|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
309-666 |
0e+00 |
|
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: 531.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 309 KGNIRVFCRVRPVLAGESTPSPGFLVFPPGPAGpsdpptGLSLSRSDDRRstltgapaptvrHDFSFDRVFPPGSKQEEV 388
Cdd:cd01366 1 KGNIRVFCRVRPLLPSEENEDTSHITFPDEDGQ------TIELTSIGAKQ------------KEFSFDKVFDPEASQEDV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 389 FEEIAMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGDpqleGLIPRAMRHLFSVAQEMSGQGWTYSFVASYVEIYNE 468
Cdd:cd01366 63 FEEVSPLVQSALDGYNVCIFAYGQTGSGKTYTMEGPPESP----GIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 469 TVRDLLATGPRKGQggECEIRRASPgSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQIS 548
Cdd:cd01366 139 TIRDLLAPGNAPQK--KLEIRHDSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 549 GEHAARGLQCGAPLNLVGLAGSERLDPGlhlgPGERDRLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNS 628
Cdd:cd01366 216 GRNLQTGEISVGKLNLVDLAGSERLNKS----GATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDS 291
|
330 340 350
....*....|....*....|....*....|....*...
gi 6979905 629 LGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVI 666
Cdd:cd01366 292 LGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
311-667 |
1.42e-124 |
|
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: 373.06 E-value: 1.42e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 311 NIRVFCRVRPVLAGEST-PSPGFLVFPPGpagpsdpptglslsrsDDRRSTLTGAPAPTVRHDFSFDRVFPPGSKQEEVF 389
Cdd:smart00129 1 NIRVVVRVRPLNKREKSrKSPSVVPFPDK----------------VGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 390 EEIAM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGgprgDPQLEGLIPRAMRHLFSVAQEMSgQGWTYSFVASYVEIYNE 468
Cdd:smart00129 65 EETAApLVDSVLEGYNATIFAYGQTGSGKTYTMIG----TPDSPGIIPRALKDLFEKIDKRE-EGWQFSVKVSYLEIYNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 469 TVRDLLATGPRKgqggeCEIRRasPGSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQIS 548
Cdd:smart00129 140 KIRDLLNPSSKK-----LEIRE--DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 549 GE--HAARGLQCGAPLNLVGLAGSERLDPGLHLGpgerDRLRETQAINSSLSTLGLVIMALSN--KESHVPYRNSKLTYL 624
Cdd:smart00129 213 QKikNSSSGSGKASKLNLVDLAGSERAKKTGAEG----DRLKEAGNINKSLSALGNVINALAQhsKSRHIPYRDSKLTRL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 6979905 625 LQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVIG 667
Cdd:smart00129 289 LQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNK 331
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
317-664 |
1.07e-119 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 359.96 E-value: 1.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 317 RVRPVLAGESTPSPGFLVfppgpagpSDPPTGLSLSRSDDRRSTLTGapaptvrHDFSFDRVFPPGSKQEEVFEEIAM-L 395
Cdd:pfam00225 1 RVRPLNEREKERGSSVIV--------SVESVDSETVESSHLTNKNRT-------KTFTFDKVFDPEATQEDVYEETAKpL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 396 VQSALDGYPVCIFAYGQTGSGKTFTMEGgprgDPQLEGLIPRAMRHLFSVAQEMSGQgWTYSFVASYVEIYNETVRDLLA 475
Cdd:pfam00225 66 VESVLEGYNVTIFAYGQTGSGKTYTMEG----SDEQPGIIPRALEDLFDRIQKTKER-SEFSVKVSYLEIYNEKIRDLLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 476 tgPRKGQGGECEIRRASpgSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQISGEH---A 552
Cdd:pfam00225 141 --PSNKNKRKLRIREDP--KKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNrstG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 553 ARGLQCGAPLNLVGLAGSERLDpglHLGPGERDRLRETQAINSSLSTLGLVIMALSNKES-HVPYRNSKLTYLLQNSLGG 631
Cdd:pfam00225 217 GEESVKTGKLNLVDLAGSERAS---KTGAAGGQRLKEAANINKSLSALGNVISALADKKSkHIPYRDSKLTRLLQDSLGG 293
|
330 340 350
....*....|....*....|....*....|...
gi 6979905 632 SAKMLMFVNISPLEENVSESLNSLRFASKVNQC 664
Cdd:pfam00225 294 NSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
311-661 |
4.04e-109 |
|
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: 332.68 E-value: 4.04e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 311 NIRVFCRVRPVLAGESTPSPGFLVFPPGpagpsdpptglslsrsddrRSTLTGAPAPTVR--HDFSFDRVFPPGSKQEEV 388
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAKSVISVDGG-------------------KSVVLDPPKNRVAppKTFAFDAVFDSTSTQEEV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 389 FEEIAM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPrgdPQLEGLIPRAMRHLFSVAQEMSGQGWTYSFVASYVEIYN 467
Cdd:cd00106 62 YEGTAKpLVDSALEGYNGTIFAYGQTGSGKTYTMLGPD---PEQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 468 ETVRDLLATGPRKGQggecEIRraSPGSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQI 547
Cdd:cd00106 139 EKIYDLLSPVPKKPL----SLR--EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 548 sgeHAARGLQCGAP-----LNLVGLAGSERLDpglHLGpGERDRLRETQAINSSLSTLGLVIMALS-NKESHVPYRNSKL 621
Cdd:cd00106 213 ---KQRNREKSGESvtsskLNLVDLAGSERAK---KTG-AEGDRLKEGGNINKSLSALGKVISALAdGQNKHIPYRDSKL 285
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 6979905 622 TYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKV 661
Cdd:cd00106 286 TRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRA 325
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
311-663 |
5.15e-84 |
|
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: 267.79 E-value: 5.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 311 NIRVFCRVRPVLAGESTPSPGFLVFppgpagpSDPPTG-LSLSRSDDrrstlTGAPAPTVrhdFSFDRVFPPGSKQEEVF 389
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVD-------VDEKRGqVSVRNPKA-----TANEPPKT---FTFDAVFDPNSKQLDVY 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 390 EEIAM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPrGDPQLEGLIPRAMRHLF-SVAQEMSGQgwTYSFVASYVEIYN 467
Cdd:cd01371 67 DETARpLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKR-EDPELRGIIPNSFAHIFgHIARSQNNQ--QFLVRVSYLEIYN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 468 ETVRDLLAtgprKGQGGECEIRRaSPGS----EELT---VTNAryvpvsceKEVEALLHLAHQNRAVAHTAQNKRSSRSH 540
Cdd:cd01371 144 EEIRDLLG----KDQTKRLELKE-RPDTgvyvKDLSmfvVKNA--------DEMEHVMNLGNKNRSVGATNMNEDSSRSH 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 541 SVFQLQIS----GEHAARGLQCGApLNLVGLAGSERLDPGLHLGpgerDRLRETQAINSSLSTLGLVIMAL-SNKESHVP 615
Cdd:cd01371 211 AIFTITIEcsekGEDGENHIRVGK-LNLVDLAGSERQSKTGATG----ERLKEATKINLSLSALGNVISALvDGKSTHIP 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 6979905 616 YRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQ 663
Cdd:cd01371 286 YRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKN 333
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
312-658 |
6.09e-81 |
|
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: 260.34 E-value: 6.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 312 IRVFCRVRPVLAGEStpspgflvfppgPAGPSDPptglsLSRSDDRRSTLTGApaptvRHDFSFDRVFPPGSKQEEVFEE 391
Cdd:cd01372 3 VRVAVRVRPLLPKEI------------IEGCRIC-----VSFVPGEPQVTVGT-----DKSFTFDYVFDPSTEQEEVYNT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 392 -IAMLVQSALDGYPVCIFAYGQTGSGKTFTMEGG---PRGDPQLeGLIPRAMRHLFSVAQEMSGQgWTYSFVASYVEIYN 467
Cdd:cd01372 61 cVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAytaEEDEEQV-GIIPRAIQHIFKKIEKKKDT-FEFQLKVSFLEIYN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 468 ETVRDLLATGPRKGqgGECEIRRASPGseELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQI 547
Cdd:cd01372 139 EEIRDLLDPETDKK--PTISIREDSKG--GITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 548 SGEHAARGLQCGAP----------LNLVGLAGSERLDPGLHLGpgerDRLRETQAINSSLSTLGLVIMAL---SNKESHV 614
Cdd:cd01372 215 EQTKKNGPIAPMSAddknstftskFHFVDLAGSERLKRTGATG----DRLKEGISINSGLLALGNVISALgdeSKKGAHV 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 6979905 615 PYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFA 658
Cdd:cd01372 291 PYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYA 334
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
311-663 |
9.15e-80 |
|
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: 256.49 E-value: 9.15e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 311 NIRVFCRVRPvLAGESTPSPGFLVFPpgpagpSDPPTGLSLSRSDDRRStltgapaptvrhdFSFDRVFPPGSKQEEVFE 390
Cdd:cd01369 3 NIKVVCRFRP-LNELEVLQGSKSIVK------FDPEDTVVIATSETGKT-------------FSFDRVFDPNTTQEDVYN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 391 EIAM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPrGDPQLEGLIPRAMRHLFSVAQEMSgQGWTYSFVASYVEIYNET 469
Cdd:cd01369 63 FAAKpIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKL-GDPESMGIIPRIVQDIFETIYSMD-ENLEFHVKVSYFEIYMEK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 470 VRDLLatGPRKGQggeCEIRRASpgSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQISG 549
Cdd:cd01369 141 IRDLL--DVSKTN---LSVHEDK--NRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 550 EHAARGLQCGAPLNLVGLAGSERLDPglhlgPGERDR-LRETQAINSSLSTLGLVIMALSNKE-SHVPYRNSKLTYLLQN 627
Cdd:cd01369 214 ENVETEKKKSGKLYLVDLAGSEKVSK-----TGAEGAvLDEAKKINKSLSALGNVINALTDGKkTHIPYRDSKLTRILQD 288
|
330 340 350
....*....|....*....|....*....|....*.
