|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
328-685 |
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: 538.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 328 KGNIRVFCRVRPVLEGESTPSPGFLVFPPGPAGpsdpptRLCLSRSDDRRstltrapaaatrHDFSFDRVFPPGSKQEEV 407
Cdd:cd01366 1 KGNIRVFCRVRPLLPSEENEDTSHITFPDEDGQ------TIELTSIGAKQ------------KEFSFDKVFDPEASQEDV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 408 FEEISMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGDpqleGLIPRAMRHLFSVAQEMSGQGWTYSFVASYVEIYNE 487
Cdd:cd01366 63 FEEVSPLVQSALDGYNVCIFAYGQTGSGKTYTMEGPPESP----GIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 488 TVRDLLATGtrKGQGGDCEIRRAgPGSEELTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHSVFQLQIS 567
Cdd:cd01366 139 TIRDLLAPG--NAPQKKLEIRHD-SEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 568 GEHAARGLQCGAPLNLVDLAGSERLDPGltlgPGERDRLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNS 647
Cdd:cd01366 216 GRNLQTGEISVGKLNLVDLAGSERLNKS----GATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDS 291
|
330 340 350
....*....|....*....|....*....|....*...
gi 54312052 648 LGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVI 685
Cdd:cd01366 292 LGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
330-686 |
4.22e-127 |
|
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: 379.99 E-value: 4.22e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 330 NIRVFCRVRPVLEGEST-PSPGFLVFPPGpagpsdpptrlclsrsDDRRSTLTRAPAAATRHDFSFDRVFPPGSKQEEVF 408
Cdd:smart00129 1 NIRVVVRVRPLNKREKSrKSPSVVPFPDK----------------VGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 409 EEISM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGgprgDPQLEGLIPRAMRHLFSVAQEMSgQGWTYSFVASYVEIYNE 487
Cdd:smart00129 65 EETAApLVDSVLEGYNATIFAYGQTGSGKTYTMIG----TPDSPGIIPRALKDLFEKIDKRE-EGWQFSVKVSYLEIYNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 488 TVRDLLATgtrkgQGGDCEIRRagPGSEELTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHSVFQLQIS 567
Cdd:smart00129 140 KIRDLLNP-----SSKKLEIRE--DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 568 GE--HAARGLQCGAPLNLVDLAGSERLDPGLTLGpgerDRLRETQAINSSLSTLGLVIMALSN--KESHVPYRNSKLTYL 643
Cdd:smart00129 213 QKikNSSSGSGKASKLNLVDLAGSERAKKTGAEG----DRLKEAGNINKSLSALGNVINALAQhsKSRHIPYRDSKLTRL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 54312052 644 LQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVIG 686
Cdd:smart00129 289 LQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNK 331
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
336-683 |
2.37e-120 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 362.28 E-value: 2.37e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 336 RVRPVLEGESTPSPGFLVFPPGPAGPSDPPTRLCLSRSDdrrstltrapaaatrHDFSFDRVFPPGSKQEEVFEE-ISML 414
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESSHLTNKNRT---------------KTFTFDKVFDPEATQEDVYEEtAKPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 415 VQSALDGYPVCIFAYGQTGSGKTFTMEGgprgDPQLEGLIPRAMRHLFSVAQEMSGQgWTYSFVASYVEIYNETVRDLLA 494
Cdd:pfam00225 66 VESVLEGYNVTIFAYGQTGSGKTYTMEG----SDEQPGIIPRALEDLFDRIQKTKER-SEFSVKVSYLEIYNEKIRDLLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 495 TGTRKGQggDCEIRRAGpgSEELTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHSVFQLQISGEH---A 571
Cdd:pfam00225 141 PSNKNKR--KLRIREDP--KKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNrstG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 572 ARGLQCGAPLNLVDLAGSERLDpglTLGPGERDRLRETQAINSSLSTLGLVIMALSNKES-HVPYRNSKLTYLLQNSLGG 650
Cdd:pfam00225 217 GEESVKTGKLNLVDLAGSERAS---KTGAAGGQRLKEAANINKSLSALGNVISALADKKSkHIPYRDSKLTRLLQDSLGG 293
|
330 340 350
....*....|....*....|....*....|...
gi 54312052 651 SAKMLMFVNISPLEENVSESLNSLRFASKVNQC 683
Cdd:pfam00225 294 NSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
330-680 |
9.54e-113 |
|
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: 342.70 E-value: 9.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 330 NIRVFCRVRPVLEGESTPSPGFLVFPPGpagpsdpptrlclsrsddrRSTLTRAPA--AATRHDFSFDRVFPPGSKQEEV 407
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAKSVISVDGG-------------------KSVVLDPPKnrVAPPKTFAFDAVFDSTSTQEEV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 408 FEEI-SMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPrgdPQLEGLIPRAMRHLFSVAQEMSGQGWTYSFVASYVEIYN 486
Cdd:cd00106 62 YEGTaKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPD---PEQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 487 ETVRDLLAtgtrKGQGGDCEIRRAGpgSEELTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHSVFQLQI 566
Cdd:cd00106 139 EKIYDLLS----PVPKKPLSLREDP--KRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 567 sgeHAARGLQCGAP-----LNLVDLAGSERLDPGLTlgpgERDRLRETQAINSSLSTLGLVIMALS-NKESHVPYRNSKL 640
Cdd:cd00106 213 ---KQRNREKSGESvtsskLNLVDLAGSERAKKTGA----EGDRLKEGGNINKSLSALGKVISALAdGQNKHIPYRDSKL 285
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 54312052 641 TYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKV 680
Cdd:cd00106 286 TRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRA 325
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
330-682 |
4.22e-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: 268.56 E-value: 4.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 330 NIRVFCRVRPVLEGESTPSpgflvfppgpagpsdpptRLCLSRSDDRRSTLT----RAPAAATRHDFSFDRVFPPGSKQE 405
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAG------------------ALQIVDVDEKRGQVSvrnpKATANEPPKTFTFDAVFDPNSKQL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 406 EVFEEISM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPrGDPQLEGLIPRAMRHLF-SVAQEMSGQgwTYSFVASYVE 483
Cdd:cd01371 64 DVYDETARpLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKR-EDPELRGIIPNSFAHIFgHIARSQNNQ--QFLVRVSYLE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 484 IYNETVRDLLAtgtrKGQGGDCEIR-RAGPGS--EELT---VTNAryvpvsceKEVEALLHLAQQNRAVARTAQNERSSR 557
Cdd:cd01371 141 IYNEEIRDLLG----KDQTKRLELKeRPDTGVyvKDLSmfvVKNA--------DEMEHVMNLGNKNRSVGATNMNEDSSR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 558 SHSVFQLQIS----GEHAARGLQCGApLNLVDLAGSERLDPGLTLGpgerDRLRETQAINSSLSTLGLVIMAL-SNKESH 632
Cdd:cd01371 209 SHAIFTITIEcsekGEDGENHIRVGK-LNLVDLAGSERQSKTGATG----ERLKEATKINLSLSALGNVISALvDGKSTH 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 54312052 633 VPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQ 682
Cdd:cd01371 284 IPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKN 333
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
331-677 |
1.41e-83 |
|
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: 267.66 E-value: 1.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 331 IRVFCRVRPVLEGEStpspgflvfppgpagpsDPPTRLCLSRSDDrrstlTRAPAAATRHDFSFDRVFPPGSKQEEVFEE 410
Cdd:cd01372 3 VRVAVRVRPLLPKEI-----------------IEGCRICVSFVPG-----EPQVTVGTDKSFTFDYVFDPSTEQEEVYNT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 411 -ISMLVQSALDGYPVCIFAYGQTGSGKTFTMEGG---PRGDPQLeGLIPRAMRHLFSVAQEMSGQgWTYSFVASYVEIYN 486
Cdd:cd01372 61 cVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAytaEEDEEQV-GIIPRAIQHIFKKIEKKKDT-FEFQLKVSFLEIYN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 487 ETVRDLLATGTRKGqgGDCEIRRAGPGseELTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHSVFQLQI 566
Cdd:cd01372 139 EEIRDLLDPETDKK--PTISIREDSKG--GITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 567 SGEHAARGLQCGAP----------LNLVDLAGSERLDPGLTLGpgerDRLRETQAINSSLSTLGLVIMAL---SNKESHV 633
Cdd:cd01372 215 EQTKKNGPIAPMSAddknstftskFHFVDLAGSERLKRTGATG----DRLKEGISINSGLLALGNVISALgdeSKKGAHV 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 54312052 634 PYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFA 677
Cdd:cd01372 291 PYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYA 334
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
330-682 |
4.12e-82 |
|
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: 263.04 E-value: 4.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 330 NIRVFCRVRPVLEGEstpspgflVFPPGPAGPSDPPTRLCLSRSDDRRSTltrapaaatrhdFSFDRVFPPGSKQEEVFE 409
Cdd:cd01369 3 NIKVVCRFRPLNELE--------VLQGSKSIVKFDPEDTVVIATSETGKT------------FSFDRVFDPNTTQEDVYN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 410 EISM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPrGDPQLEGLIPRAMRHLFSVAQEMSgQGWTYSFVASYVEIYNET 488
Cdd:cd01369 63 FAAKpIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKL-GDPESMGIIPRIVQDIFETIYSMD-ENLEFHVKVSYFEIYMEK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 489 VRDLLATGTR-------KGQGgdceirragpgseeLTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHSV 561
Cdd:cd01369 141 IRDLLDVSKTnlsvhedKNRG--------------PYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 562 FQLQISGEHAARGLQCGAPLNLVDLAGSERLDP----GLTLgpgerdrlRETQAINSSLSTLGLVIMALSNKE-SHVPYR 636
Cdd:cd01369 207 FLINVKQENVETEKKKSGKLYLVDLAGSEKVSKtgaeGAVL--------DEAKKINKSLSALGNVINALTDGKkTHIPYR 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 54312052 637 NSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQ 682
