstcSVIEKPLDKFLPNQAGKKK 440
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE--------------EEEEKSRLKKEEKEEEKSE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 441 VSpDKMIEMQAKIDE------ERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIvggvDLL 514
Cdd:pfam02463 769 LS-LKEKELAEEREKteklkvEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL----ELK 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 515 AKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEH 594
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
|
250
....*....|....*...
gi 578810113 595 QREIEGLLENIRQLSREL 612
Cdd:pfam02463 924 KEEAEILLKYEEEPEELL 941
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
445-612 |
4.74e-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: 39.24 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 445 KMIEMQAKIDEE---RKALETKlDMEEEERnkaraeLEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLlAKAEEQE 521
Cdd:pfam00261 65 KLEEAEKAADESergRKVLENR-ALKDEEK------MEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDL-ERAEERA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 522 KLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYtslQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGL 601
Cdd:pfam00261 137 ELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKY---EEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDEL 213
|
170
....*....|....
gi 578810113 602 L---ENIRQLSREL 612
Cdd:pfam00261 214 EaekEKYKAISEEL 227
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
513-618 |
4.81e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.10 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 513 LLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEqERLD-----IEEKYTSLQEeaqgKTKKLKKVWTMLMAAKSEM 587
Cdd:pfam12072 55 LLEAKEEIHKLRAEAERELKERRNELQRQERRLLQKE-ETLDrkdesLEKKEESLEK----KEKELEAQQQQLEEKEEEL 129
|
90 100 110
....*....|....*....|....*....|.
gi 578810113 588 ADLQQEHQREieglLENIRQLSRELRLQMLI 618
Cdd:pfam12072 130 EELIEEQRQE----LERISGLTSEEAKEILL 156
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
451-614 |
4.82e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 451 AKIDEERKALETKLDmEEEERNKARAELEKREKDLLKaqqEHQSLLEKLSALEK-KVIVGGVDLLaKAEEQEKLLEESNM 529
Cdd:PRK03918 317 SRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEK---RLEELEERHELYEEaKAKKEELERL-KKRLTGLTPEKLEK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 530 ELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQ------EEAQGK--------------------TKKLKKVWTMLMAA 583
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKkaieelKKAKGKcpvcgrelteehrkelleeyTAELKRIEKELKEI 471
|
170 180 190
....*....|....*....|....*....|.
gi 578810113 584 KSEMADLQQEhQREIEGLLENIRQLSRELRL 614
Cdd:PRK03918 472 EEKERKLRKE-LRELEKVLKKESELIKLKEL 501
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
454-572 |
5.10e-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: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 454 DEERKALETKLDMEEEERNKA-----RAELEKREKDLLKAQQEHQsllEKLSALEKKVIVGGVDLLAKAEEQEKL----L 524
Cdd:pfam15558 35 EELRRRDQKRQETLERERRLLlqqsqEQWQAEKEQRKARLGREER---RRADRREKQVIEKESRWREQAEDQENQrqekL 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578810113 525 EESNMELEERRKRAEQLRRELEE-----KEQERLDIEEKytsLQEEAQGKTKK 572
Cdd:pfam15558 112 ERARQEAEQRKQCQEQRLKEKEEelqalREQNSLQLQER---LEEACHKRQLK 161
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
456-611 |
5.22e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 456 ERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSalekkvivggvdllaKAEEQEKLLEESNMELEERR 535
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII---------------KNNSEIKDLTNQDSVKELII 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578810113 536 KRAEQLRRELEEKEQErldIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQ---REIEGLLENIRQLSRE 611
Cdd:TIGR04523 457 KNLDNTRESLETQLKV---LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKdltKKISSLKEKIEKLESE 532
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
351-612 |
5.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 351 INEDPKDALLRQFQKEIEELKKKLEEGEEIsgsdisgseeDDDEEGEVGEDGEKRKKRRGSSSSSSSDSTCSVIEKPLDK 430
Cdd:PRK03918 445 LTEEHRKELLEEYTAELKRIEKELKEIEEK----------ERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 431 FLPNQAGKKKVSPDKMIEMQAKIDEERKALETKLDmEEEERNKARAELEKREKDLLkaqqehqsllEKLSALEKKVIVGG 510
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELE----------EELAELLKELEELG 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 511 VDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYtslqeeaqgktKKLKKVWTMLMAAKSEMADL 590
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF-----------EELAETEKRLEELRKELEEL 652
|
250 260
....*....|....*....|...