gi 6979905 628 SLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQ 663
Cdd:cd01369 289 SLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKT 324
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
310-672 |
1.95e-76 |
|
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: 249.19 E-value: 1.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 310 GNIRVFCRVRPVLAGESTPSPGFLVFPPGPAGPSDPPTGLSLSRSDDRRstltgapaptVRHDFSFDRVF----PPGSK- 384
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKATRE----------VPKSFSFDYSYwshdSEDPNy 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 385 --QEEVFEEIAM-LVQSALDGYPVCIFAYGQTGSGKTFTMeggpRGDPQLEGLIPRAMRHLFS-----VAQEMSgqgwtY 456
Cdd:cd01365 71 asQEQVYEDLGEeLLQHAFEGYNVCLFAYGQTGSGKSYTM----MGTQEQPGIIPRLCEDLFSriadtTNQNMS-----Y 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 457 SFVASYVEIYNETVRDLLATGPrKGQGGECEIRRaSPgSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRS 536
Cdd:cd01365 142 SVEVSYMEIYNEKVRDLLNPKP-KKNKGNLKVRE-HP-VLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 537 SRSHSVFQLQISGEH--AARGLQCG--APLNLVGLAGSERLDPGlhlgPGERDRLRETQAINSSLSTLGLVIMAL----- 607
Cdd:cd01365 219 SRSHAVFTIVLTQKRhdAETNLTTEkvSKISLVDLAGSERASST----GATGDRLKEGANINKSLTTLGKVISALadmss 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6979905 608 ---SNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCViGTAQAN 672
Cdd:cd01365 295 gksKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIV-NRAVVN 361
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
311-660 |
3.31e-76 |
|
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: 248.01 E-value: 3.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 311 NIRVFCRVRPVLAGESTPSPGFLVFPPGPAGPSDPPTGLSLSRSDDRRstltgapaptvrhdFSFDRVFPPGSKQEEVFE 390
Cdd:cd01364 3 NIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSSTKT--------------YTFDMVFGPEAKQIDVYR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 391 EIAM-LVQSALDGYPVCIFAYGQTGSGKTFTMEG--GPRGDPQLE-----GLIPRAMRHLFsvaQEMSGQGWTYSFVASY 462
Cdd:cd01364 69 SVVCpILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrSPNEEYTWEldplaGIIPRTLHQLF---EKLEDNGTEYSVKVSY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 463 VEIYNETVRDLLAT--GPRKGQGGECEIRRAS----PGSEELTVTNAryvpvsceKEVEALLHLAHQNRAVAHTAQNKRS 536
Cdd:cd01364 146 LEIYNEELFDLLSPssDVSERLRMFDDPRNKRgviiKGLEEITVHNK--------DEVYQILEKGAAKRKTAATLMNAQS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 537 SRSHSVFQLQISGEHAARG----LQCGApLNLVGLAGSERLD-PGlhlgpGERDRLRETQAINSSLSTLGLVIMALSNKE 611
Cdd:cd01364 218 SRSHSVFSITIHIKETTIDgeelVKIGK-LNLVDLAGSENIGrSG-----AVDKRAREAGNINQSLLTLGRVITALVERA 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 6979905 612 SHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASK 660
Cdd:cd01364 292 PHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHR 340
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
373-660 |
8.51e-75 |
|
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: 243.39 E-value: 8.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 373 FSFDRVFPPGSKQEEVFEEIAM-LVQSALDGYPVCIFAYGQTGSGKTFTMeggpRGDPQLEGLIPRAMRHLFSVAQEMSG 451
Cdd:cd01374 41 FTFDHVFGGDSTNREVYELIAKpVVKSALEGYNGTIFAYGQTSSGKTFTM----SGDEDEPGIIPLAIRDIFSKIQDTPD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 452 QgwTYSFVASYVEIYNETVRDLLAtgprkGQGGECEIRRASPGSeeLTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTA 531
Cdd:cd01374 117 R--EFLLRVSYLEIYNEKINDLLS-----PTSQNLKIRDDVEKG--VYVAGLTEEIVSSPEHALSLIARGEKNRHVGETD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 532 QNKRSSRSHSVFQLQIsgEHAARGLQCGAP-----LNLVGLAGSERLDPGLHLGpgerDRLRETQAINSSLSTLGLVIMA 606
Cdd:cd01374 188 MNERSSRSHTIFRITI--ESSERGELEEGTvrvstLNLIDLAGSERAAQTGAAG----VRRKEGSHINKSLLTLGTVISK 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6979905 607 LSNKES--HVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASK 660
Cdd:cd01374 262 LSEGKVggHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASR 317
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
342-660 |
5.58e-71 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 240.80 E-value: 5.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 342 PSDPPTGLSLSRSDDRRSTLTgapapTVRHDFSFDRVFPPGSKQEEVFEE-IAMLVQSALDGYPVCIFAYGQTGSGKTFT 420
Cdd:COG5059 32 PGELGERLINTSKKSHVSLEK-----SKEGTYAFDKVFGPSATQEDVYEEtIKPLIDSLLLGYNCTVFAYGQTGSGKTYT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 421 MEGgprgDPQLEGLIPRAMRHLFS-VAQEMSGQgwTYSFVASYVEIYNETVRDLLatgprkgqgGECEIRRAS--PGSEE 497
Cdd:COG5059 107 MSG----TEEEPGIIPLSLKELFSkLEDLSMTK--DFAVSISYLEIYNEKIYDLL---------SPNEESLNIreDSLLG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 498 LTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQISGEHAARGLQCGAPLNLVGLAGSERLDPGL 577
Cdd:COG5059 172 VKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 578 HLGpgerDRLRETQAINSSLSTLGLVIMALSNKES--HVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSL 655
Cdd:COG5059 252 NRG----TRLKEGASINKSLLTLGNVINALGDKKKsgHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
|
....*
gi 6979905 656 RFASK 660
Cdd:COG5059 328 KFASR 332
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
311-662 |
2.88e-65 |
|
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: 218.75 E-value: 2.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 311 NIRVFCRVRPVLAGESTP---------SPGFLVFPPGPagpSDPPTGLSLSRSDDRRSTLTGapaptvRHDFSFDRVFPP 381
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEgfrrivkvmDNHMLVFDPKD---EEDGFFHGGSNNRDRRKRRNK------ELKYVFDRVFDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 382 GSKQEEVFEE-IAMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRgDPqleGLIPRAMRHLFSVAQEMSGQGwTYSFVA 460
Cdd:cd01370 72 TSTQEEVYEEtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQ-EP---GLMVLTMKELFKRIESLKDEK-EFEVSM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 461 SYVEIYNETVRDLLATgprkgQGGECEIRRASpgSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSH 540
Cdd:cd01370 147 SYLEIYNETIRDLLNP-----SSGPLELREDA--QNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 541 SVFQLQISGEHAARGLQCG---APLNLVGLAGSERLDPGLHLGpgerDRLRETQAINSSLSTLGLVIMALSN---KESHV 614
Cdd:cd01370 220 AVLQITVRQQDKTASINQQvrqGKLSLIDLAGSERASATNNRG----QRLKEGANINRSLLALGNCINALADpgkKNKHI 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 6979905 615 PYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVN 662
Cdd:cd01370 296 PYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAK 343
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
311-661 |
1.24e-63 |
|
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: 214.68 E-value: 1.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 311 NIRVFCRVRPvlAGESTPSPGFlvfppgpagpsdpptGLSLSRSDDRRSTLTGAPAPTvrhdFSFDRVFPPGSKQEEVFE 390
Cdd:cd01373 2 AVKVFVRIRP--PAEREGDGEY---------------GQCLKKLSSDTLVLHSKPPKT----FTFDHVADSNTNQESVFQ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 391 EIAM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGDPQ----LEGLIPRAMRHLFSVAQ---EMSGQGWTYSFVASY 462
Cdd:cd01373 61 SVGKpIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDNEsphgLRGVIPRIFEYLFSLIQrekEKAGEGKSFLCKCSF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 463 VEIYNETVRDLLATGPRKGQGGEcEIRRAspgseeLTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSV 542
Cdd:cd01373 141 LEIYNEQIYDLLDPASRNLKLRE-DIKKG------VYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 543 FQLQISG--EHAARGLQCGAPLNLVGLAGSERLDPGlhlgPGERDRLRETQAINSSLSTLGLVIMALSN----KESHVPY 616
Cdd:cd01373 214 FTCTIESweKKACFVNIRTSRLNLVDLAGSERQKDT----HAEGVRLKEAGNINKSLSCLGHVINALVDvahgKQRHVCY 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 6979905 617 RNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKV 661
Cdd:cd01373 290 RDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRA 334
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
342-661 |
5.11e-63 |
|
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: 212.44 E-value: 5.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 342 PSDPPTGLSLSRSDDRRST-------LTGAPAPTVRHDFSF--DRVFPpGSKQEEVFEEIAM-LVQSALDGYPVCIFAYG 411
Cdd:cd01375 10 PTDDFAHEMIKYGEDGKSIsihlkkdLRRGVVNNQQEDWSFkfDGVLH-NASQELVYETVAKdVVSSALAGYNGTIFAYG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 412 QTGSGKTFTMEGGPRGDPQlEGLIPRAMRHLFSVAQEMSGQgwTYSFVASYVEIYNETVRDLLATGPRKGQG-GECEIRR 490
Cdd:cd01375 89 QTGAGKTFTMTGGTENYKH-RGIIPRALQQVFRMIEERPTK--AYTVHVSYLEIYNEQLYDLLSTLPYVGPSvTPMTILE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 491 ASPgsEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQISGEH--AARGLQCGAPLNLVGLA 568
Cdd:cd01375 166 DSP--QNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSrtLSSEKYITSKLNLVDLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 569 GSERLDpglHLGPGERdRLRETQAINSSLSTLGLVIMALSNKE-SHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEEN 647
Cdd:cd01375 244 GSERLS---KTGVEGQ-VLKEATYINKSLSFLEQAIIALSDKDrTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQ 319
|
330
....*....|....
gi 6979905 648 VSESLNSLRFASKV 661
Cdd:cd01375 320 LEETLSTLRFASRV 333
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
311-662 |
3.10e-62 |
|
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: 210.05 E-value: 3.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 311 NIRVFCRVRPvlagestpspgflvFPPGPAGPSDPPT-----GLSLSRSDDRRSTLTgapaptvrHDFSFDRVFPPGSKQ 385
Cdd:cd01376 1 NVRVAVRVRP--------------FVDGTAGASDPSCvsgidSCSVELADPRNHGET--------LKYQFDAFYGEESTQ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 386 EEVFE-EIAMLVQSALDGYPVCIFAYGQTGSGKTFTMEGgprgDPQLEGLIPRAMRHLFSVAQEmsgQGWTYSFVASYVE 464
Cdd:cd01376 59 EDIYArEVQPIVPHLLEGQNATVFAYGSTGAGKTFTMLG----SPEQPGLMPLTVMDLLQMTRK---EAWALSFTMSYLE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 465 IYNETVRDLLatgprKGQGGECEIRRASPGSeeLTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQ 544
Cdd:cd01376 132 IYQEKILDLL-----EPASKELVIREDKDGN--ILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 545 LQ-ISGEHAARGLQCGAPLNLVGLAGSE---RLDpglhlgpGERDRLRETQAINSSLSTLGLVIMALSNKESHVPYRNSK 620
Cdd:cd01376 205 IKvDQRERLAPFRQRTGKLNLIDLAGSEdnrRTG-------NEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSK 277
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 6979905 621 LTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVN 662
Cdd:cd01376 278 LTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
312-658 |
1.07e-60 |
|
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: 206.86 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 312 IRVFCRVRPVLAGE--STPSPGFLVFppgpagpSDPPTGLSLSRSDDRRSTLTGAPAPTVRhdFSFDRVFPPGSKQEEVF 389
Cdd:cd01368 3 VKVYLRVRPLSKDEleSEDEGCIEVI-------NSTTVVLHPPKGSAANKSERNGGQKETK--FSFSKVFGPNTTQKEFF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 390 EEIAM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGdpqlEGLIPRAMRHLFSVAQEmsgqgwtYSFVASYVEIYNE 468
Cdd:cd01368 74 QGTALpLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGD----GGILPRSLDVIFNSIGG-------YSVFVSYIEIYNE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 469 TVRDLLATGPRKGQGGECEIRRASPGSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQ---L 545
Cdd:cd01368 143 YIYDLLEPSPSSPTKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTiklV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 546 QISGEHAARGLQCG-----APLNLVGLAGSERLDPGLHLGpgerDRLRETQAINSSLSTLGLVIMALSNKE-----SHVP 615
Cdd:cd01368 223 QAPGDSDGDVDQDKdqitvSQLSLVDLAGSERTSRTQNTG----ERLKEAGNINTSLMTLGTCIEVLRENQlqgtnKMVP 298
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 6979905 616 YRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFA 658
Cdd:cd01368 299 FRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
311-661 |
1.24e-52 |
|
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: 184.42 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 311 NIRVFCRVRPVLAGESTPSPGFLVFPPgpagPSDPPTGLSLSRSDDRRSTLTgapaptvRHDFSFDRVFPPGSKQEEVFE 390
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVP----SKLTLIVHEPKLKVDLTKYIE-------NHTFRFDYVFDESSSNETVYR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 391 EIAM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGDPQLEGLIPRAMRHLFSVAQEMSGQGwTYSFVASYVEIYNET 469
Cdd:cd01367 70 STVKpLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAARDVFRLLNKLPYKD-NLGVTVSFFEIYGGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 470 VRDLLATGPRkgqggeCEIRRASPGseELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQISg 549
Cdd:cd01367 149 VFDLLNRKKR------VRLREDGKG--EVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILR- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 550 ehAARGLQCGAPLNLVGLAGSER-LDPGLHlgpgERDRLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNS 628
Cdd:cd01367 220 --DRGTNKLHGKLSFVDLAGSERgADTSSA----DRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDS 293
|
330 340 350
....*....|....*....|....*....|....