Cdd:cd01369 279 DSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKT 324
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
330-679 |
9.56e-79 |
|
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: 255.33 E-value: 9.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 330 NIRVFCRVRPVLEGESTPSpgflvfppgpagpsdppTRLCLSRSDDRRSTLTR---APAAATRHDFSFDRVFPPGSKQEE 406
Cdd:cd01364 3 NIQVVVRCRPFNLRERKAS-----------------SHSVVEVDPVRKEVSVRtggLADKSSTKTYTFDMVFGPEAKQID 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 407 VFEE-ISMLVQSALDGYPVCIFAYGQTGSGKTFTMEG--GPRGDPQLE-----GLIPRAMRHLFsvaQEMSGQGWTYSFV 478
Cdd:cd01364 66 VYRSvVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrSPNEEYTWEldplaGIIPRTLHQLF---EKLEDNGTEYSVK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 479 ASYVEIYNETVRDLLAT--GTRKGQGGDCEIRRAG----PGSEELTVTNAryvpvsceKEVEALLHLAQQNRAVARTAQN 552
Cdd:cd01364 143 VSYLEIYNEELFDLLSPssDVSERLRMFDDPRNKRgviiKGLEEITVHNK--------DEVYQILEKGAAKRKTAATLMN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 553 ERSSRSHSVFQLQISGEHAARG----LQCGApLNLVDLAGSERLD-PGltlgpGERDRLRETQAINSSLSTLGLVIMALS 627
Cdd:cd01364 215 AQSSRSHSVFSITIHIKETTIDgeelVKIGK-LNLVDLAGSENIGrSG-----AVDKRAREAGNINQSLLTLGRVITALV 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 54312052 628 NKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASK 679
Cdd:cd01364 289 ERAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHR 340
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
329-691 |
1.21e-78 |
|
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: 255.36 E-value: 1.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 329 GNIRVFCRVRPVLEGESTPSPGFLVFPPgpagpsdpPTRLCLSRsdDRRSTLTRAPAAATRHDFSFDRVF----PPGSK- 403
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMS--------GKETTLKN--PKQADKNNKATREVPKSFSFDYSYwshdSEDPNy 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 404 --QEEVFEEISM-LVQSALDGYPVCIFAYGQTGSGKTFTMeggpRGDPQLEGLIPRAMRHLFS-----VAQEMSgqgwtY 475
Cdd:cd01365 71 asQEQVYEDLGEeLLQHAFEGYNVCLFAYGQTGSGKSYTM----MGTQEQPGIIPRLCEDLFSriadtTNQNMS-----Y 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 476 SFVASYVEIYNETVRDLLaTGTRKGQGGDCEIRR---AGPGSEELTVtnaryVPVSCEKEVEALLHLAQQNRAVARTAQN 552
Cdd:cd01365 142 SVEVSYMEIYNEKVRDLL-NPKPKKNKGNLKVREhpvLGPYVEDLSK-----LAVTSYEDIQDLMDEGNKSRTVAATNMN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 553 ERSSRSHSVFQLQISGEH--AARGLQCG--APLNLVDLAGSERLDPGLTLGpgerDRLRETQAINSSLSTLGLVIMAL-- 626
Cdd:cd01365 216 DTSSRSHAVFTIVLTQKRhdAETNLTTEkvSKISLVDLAGSERASSTGATG----DRLKEGANINKSLTTLGKVISALad 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54312052 627 ------SNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCViGTAQAN 691
Cdd:cd01365 292 mssgksKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIV-NRAVVN 361
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
379-679 |
4.79e-77 |
|
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: 249.56 E-value: 4.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 379 TLTRAPAAATRhdFSFDRVFPPGSKQEEVFEEISM-LVQSALDGYPVCIFAYGQTGSGKTFTMeggpRGDPQLEGLIPRA 457
Cdd:cd01374 30 TIYLVEPPSTS--FTFDHVFGGDSTNREVYELIAKpVVKSALEGYNGTIFAYGQTSSGKTFTM----SGDEDEPGIIPLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 458 MRHLFSVAQEMSGQgwTYSFVASYVEIYNETVRDLLAtgtrkGQGGDCEIR---RAGPGSEELTVTNaryvpVSCEKEVE 534
Cdd:cd01374 104 IRDIFSKIQDTPDR--EFLLRVSYLEIYNEKINDLLS-----PTSQNLKIRddvEKGVYVAGLTEEI-----VSSPEHAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 535 ALLHLAQQNRAVARTAQNERSSRSHSVFQLQIsgEHAARGLQCGAP-----LNLVDLAGSERLDPGLTLGpgerDRLRET 609
Cdd:cd01374 172 SLIARGEKNRHVGETDMNERSSRSHTIFRITI--ESSERGELEEGTvrvstLNLIDLAGSERAAQTGAAG----VRRKEG 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54312052 610 QAINSSLSTLGLVIMALSNKES--HVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASK 679
Cdd:cd01374 246 SHINKSLLTLGTVISKLSEGKVggHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASR 317
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
392-679 |
9.07e-73 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 246.19 E-value: 9.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 392 FSFDRVFPPGSKQEEVFEE-ISMLVQSALDGYPVCIFAYGQTGSGKTFTMEGgprgDPQLEGLIPRAMRHLFS-VAQEMS 469
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEEtIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG----TEEEPGIIPLSLKELFSkLEDLSM 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 470 GQgwTYSFVASYVEIYNETVRDLLatgtrkgqgGDCE----IRRagPGSEELTVTNARYVPVSCEKEVEALLHLAQQNRA 545
Cdd:COG5059 134 TK--DFAVSISYLEIYNEKIYDLL---------SPNEeslnIRE--DSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 546 VARTAQNERSSRSHSVFQLQISGEHAARGLQCGAPLNLVDLAGSERLDPGLTLGpgerDRLRETQAINSSLSTLGLVIMA 625
Cdd:COG5059 201 TASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVDLAGSERAARTGNRG----TRLKEGASINKSLLTLGNVINA 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 54312052 626 LSNKES--HVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASK 679
Cdd:COG5059 277 LGDKKKsgHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASR 332
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
330-681 |
1.28e-67 |
|
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: 225.69 E-value: 1.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 330 NIRVFCRVRPVLEGESTP---------SPGFLVFPPGPagpSDPPTRLCLSRSDDRRSTLTRapaaatRHDFSFDRVFPP 400
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEgfrrivkvmDNHMLVFDPKD---EEDGFFHGGSNNRDRRKRRNK------ELKYVFDRVFDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 401 GSKQEEVFEEISM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRgDPqleGLIPRAMRHLFSVAQEMSGQGwTYSFVA 479
Cdd:cd01370 72 TSTQEEVYEETTKpLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQ-EP---GLMVLTMKELFKRIESLKDEK-EFEVSM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 480 SYVEIYNETVRDLLATgtrkgQGGDCEIRRagPGSEELTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSH 559
Cdd:cd01370 147 SYLEIYNETIRDLLNP-----SSGPLELRE--DAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 560 SVFQLQISGEHAARGLQCG---APLNLVDLAGSERLDPGLTLGpgerDRLRETQAINSSLSTLGLVIMALSN---KESHV 633
Cdd:cd01370 220 AVLQITVRQQDKTASINQQvrqGKLSLIDLAGSERASATNNRG----QRLKEGANINRSLLALGNCINALADpgkKNKHI 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 54312052 634 PYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVN 681
Cdd:cd01370 296 PYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAK 343
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
330-680 |
3.65e-66 |
|
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: 221.61 E-value: 3.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 330 NIRVFCRVRPVLEGESTPSPGflvfppgpagpsdpptrLCLSRsddRRSTLTRAPAAATRHdFSFDRVFPPGSKQEEVFE 409
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYG-----------------QCLKK---LSSDTLVLHSKPPKT-FTFDHVADSNTNQESVFQ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 410 EISM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGDPQ----LEGLIPRAMRHLFSVAQ---EMSGQGWTYSFVASY 481
Cdd:cd01373 61 SVGKpIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDNEsphgLRGVIPRIFEYLFSLIQrekEKAGEGKSFLCKCSF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 482 VEIYNETVRDLLATGTRkgqggDCEIRR-AGPGseeLTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHS 560
Cdd:cd01373 141 LEIYNEQIYDLLDPASR-----NLKLREdIKKG---VYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 561 VFQLQISG--EHAARGLQCGAPLNLVDLAGSERLDPGLTlgpgERDRLRETQAINSSLSTLGLVIMALSN----KESHVP 634
Cdd:cd01373 213 VFTCTIESweKKACFVNIRTSRLNLVDLAGSERQKDTHA----EGVRLKEAGNINKSLSCLGHVINALVDvahgKQRHVC 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 54312052 635 YRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKV 680
Cdd:cd01373 289 YRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRA 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
330-681 |
2.04e-64 |
|
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: 216.21 E-value: 2.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 330 NIRVFCRVRPvlegestpspgflvFPPGPAGPSDPPtrlCLSRSDDRRSTLTRAPAAATRHDFSFDRVFPPGSKQEEVFE 409
Cdd:cd01376 1 NVRVAVRVRP--------------FVDGTAGASDPS---CVSGIDSCSVELADPRNHGETLKYQFDAFYGEESTQEDIYA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 410 -EISMLVQSALDGYPVCIFAYGQTGSGKTFTMEGgprgDPQLEGLIPRAMRHLFSVAQEmsgQGWTYSFVASYVEIYNET 488
Cdd:cd01376 64 rEVQPIVPHLLEGQNATVFAYGSTGAGKTFTMLG----SPEQPGLMPLTVMDLLQMTRK---EAWALSFTMSYLEIYQEK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 489 VRDLLatgtrKGQGGDCEIRRAGPGSeeLTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHSVFQLQ-IS 567
Cdd:cd01376 137 ILDLL-----EPASKELVIREDKDGN--ILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKvDQ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 568 GEHAARGLQCGAPLNLVDLAGSErlDPGLTLGPGERdrLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNS 647
Cdd:cd01376 210 RERLAPFRQRTGKLNLIDLAGSE--DNRRTGNEGIR--LKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDS 285
|
330 340 350
....*....|....*....|....*....|....