gi 578810113 591 QQEH-QREIEGLLENIRQLSREL 612
Cdd:PRK03918 653 EKKYsEEEYEELREEYLELSREL 675
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
450-610 |
7.00e-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: 39.95 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 450 QAKIDEErkALETKLDMEEEERNK--ARAELEKREKDLLKAQQEHQSLLEKLSALEKkvivggvdLLAKAEEQEKLLEES 527
Cdd:pfam02463 155 RLEIEEE--AAGSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKA--------LEYYQLKEKLELEEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 528 NMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQ 607
Cdd:pfam02463 225 YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
...
gi 578810113 608 LSR 610
Cdd:pfam02463 305 LER 307
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
476-615 |
7.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 476 AELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDI 555
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578810113 556 EEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQR---EIEGLLENIRQLSRELRLQ 615
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDleqQRKQLEAQIAELQSEIAER 148
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
444-573 |
7.25e-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: 39.67 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 444 DKMIEMQAKIDEERKALETkldMEEEER--NKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvdllakaEEQE 521
Cdd:pfam05622 304 ERLTELQQLLEDANRRKNE---LETQNRlaNQRILELQQQVEELQKALQEQGSKAEDSSLLKQKL-----------EEHL 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578810113 522 KLLEESNMELEERR---------------KRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKL 573
Cdd:pfam05622 370 EKLHEAQSELQKKKeqieelepkqdsnlaQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTL 436
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
518-595 |
7.67e-03 |
|
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.
Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 37.19 E-value: 7.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578810113 518 EEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQ 595
Cdd:pfam17675 37 KETPEELEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEALDEEEEEFWREYNALQLQLLEFQDERD 114
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
453-544 |
7.92e-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: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 453 IDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIvggVDLLAKAEEQ-EKLLEESNMEL 531
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIA---EEAKAEAEAEaERIIAQAEAEI 105
|
90
....*....|....
gi 578810113 532 EERRKRA-EQLRRE 544
Cdd:COG0711 106 EQERAKAlAELRAE 119
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
450-575 |
7.94e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 450 QAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIvggvDLLAKAEEQEKLLEESNM 529
Cdd:PRK12705 51 EAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLE----EREKALSARELELEELEK 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578810113 530 ELEERRKRAEQLRRElEEKEQ--ERLDIEekytsLQEEAQGKTKKLKK 575
Cdd:PRK12705 127 QLDNELYRVAGLTPE-QARKLllKLLDAE-----LEEEKAQRVKKIEE 168
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
447-635 |
8.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 447 IEMQAKIDEERKALETKLDMEEEERNKARAELE---KREKDLlkaQQEHQSLLEKLS------ALEKKvIVGGVDLLAKA 517
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESDL---EQDYQAASDHLNlvqtalRQQEK-IERYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 518 EEQeklLEESNMELEERRKRAEQLRRELEEKEQERLDIeekytslqeeaqgktkklkkvwtmlmaaKSEMADLQQ----E 593
Cdd:PRK04863 361 EER---LEEQNEVVEEADEQQEENEARAEAAEEEVDEL----------------------------KSQLADYQQaldvQ 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578810113 594 HQREIE-----GLLENIRQLsreLRLQMLIIDNFiprdyQEMIENYV 635
Cdd:PRK04863 410 QTRAIQyqqavQALERAKQL---CGLPDLTADNA-----EDWLEEFQ 448
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
438-613 |
9.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 438 KKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVivggvDLLAKA 517
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810113 518 EEQEKLLEESNME-LEERRKRAEQLrreleekeQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAA--KSEMADLQQ-- 592
Cdd:COG4717 370 QEIAALLAEAGVEdEEELRAALEQA--------EEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEel 441
|
170 180
....*....|....*....|..
gi 578810113 593 -EHQREIEGLLENIRQLSRELR 613
Cdd:COG4717 442 eELEEELEELREELAELEAELE 463
|
|
| |