gi 6979905 629 L-GGSAKMLMFVNISPLEENVSESLNSLRFASKV 661
Cdd:cd01367 294 FiGENSKTCMIATISPGASSCEHTLNTLRYADRV 327
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
295-474 |
1.94e-52 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 177.41 E-value: 1.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 295 EMERRRLHNQLQELKGNIRVFCRVRPVLAGESTpspgfLVFPpgpagpsdpptglslsrsdDRRSTLTGAPapTVRHDFS 374
Cdd:pfam16796 5 ETLRRKLENSIQELKGNIRVFARVRPELLSEAQ-----IDYP-------------------DETSSDGKIG--SKNKSFS 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 375 FDRVFPPGSKQEEVFEEIAMLVQSALDGYPVCIFAYGQTGSGKTFtmeggprgdpqleGLIPRAMRHLFSVAQEMSgQGW 454
Cdd:pfam16796 59 FDRVFPPESEQEDVFQEISQLVQSCLDGYNVCIFAYGQTGSGSND-------------GMIPRAREQIFRFISSLK-KGW 124
|
170 180
....*....|....*....|
gi 6979905 455 TYSFVASYVEIYNETVRDLL 474
Cdd:pfam16796 125 KYTIELQFVEIYNESSQDLL 144
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
373-660 |
8.66e-43 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 166.65 E-value: 8.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 373 FSFDRVFPPGSKQEEVFEEI-AMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGP--------RGDPQleGLIPRAMRHLF 443
Cdd:PLN03188 134 FTFDSIADPESTQEDIFQLVgAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlSGDQQ--GLTPRVFERLF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 444 SVAQE----MSGQGWTYSFVASYVEIYNETVRDLLATGPRKGQggeceIRRASPGSeeLTVTNARYVPVSCEKEVEALLH 519
Cdd:PLN03188 212 ARINEeqikHADRQLKYQCRCSFLEIYNEQITDLLDPSQKNLQ-----IREDVKSG--VYVENLTEEYVKTMKDVTQLLI 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 520 LAHQNRAVAHTAQNKRSSRSHSVFQLQISG--EHAARGLQC--GAPLNLVGLAGSERLDpglhLGPGERDRLRETQAINS 595
Cdd:PLN03188 285 KGLSNRRTGATSINAESSRSHSVFTCVVESrcKSVADGLSSfkTSRINLVDLAGSERQK----LTGAAGDRLKEAGNINR 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 596 SLSTLGLVIMAL-----SNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASK 660
Cdd:PLN03188 361 SLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQR 430
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
375-606 |
9.01e-24 |
|
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: 98.57 E-value: 9.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 375 FDRVFPPGSKQEEVFEEIAMLVQSALDGYPV-CIFAYGQTGSGKTFTMeggprgdpqlEGLIPRAMRHLFSVAQEMSGQG 453
Cdd:cd01363 22 FYRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETM----------KGVIPYLASVAFNGINKGETEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 454 WTYsfvasyveiynetvrdllatgprkgqggeceirraspgSEELTVTNaryvpvscEKEVEALLHLAHQNRaVAHTAQN 533
Cdd:cd01363 92 WVY--------------------------------------LTEITVTL--------EDQILQANPILEAFG-NAKTTRN 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6979905 534 KRSSRSHSVFQLqisgehaarglqcgaplnLVGLAGSERldpglhlgpgerdrlretqaINSSLSTLGLVIMA 606
Cdd:cd01363 125 ENSSRFGKFIEI------------------LLDIAGFEI--------------------INESLNTLMNVLRA 159
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
298-607 |
1.70e-12 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 70.54 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 298 RRRLHNQLQELKgNIRVFCRVRPVL--AGESTPSPGFlvfppGPAGPSDPPTGLSLSRSDDRRSTltgapaptvrHDFSF 375
Cdd:COG5059 294 TRLLQDSLGGNC-NTRVICTISPSSnsFEETINTLKF-----ASRAKSIKNKIQVNSSSDSSREI----------EEIKF 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 376 DRVFPPGSKQEEVFEEIAMLVQSALDGypvcIFAYGQTGSGKTFTMEggprgdPQLEGLIPRAMRHLFSVAQEMSGQGWT 455
Cdd:COG5059 358 DLSEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK------SRIDLIMKSIISGTFERKKLLKEEGWK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 456 YSFVASYVEIYNETVRDLLATGPRK-----GQGGECEIRRASPGSEELTVTNARYvpvscEKEVeallhlAHQNRAVAHT 530
Cdd:COG5059 428 YKSTLQFLRIEIDRLLLLREEELSKkktkiHKLNKLRHDLSSLLSSIPEETSDRV-----ESEK------ASKLRSSAST 496
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6979905 531 AQNKRSSRSHSVFQLQISGEHAARGLQCgapLNLVGLAGSERLdpglhLGPGERDRLRETQAINSSLSTLGLVIMAL 607
Cdd:COG5059 497 KLNLRSSRSHSKFRDHLNGSNSSTKELS---LNQVDLAGSERK-----VSQSVGELLRETQSLNKSLSSLGDVIHAL 565
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-308 |
1.90e-12 |
|
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: 70.86 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRE 225
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 226 RLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQL 305
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
...
gi 6979905 306 QEL 308
Cdd:TIGR02168 946 SEE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-312 |
1.14e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLElenrglrEQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELE-------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMER 298
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170
....*....|....
gi 6979905 299 RRLHNQLQELKGNI 312
Cdd:TIGR02168 841 EDLEEQIEELSEDI 854
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-313 |
2.02e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMER 298
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170
....*....|....*
gi 6979905 299 RRLHNQLQELKGNIR 313
Cdd:COG1196 410 EALLERLERLEEELE 424
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-313 |
4.81e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRE 225
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 226 RLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQL 305
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
....*...
gi 6979905 306 QELKGNIR 313
Cdd:COG1196 396 AELAAQLE 403
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
137-311 |
1.35e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 137 AWDLKGQLCDLNEELKRYREKTQMLELENR--GLREQLREVQEQATTLGTERNTLEGELASVR-SRAEQDQQRLEtlsar 213
Cdd:COG4913 267 ARERLAELEYLRAALRLWFAQRRLELLEAEleELRAELARLEAELERLEARLDALREELDELEaQIRGNGGDRLE----- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 214 vlELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQvtlLAEQGDRLYG 293
Cdd:COG4913 342 --QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRD 416
|
170
....*....|....*...
gi 6979905 294 LEMERRRLHNQLQELKGN 311
Cdd:COG4913 417 LRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-313 |
1.77e-10 |
|
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: 64.31 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQK-TEAQVTLLAEQGDR----LYG 293
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEEleeeLEE 451
|
170 180
....*....|....*....|
gi 6979905 294 LEMERRRLHNQLQELKGNIR 313
Cdd:TIGR02168 452 LQEELERLEEALEELREELE 471
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
147-309 |
1.89e-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: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 147 LNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRER 226
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 227 LLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQ 306
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
...
gi 6979905 307 ELK 309
Cdd:COG1196 460 ALL 462
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-308 |
1.99e-10 |
|
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: 64.31 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQK---TEAQVTLLAEQ----GDRL 291
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEierlEARL 409
|
170
....*....|....*..
gi 6979905 292 YGLEMERRRLHNQLQEL 308
Cdd:TIGR02168 410 ERLEDRRERLQQEIEEL 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
140-312 |
2.92e-10 |
|
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: 63.55 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERN--------TLEGELASVRSRAEQDQQRLETLS 211
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 212 ARVLELEECLGTR-------ERLLQELQGERLQLQEE-------RSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKT 277
Cdd:TIGR02169 322 ERLAKLEAEIDKLlaeieelEREIEEERKRRDKLTEEyaelkeeLEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
170 180 190
....*....|....*....|....*....|....*
gi 6979905 278 EAQVTLLAEQGDRLYGLEMERRRLHNQLQELKGNI 312
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-309 |
3.76e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRE 225
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 226 RLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQL 305
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
....
gi 6979905 306 QELK 309
Cdd:COG1196 438 EEEE 441
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-309 |
4.30e-10 |
|
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: 63.15 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLE-------GELASVRSRAEQDQQRLETLSA 212
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEeeieelqKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 213 RVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLY 292
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170
....*....|....*..
gi 6979905 293 GLEMERRRLHNQLQELK 309
Cdd:TIGR02168 390 QLELQIASLNNEIERLE 406
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
139-315 |
9.37e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLElenrGLREQLREVQEQATTLGTERNTLE---------GELASVRSRAEQDQQRLET 209
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 210 LSARVLELEECLGTRERLLQELQGERLQLQEERSTLST----QLEEQKRRFQATEAALSSSQEEVvclrQKTEAQVTLLA 285
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAELEEEL----EEAQEELEELE 226
|
170 180 190
....*....|....*....|....*....|
gi 6979905 286 EQGDRLYGlEMERRRLHNQLQELKGNIRVF 315
Cdd:COG4717 227 EELEQLEN-ELEAAALEERLKEARLLLLIA 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-314 |
1.15e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERL-----LQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYG 293
Cdd:TIGR02168 428 KKLEEAELKelqaeLEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
170 180
....*....|....*....|....
gi 6979905 294 ---LEMERRRLHNQLQELKGNIRV 314
Cdd:TIGR02168 508 vkaLLKNQSGLSGILGVLSELISV 531
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
147-287 |
1.34e-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: 59.17 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 147 LNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETL-SARVLE-LEECLGTR 224
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEaLQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6979905 225 ERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQ 287
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-308 |
1.34e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEqgdrlyglemer 298
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE------------ 870
|
170
....*....|
gi 6979905 299 rrLHNQLQEL 308
Cdd:TIGR02168 871 --LESELEAL 878
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
146-312 |
1.90e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.92 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEEclgtre 225
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 226 rLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAqvtllAEQGDRLYGLEMERRRLHNQL 305
Cdd:COG4372 116 -ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA-----LEQELQALSEAEAEQALDELL 189
|
....*..