gi 54312052 648 LGGSAKMLMFVNISPLEENVSESLNSLRFASKVN 681
Cdd:cd01376 286 LGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
361-680 |
4.37e-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: 213.21 E-value: 4.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 361 PSDPPTRLCLSRSDDRRST-------LTRAPAAATRHDFSF--DRVFPpGSKQEEVFEEISM-LVQSALDGYPVCIFAYG 430
Cdd:cd01375 10 PTDDFAHEMIKYGEDGKSIsihlkkdLRRGVVNNQQEDWSFkfDGVLH-NASQELVYETVAKdVVSSALAGYNGTIFAYG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 431 QTGSGKTFTMEGGPRGDPQlEGLIPRAMRHLFSVAQEMSGQgwTYSFVASYVEIYNETVRDLLATgtrkgqggdceIRRA 510
Cdd:cd01375 89 QTGAGKTFTMTGGTENYKH-RGIIPRALQQVFRMIEERPTK--AYTVHVSYLEIYNEQLYDLLST-----------LPYV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 511 GPGSEELTVT----------NARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHSVFQLQISGEH--AARGLQCG 578
Cdd:cd01375 155 GPSVTPMTILedspqnifikGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSrtLSSEKYIT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 579 APLNLVDLAGSERLDPGLTLGpgerDRLRETQAINSSLSTLGLVIMALSNKE-SHVPYRNSKLTYLLQNSLGGSAKMLMF 657
Cdd:cd01375 235 SKLNLVDLAGSERLSKTGVEG----QVLKEATYINKSLSFLEQAIIALSDKDrTHVPFRQSKLTHVLRDSLGGNCNTVMV 310
|
330 340
....*....|....*....|...
gi 54312052 658 VNISPLEENVSESLNSLRFASKV 680
Cdd:cd01375 311 ANIYGEAAQLEETLSTLRFASRV 333
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
331-677 |
3.53e-62 |
|
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: 211.10 E-value: 3.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 331 IRVFCRVRPVL--EGESTPSPGFLVFPPgpagpsdppTRLCLSRSDDRRSTLTRAPAAATRHDFSFDRVFPPGSKQEEVF 408
Cdd:cd01368 3 VKVYLRVRPLSkdELESEDEGCIEVINS---------TTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 409 EEISM-LVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGdpqlEGLIPRAMRHLFSVAQEmsgqgwtYSFVASYVEIYNE 487
Cdd:cd01368 74 QGTALpLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGD----GGILPRSLDVIFNSIGG-------YSVFVSYIEIYNE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 488 TVRDLLatgtrKGQGGDCEIRRAGPGSEE-----LTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHSVF 562
Cdd:cd01368 143 YIYDLL-----EPSPSSPTKKRQSLRLREdhngnMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 563 Q---LQISGEHAARGLQCG-----APLNLVDLAGSERLDPGLTLGpgerDRLRETQAINSSLSTLGLVIMALSNKE---- 630
Cdd:cd01368 218 TiklVQAPGDSDGDVDQDKdqitvSQLSLVDLAGSERTSRTQNTG----ERLKEAGNINTSLMTLGTCIEVLRENQlqgt 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 54312052 631 -SHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFA 677
Cdd:cd01368 294 nKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
314-493 |
4.10e-54 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 182.03 E-value: 4.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 314 EMERRRLHNQLQELKGNIRVFCRVRPVLEGESTpspgfLVFPpgpagpsdpptrlclsrsdDRRSTLTRAPAAAtrHDFS 393
Cdd:pfam16796 5 ETLRRKLENSIQELKGNIRVFARVRPELLSEAQ-----IDYP-------------------DETSSDGKIGSKN--KSFS 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 394 FDRVFPPGSKQEEVFEEISMLVQSALDGYPVCIFAYGQTGSGKTFtmeggprgdpqleGLIPRAMRHLFSVAQEMSgQGW 473
Cdd:pfam16796 59 FDRVFPPESEQEDVFQEISQLVQSCLDGYNVCIFAYGQTGSGSND-------------GMIPRAREQIFRFISSLK-KGW 124
|
170 180
....*....|....*....|
gi 54312052 474 TYSFVASYVEIYNETVRDLL 493
Cdd:pfam16796 125 KYTIELQFVEIYNESSQDLL 144
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
330-680 |
7.65e-54 |
|
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: 187.89 E-value: 7.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 330 NIRVFCRVRPVLEGESTPSPGFLVfppgpagpsDPPTRLCLSRSDDR-RSTLTRAPaaaTRHDFSFDRVFPPGSKQEEVF 408
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVV---------SVPSKLTLIVHEPKlKVDLTKYI---ENHTFRFDYVFDESSSNETVY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 409 EE-ISMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGDPQLEGLIPRAMRHLFSVAQEMSGQGwTYSFVASYVEIYNE 487
Cdd:cd01367 69 RStVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAARDVFRLLNKLPYKD-NLGVTVSFFEIYGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 488 TVRDLLATGTRkgqggdCEIRRAGPGseELTVTNARYVPVSCEKEVEALLHLAQQNRAVARTAQNERSSRSHSVFQLQIS 567
Cdd:cd01367 148 KVFDLLNRKKR------VRLREDGKG--EVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 568 gehAARGLQCGAPLNLVDLAGSERldpGLTLGPGERDRLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNS 647
Cdd:cd01367 220 ---DRGTNKLHGKLSFVDLAGSER---GADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDS 293
|
330 340 350
....*....|....*....|....*....|....
gi 54312052 648 L-GGSAKMLMFVNISPLEENVSESLNSLRFASKV 680
Cdd:cd01367 294 FiGENSKTCMIATISPGASSCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
392-679 |
5.93e-44 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 170.50 E-value: 5.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 392 FSFDRVFPPGSKQEEVFEEI-SMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGP--------RGDPQleGLIPRAMRHLF 462
Cdd:PLN03188 134 FTFDSIADPESTQEDIFQLVgAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlSGDQQ--GLTPRVFERLF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 463 SVAQE----MSGQGWTYSFVASYVEIYNETVRDLLATGTRKGQggdceIR---RAGpgseeLTVTNARYVPVSCEKEVEA 535
Cdd:PLN03188 212 ARINEeqikHADRQLKYQCRCSFLEIYNEQITDLLDPSQKNLQ-----IRedvKSG-----VYVENLTEEYVKTMKDVTQ 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 536 LLHLAQQNRAVARTAQNERSSRSHSVFQLQISG--EHAARGLQC--GAPLNLVDLAGSERldPGLTLGPGerDRLRETQA 611
Cdd:PLN03188 282 LLIKGLSNRRTGATSINAESSRSHSVFTCVVESrcKSVADGLSSfkTSRINLVDLAGSER--QKLTGAAG--DRLKEAGN 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54312052 612 INSSLSTLGLVIMAL-----SNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASK 679
Cdd:PLN03188 358 INRSLSQLGNLINILaeisqTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQR 430
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
394-625 |
1.28e-26 |
|
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: 106.66 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 394 FDRVFPPGSKQEEVFEEISMLVQSALDGYPV-CIFAYGQTGSGKTFTMeggprgdpqlEGLIPRAMRHLFSVAQEMSGQG 472
Cdd:cd01363 22 FYRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETM----------KGVIPYLASVAFNGINKGETEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 473 WTYsfvasyveiynetvrdllatgtrkgqggdceirragpgSEELTVTNaryvpvscEKEVEALLHLAQQNRaVARTAQN 552
Cdd:cd01363 92 WVY--------------------------------------LTEITVTL--------EDQILQANPILEAFG-NAKTTRN 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54312052 553 ERSSRSHSVFQLqisgehaarglqcgaplnLVDLAGSERldpgltlgpgerdrlretqaINSSLSTLGLVIMA 625
Cdd:cd01363 125 ENSSRFGKFIEI------------------LLDIAGFEI--------------------INESLNTLMNVLRA 159
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
317-626 |
7.27e-15 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 77.86 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 317 RRRLHNQLQELKgNIRVFCRVRPVLE--GESTPSPGFlvfppGPAGPSDPPT-RLCLSRSDDRRStltrapaaatrHDFS 393
Cdd:COG5059 294 TRLLQDSLGGNC-NTRVICTISPSSNsfEETINTLKF-----ASRAKSIKNKiQVNSSSDSSREI-----------EEIK 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 394 FDRVFPPGSKQEEVFEEISMLVQSALDGypvcIFAYGQTGSGKTFTMEggprgdPQLEGLIPRAMRHLFSVAQEMSGQGW 473
Cdd:COG5059 357 FDLSEDRSEIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETLK------SRIDLIMKSIISGTFERKKLLKEEGW 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 474 TYSFVASYVEIYNETVRDLLATGTRKgqggDCEIRRAGPGSEELTVTNaryvpVSCEKEVEALLH---LAQQNRAVARTA 550
Cdd:COG5059 427 KYKSTLQFLRIEIDRLLLLREEELSK----KKTKIHKLNKLRHDLSSL-----LSSIPEETSDRVeseKASKLRSSASTK 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54312052 551 QNERSSRSHSVFQLQISGEHAARGLQCgapLNLVDLAGSERLdPGLTLGpgerDRLRETQAINSSLSTLGLVIMAL 626
Cdd:COG5059 498 LNLRSSRSHSKFRDHLNGSNSSTKELS---LNQVDLAGSERK-VSQSVG----ELLRETQSLNKSLSSLGDVIHAL 565
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-327 |
2.51e-13 |
|
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: 73.55 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKE 244
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 245 RLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQL 324
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
...
gi 54312052 325 QEL 327
Cdd:TIGR02168 946 SEE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-331 |
2.41e-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: 70.47 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMER 317
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170
....*....|....
gi 54312052 318 RRLHNQLQELKGNI 331
Cdd:TIGR02168 841 EDLEEQIEELSEDI 854
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-327 |
6.66e-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: 69.32 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAA---QVTLLAEQ----GDRL 310
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlelQIASLNNEierlEARL 409
|
170
....*....|....*..
gi 54312052 311 YGLEMERRRLHNQLQEL 327
Cdd:TIGR02168 410 ERLEDRRERLQQEIEEL 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-328 |
2.63e-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: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKER 245
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 246 LVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQ 325
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
...
gi 54312052 326 ELK 328
Cdd:COG1196 460 ALL 462
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-327 |
3.96e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVR-------RRAEQSQQKLETLGARVLELE 237
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQaeeyellAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMER 317
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170
....*....|
gi 54312052 318 RRLHNQLQEL 327
Cdd:COG1196 396 AELAAQLEEL 405
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
158-332 |
4.62e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMER 317
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170
....*....|....*
gi 54312052 318 RRLHNQLQELKGNIR 332
Cdd:COG1196 410 EALLERLERLEEELE 424
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
169-332 |
8.07e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 169 ELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQ 248
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 249 ELQTERLQLQEERSTL-------STQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLH 321
Cdd:COG1196 313 ELEERLEELEEELAELeeeleelEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170
....*....|.
gi 54312052 322 NQLQELKGNIR 332
Cdd:COG1196 393 RAAAELAAQLE 403
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-328 |
9.58e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 9.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKE 244
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 245 RLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQL 324
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
....
gi 54312052 325 QELK 328
Cdd:COG1196 473 ALLE 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-332 |
1.04e-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: 65.08 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKT-----AAQVTLLAEQGDRLYG 312
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelKELQAELEELEEELEE 451
|
170 180
....*....|....*....|
gi 54312052 313 LEMERRRLHNQLQELKGNIR 332
Cdd:TIGR02168 452 LQEELERLEEALEELREELE 471
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-330 |
1.12e-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: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 174 REKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQqkletlGARVLELEECLGTKERLVQELQTE 253
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 54312052 254 RLQLQEERSTLSTQLEEREREFQASEAALSSSRAEvlcLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQELKGN 330
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
165-331 |
1.69e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.38 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEEclgtke 244
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 245 rLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAqvtllAEQGDRLYGLEMERRRLHNQL 324
Cdd:COG4372 116 -ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA-----LEQELQALSEAEAEQALDELL 189
|
....*..
gi 54312052 325 QELKGNI 331
Cdd:COG4372 190 KEANRNA 196
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
157-332 |
2.49e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 157 WDLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEEL--ASVRRRAEQSQQKLETLGA--- 231
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAssd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 232 RVLELEECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALsSSRAEVLCLRQKTAAQVTLLAEQGDRLY 311
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL-EAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|.
gi 54312052 312 GLemERRRLHNQLQELKGNIR 332
Cdd:COG4913 765 RE--LRENLEERIDALRARLN 783
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-334 |
2.88e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 149 KKPGKRPAWDLKgQLCDLHEELKQYREKT---QTLDRENQGLREQLREVQEQATTLGTERNTLE---------EELASVR 216
Cdd:COG4717 60 KPQGRKPELNLK-ELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 217 RRAEQSQQKLETLGARVLELEECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKT 296
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190
....*....|....*....|....*....|....*...
gi 54312052 297 AAQVTLLAEQGDRLYGlEMERRRLHNQLQELKGNIRVF 334
Cdd:COG4717 219 QEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIA 255
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-328 |
3.20e-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: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKE 244
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 245 RLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQL 324
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
....
gi 54312052 325 QELK 328
Cdd:COG1196 438 EEEE 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
159-332 |
4.26e-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: 63.16 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTER-NTLEEELASV-------RRRAEQSQQKLETLG 230
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELeaeiaslERSIAEKERELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 231 ARVLELEECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRL 310
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
170 180
....*....|....*....|..
gi 54312052 311 YGLEMERRRLHNQLQELKGNIR 332
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELA 423
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-328 |
5.21e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKER 245
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 246 LVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQ 325
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
...
gi 54312052 326 ELK 328
Cdd:COG1196 467 ELL 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-327 |
8.21e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTE-------RNTLEEELASVRRRAEQSQQKLETLGA 231
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarleerRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 232 RVLELEECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLY 311
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170
....*....|....*.
gi 54312052 312 GLEMERRRLHNQLQEL 327
Cdd:COG1196 418 RLEEELEELEEALAEL 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-327 |
9.60e-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: 62.01 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMER 317
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
170
....*....|
gi 54312052 318 RRLHNQLQEL 327
Cdd:TIGR02169 472 YDLKEEYDRV 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-328 |
1.32e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLE-------TLGARVLELEE 238
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEelaeellEALRAAAELAA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 239 CLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERR 318
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
170
....*....|
gi 54312052 319 RLHNQLQELK 328
Cdd:COG1196 481 ELLEELAEAA 490
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
158-329 |
1.70e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.54 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREK-------TQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLG 230
Cdd:COG1340 26 ELKEKRDELNEELKELAEKrdelnaqVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 231 ARVLELEECLGTKERLVQELQTERLQLQEER------STLSTQLEEREREFQASEaALSSSRAEVLCLRQKtaaqvtlLA 304
Cdd:COG1340 106 KAGGSIDKLRKEIERLEWRQQTEVLSPEEEKelvekiKELEKELEKAKKALEKNE-KLKELRAELKELRKE-------AE 177
|
170 180
....*....|....*....|....*
gi 54312052 305 EQGDRLYGLEMERRRLHNQLQELKG 329
Cdd:COG1340 178 EIHKKIKELAEEAQELHEEMIELYK 202
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-328 |
2.41e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGL---REQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLG 241
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 242 TKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLH 321
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
....*..
gi 54312052 322 NQLQELK 328
Cdd:COG1196 442 EALEEAA 448
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
166-306 |
2.68e-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: 58.01 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETL-GARVLE-LEECLGTK 243
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEaLQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54312052 244 ERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQ 306
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-327 |
3.41e-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: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAA---QVTLLAEQGDRLYG-- 312
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterRLEDLEEQIEELSEdi 854
|
170 180
....*....|....*....|....
gi 54312052 313 ---------LEMERRRLHNQLQEL 327
Cdd:TIGR02168 855 eslaaeieeLEELIEELESELEAL 878
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-333 |
3.49e-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: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 169 ELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLG-TKERLv 247
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQiLRERL- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 248 QELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQEL 327
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
....*.
gi 54312052 328 KGNIRV 333
Cdd:TIGR02168 392 ELQIAS 397
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
167-332 |
4.05e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 167 HEELKQYREKTQTLDrenQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERL 246
Cdd:COG4372 12 RLSLFGLRPKTGILI---AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 247 VQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQE 326
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
....*.
gi 54312052 327 LKGNIR 332
Cdd:COG4372 169 LEQELQ 174
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
162-332 |
6.19e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECL- 240
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLe 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 241 ----------GTKERL---VQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQG 307
Cdd:PRK02224 332 ecrvaaqahnEEAESLredADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
170 180
....*....|....*....|....*
gi 54312052 308 DRLYGLEMERRRLHNQLQELKGNIR 332
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLR 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-328 |
1.38e-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: 58.53 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLgtkerlvQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMER 317
Cdd:TIGR02168 810 AEL-------TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
170
....*....|.
gi 54312052 318 RRLHNQLQELK 328
Cdd:TIGR02168 883 ASLEEALALLR 893
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-332 |
1.39e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 169 ELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAE--------QSQQKLETLGARVLELEECL 240
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeeqlRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 241 GTKERLVQELQTERLQLQEERSTLSTQLEEREREFQ-------ASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGL 313
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170
....*....|....*....
gi 54312052 314 EMERRRLHNQLQELKGNIR 332
Cdd:TIGR02169 391 REKLEKLKREINELKRELD 409
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
180-332 |
1.80e-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: 58.14 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 180 LDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQELQTERLQLQE 259
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54312052 260 ERSTLSTQLEEREREFQASEAALSSSRAEVlclrQKTAAQVTLLAEQGDRLYG-LEMERRRLHNQLQELKGNIR 332
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREALDELRAeLTLLNEEAANLRERLESLER 831
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-313 |
2.11e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 168 EELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLV 247
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54312052 248 QELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRqktaAQVTLLAEQGDRLYGL 313
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR----AVEEVLKASIQGVHGT 526
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
158-327 |
2.12e-08 |
|
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: 57.00 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNT-------LEEELASVRRRAEQSQQKLETLG 230
Cdd:pfam19220 115 DKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATarerlalLEQENRRLQALSEEQAAELAELT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 231 ARVLELEECLGTKERLVQELQTERLQLQEERSTLSTQLEErEREFQASEAALSSSRAEVLCLRQKTAAQvtLLAEQGDRL 310
Cdd:pfam19220 195 RRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEE-AVEAHRAERASLRMKLEALTARAAATEQ--LLAEARNQL 271
|
170
....*....|....*..
gi 54312052 311 YGLEMERRRLHNQLQEL 327
Cdd:pfam19220 272 RDRDEAIRAAERRLKEA 288
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
158-306 |
3.24e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.06 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:COG4372 63 QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREF--QASEAALSSSRAEVLCLRQKTAAQVTLLAEQ 306
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
158-295 |
5.19e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQ-EQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLEL 236
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 54312052 237 EECLgtkERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQK 295
Cdd:COG4913 379 AEEF---AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-333 |
6.04e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ecLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYG---LE 314
Cdd:TIGR02168 435 --LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkaLL 512
|
170
....*....|....*....
gi 54312052 315 MERRRLHNQLQELKGNIRV 333
Cdd:TIGR02168 513 KNQSGLSGILGVLSELISV 531
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
158-331 |
1.10e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDrenqgLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 EclgtkERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEvlclrqktaaqvtLLAEQGDRLYGLEMER 317
Cdd:COG3206 261 Q-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ-------------LQQEAQRILASLEAEL 322
|
170
....*....|....