gi 6979905 306 QELKGNI 312
Cdd:COG4372 190 KEANRNA 196
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-312 |
2.18e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMER 298
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
170 180
....*....|....*....|.
gi 6979905 299 RRL-------HNQLQELKGNI 312
Cdd:TIGR02168 918 EELreklaqlELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-313 |
2.75e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 150 ELKRYREKTQMLElenrglrEQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQ 229
Cdd:TIGR02168 678 EIEELEEKIEELE-------EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 230 ELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVvclrQKTEAQVTLLAEQGDRLYG-LEMERRRLHNQLQEL 308
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREALDELRAeLTLLNEEAANLRERL 826
|
....*
gi 6979905 309 KGNIR 313
Cdd:TIGR02168 827 ESLER 831
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-308 |
3.57e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMER 298
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
170
....*....|
gi 6979905 299 RRLHNQLQEL 308
Cdd:TIGR02169 472 YDLKEEYDRV 481
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
150-313 |
7.50e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 150 ELKRYREKTQMLeleNRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQ 229
Cdd:COG4372 14 SLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 230 ELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQELK 309
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
....
gi 6979905 310 GNIR 313
Cdd:COG4372 171 QELQ 174
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
143-313 |
7.93e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 7.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 143 QLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECL- 221
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLe 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 222 ----------GTRERLLQE---LQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQG 288
Cdd:PRK02224 332 ecrvaaqahnEEAESLREDaddLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
170 180
....*....|....*....|....*
gi 6979905 289 DRLYGLEMERRRLHNQLQELKGNIR 313
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLR 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
142-313 |
8.71e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 142 GQLCDLNEELKRYREKTQMLELENRGLReqLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECL 221
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 222 ---GTRErlLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVT----LLAEQGDRLYGL 294
Cdd:COG4913 333 rgnGGDR--LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEaleeELEALEEALAEA 410
|
170
....*....|....*....
gi 6979905 295 EMERRRLHNQLQELKGNIR 313
Cdd:COG4913 411 EAALRDLRRELRELEAEIA 429
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
139-308 |
9.22e-09 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 58.16 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQlrevqeqATTLGTERNTLEGELASVRSR---AEQDQQRLETLS---- 211
Cdd:pfam19220 115 DKTAQAEALERQLAAETEQNRALEEENKALREE-------AQAAEKALQRAEGELATARERlalLEQENRRLQALSeeqa 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 212 -------ARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEvvcLRQKTEAQVTLL 284
Cdd:pfam19220 188 aelaeltRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEA---LTARAAATEQLL 264
|
170 180
....*....|....*....|....
gi 6979905 285 AEQGDRLYGLEMERRRLHNQLQEL 308
Cdd:pfam19220 265 AEARNQLRDRDEAIRAAERRLKEA 288
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
131-254 |
1.63e-08 |
|
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: 53.84 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 131 RAGKRPAWDLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETL 210
Cdd:pfam10473 13 KESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKK 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 6979905 211 SARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKR 254
Cdd:pfam10473 93 QERVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-287 |
2.51e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6979905 219 -ECLGTRERL------LQELQGERLQLQEE-RSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEA--QVTLLAEQ 287
Cdd:TIGR02168 915 rELEELREKLaqlelrLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgPVNLAAIE 993
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
155-313 |
2.79e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 155 REKTQMLELENRGLREQLREVQEQATTLGTERNTLEG----------------ELASVR---SRAEQDQQRLETLSARVL 215
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeiDVASAEreiAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 216 ELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSqEEVVCLRQKTEAQVTLLAEQGDRLYGLe 295
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-EDLARLELRALLEERFAAALGDAVERE- 766
|
170
....*....|....*...
gi 6979905 296 mERRRLHNQLQELKGNIR 313
Cdd:COG4913 767 -LRENLEERIDALRARLN 783
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
156-308 |
4.80e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.68 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 156 EKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGER 235
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6979905 236 LQLQEERSTLSTQ---LEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRL--YGLEMERRRLHNQLQEL 308
Cdd:COG4372 111 EELQEELEELQKErqdLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeqELQALSEAEAEQALDEL 188
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
139-315 |
7.01e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELEnrglrEQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVDLS-----EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 EclgtrERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVvclrqKTEAQVTLLAEQGDRLyGLEMER 298
Cdd:COG3206 261 Q-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL-----QQEAQRILASLEAELE-ALQARE 329
|
170
....*....|....*..
gi 6979905 299 RRLHNQLQELKGNIRVF 315
Cdd:COG3206 330 ASLQAQLAQLEARLAEL 346
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
149-312 |
7.55e-08 |
|
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: 55.95 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 149 EELKRYREKTQMLELEnrglreqLREVQEQATTLGTERNTLEGEL---ASVRSRAEQDQQRLEtlsARVLELEECLGTRE 225
Cdd:pfam01576 12 EELQKVKERQQKAESE-------LKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLA---ARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 226 RLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLR---QKTEAQVTLLAEQGDRlygLEMERRRLH 302
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEakiKKLEEDILLLEDQNSK---LSKERKLLE 158
|
170
....*....|
gi 6979905 303 NQLQELKGNI 312
Cdd:pfam01576 159 ERISEFTSNL 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-312 |
1.19e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEE 219
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 220 CLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLY-GLEMER 298
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEnKIEDDE 967
|
170
....*....|....
gi 6979905 299 RRLHNQLQELKGNI 312
Cdd:TIGR02168 968 EEARRRLKRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
140-309 |
1.22e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLcdlnEELKRYREKTQmlelENRGLREQLREVQEQAT-----TLGTERNTLEGELASVRSRAEQDQQRLETLSARV 214
Cdd:COG1196 198 LERQL----EPLERQAEKAE----RYRELKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 215 LELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGL 294
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170
....*....|....*
gi 6979905 295 EMERRRLHNQLQELK 309
Cdd:COG1196 350 EEELEEAEAELAEAE 364
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
139-313 |
1.40e-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: 54.00 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERLLQEL----------------QGERL-----QLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKT 277
Cdd:COG4942 104 EELAELLRALYRLgrqpplalllspedflDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6979905 278 EAQ----VTLLAEQGDRLYGLEMERRRLHNQLQELKGNIR 313
Cdd:COG4942 184 EEEraalEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
147-323 |
2.00e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 147 LNEELKRYREKTQMLELEnrglREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEEclgtRER 226
Cdd:PRK03918 212 ISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 227 LLQELQGErlqlQEERSTLSTQLEEQKRRFQATEAALSSSQEEvvclRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQ 306
Cdd:PRK03918 284 ELKELKEK----AEEYIKLSEFYEEYLDELREIEKRLSRLEEE----INGIEERIKELEEKEERLEELKKKLKELEKRLE 355
|
170
....*....|....*..
gi 6979905 307 ELKGNIRVFCRVRPVLA 323
Cdd:PRK03918 356 ELEERHELYEEAKAKKE 372
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-307 |
3.26e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQmlELENRGLR-EQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLEL 217
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVE--EVEERLERaEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 218 EECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATE------AALSSSQEEVVCLRQKTEAQVTLLAEQGDRL 291
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRERL 629
|
170
....*....|....*.
gi 6979905 292 ygleMERRRLHNQLQE 307
Cdd:PRK02224 630 ----AEKRERKRELEA 641
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
141-309 |
3.79e-07 |
|
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: 53.15 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 141 KGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTL-------------EGELASVRSRAEQDQQRL 207
Cdd:pfam05622 189 KRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLretneelrcaqlqQAELSQADALLSPSSDPG 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 208 ETLSARVLELEeclgTRERLLQ-ELQGERLQLQEERS------TLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQ 280
Cdd:pfam05622 269 DNLAAEIMPAE----IREKLIRlQHENKMLRLGQEGSyrerltELQQLLEDANRRKNELETQNRLANQRILELQQQVEEL 344
|
170 180
....*....|....*....|....*....
gi 6979905 281 VTLLAEQGDRLYGLEMERRRLHNQLQELK 309
Cdd:pfam05622 345 QKALQEQGSKAEDSSLLKQKLEEHLEKLH 373
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
139-310 |
4.77e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKtqmleleNRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:COG1340 26 ELKEKRDELNEELKELAEK-------RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTR--------------ERLLQELQGERLQLQEERsTLSTQLEEQKRRFQATEAALsSSQEEVVCLRQKTEAQVTLL 284
Cdd:COG1340 99 KELAELnkaggsidklrkeiERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKAL-EKNEKLKELRAELKELRKEA 176
|
170 180
....*....|....*....|....*.
gi 6979905 285 AEQGDRLYGLEMERRRLHNQLQELKG 310
Cdd:COG1340 177 EEIHKKIKELAEEAQELHEEMIELYK 202
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
139-336 |
5.79e-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: 52.07 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASV------------------RSRA 200
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpplalllsPEDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 201 EQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKteaq 280
Cdd:COG4942 132 LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE---- 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6979905 281 vtlLAEQGDRLYGLEMERRRLHNQLQELKGNIRVfcRVRPVLAGESTPSPGFLVFP 336
Cdd:COG4942 208 ---LAELAAELAELQQEAEELEALIARLEAEAAA--AAERTPAAGFAALKGKLPWP 258
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-306 |
9.42e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTE---AQVTLLAEQGDRLYGLE 295
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAeaaARLLLLLEAEADYEGFL 507
|
170
....*....|.
gi 6979905 296 MERRRLHNQLQ 306
Cdd:COG1196 508 EGVKAALLLAG 518
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-309 |
9.91e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRL-------ETLS 211
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIeeleeeiEELR 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 212 ARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQ----------EEVVCLRQKTEAQV 281
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegSPHVETIEEDRERV 477
|
170 180
....*....|....*....|....*...
gi 6979905 282 TLLAEqgdRLYGLEMERRRLHNQLQELK 309
Cdd:PRK02224 478 EELEA---ELEDLEEEVEEVEERLERAE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-313 |
1.07e-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: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLE-----LENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSAR 213
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEealndLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 214 VLELEEclgtrerLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAAlsssqeevvclrqkteaqvtlLAEQGDRLYG 293
Cdd:TIGR02169 835 IQELQE-------QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA---------------------LRDLESRLGD 886
|
170 180
....*....|....*....|
gi 6979905 294 LEMERRRLHNQLQELKGNIR 313
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIE 906
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-294 |
1.13e-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: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 149 EELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLL 228
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6979905 229 QELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRqkteAQVTLLAEQGDRLYGL 294
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR----AVEEVLKASIQGVHGT 526
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
140-289 |
1.38e-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: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQMLE--LENRGLREQLREvqeqattlgTERNTLEGELASVRSRAEQDQQRLETLSARVLEL 217
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEqkLNRLTLEKEYLE---------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6979905 218 EECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGD 289
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
140-276 |
2.49e-06 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 50.02 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQMLELEnrgLREQLREVQEQATTLgTErntlegELASVRSRAEQDQQRLETLSARVLELEE 219
Cdd:pfam04849 183 LRSEASHLKTETDTYEEKEQQLMSD---CVEQLSEANQQMAEL-SE------ELARKMEENLRQQEEITSLLAQIVDLQH 252
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6979905 220 CLGT----RERLLQELQGER---LQLQEErstlstqLEEQKRRFQATEAALSSSQEEVVCLRQK 276
Cdd:pfam04849 253 KCKElgieNEELQQHLQASKeaqRQLTSE-------LQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
137-259 |
2.61e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 137 AWDLKGQLCDLNEELKRYREKTQMLelenRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARV-- 214
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLea 738
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6979905 215 ------LELEECLGTR----------ERLLQELQGERLQLQEERSTLSTQLEEQKRRFQAT 259
Cdd:COG4913 739 aedlarLELRALLEERfaaalgdaveRELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
139-271 |
2.83e-06 |
|
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: 49.15 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTER--NTLEGELASvrsrAEQDQQRLETlsaRVLE 216
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIES----LKRRISDLED---EILE 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6979905 217 LEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVV 271
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
140-308 |
3.93e-06 |
|
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: 50.17 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLN---EELKRYR----EKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRS-RAEQDQQRLeTLS 211
Cdd:pfam01576 410 LEGQLQELQarlSESERQRaelaEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQElLQEETRQKL-NLS 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 212 ARVLELE-ECLGTRERLLQELQGERlQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDR 290
Cdd:pfam01576 489 TRLRQLEdERNSLQEQLEEEEEAKR-NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
170
....*....|....*...