gi 54312052 318 RRLHNQLQELKGNI 331
Cdd:COG3206 323 EALQAREASLQAQL 336
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
167-270 |
1.14e-07 |
|
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: 51.14 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 167 HEELKQYREKTqTLDRENQglREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERL 246
Cdd:pfam10473 33 LEMSEENQELA-ILEAENS--KAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESLNSSLENL 109
|
90 100
....*....|....*....|....*...
gi 54312052 247 VQELQTERLQLQEERST----LSTQLEE 270
Cdd:pfam10473 110 LEEKEQEKVQMKEESKTavemLQTQLKE 137
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-332 |
2.20e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYREKTQTLdrenqglrEQLREVQEQATTLGTERNTLEEELAsvRRRAEQSQQKLETLGARVLELEECLG 241
Cdd:COG4913 236 DLERAHEALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 242 TKERLVQELQTERLQLQEERSTLSTQ----------------------LEEREREFQASEAALSS-------SRAEVLCL 292
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQirgnggdrleqlereierlereLEERERRRARLEALLAAlglplpaSAEEFAAL 385
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 54312052 293 RQKTAAQVT----LLAEQGDRLYGLEMERRRLHNQLQELKGNIR 332
Cdd:COG4913 386 RAEAAALLEaleeELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-332 |
2.28e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLE-------TLG 230
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEnvkselkELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 231 ARVLELEECLGT-KERL-----------VQELQTERLQLQEERSTLSTQLEEREREFQAS---EAALSSSRAEVLCLRQK 295
Cdd:TIGR02169 765 ARIEELEEDLHKlEEALndlearlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtleKEYLEKEIQELQEQRID 844
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54312052 296 TAAQVTLLAEQ-------------------------GDRLYGLEMERRRLHNQLQELKGNIR 332
Cdd:TIGR02169 845 LKEQIKSIEKEienlngkkeeleeeleeleaalrdlESRLGDLKKERDELEAQLRELERKIE 906
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-287 |
2.86e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRA 287
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-326 |
3.25e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLrEQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASE------AALSSSRAEVLCLRQKTAAQVTLLAEQGDRLy 311
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRERL- 629
|
170
....*....|....*
gi 54312052 312 gleMERRRLHNQLQE 326
Cdd:PRK02224 630 ---AEKRERKRELEA 641
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
162-332 |
4.34e-07 |
|
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: 52.07 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQAttlgterntlEEELASVRRRAEQSQQKLETLGARVLELEECLg 241
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQ----------QEEAESSREQLQELEEQLATERSARREAEAEL- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 242 tkERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAAL------SSSRAEVLC-LRQKTAaqvTLLAEQgDRLYGLE 314
Cdd:pfam09787 117 --ERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLtsksqsSSSQSELENrLHQLTE---TLIQKQ-TMLEALS 190
|
170
....*....|....*...
gi 54312052 315 MERRRLHNQLQELKGNIR 332
Cdd:pfam09787 191 TEKNSLVLQLERMEQQIK 208
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
158-326 |
4.62e-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: 52.46 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQEL-QTERLQL--------QEERS-----TLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLL 303
Cdd:COG4942 104 EELAELLRALYRLgRQPPLALllspedflDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180
....*....|....*....|...
gi 54312052 304 AEQGDRLYGLEMERRRLHNQLQE 326
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEK 206
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
166-346 |
6.02e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQGLREQLREVQEQATtlgtERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKER 245
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 246 L------------------VQELQTERLQLQEERSTLST---QLEEREREFQASEAALSSSRAEV-LCLRQKTAA-QVTL 302
Cdd:PRK03918 374 LerlkkrltgltpeklekeLEELEKAKEEIEEEISKITArigELKKEIKELKKAIEELKKAKGKCpVCGRELTEEhRKEL 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 54312052 303 LAEQGDRLYGLEMERRRLHNQLQELKgniRVFCRVRPVLEGEST 346
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLR---KELRELEKVLKKESE 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-306 |
6.86e-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: 52.75 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54312052 238 -ECLGTKERLV------QELQTERLQLQEE-RSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAA--QVTLLAEQ 306
Cdd:TIGR02168 915 rELEELREKLAqlelrlEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgPVNLAAIE 993
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-328 |
9.65e-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: 52.37 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELkqyREKTQTLDREN------QGLREQLREVQeqATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLE 235
Cdd:TIGR02168 190 RLEDILNEL---ERQLKSLERQAekaeryKELKAELRELE--LALLVLRLEELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 236 LEECLGTKERLVQELQTERLQLQEERSTLSTQ---LEEREREFQASEAALSSSRAEVLCLRQKTAAQV----TLLAEQGD 308
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEisrLEQQKQILRERLANLERQLEELEAQLEELESKLdelaEELAELEE 344
|
170 180
....*....|....*....|
gi 54312052 309 RLYGLEMERRRLHNQLQELK 328
Cdd:TIGR02168 345 KLEELKEELESLEAELEELE 364
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
168-333 |
9.75e-07 |
|
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: 52.48 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 168 EELKQYREKTQ-TLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQS-------QQKLETLGARVLELEEC 239
Cdd:pfam01576 200 EKGRQELEKAKrKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEEtaqknnaLKKIRELEAQISELQED 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 240 LGTKERLVQELQTERLQLQEERSTLSTQLEE--------------REREF----QASEAALSSSRAEVLCLRQKTAAQVT 301
Cdd:pfam01576 280 LESERAARNKAEKQRRDLGEELEALKTELEDtldttaaqqelrskREQEVtelkKALEEETRSHEAQLQEMRQKHTQALE 359
|
170 180 190
....*....|....*....|....*....|....*.
gi 54312052 302 LLAEQGDRL----YGLEMERRRLHNQLQELKGNIRV 333
Cdd:pfam01576 360 ELTEQLEQAkrnkANLEKAKQALESENAELQAELRT 395
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
148-328 |
1.03e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.36 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 148 GKKPGKRPAWDLKgqlcdlHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNT-------------LEEELAS 214
Cdd:TIGR00606 730 GLAPGRQSIIDLK------EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakvcltdvtimerFQMELKD 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 215 VRRRAEQ-----------------------SQQKLETLGARVLELEECLGTKERLVQ-------ELQTERLQLQE---ER 261
Cdd:TIGR00606 804 VERKIAQqaaklqgsdldrtvqqvnqekqeKQHELDTVVSKIELNRKLIQDQQEQIQhlksktnELKSEKLQIGTnlqRR 883
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 54312052 262 STLSTQLEEREREFQASEAALSSSRAEVLCLRQktaAQVTLLAEQGDRLYGLEMERRRLHNQLQELK 328
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLET---FLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
166-328 |
1.24e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKEr 245
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 246 LVQELQTERLQLQEERSTLsTQLEEREREFQASEAALSSSRAEV--------LCLRQKTAAQVTLLAEQGDRLYGLEMER 317
Cdd:COG4717 130 LYQELEALEAELAELPERL-EELEERLEELRELEEELEELEAELaelqeeleELLEQLSLATEEELQDLAEELEELQQRL 208
|
170
....*....|.
gi 54312052 318 RRLHNQLQELK 328
Cdd:COG4717 209 AELEEELEEAQ 219
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
166-274 |
1.56e-06 |
|
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: 49.13 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGT--------ERNTLEEELASVRRRAEQSQQKLETLgARVLELE 237
Cdd:pfam15619 72 LRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKIQDL-ERKLELE 150
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 54312052 238 EC-----LGTKERLVQELQTERLQLQEERSTLSTQLEERERE 274
Cdd:pfam15619 151 NKsfrrqLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
160-328 |
1.57e-06 |
|
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: 51.23 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 160 KGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEE-------------ELASVRRRAEQSQQKL 226
Cdd:pfam05622 189 KRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLREtneelrcaqlqqaELSQADALLSPSSDPG 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 227 ETLGARVLELEeclgTKERLVQeLQTE--RLQLQEERS------TLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAA 298
Cdd:pfam05622 269 DNLAAEIMPAE----IREKLIR-LQHEnkMLRLGQEGSyrerltELQQLLEDANRRKNELETQNRLANQRILELQQQVEE 343
|
170 180 190
....*....|....*....|....*....|
gi 54312052 299 QVTLLAEQGDRLYGLEMERRRLHNQLQELK 328
Cdd:pfam05622 344 LQKALQEQGSKAEDSSLLKQKLEEHLEKLH 373
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
165-327 |
1.83e-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: 51.28 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRR---AEQSQQKLEtlgaRVLELEECLG 241
Cdd:pfam05557 315 ELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKEltmSNYSPQLLE----RIEEAEDMTQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 242 TKERLVQELQTERLQLQEERSTLSTQLEEREREF-----QASEAALSSSRAEVLCLRQKtaaqvtllaeqgdrLYGLEME 316
Cdd:pfam05557 391 KMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELqalrqQESLADPSYSKEEVDSLRRK--------------LETLELE 456
|
170
....*....|.
gi 54312052 317 RRRLHNQLQEL 327
Cdd:pfam05557 457 RQRLREQKNEL 467
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
159-326 |
1.95e-06 |
|
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: 51.27 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYR-EKTQ-------------TLDRENQGLREQLREVQEQATTLGTERN----TLEEELASVRRRAE 220
Cdd:pfam15921 379 LQKLLADLHKREKELSlEKEQnkrlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 221 qSQQKLETLGARVLELEECLgtkERLVQELQTERLQLQ-EER--STLSTQLEEREREFQASEAALSSSRAEVLCLRQkta 297
Cdd:pfam15921 459 -SLEKVSSLTAQLESTKEML---RKVVEELTAKKMTLEsSERtvSDLTASLQEKERAIEATNAEITKLRSRVDLKLQ--- 531
|
170 180
....*....|....*....|....*....