gi 6979905 291 LYGLEMERRRLHNQLQEL 308
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDL 585
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
143-309 |
4.50e-06 |
|
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: 50.17 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 143 QLCDLNEEL---KRYR---EKT-QMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRA-EQDQQRLEtLSARV 214
Cdd:pfam01576 357 ALEELTEQLeqaKRNKanlEKAkQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLsESERQRAE-LAEKL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 215 LELEECLGTRERLLQELQGERLQLQEERSTLSTQLEE-QKRRFQATEAALSSSQEevvcLRQkTEAQVTLLAEQGDRlyg 293
Cdd:pfam01576 436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDtQELLQEETRQKLNLSTR----LRQ-LEDERNSLQEQLEE--- 507
|
170 180
....*....|....*....|....
gi 6979905 294 lEMERRR--------LHNQLQELK 309
Cdd:pfam01576 508 -EEEAKRnverqlstLQAQLSDMK 530
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
146-308 |
8.41e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSR---AEQDQQRLEtlsaRVLELEECLG 222
Cdd:pfam05557 315 ELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKEltmSNYSPQLLE----RIEEAEDMTQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 223 TRERLLQELQGERLQLQEERSTLSTQ-----LEEQKRRFQATEAALSSSQEEVVCLRQKTEAqvtllaeqgdrlygLEME 297
Cdd:pfam05557 391 KMQAHNEEMEAQLSVAEEELGGYKQQaqtleRELQALRQQESLADPSYSKEEVDSLRRKLET--------------LELE 456
|
170
....*....|.
gi 6979905 298 RRRLHNQLQEL 308
Cdd:pfam05557 457 RQRLREQKNEL 467
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
146-309 |
8.99e-06 |
|
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: 49.02 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELKRyREKTQM--------LELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLEL 217
Cdd:pfam01576 191 DLEERLKK-EEKGRQelekakrkLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 218 EECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEevvcLRQKTEAQVTLLAEqgdrlyGLEME 297
Cdd:pfam01576 270 EAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE----LRSKREQEVTELKK------ALEEE 339
|
170
....*....|..
gi 6979905 298 RRRLHNQLQELK 309
Cdd:pfam01576 340 TRSHEAQLQEMR 351
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
143-301 |
9.97e-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: 48.97 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 143 QLCDLNEELKRYREKTQMLELENRGLREQLREVQEQattlgTERNTLEGElasvrsRAEQDQQRLETLSARVLELEecLG 222
Cdd:pfam17380 436 EVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE-----RKRKKLELE------KEKRDRKRAEEQRRKILEKE--LE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 223 TRERLLQELQGERLQLQEERSTLSTQL-EEQKRRFQATEAALSSSQEEvvclRQKTEAQVTLLAEQGDRLYGLEMERRRL 301
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIyEEERRREAEEERRKQQEMEE----RRRIQEQMRKATEERSRLEAMEREREMM 578
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
147-313 |
1.18e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 147 LNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEeclgtRER 226
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----KLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 227 LLQELQGERLQLQEERSTLSTQLEEQKRRFQA---TEAALSSSQEEVVCLRQK-TEAQVTLLAEQGDRLYGLEMERRRLH 302
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQ 205
|
170
....*....|.
gi 6979905 303 NQLQELKGNIR 313
Cdd:COG4717 206 QRLAELEEELE 216
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
169-313 |
1.38e-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: 48.80 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 169 REQLREVQEQATTLGTErNTLEGELASVRSRAEQdQQRLETLSAR-----------VLELEECLGTRERLLQELQGERLQ 237
Cdd:COG3096 498 RELLRRYRSQQALAQRL-QQLRAQLAELEQRLRQ-QQNAERLLEEfcqrigqqldaAEELEELLAELEAQLEELEEQAAE 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 238 LQEERSTLSTQLEE---QKRRFQATEAALSSSQEEVVCLRQKTEAQVT-------LLAEQGDRLYGLEMERRRLHNQLQE 307
Cdd:COG3096 576 AVEQRSELRQQLEQlraRIKELAARAPAWLAAQDALERLREQSGEALAdsqevtaAMQQLLEREREATVERDELAARKQA 655
|
....*.
gi 6979905 308 LKGNIR 313
Cdd:COG3096 656 LESQIE 661
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
141-258 |
1.46e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 141 KGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQAT----------------------TLGTERNTLEGELASVRS 198
Cdd:pfam00038 3 KEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGaepsrlyslyekeiedlrrqldTLTVERARLQLELDNLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 199 RAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQA 258
Cdd:pfam00038 83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEE 142
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
140-308 |
1.66e-05 |
|
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: 46.05 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEqattlgtERNTLEGELAsvrsRAEQDQQRLETLSARVLELEE 219
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQE-------EVEELRKQLE----NYEKDKQSLKNLKARLKVLEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 220 CLgTRERLLQELQGERL-QLQEERstlstqlEEQKRRFQAteaalssSQEEVvclRQKTEAQVTLLaEQGDRLYGLEMER 298
Cdd:pfam13851 100 EL-KDLKWEHEVLEQRFeKVERER-------DELYDKFEA-------AIQDV---QQKTGLKNLLL-EKKLQALGETLEK 160
|
170
....*....|
gi 6979905 299 RRLhnQLQEL 308
Cdd:pfam13851 161 KEA--QLNEV 168
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
140-257 |
2.07e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKR---YREKTQMLELENRGLREQLREVQEQATTLGTERNTLEgelaSVRSRAEQDQQRLETLSARVLE 216
Cdd:pfam05557 226 LKEEVEDLKRKLEReekYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPE----DLSRRIEQLQQREIVLKEENSS 301
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6979905 217 LEECLGTRERLLQELQGE----RLQLQEERSTLSTQlEEQKRRFQ 257
Cdd:pfam05557 302 LTSSARQLEKARRELEQElaqyLKKIEDLNKKLKRH-KALVRRLQ 345
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-308 |
2.09e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 166 RGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEEclgTRERLLQELQGERLQLQEERSTL 245
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL---ELEEALLAEEEEERELAEAEEER 716
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6979905 246 STQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQEL 308
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
140-310 |
2.39e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQE------QATTLGTER-------NTLEGELASVRSRAEQDQQR 206
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYeeyldelREIEKRLSRLEEEINGIEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 207 LETLSARVLELEECLGTRERLLQELQ--GERLQLQEERSTLSTQLEEQKRRFqaTEAALSSSQEEVVCLRQKTEAQVTLL 284
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEI 407
|
170 180
....*....|....*....|....*.
gi 6979905 285 AEQGDRLYGLEMERRRLHNQLQELKG 310
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKK 433
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
140-308 |
3.04e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQ-------EQATTLGTERNTLEGELASVRSRAEQDQQRLETLSA 212
Cdd:pfam01576 382 LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQarlseseRQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 213 RVLELEECLGTRERLLQELQGERL-------QLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEaqvtlla 285
Cdd:pfam01576 462 DVSSLESQLQDTQELLQEETRQKLnlstrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE------- 534
|
170 180
....*....|....*....|...
gi 6979905 286 EQGDRLYGLEMERRRLHNQLQEL 308
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEAL 557
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
147-254 |
6.87e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 147 LNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVleleeclgtrer 226
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV------------ 73
|
90 100
....*....|....*....|....*...
gi 6979905 227 llQELQGERLQLQEERSTLSTQLEEQKR 254
Cdd:COG1340 74 --KELKEERDELNEKLNELREELDELRK 99
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
143-269 |
7.62e-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: 46.12 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 143 QLCDLNEELKRYREKTQMLELEN--RGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEEC 220
Cdd:TIGR00618 374 QHTLTQHIHTLQQQKTTLTQKLQslCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQC 453
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 6979905 221 LGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEE 269
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
139-368 |
8.65e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETL-------S 211
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 212 ARVLELEECLG--------TRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVvcLRQKTEAQvTL 283
Cdd:COG3883 100 GSVSYLDVLLGsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL--EAAKAELE-AQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 284 LAEQGDRLYGLEMERRRLHNQLQELKGNIRVFCRVRPVLAGESTPSPGFLVFPPGPAGPSDPPTGLSLSRSDDRRSTLTG 363
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
|
....*
gi 6979905 364 APAPT 368
Cdd:COG3883 257 AAAGS 261
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
143-315 |
8.92e-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: 45.66 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 143 QLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASV-----RSRAEQDQQRLETLSARVLEL 217
Cdd:pfam07888 210 QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMaaqrdRTQAELHQARLQAAQLTLQLA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 218 EECLGTRErllqelqgERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEME 297
Cdd:pfam07888 290 DASLALRE--------GRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSE 361
|
170
....*....|....*...
gi 6979905 298 RRRlhnQLQELKGNIRVF 315
Cdd:pfam07888 362 SRR---ELQELKASLRVA 376
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
162-307 |
9.21e-05 |
|
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: 45.88 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 162 ELENRGLreqlrEVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQ-E 240
Cdd:pfam15921 420 ELDDRNM-----EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEsS 494
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6979905 241 ER--STLSTQLEEQKRRFQATEAalsssqeEVVCLRQKTE---AQVTLLAEQGDRLYGLEMERRRLHNQLQE 307
Cdd:pfam15921 495 ERtvSDLTASLQEKERAIEATNA-------EITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAE 559
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
177-276 |
9.78e-05 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.38 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 177 EQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRF 256
Cdd:pfam08614 50 ASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLN 129
|
90 100
....*....|....*....|
gi 6979905 257 QATEAALSSSQEEVVCLRQK 276
Cdd:pfam08614 130 QDLQDELVALQLQLNMAEEK 149
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-270 |
1.28e-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: 45.44 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLG-----------------TRERLLQ------------------------ELQGERLQLQEERSTL---STQLEEQKR 254
Cdd:TIGR02169 938 DPKGedeeipeeelsledvqaELQRVEEeiralepvnmlaiqeyeevlkrldELKEKRAKLEEERKAIlerIEEYEKKKR 1017
|
170
....*....|....*..