gi 54312052 298 aQVTLLAEQGDRLYGLEMERRRLHNQLQE 326
Cdd:pfam15921 532 -ELQHLKNEGDHLRNVQTECEALKLQMAE 559
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
165-300 |
1.95e-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: 51.22 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVqEQATT--------LGTERNTLEEELASVRRRAEQSQQKLETLGARVLEL 236
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNrltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54312052 237 EECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQasEAALSSSRAEVLCLRQKTAAQV 300
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE--ELEAQIEKKRKRLSELKAKLEA 928
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
168-331 |
2.88e-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: 50.94 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 168 EELKQYREKTQTLDREnqglreqLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLV 247
Cdd:pfam01576 12 EELQKVKERQQKAESE-------LKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 248 QELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLR---QKTAAQVTLLAEQGDRlygLEMERRRLHNQL 324
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEakiKKLEEDILLLEDQNSK---LSKERKLLEERI 161
|
....*..
gi 54312052 325 QELKGNI 331
Cdd:pfam01576 162 SEFTSNL 168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
175-328 |
3.48e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 175 EKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQELQTER 254
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 255 LQLQEERSTLSTQLEERERE------FQASEAALSSSRAEVlcLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQELK 328
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQY--LKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
158-502 |
3.63e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETL-------G 230
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 231 ARVLELEECLGTKE-------------------RLVQELQTERLQLQEERStlstQLEEREREFQASEAALSSSRAEVLc 291
Cdd:COG3883 100 GSVSYLDVLLGSESfsdfldrlsalskiadadaDLLEELKADKAELEAKKA----ELEAKLAELEALKAELEAAKAELE- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 292 lrqktaaqvTLLAEQGDRLYGLEMERRRLHNQLQELKGNIRVFCRVRPVLEGESTPSPGFLVFPPGPAGPSDPPTRLCLS 371
Cdd:COG3883 175 ---------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 372 RSDDRRSTLTRAP---AAATRHDFSFDRVFPPGSKQEEVFEEISMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGDP 448
Cdd:COG3883 246 AAGAGAAGAAGAAagsAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGG 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 54312052 449 QLEGLIPRAMRHLFSVAQEMSGQGWTYSFVASYVEIYNETVRDLLATGTRKGQG 502
Cdd:COG3883 326 ASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYVGGA 379
|
|
| SYCE1 |
pfam15233 |
Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal ... |
187-319 |
4.68e-06 |
|
Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal complex central element protein 1, a component of the synaptonemal complex involved in meiosis, and synaptonemal complex central element protein 1-like, which may be involved in meiosis.
Pssm-ID: 464575 [Multi-domain] Cd Length: 152 Bit Score: 47.11 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 187 LREQLREVQeQAttlgteRNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQELQTERLQLQEERSTLST 266
Cdd:pfam15233 10 LINRINELQ-QA------KKKSSEELGEAQALWEALQRELDSLNGEKVHLEEVLNKKQEALRILQLHCQEKESEAQRQHT 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 54312052 267 QLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRR 319
Cdd:pfam15233 83 LNEECKQRIEQYTFQIQEEKLKHRKQRMDFEEQLEDLMEQHKDLWEFHVPQRL 135
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-277 |
5.20e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 156 AWDLKGQLCDLHEELKQYRE---KTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGAR 232
Cdd:COG4913 663 VASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 54312052 233 V-LELEECLGTK----------ERLVQELQTERLQLQEERSTLSTQLEEREREFQA 277
Cdd:COG4913 743 ArLELRALLEERfaaalgdaveRELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
158-309 |
5.38e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASV---------------------- 215
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpplalllspedf 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 216 -----------------RRRAEQSQQKLETLGARVLELEECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQAS 278
Cdd:COG4942 132 ldavrrlqylkylaparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190
....*....|....*....|....*....|.
gi 54312052 279 EAALSSSRAEVLCLRQKTAAQVTLLAEQGDR 309
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
158-271 |
9.21e-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: 47.61 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREV---------QEQATTLGTERNTLEEELASVRRRAEQSQQKLET 228
Cdd:COG1579 49 AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLKRRISDLEDEILELMERIEELEEELAE 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 54312052 229 LGARVLELEECLGTK----ERLVQELQTERLQLQEERSTLSTQLEER 271
Cdd:COG1579 129 LEAELAELEAELEEKkaelDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-296 |
9.35e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQyREKTQTLDRENqGLREQLREVQEQATTLGTERNTLEE---ELASVRRRAEQSQQKLETLGARVL 234
Cdd:PRK02224 184 DQRGSLDQLKAQIEE-KEEKDLHERLN-GLESELAELDEEIERYEEQREQAREtrdEADEVLEEHEERREELETLEAEIE 261
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54312052 235 ELEECLGTKERlvqelqtERLQLQEERSTLSTQLEER--EREFQASEAALSSSRAEVLCLRQKT 296
Cdd:PRK02224 262 DLRETIAETER-------EREELAEEVRDLRERLEELeeERDDLLAEAGLDDADAEAVEARREE 318
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
165-342 |
1.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQyrEKTQTLDRENQgLREQLREVQEQATTLGTERNTLE---EELASVRRRAEQSQQKLETLGARVLELEECLG 241
Cdd:PRK03918 193 ELIKEKEK--ELEEVLREINE-ISSELPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 242 TKERLVQELQTERLQLQE------ERSTLSTQLEEREREFQASEAALSSSRAEvlclRQKTAAQVTLLAEQGDRLYGLEM 315
Cdd:PRK03918 270 ELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEE----INGIEERIKELEEKEERLEELKK 345
|
170 180
....*....|....*....|....*..
gi 54312052 316 ERRRLHNQLQELKGNIRVFCRVRPVLE 342
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKE 372
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
168-272 |
1.12e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.92 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 168 EELKQYREKTQTLDRENQGL-REQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERL 246
Cdd:COG0542 411 EELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|....*.
gi 54312052 247 VQELQTERLQLQEERSTLSTQLEERE 272
Cdd:COG0542 491 EKELAELEEELAELAPLLREEVTEED 516
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
159-301 |
1.43e-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: 46.44 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLG-----------------TERNTLEEELASVRRRAEQ 221
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRkqlenyekdkqslknlkARLKVLEKELKDLKWEHEV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 222 SQQKLETLgarVLELEECLGTKERLVQELQtERLQLQE---ER--STLSTQLEEREREFQASEAALSssraevlcLRQKT 296
Cdd:pfam13851 111 LEQRFEKV---ERERDELYDKFEAAIQDVQ-QKTGLKNlllEKklQALGETLEKKEAQLNEVLAAAN--------LDPDA 178
|
....*
gi 54312052 297 AAQVT 301
Cdd:pfam13851 179 LQAVT 183
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
159-332 |
1.52e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYREKTQTLDRENQGLREQLR---EVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLE 235
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDdedELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 236 LEeclgtkerlvqELQTERLQLQEERSTLSTQLEErerefqaseaalsssraevlclRQKTAAQVT-LLAEQGDRLYGLE 314
Cdd:PRK04863 598 LA-----------ARAPAWLAAQDALARLREQSGE----------------------EFEDSQDVTeYMQQLLERERELT 644
|
170
....*....|....*...
gi 54312052 315 MERRRLHNQLQELKGNIR 332
Cdd:PRK04863 645 VERDELAARKQALDEEIE 662
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
153-313 |
1.57e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 153 KRPAWDLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATtlgtERNTLEEELASVRRRAEQSQQKLETlgAR 232
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSL--AT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 233 VLELEECLGTKERLVQE---LQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLclrQKTAAQVTLLAEQGDR 309
Cdd:COG4717 191 EEELQDLAEELEELQQRlaeLEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL---LLIAAALLALLGLGGS 267
|
....
gi 54312052 310 LYGL 313
Cdd:COG4717 268 LLSL 271
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
165-331 |
1.59e-05 |
|
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: 48.09 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQ--------------EQATTLGTERNTLEEELASVRRRAEQSQQKLETlg 230
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQneieklkkenqsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 231 arvleLEECLGTKERLVQELQTERLQ-------LQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLL 303
Cdd:TIGR04523 417 -----LQQEKELLEKEIERLKETIIKnnseikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
170 180
....*....|....*....|....*...
gi 54312052 304 AEQGDRLYGLEMERRRLHNQLQELKGNI 331
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKI 519
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
159-327 |
1.79e-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: 48.25 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEE-------ELASVRRRAEQSQQKLETLGA 231
Cdd:pfam01576 382 LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEklsklqsELESVSSLLNEAEGKNIKLSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 232 RVLELEECLGTKERLVQELQTERL-------QLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKtaaqvtlLA 304
Cdd:pfam01576 462 DVSSLESQLQDTQELLQEETRQKLnlstrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK-------LE 534
|
170 180
....*....|....*....|...
gi 54312052 305 EQGDRLYGLEMERRRLHNQLQEL 327
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEAL 557
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
189-330 |
1.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 189 EQLREVQEQATTLGTERNTLE--EELASVRRRAEQSQQKLETLGA--RVLELEECLGTKERLVQELQTERLQLQEERSTL 264
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54312052 265 STQLEEREREFQASEAALSSSraevlclrqktaaqvtllaeQGDRLYGLEMERRRLHNQLQELKGN 330
Cdd:COG4913 315 EARLDALREELDELEAQIRGN--------------------GGDRLEQLEREIERLERELEERERR 360
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
162-288 |
2.01e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.54 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYREKTQTLD--RENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELeec 239
Cdd:COG3524 192 RLRDAREALLAFRNRNGILDpeATAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAE--- 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 54312052 240 lgtKERLVQELQTERL-QLQEERSTLSTQLEEREREFQASEAALSSSRAE 288
Cdd:COG3524 269 ---RARLTGASGGDSLaSLLAEYERLELEREFAEKAYTSALAALEQARIE 315
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
158-326 |
2.53e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQtldrenqGLREQLREVQEQATTLGTERNTLEEELASVRrraeqsqqkletlgARVLELE 237
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHE-------ELEEKYKELSASSEELSEEKDALLAQRAAHE--------------ARIRELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMER 317
Cdd:pfam07888 136 EDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTI 215
|
....*....
gi 54312052 318 RRLHNQLQE 326
Cdd:pfam07888 216 TTLTQKLTT 224
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
162-290 |
3.28e-05 |
|
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: 46.29 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYREKTQTLDRENQGLREQLR----EVQEQATTLGTERNTLEEELASVRRR------AEQSQQKLEtlgA 231
Cdd:pfam09787 94 QLQELEEQLATERSARREAEAELERLQEELRyleeELRRSKATLQSRIKDREAEIEKLRNQltsksqSSSSQSELE---N 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 54312052 232 RVLELEECLGTKERLVQELQTERlqlqeerSTLSTQLEERERefQASEAALSSSRAEVL 290
Cdd:pfam09787 171 RLHQLTETLIQKQTMLEALSTEK-------NSLVLQLERMEQ--QIKELQGEGSNGTSI 220
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
187-327 |
5.11e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 43.40 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 187 LREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETL----GARVLELEEclgTKERLvQELQTERLQLQEERS 262
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvlhAEDIKALQA---LREEL-NELKAEIAELKAEAE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54312052 263 TLSTQLEEREREFQASEAALSSSRAEvlcLRQKTAAqvtlLAEQgdrlyglemeRRRLHNQLQEL 327
Cdd:pfam07926 82 SAKAELEESEESWEEQKKELEKELSE---LEKRIED----LNEQ----------NKLLHDQLESL 129
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
166-319 |
6.13e-05 |
|
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: 46.35 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAE-----------QSQQKLETLGARVL 234
Cdd:pfam10174 399 LQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIErlkeqreredrERLEELESLKKENK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 235 ELEECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLR------QKTAAQVTLLAEQGD 308
Cdd:pfam10174 479 DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEnqlkkaHNAEEAVRTNPEIND 558
|
170
....*....|.
gi 54312052 309 RLYGLEMERRR 319
Cdd:pfam10174 559 RIRLLEQEVAR 569
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
178-331 |
6.44e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 178 QTLDRENQGLREQLREVQEqattlgtERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQELQT----- 252
Cdd:COG1579 13 QELDSELDRLEHRLKELPA-------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 253 ----ERLQLQEERSTLSTQ---LEEREREFQASEAALSSSRAEVLCLRQKTAAQV-TLLAEQGDRLYGLEMERRRLHNQL 324
Cdd:COG1579 86 rnnkEYEALQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELeEKKAELDEELAELEAELEELEAER 165
|
....*..
gi 54312052 325 QELKGNI 331
Cdd:COG1579 166 EELAAKI 172
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
162-277 |
6.81e-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: 44.15 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLEtlgarvlELEECLG 241
Cdd:pfam08614 51 SIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLK-------DREEELR 123
|
90 100 110
....*....|....*....|....*....|....*.
gi 54312052 242 TKERLVQELQTERLQLQEERStlstQLEEREREFQA 277
Cdd:pfam08614 124 EKRKLNQDLQDELVALQLQLN----MAEEKLRKLEK 155
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-331 |
7.25e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 190 QLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLEtLGARVLELEECLGTKErlVQELQTERLQLQEERSTLSTQLE 269
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALLVLR--LEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54312052 270 EREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQELKGNI 331
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
162-306 |
8.90e-05 |
|
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: 44.60 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYREKTQTLDRE---NQGLRE---QLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLE 235
Cdd:pfam12795 52 ELRELRQELAALQAKAEAAPKEilaSLSLEEleqRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQ 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54312052 236 LEECL-GTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEA--ALSSSRAEVLCLR-QKTAAQVTLLAEQ 306
Cdd:pfam12795 132 IRNRLnGPAPPGEPLSEAQRWALQAELAALKAQIDMLEQELLSNNNrqDLLKARRDLLTLRiQRLEQQLQALQEL 206
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
158-273 |
9.08e-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: 45.89 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQT---LDRENQGLR---EQLREVQEQATTLGTERNTLEEELAS----------------- 214
Cdd:pfam05557 201 ELEKELERLREHNKHLNENIENkllLKEEVEDLKrklEREEKYREEAATLELEKEKLEQELQSwvklaqdtglnlrsped 280
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54312052 215 VRRRAEQSQQKLETLGARVLELEECLGTKERLVQELQTE----RLQLQEERSTLSTQLEERER 273
Cdd:pfam05557 281 LSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaqyLKKIEDLNKKLKRHKALVRR 343
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-332 |
1.00e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 189 EQLREVQEQATTLGTERntLEEELASVRRRAEQSQQKLETLGAR--VLELEECLGTKERLVQELQTERLQLQEERSTLST 266
Cdd:COG3206 163 EQNLELRREEARKALEF--LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54312052 267 QLEEREREFQASEAALSSSRA--EVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQELKGNIR 332
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ 308
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
180-329 |
1.17e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.62 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 180 LDRENQGLREQLREVQEQAttlgterNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTK-ERLVQELQTERLQLQ 258
Cdd:smart00787 149 LDENLEGLKEDYKLLMKEL-------ELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTElDRAKEKLKKLLQEIM 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54312052 259 EERStlstQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEqgDRLYGL-EMERRRL-HNQLQELKG 329
Cdd:smart00787 222 IKVK----KLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ--CRGFTFkEIEKLKEqLKLLQSLTG 288
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
180-332 |
1.20e-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: 45.55 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 180 LDRENQGLRE---QLREVQEQATTLGTE----RNTLEEELASVRrraeQSQQKLETLGARVLELEECLGTKERLVQELQT 252
Cdd:pfam01576 786 IDAANKGREEavkQLKKLQAQMKDLQREleeaRASRDEILAQSK----ESEKKLKNLEAELLQLQEDLAASERARRQAQQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 253 ERLQLQEE-------RSTLS----------TQLEEREREFQASEAALSS----SRAEVLCLRQKTAAQVTLLAEQGDRLY 311
Cdd:pfam01576 862 ERDELADEiasgasgKSALQdekrrleariAQLEEELEEEQSNTELLNDrlrkSTLQVEQLTTELAAERSTSQKSESARQ 941
|
170 180
....*....|....*....|.
gi 54312052 312 GLEMERRRLHNQLQELKGNIR 332
Cdd:pfam01576 942 QLERQNKELKAKLQEMEGTVK 962
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
165-279 |
1.26e-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: 45.40 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLET--------------LG 230
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKlkkenqsykqeiknLE 390
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 54312052 231 ARVLELEECLGTKERLVQELQTERLQLQEERSTLSTQLEE--REREFQASE 279
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlkETIIKNNSE 441
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
173-306 |
1.31e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 173 YREKTQTLDRENQglreQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQELQT 252
Cdd:pfam10174 354 LEEKESFLNKKTK----QLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQT 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54312052 253 ERLQLQEERSTLSTQL-----------EEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQ 306
Cdd:pfam10174 430 DSSNTDTALTTLEEALsekeriierlkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEK 494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
159-329 |
1.38e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQE------QATTLGTERNTLEEELASVRRRAEQSQQKLETLGAR 232
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 233 VLELEEclgtKERLVQELQTERLQLQEERStlstQLEEREREFQ---ASEAALSSSRAEVLCLRQKTAAQVTLLAEQ--- 306
Cdd:PRK03918 330 IKELEE----KEERLEELKKKLKELEKRLE----ELEERHELYEeakAKKEELERLKKRLTGLTPEKLEKELEELEKake 401
|
170 180 190
....*....|....*....|....*....|..
gi 54312052 307 ---------GDRLYGLEMERRRLHNQLQELKG 329
Cdd:PRK03918 402 eieeeiskiTARIGELKKEIKELKKAIEELKK 433
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
165-274 |
1.87e-04 |
|
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: 41.44 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQ-------GLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:pfam20492 10 ELEERLKQYEEETKKAQEELEeseetaeELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQ 89
|
90 100 110
....*....|....*....|....*....|....*..
gi 54312052 238 EclgtkerLVQELQTERLQLQEERSTLSTQLEERERE 274
Cdd:pfam20492 90 E-------EIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
159-279 |
1.87e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYREKTQTLDRENQGLREQL---REVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLE 235
Cdd:COG3096 517 LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLdaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 54312052 236 LE----ECLGTKERLVQ--ELQTERLQLQEERSTLSTQLEEREREFQASE 279
Cdd:COG3096 597 LAarapAWLAAQDALERlrEQSGEALADSQEVTAAMQQLLEREREATVER 646
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
165-327 |
1.91e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTE---------------------RNTLEEELASVRRRAEQSQ 223
Cdd:PRK02224 353 DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelrerfgdapvdlgnaedfLEELREERDELREREAELE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 224 QKLETLGARVLELE---------EC------------LGTKERLVQELQTERLQLQEERSTLSTQLEererefQASEAAL 282
Cdd:PRK02224 433 ATLRTARERVEEAEalleagkcpECgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLE------RAEDLVE 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 54312052 283 SSSRAEVLCLRQKTAAQvtLLAEQGDRLYGLEMERRRLHNQLQEL 327
Cdd:PRK02224 507 AEDRIERLEERREDLEE--LIAERRETIEEKRERAEELRERAAEL 549
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-326 |
2.21e-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: 44.78 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYR------EKT-QTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVL 234
Cdd:pfam01576 357 ALEELTEQLEQAKrnkanlEKAkQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLS 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 235 ELEECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEaalsssraevlclRQKTAAqvtllaeqGDRLYGLE 314
Cdd:pfam01576 437 KLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET-------------RQKLNL--------STRLRQLE 495
|
170
....*....|..
gi 54312052 315 MERRRLHNQLQE 326
Cdd:pfam01576 496 DERNSLQEQLEE 507
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
162-328 |
2.24e-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: 44.72 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHE-ELKQYREKTQTLDRENQGLREQLREVQEQATTLGT----ERNTLEEELASVRRRAEQSQQKLETlgaRVLEL 236
Cdd:pfam15921 271 QLISEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYED---KIEEL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 237 EECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQK-TAAQVT---LLAEQGDRlyg 312
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdTGNSITidhLRRELDDR--- 424
|
170
....*....|....*.