gi 6979905 255 R-FQATEAALSSSQEEV 270
Cdd:TIGR02169 1018 EvFMEAFEAINENFNEI 1034
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
161-309 |
1.45e-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: 45.17 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 161 LELENRGLRE---QLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQ 237
Cdd:pfam01576 786 IDAANKGREEavkQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 238 LQEE---RSTLSTQLEEQKRRFQATEAALSSSQEEVVC-----------LRQKTEAQVTLLAEQGDRLYGLEMERRRLHN 303
Cdd:pfam01576 866 LADEiasGASGKSALQDEKRRLEARIAQLEEELEEEQSntellndrlrkSTLQVEQLTTELAAERSTSQKSESARQQLER 945
|
....*.
gi 6979905 304 QLQELK 309
Cdd:pfam01576 946 QNKELK 951
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
149-252 |
1.54e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 149 EELKRYREKTQMLELENRGL-REQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERL 227
Cdd:COG0542 411 EELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|....*
gi 6979905 228 LQELQGERLQLQEERSTLSTQLEEQ 252
Cdd:COG0542 491 EKELAELEEELAELAPLLREEVTEE 515
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-308 |
1.66e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRyREKTQMLELENrGLREQLREVQEQATTLGTERNTLE---GELASVRSRAEQDQQRLETLSARVL 215
Cdd:PRK02224 184 DQRGSLDQLKAQIEE-KEEKDLHERLN-GLESELAELDEEIERYEEQREQARetrDEADEVLEEHEERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 216 ELE----ECLGTRERL---LQELQGERLQLQEERSTL----------STQLEEQKRRFQATEAALSSSQEEVVCLRQKTE 278
Cdd:PRK02224 262 DLRetiaETEREREELaeeVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190
....*....|....*....|....*....|
gi 6979905 279 AQVTLLAEQGDRlygLEMERRRLHNQLQEL 308
Cdd:PRK02224 342 EEAESLREDADD---LEERAEELREEAAEL 368
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
141-313 |
1.67e-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: 45.01 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 141 KGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRL----------ETL 210
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknKSL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 211 SARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEqkrrfqateaaLSSSQEEVVC-LRQKT---EAQVTLLAE 286
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-----------LKDEQNKIKKqLSEKQkelEQNNKKIKE 285
|
170 180 190
....*....|....*....|....*....|..
gi 6979905 287 QGDRLYGLEMERRRLHNQ-----LQELKGNIR 313
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQkeqdwNKELKSELK 317
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
146-271 |
1.89e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELkryREKTQMLELENRGLREQLREVQEQAttlgTERNTLEGELASVRSRAEQD----QQRLETLSARVLE-LEEC 220
Cdd:PRK04863 985 DLNEKL---RQRLEQAEQERTRAREQLRQAQAQL----AQYNQVLASLKSSYDAKRQMlqelKQELQDLGVPADSgAEER 1057
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6979905 221 LGT-RERLLQEL---QGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVV 271
Cdd:PRK04863 1058 ARArRDELHARLsanRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
146-313 |
2.00e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLE------GELASVRSRAEQDQQRLETLSARVLELEE 219
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRE 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 220 CLGT-RER---LLQELQGERLQ-LQEERSTLST----------QLEEQKRRFQATEAALSSSQEEVVCLRQKTEAqvtlL 284
Cdd:PRK02224 628 RLAEkRERkreLEAEFDEARIEeAREDKERAEEyleqveekldELREERDDLQAEIGAVENELEELEELRERREA----L 703
|
170 180
....*....|....*....|....*....
gi 6979905 285 AEQGDRLYGLEMERRRLHNQLQELKGNIR 313
Cdd:PRK02224 704 ENRVEALEALYDEAEELESMYGDLRAELR 732
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
166-313 |
2.13e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 166 RGLREQLREVQEQATTLGTerntLEGELASVRSRAEQdQQRLETLSAR-----------VLELEECLGTRERLLQELQGE 234
Cdd:PRK04863 499 RELLRRLREQRHLAEQLQQ----LRMRLSELEQRLRQ-QQRAERLLAEfckrlgknlddEDELEQLQEELEARLESLSES 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 235 RLQLQEERSTLSTQLEE---QKRRFQATEAALSSSQEEVVCLR------QKTEAQVT-LLAEQGDRLYGLEMERRRLHNQ 304
Cdd:PRK04863 574 VSEARERRMALRQQLEQlqaRIQRLAARAPAWLAAQDALARLReqsgeeFEDSQDVTeYMQQLLERERELTVERDELAAR 653
|
....*....
gi 6979905 305 LQELKGNIR 313
Cdd:PRK04863 654 KQALDEEIE 662
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
129-309 |
2.27e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 129 GKRAGKRPAWD-----LKGQLCDLNEELKRYREKTQMLElenrglrEQLREVQEQATTLGTERNTLEGELASVRSRAEQD 203
Cdd:pfam07888 62 ERYKRDREQWErqrreLESRVAELKEELRQSREKHEELE-------EKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 204 QQRLETLSARVLELEECLgtrERLLQELQGERLQLQEERstlsTQLEEQKRRFQATEAALSSSQEEVVCLR-----QKTE 278
Cdd:pfam07888 135 EEDIKTLTQRVLERETEL---ERMKERAKKAGAQRKEEE----AERKQLQAKLQQTEEELRSLSKEFQELRnslaqRDTQ 207
|
170 180 190
....*....|....*....|....*....|....*.
gi 6979905 279 AQ-----VTLLAEQGDRLYGLEMERRRLHNQLQELK 309
Cdd:pfam07888 208 VLqlqdtITTLTQKLTTAHRKEAENEALLEELRSLQ 243
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
142-308 |
2.47e-04 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 42.50 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 142 GQLCDLNeeLKRYREKTQMLELENRGLREQLREVQEQ-ATTLGTERNTLEgelasvRSRAEQDQQRLEtlsarvleleec 220
Cdd:pfam06785 46 GSLCLLL--LLYYWEDALKEKFEKSFLEEKEAKLTELdAEGFKILEETLE------ELQSEEERLEEE------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 221 lgtrerlLQELQGERLQLQEERSTLSTQLEEQKRRFQA----TEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEM 296
Cdd:pfam06785 106 -------LSQKEEELRRLTEENQQLQIQLQQISQDFAEfrleSEEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLES 178
|
170
....*....|..
gi 6979905 297 ERRRLHNQLQEL 308
Cdd:pfam06785 179 KVRDLNYEIKTL 190
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
137-308 |
2.86e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 137 AWDLKGQLCDLNEELKRYREKTQMLELENRGLREQ--------------LREVQEQATTLGTERNTLEGELASVRSRAEQ 202
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgnaedfLEELREERDELREREAELEATLRTARERVEE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 203 DQQRLET-----------LSARVLELEEClgtRERlLQELQGERLQLQEERSTLSTQLEEQKrrfqateaALSSSQEEVV 271
Cdd:PRK02224 445 AEALLEAgkcpecgqpveGSPHVETIEED---RER-VEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIE 512
|
170 180 190
....*....|....*....|....*....|....*..
gi 6979905 272 CLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQEL 308
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
169-265 |
3.12e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 169 REQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEEclgTRERLLQELQgerlQLQEERstLSTQ 248
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEE---KQQELEAQLE----QLQEKA--AETS 211
|
90
....*....|....*..
gi 6979905 249 LEEQKRRFQATEAALSS 265
Cdd:PRK11448 212 QERKQKRKEITDQAAKR 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
159-309 |
3.23e-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: 42.60 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 159 QMLELENRGLREQLREVQEqattlgtERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQgERLQL 238
Cdd:COG1579 13 QELDSELDRLEHRLKELPA-------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-EQLGN 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6979905 239 ---QEERSTLSTQLEEQKRRFQATEAALSSSQEEvvcLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQELK 309
Cdd:COG1579 85 vrnNKEYEALQKEIESLKRRISDLEDEILELMER---IEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
141-239 |
3.48e-04 |
|
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: 43.95 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 141 KGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARV----LE 216
Cdd:pfam15921 740 RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALdkasLQ 819
|
90 100
....*....|....*....|...
gi 6979905 217 LEECLGTRERllQELQGERLQLQ 239
Cdd:pfam15921 820 FAECQDIIQR--QEQESVRLKLQ 840
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
139-310 |
3.61e-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: 44.01 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQ--MLELENRGLR-----EQLREVQEQATTLGTErntLEGELASvRSRAEQDQQRL-ETL 210
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQaaLARLEEETAQknnalKKIRELEAQISELQED---LESERAA-RNKAEKQRRDLgEEL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 211 SARVLELEECLGT----------RERLLQELQ--------GERLQLQEER-------STLSTQLEEQKRRFQATEAALSS 265
Cdd:pfam01576 302 EALKTELEDTLDTtaaqqelrskREQEVTELKkaleeetrSHEAQLQEMRqkhtqalEELTEQLEQAKRNKANLEKAKQA 381
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6979905 266 SQEEVvclrqkTEAQVTLLAEQGDRLYGlEMERRRLHNQLQELKG 310
Cdd:pfam01576 382 LESEN------AELQAELRTLQQAKQDS-EHKRKKLEGQLQELQA 419
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-292 |
3.66e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 193 LASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVC 272
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100
....*....|....*....|
gi 6979905 273 LRQKTEAQVTLLAEQGDRLY 292
Cdd:COG4942 95 LRAELEAQKEELAELLRALY 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-312 |
3.68e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 162 ELENR--GLREQlREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLEtlsarvleleeclgtrERLLQELQGERLQLQ 239
Cdd:COG1196 197 ELERQlePLERQ-AEKAERYRELKEELKELEAELLLLKLRELEAELEEL----------------EAELEELEAELEELE 259
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6979905 240 EERSTLSTQLEEQKRRFQATEAALSSSQEEvvclrqkteaqvtlLAEQGDRLYGLEMERRRLHNQLQELKGNI 312
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAE--------------EYELLAELARLEQDIARLEERRRELEERL 318
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
139-313 |
4.21e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENrgLREQLREVQEQATTLgteRNTLEGELASvRSRAEQDQQRLETLSARVLELE 218
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEELDLDE--AEEKNEEIQERIDQL---YDILEREVKA-RKYVEKNSDTLPDFLEHAKEQN 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTR-ERLLQ-------ELQgERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVvclrQKTEAQVTLLAEQ--- 287
Cdd:PRK04778 327 KELKEEiDRVKQsytlnesELE-SVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEEL----EEILKQLEEIEKEqek 401
|
170 180
....*....|....*....|....*..
gi 6979905 288 -GDRLYGLEMERRRLHNQLQELKGNIR 313
Cdd:PRK04778 402 lSEMLQGLRKDELEAREKLERYRNKLH 428
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
173-291 |
4.31e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 173 REVQEQATTLGTERN---TLEGELASVR---SRAEQDQQRLETLSARVLELEECLGTRERLL-QELQGERLQLQEERST- 244
Cdd:PRK09039 60 SQIAELADLLSLERQgnqDLQDSVANLRaslSAAEAERSRLQALLAELAGAGAAAEGRAGELaQELDSEKQVSARALAQv 139
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 6979905 245 --LSTQLEEQKRRFQATEAALSSSQEEvvclrqKTEAQVTlLAEQGDRL 291
Cdd:PRK09039 140 elLNQQIAALRRQLAALEAALDASEKR------DRESQAK-IADLGRRL 181
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
169-269 |
4.56e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 43.13 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 169 REQLREVQEQATTLGTERNTLEGELASVRSRAEQD----QQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERST 244
Cdd:pfam15070 287 RQELQETQERLEALTQQNQQLQAQLSLLANPGEGDglesEEEEEEAPRPSLSIPEDFESREAMVAFFNSALAQAEEERAE 366
|
90 100
....*....|....*....|....*
gi 6979905 245 LSTQLEEQKRRFQATEAALSSSQEE 269
Cdd:pfam15070 367 LRRQLKEQKRRCRRLAQQAAPAQEE 391
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
139-252 |
4.60e-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: 42.22 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKtQMlelENRGLREqLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELE 218
Cdd:COG1579 63 RLELEIEEVEARIKKYEEQ-LG---NVRNNKE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
90 100 110
....*....|....*....|....*....|....*...
gi 6979905 219 ECL----GTRERLLQELQGERLQLQEERSTLSTQLEEQ 252
Cdd:COG1579 138 AELeekkAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
130-314 |
4.90e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 130 KRAGKRPAWDLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASV----------RSR 199
Cdd:pfam01576 210 KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELqedleseraaRNK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 200 AEQDQQRL-ETLSARVLELEECLGTRErLLQELQGERLQlqeERSTLSTQLEEQKRRFQAteaalsssqeEVVCLRQKTE 278
Cdd:pfam01576 290 AEKQRRDLgEELEALKTELEDTLDTTA-AQQELRSKREQ---EVTELKKALEEETRSHEA----------QLQEMRQKHT 355
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6979905 279 AQVTLLAEQGDRL----YGLEMERRRLHNQLQELKGNIRV 314
Cdd:pfam01576 356 QALEELTEQLEQAkrnkANLEKAKQALESENAELQAELRT 395
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
192-312 |
5.62e-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: 42.22 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 192 ELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSS--SQEE 269
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKE 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 6979905 270 VVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQELKGNI 312
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-313 |
5.72e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 149 EELKRYREKTQMLELenrglreQLREVQEQATTLGTERNTLE---------GEL-ASVRSRAEQDQQR-LETLSARVLEL 217
Cdd:TIGR02169 177 EELEEVEENIERLDL-------IIDEKRQQLERLRREREKAEryqallkekREYeGYELLKEKEALERqKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 218 EECLGTRERLLQELQGERLQLQEERSTLSTQL----EEQKRRFQATEAALSSSQEEvvcLRQKTEAQVTLLAEQGDRLYG 293
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgEEEQLRVKEKIGELEAEIAS---LERSIAEKERELEDAEERLAK 326
|
170 180
....*....|....*....|
gi 6979905 294 LEMERRRLHNQLQELKGNIR 313
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIE 346
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
167-309 |
5.97e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 167 GLREQLreVQEQATTLGTERNTLE---GELASVRSRAEQDQQRLETLSARVleleeclgtrERLLQELQGERLQLQEERS 243
Cdd:PRK00409 498 GLPENI--IEEAKKLIGEDKEKLNeliASLEELERELEQKAEEAEALLKEA----------EKLKEELEEKKEKLQEEED 565
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6979905 244 TLstqLEEQKRRFQ-ATEAALSSSQEEVVCLRQKTEAQVTLLAEQgdrlyGLEMERRRLHNQLQELK 309
Cdd:PRK00409 566 KL---LEEAEKEAQqAIKEAKKEADEIIKELRQLQKGGYASVKAH-----ELIEARKRLNKANEKKE 624
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
140-313 |
6.91e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREktqmLELENRGLREQLREVQEQATTLGTErntLEGELASVRSRAEQDQQRLETLSARVLELEE 219
Cdd:PRK03918 537 LKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKE---LEELGFESVEELEERLKELEPFYNEYLELKD 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 220 CLGTRERLLQELQGERLQLQEERSTLS---TQLEEQKRRFQatEAALSSSQEEVVCLRQKTEaqvtllaEQGDRLYGLEM 296
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAeteKRLEELRKELE--ELEKKYSEEEYEELREEYL-------ELSRELAGLRA 680
|
170
....*....|....*..
gi 6979905 297 ERRRLHNQLQELKGNIR 313
Cdd:PRK03918 681 ELEELEKRREEIKKTLE 697
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
138-307 |
7.55e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 41.04 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 138 WDLKGQLCDLNEE--------------LKRYREKT-------QMLELENRGLREQLREVQEQATTLGTERNTLEGELasv 196
Cdd:pfam15619 21 AELQSKLEELRKEnrllkrlqkrqekaLGKYEGTEselpqliARHNEEVRVLRERLRRLQEKERDLERKLKEKEAEL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 197 rSRAEQDQQRLETLSarvleleeclgtRERLLqelqGERLQLQEERSTLSTQLEEQKRRFQATEAAL-----SSSQEEVV 271
Cdd:pfam15619 98 -LRLRDQLKRLEKLS------------EDKNL----AEREELQKKLEQLEAKLEDKDEKIQDLERKLelenkSFRRQLAA 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 6979905 272 CLRQKTEAQVTLLAeqgdrlygLEMERRRLHNQLQE 307
Cdd:pfam15619 161 EKKKHKEAQEEVKI--------LQEEIERLQQKLKE 188
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
146-308 |
7.66e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSrAEQDQQRLETLSARVLELEECLGTRE 225
Cdd:pfam12795 27 SLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLS-LEELEQRLLQTSAQLQELQNQLAQLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 226 RLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEvvcLRQKTEAQVTLLAEQgdrlygLEMERRRL--HN 303
Cdd:pfam12795 106 SQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEA---QRWALQAELAALKAQ------IDMLEQELlsNN 176
|
....*
gi 6979905 304 QLQEL 308
Cdd:pfam12795 177 NRQDL 181
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
143-311 |
7.80e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 143 QLCDLNEELKR--------YREKTQMLElENRGLREQLRE----------------VQEQATTLGTE----RNTLEGELA 194
Cdd:pfam15905 95 RLQALEEELEKveaklnaaVREKTSLSA-SVASLEKQLLEltrvnellkakfsedgTQKKMSSLSMElmklRNKLEAKMK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 195 SVRSRAEQ-------DQQRLETLSARVLELEECLGTRERLLQELQGERLQLQE---ERSTLSTQLEEQKRRFQATEAALS 264
Cdd:pfam15905 174 EVMAKQEGmegklqvTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEyitELSCVSEQVEKYKLDIAQLEELLK 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6979905 265 SSQEEVVCLRQKTEAQVTLLAEQ----GDRLYGLEMERRRLHNQLQELKGN 311
Cdd:pfam15905 254 EKNDEIESLKQSLEEKEQELSKQikdlNEKCKLLESEKEELLREYEEKEQT 304
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
146-311 |
8.53e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEEL------KRYREKTQMLELENRGLREQLREVQEQATTLGTERNTlegelasvrsraeQDQQRLETLSARvlELEE 219
Cdd:PRK11281 64 DLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE-------------ETRETLSTLSLR--QLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 220 CLGTRERLLQELQGERLQLQEERSTLSTQLE-------EQKRRFQATEAALSSSQEEVVCLRqkTEAQVTLLAEQGdrLY 292
Cdd:PRK11281 129 RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqaalyANSQRLQQIRNLLKGGKVGGKALR--PSQRVLLQAEQA--LL 204
|
170
....*....|....*....
gi 6979905 293 GLEMERRRlhnqlQELKGN 311
Cdd:PRK11281 205 NAQNDLQR-----KSLEGN 218
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
143-309 |
8.82e-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: 42.85 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 143 QLCDLNEELKRYREKTQMLELEN-------RGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLS---- 211
Cdd:pfam01576 104 HIQDLEEQLDEEEAARQKLQLEKvtteakiKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSklkn 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 212 ---ARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVvclrqkTEAQVTLLAEQG 288
Cdd:pfam01576 184 kheAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEEL------QAALARLEEETA 257
|
170 180
....*....|....*....|.
gi 6979905 289 DRLYGLEmERRRLHNQLQELK 309
Cdd:pfam01576 258 QKNNALK-KIRELEAQISELQ 277
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
146-315 |
9.71e-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: 42.31 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELKRYREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLsarvleLEEclgtRE 225
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL------KKE----NQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 226 RLLQELQgerlQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTE---AQVTLLAEQGDRL----YGLEMER 298
Cdd:TIGR04523 381 SYKQEIK----NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErlkETIIKNNSEIKDLtnqdSVKELII 456
|
170
....*....|....*..
gi 6979905 299 RRLHNQLQELKGNIRVF 315
Cdd:TIGR04523 457 KNLDNTRESLETQLKVL 473
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
143-308 |
1.01e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 143 QLCDLNEELKRYREKTQMLELENRGLREQLREVQEQATTlgterntlegelasvrsrAEQDQQRLETLSARVL-ELEEcl 221
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE------------------AQQNYERELVLHAEDIkALQA-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 222 gTRERLlQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALsssQEEVVCLRQKTEAqvtlLAEQgdrlyglemeRRRL 301
Cdd:pfam07926 62 -LREEL-NELKAEIAELKAEAESAKAELEESEESWEEQKKEL---EKELSELEKRIED----LNEQ----------NKLL 122
|
....*..
gi 6979905 302 HNQLQEL 308
Cdd:pfam07926 123 HDQLESL 129
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
149-313 |
1.09e-03 |
|
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: 42.26 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 149 EELKRYREKTQMLELENRGLREQLrevQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSarvlELEECLGTRERLL 228
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCT---PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT----QKREAQEEQLKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 229 QELQGERLQLQEERSTLSTQLEEQKRRFQATEAA-LSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQE 307
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRARKAApLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
....*.
gi 6979905 308 LKGNIR 313
Cdd:TIGR00618 340 IEEQRR 345
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
160-276 |
1.21e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 160 MLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARvleleeclgTRERLLQELQGERLQLQ 239
Cdd:COG1842 27 MLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEK---------GREDLAREALERKAELE 97
|
90 100 110
....*....|....*....|....*....|....*..
gi 6979905 240 EERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQK 276
Cdd:COG1842 98 AQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
140-310 |
1.50e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQmleLENRGLREQLREVQEQATTLGTERNTLEGELasvrSRAEQDQQRL-ETLSARVLELE 218
Cdd:pfam09787 66 LRGQIQQLRTELQELEAQQQ---EEAESSREQLQELEEQLATERSARREAEAEL----ERLQEELRYLeEELRRSKATLQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRErllQELQGERLQLQEERSTLSTQLEEQKRRFQATEAalsssqeevvcLRQKTEAQVTLLAEQGDRLYGLEmer 298
Cdd:pfam09787 139 SRIKDRE---AEIEKLRNQLTSKSQSSSSQSELENRLHQLTET-----------LIQKQTMLEALSTEKNSLVLQLE--- 201
|
170
....*....|..
gi 6979905 299 rRLHNQLQELKG 310
Cdd:pfam09787 202 -RMEQQIKELQG 212
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
173-312 |
1.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 173 REVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQ 252
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 253 KRRFQATEAALSSSQEEVvclrQKTEAQVTLLAEQgdrLYGLEMERRRLHNQLQELKGNI 312
Cdd:COG4372 86 NEQLQAAQAELAQAQEEL----ESLQEEAEELQEE---LEELQKERQDLEQQRKQLEAQI 138
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
140-313 |
1.60e-03 |
|
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: 41.88 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQMLeLENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQD-------QQRLETLSA 212
Cdd:TIGR00618 499 LQEEPCPLCGSCIHPNPARQDI-DNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLkeqmqeiQQSFSILTQ 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 213 RVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLY 292
Cdd:TIGR00618 578 CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQ 657
|
170 180
....*....|....*....|.
gi 6979905 293 GLEMERRRLHNQLQELKGNIR 313
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASR 678
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
150-269 |
1.78e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 150 ELKRYREKTQMLELENRGLREQLREvqeqattlgtERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLgTRERLlq 229
Cdd:pfam07888 273 ELHQARLQAAQLTLQLADASLALRE----------GRARWAQERETLQQSAEADKDRIEKLSAELQRLEERL-QEERM-- 339
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 6979905 230 ELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEE 269
Cdd:pfam07888 340 EREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKE 379
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
146-309 |
1.84e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 146 DLNEELKRYREKTQMLELEnrglreQLREVQEQATTLGTERNTLEGELASVRSRAEqdqqRLETLSARVLELEECLGTRE 225
Cdd:PRK03918 500 ELAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 226 RLLQELQGERLQLQEErstlstQLEEQKRRFQATEAA------LSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERR 299
Cdd:PRK03918 570 EELAELLKELEELGFE------SVEELEERLKELEPFyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
170
....*....|
gi 6979905 300 RLHNQLQELK 309
Cdd:PRK03918 644 ELRKELEELE 653
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
154-269 |
1.90e-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: 41.21 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 154 YREKTQMLELENRGLREQ--------LREVQEQATTLGTERNTLEGELASVrsraeqdQQRLETLSARVLELEECL---- 221
Cdd:pfam05622 280 IREKLIRLQHENKMLRLGqegsyrerLTELQQLLEDANRRKNELETQNRLA-------NQRILELQQQVEELQKALqeqg 352
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6979905 222 ------GTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQAT--------EAALSSSQEE 269
Cdd:pfam05622 353 skaedsSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNlaqkidelQEALRKKDED 414
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
148-254 |
2.30e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 148 NEELKRYREKTQMLElenrglrEQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEEclgtrerL 227
Cdd:pfam20492 26 QEELEESEETAEELE-------EERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQE-------E 91
|
90 100
....*....|....*....|....*..
gi 6979905 228 LQELQGERLQLQEERSTLSTQLEEQKR 254
Cdd:pfam20492 92 IARLEEEVERKEEEARRLQEELEEARE 118
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
164-279 |
2.94e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.81 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 164 ENRGLREQLREvqeqattLGTERNTLEGELASvrsraeqDQQRLETLSARVLELEEclgtrerLLQELQGERLQLQEERS 243
Cdd:pfam05911 682 ENKRLKEEFEQ-------LKSEKENLEVELAS-------CTENLESTKSQLQESEQ-------LIAELRSELASLKESNS 740
|
90 100 110
....*....|....*....|....*....|....*.
gi 6979905 244 TLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEA 279
Cdd:pfam05911 741 LAETQLKCMAESYEDLETRLTELEAELNELRQKFEA 776
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
137-306 |
3.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 137 AWDLKGQLCDLNEELKR---YREKTQMLELENRGLREQLREVQEQATtlgtERNTLEGELASVRSR-AEQDQQRLETLSA 212
Cdd:COG4717 349 LQELLREAEELEEELQLeelEQEIAALLAEAGVEDEEELRAALEQAE----EYQELKEELEELEEQlEELLGELEELLEA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 213 RVLE-LEECLGTRERLLQELQGERLQLQEERSTLSTQLEEqkrrfQATEAALSSSQEEvvclRQKTEAQVTLLAEQGDRL 291
Cdd:COG4717 425 LDEEeLEEELEELEEELEELEEELEELREELAELEAELEQ-----LEEDGELAELLQE----LEELKAELRELAEEWAAL 495
|
170
....*....|....*....
gi 6979905 292 ----YGLEMERRRLHNQLQ 306
Cdd:COG4717 496 klalELLEEAREEYREERL 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
131-258 |
3.37e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 131 RAGKRPAWDLKGQLCDLNEELKR---YREKTQMLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRL 207
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6979905 208 ETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQA 258
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-270 |
3.49e-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: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 147 LNEELKRYREKTQMLelenRGLREQLREVQEQ-ATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELeeclgtre 225
Cdd:COG3206 279 LAELSARYTPNHPDV----IALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL-------- 346
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6979905 226 rllQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEV 270
Cdd:COG3206 347 ---PELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
140-290 |
3.84e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREktqmlelENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEE 219
Cdd:COG4372 92 AQAELAQAQEELESLQE-------EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6979905 220 CLGTRERLLQELqgERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDR 290
Cdd:COG4372 165 ELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
148-313 |
4.39e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 148 NEELKRYREKTQMLELENRGLREQLREVQEQATTLGtERNTLEGELASVRSRAEQDQQRLETLSArVLELEECLGTRERL 227
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKK-ATESLEEQLAAAEAEQELEESKRETETG-IQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 228 LQELQGErlqLQEERSTLSTqlEEQKRRFQATEAALSSSQEEvvcLRQKTEAQVTLLAEQG-DRLYGLEMERRRLHNQLQ 306
Cdd:COG5185 352 LTENLEA---IKEEIENIVG--EVELSKSSEELDSFKDTIES---TKESLDEIPQNQRGYAqEILATLEDTLKAADRQIE 423
|
....*..
gi 6979905 307 ELKGNIR 313
Cdd:COG5185 424 ELQRQIE 430
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
212-307 |
4.87e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 37.98 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 212 ARVLELEECLGTRERLLQELQGE---RLQLQEERSTLSTQLEEQKRRFQateAALSSSQEEVvclRQkteaqvtLLAEQG 288
Cdd:pfam09744 47 EHNVELEELREDNEQLETQYEREkalRKRAEEELEEIEDQWEQETKDLL---SQVESLEEEN---RR-------LEADHV 113
|
90
....*....|....*....
gi 6979905 289 DRLYGLEMERRRLHNQLQE 307
Cdd:pfam09744 114 SRLEEKEAELKKEYSKLHE 132
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
168-302 |
5.43e-03 |
|
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: 37.66 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 168 LREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLST 247
Cdd:pfam10473 8 VLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTK 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6979905 248 QLEEQKRRFQATEAALSSSQEevvCLRQKTEAQVTLLAEQGDRLYGLEMERRRLH 302
Cdd:pfam10473 88 ELQKKQERVSELESLNSSLEN---LLEEKEQEKVQMKEESKTAVEMLQTQLKELN 139
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-309 |
5.56e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 153 RYREKTQmlELENRglreqLREVQEQATTLGTERNTLEGELASVRSRAEQDQQ------RLETLSARVL-----ELEECL 221
Cdd:TIGR02168 169 KYKERRK--ETERK-----LERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaELRELELALLvlrleELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 222 GTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRL 301
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
....*...
gi 6979905 302 HNQLQELK 309
Cdd:TIGR02168 322 EAQLEELE 329
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
140-300 |
6.41e-03 |
|
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: 39.81 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 140 LKGQLCDLNEELKRYREKTQMLELENRGLREQLRE--------------VQEQATTLGTERNTLEGELASV--------R 197
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDkdkqlaglkervksLQTDSSNTDTALTTLEEALSEKeriierlkE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 198 SRAEQDQQR---LETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLR 274
Cdd:pfam10174 458 QREREDRERleeLESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLE 537
|
170 180 190
....*....|....*....|....*....|..
gi 6979905 275 ------QKTEAQVTLLAEQGDRLYGLEMERRR 300
Cdd:pfam10174 538 nqlkkaHNAEEAVRTNPEINDRIRLLEQEVAR 569
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
147-307 |
7.23e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 147 LNEELKRYreKTQMLELENRGlREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRER 226
Cdd:pfam01576 336 LEEETRSH--EAQLQEMRQKH-TQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEG 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 227 LLQELQG-------ERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQ-------GDRLY 292
Cdd:pfam01576 413 QLQELQArlseserQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEEtrqklnlSTRLR 492
|
170
....*....|....*
gi 6979905 293 GLEMERRRLHNQLQE 307
Cdd:pfam01576 493 QLEDERNSLQEQLEE 507
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
176-266 |
7.28e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 39.31 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 176 QEQATTLGTERNTLEGELASVRSRAEQDQQRLETlsarvleleeclgtrerLLQELQGERLQLQEERSTLSTQLEEQKRR 255
Cdd:PRK10920 59 KQQAQNQTATNDALANQLTALQKAQESQKQELEG-----------------ILKQQAKALDQANRQQAALAKQLDELQQK 121
|
90
....*....|.
gi 6979905 256 FqateAALSSS 266
Cdd:PRK10920 122 V----ATISGS 128
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
150-300 |
7.40e-03 |
|
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: 39.72 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 150 ELKRYREkTQMLELENRGLREQLREVQEQATTLGT-----ERNTLEGELASVRSRAEQDQQRLETLsaRVLELEeclgtR 224
Cdd:pfam17380 373 EISRMRE-LERLQMERQQKNERVRQELEAARKVKIleeerQRKIQQQKVEMEQIRAEQEEARQREV--RRLEEE-----R 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 225 ERLLQELQGERLQLQEERSTLSTQLEEQKRR-----FQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDR-LYGLEMER 298
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKkleleKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRkLLEKEMEE 524
|
..
gi 6979905 299 RR 300
Cdd:pfam17380 525 RQ 526
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
139-307 |
7.60e-03 |
|
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: 39.42 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKRYREKTQMLELENRGLREQLREVQeqattlgTERNTLEGELASVRSRAEQdQQRLETLSARVLELE 218
Cdd:pfam10174 555 EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVE-------NEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHG 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 219 ECLGTRERLLQELQGERLQLQEERSTLSTQLEE-------QKRRFQATEAALSSSQEEvvclrqkteaqvtlLAEQGDRL 291
Cdd:pfam10174 627 QQEMKKKGAQLLEEARRREDNLADNSQQLQLEElmgalekTRQELDATKARLSSTQQS--------------LAEKDGHL 692
|
170
....*....|....*.
gi 6979905 292 YGLEMERRRlhnQLQE 307
Cdd:pfam10174 693 TNLRAERRK---QLEE 705
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
139-269 |
8.33e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 139 DLKGQLCDLNEELKR-----YREKTQMLElENRGLREQLREVQEQATtlgTERNTLEGELASVRSRAEQDQQRLETLSAR 213
Cdd:PRK04863 953 DAKQQAFALTEVVQRrahfsYEDAAEMLA-KNSDLNEKLRQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKSS 1028
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6979905 214 VLELEECLGTRERLLQEL-----QGERLQLQEERSTLSTQLEEQKRRFQATEAALSSSQEE 269
Cdd:PRK04863 1029 YDAKRQMLQELKQELQDLgvpadSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAE 1089
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
142-262 |
8.40e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6979905 142 GQLCDLNEELKRYREKtqmLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAE---QDQQRLETL-------- 210
Cdd:PRK04863 547 GKNLDDEDELEQLQEE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPawlAAQDALARLreqsgeef 623
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6979905 211 --SARVLELEECLGTRERllqELQGERLQLQEERStlstQLEEQKRRFQATEAA 262
Cdd:PRK04863 624 edSQDVTEYMQQLLERER---ELTVERDELAARKQ----ALDEEIERLSQPGGS 670
|
|
| |