gi 54312052 313 lEMERRRLHNQLQELK 328
Cdd:pfam15921 425 -NMEVQRLEALLKAMK 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-325 |
2.25e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 156 AWDLKGQLCDLHEELKQ---YREKTQTLDRENQGLREQLREVQEQATT---LGTERNTLEEELASVR--RRAEQSQQKLE 227
Cdd:COG4717 349 LQELLREAEELEEELQLeelEQEIAALLAEAGVEDEEELRAALEQAEEyqeLKEELEELEEQLEELLgeLEELLEALDEE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 228 TLGARVLELEECLgtkerlvQELQTERLQLQEERSTLSTQLEEREREFQASEAalsssRAEvlclRQKTAAQVTLLAEQG 307
Cdd:COG4717 429 ELEEELEELEEEL-------EELEEELEELREELAELEAELEQLEEDGELAEL-----LQE----LEELKAELRELAEEW 492
|
170 180
....*....|....*....|..
gi 54312052 308 DRL----YGLEMERRRLHNQLQ 325
Cdd:COG4717 493 AALklalELLEEAREEYREERL 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-333 |
2.25e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 195 QEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERL--VQELQTERLQLQEERstlsTQLEERE 272
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAEL----ERLDASS 684
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54312052 273 REFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQELKGNIRV 333
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
186-328 |
2.36e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 186 GLREQLreVQEQATTLGTERNTLEEELASVrrraEQSQQKLETlgaRVLELEECLGTKERLVQELQTERLQLQEERSTLs 265
Cdd:PRK00409 498 GLPENI--IEEAKKLIGEDKEKLNELIASL----EELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL- 567
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54312052 266 tqLEEREREFQASEAALSSSRAEVL-CLRQKTAAQVTLLAEQgdrlyGLEMERRRLHNQLQELK 328
Cdd:PRK00409 568 --LEEAEKEAQQAIKEAKKEADEIIkELRQLQKGGYASVKAH-----ELIEARKRLNKANEKKE 624
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
168-281 |
2.63e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 168 EELKQYREKtqtLDREnqgLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEEclgtKERLV 247
Cdd:PRK12704 64 EEIHKLRNE---FEKE---LRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEK----KEEEL 133
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 54312052 248 QELQTERLQLQEERSTLSTQ------LEEREREFQAsEAA 281
Cdd:PRK12704 134 EELIEEQLQELERISGLTAEeakeilLEKVEEEARH-EAA 172
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
160-258 |
2.75e-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: 44.34 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 160 KGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVR---RRAEQSQQKLE-TLGARVLE 235
Cdd:pfam15921 740 RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRsqeRRLKEKVANMEvALDKASLQ 819
|
90 100
....*....|....*....|...
gi 54312052 236 LEECLGTKERlvQELQTERLQLQ 258
Cdd:pfam15921 820 FAECQDIIQR--QEQESVRLKLQ 840
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
172-280 |
2.84e-04 |
|
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: 43.91 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 172 QYREKTQTLDRENQGLREQ--------LREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE---ECL 240
Cdd:pfam05622 279 EIREKLIRLQHENKMLRLGqegsyrerLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGskaEDS 358
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 54312052 241 GTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEA 280
Cdd:pfam05622 359 SLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLA 398
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
159-295 |
3.19e-04 |
|
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: 43.48 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYREKTQTLDRENQGLREQ----LREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVL 234
Cdd:pfam04849 169 LQEKLRGLEEENLKLRSEASHLKTETDTYEEKeqqlMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQIV 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54312052 235 ELEECLGT----KERLVQELQTER---LQLQEErstlstqLEEREREFQASEAALSSSRAEVLCLRQK 295
Cdd:pfam04849 249 DLQHKCKElgieNEELQQHLQASKeaqRQLTSE-------LQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
161-327 |
3.66e-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: 42.12 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 161 GQLCdlHEELKQYREKTQTLDRENQGLREQLREVQEQ-ATTLGTERNTLEEELASVRRRAEQSQQKLETLgarvleleec 239
Cdd:pfam06785 46 GSLC--LLLLLYYWEDALKEKFEKSFLEEKEAKLTELdAEGFKILEETLEELQSEEERLEEELSQKEEEL---------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 240 lgtkerlvqelqterLQLQEERSTLSTQLEEREREFQA----SEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEM 315
Cdd:pfam06785 114 ---------------RRLTEENQQLQIQLQQISQDFAEfrleSEEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLES 178
|
170
....*....|..
gi 54312052 316 ERRRLHNQLQEL 327
Cdd:pfam06785 179 KVRDLNYEIKTL 190
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
158-332 |
4.08e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDL---HEELKQ--YREKTQTLDRENQGLREQLREVQEQATTLGTER----------------NTLEEELASvR 216
Cdd:PRK04778 227 ELPDQLQELkagYRELVEegYHLDHLDIEKEIQDLKEQIDENLALLEELDLDEaeekneeiqeridqlyDILEREVKA-R 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 217 RRAEQSQQKLETLGARVLELEECLGTK-ERLVQ-------ELQTERlQLQEERSTLSTQLEEREREFQASEAALSSSRAE 288
Cdd:PRK04778 306 KYVEKNSDTLPDFLEHAKEQNKELKEEiDRVKQsytlnesELESVR-QLEKQLESLEKQYDEITERIAEQEIAYSELQEE 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 54312052 289 VlclrQKTAAQVTLLAEQ----GDRLYGLEMERRRLHNQLQELKGNIR 332
Cdd:PRK04778 385 L----EEILKQLEEIEKEqeklSEMLQGLRKDELEAREKLERYRNKLH 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-328 |
4.08e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 168 EELKQYREKTQTLDrenqglrEQLREVQEQATTLGTERNTLEEELASVRRraeqsqqKLETLGARVLELEEclgTKERLv 247
Cdd:PRK03918 179 ERLEKFIKRTENIE-------ELIKEKEKELEEVLREINEISSELPELRE-------ELEKLEKEVKELEE---LKEEI- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 248 QELQTERLQLQEERSTLS---TQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTL---LAEQGDRLYGLEMERRRLH 321
Cdd:PRK03918 241 EELEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLsefYEEYLDELREIEKRLSRLE 320
|
....*..
gi 54312052 322 NQLQELK 328
Cdd:PRK03918 321 EEINGIE 327
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
182-327 |
4.12e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 182 RENQGLREQLREVQEQATTLGTERntlEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQELQTERLQLQEER 261
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGG---SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54312052 262 STLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQEL 327
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
181-321 |
4.91e-04 |
|
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: 40.74 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 181 DRENQGLREQLREVQEQATTL-----GTERN--TLEEELASVRRRAEQSQQKLETLGARVLELEECLgtkerlvQELQTE 253
Cdd:pfam10473 2 EKKQLHVLEKLKESERKADSLkdkveNLEREleMSEENQELAILEAENSKAEVETLKAEIEEMAQNL-------RDLELD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54312052 254 RLQLQEERSTLSTQLEEREREFQASEAALSSSRAevlCLRQKTAAQVTLLAEQGDRLYGLEMERRRLH 321
Cdd:pfam10473 75 LVTLRSEKENLTKELQKKQERVSELESLNSSLEN---LLEEKEQEKVQMKEESKTAVEMLQTQLKELN 139
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
166-331 |
5.63e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQG--------------LREQLREVQEQAT-------TLGTERNTLEEELAsvRRRAEQSQQ 224
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSykqeiknlesqindLESKIQNQEKLNQqkdeqikKLQQEKELLEKEIE--RLKETIIKN 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 225 KLEtlgarVLELEECLGTKERLVQELQTERLQLQEERSTLS-------TQLEEREREFQASEAALSSSRAEVLCLRQKTA 297
Cdd:TIGR04523 439 NSE-----IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
170 180 190
....*....|....*....|....*....|....*..
gi 54312052 298 ---AQVTLLAEQGDRlygLEMERRRLHNQLQELKGNI 331
Cdd:TIGR04523 514 dltKKISSLKEKIEK---LESEKKEKESKISDLEDEL 547
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-310 |
5.66e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATtlgteRNTLEEELASVRRRAEQSQQKLETLGARVLELEECLG 241
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLA-----DNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLA 686
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54312052 242 TKERLVQELQTERLQlqeerstlstQLEER-EREFQASEAALSSSRAEVLCL------RQKTAAQVTLLAEQGDRL 310
Cdd:pfam10174 687 EKDGHLTNLRAERRK----------QLEEIlEMKQEALLAAISEKDANIALLelssskKKKTQEEVMALKREKDRL 752
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
188-284 |
7.45e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 188 REQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLgtkerlvQELQTERLQLQEERstLSTQ 267
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQ-------QELEAQLEQLQEKA--AETS 211
|
90
....*....|....*..
gi 54312052 268 LEEREREFQASEAALSS 284
Cdd:PRK11448 212 QERKQKRKEITDQAAKR 228
|
|
| SynN |
cd00179 |
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ... |
175-289 |
7.95e-04 |
|
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain
Pssm-ID: 238105 [Multi-domain] Cd Length: 151 Bit Score: 40.35 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 175 EKTQTLDRENQGLREQLREVQEQATTLGTE-------RNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGT----- 242
Cdd:cd00179 6 EEVEEIRGNIDKISEDVEELQKLHSQLLTApdadpelKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSsvdri 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54312052 243 ----KERLVQELQ--------TERLQLQEERSTLSTQLEE--REREFQASEAALSSSRAEV 289
Cdd:cd00179 86 rktqHSGLSKKFVevmtefnkAQRKYRERYKERIQRQLEItgGEATDEELEDMLESGNSEI 146
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
162-330 |
9.14e-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: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYREKTQTLDRE-------NQGLREQLRE----------------VQEQATTLGTE----RNTLEEELAS 214
Cdd:pfam15905 95 RLQALEEELEKVEAKLNAAVREktslsasVASLEKQLLEltrvnellkakfsedgTQKKMSSLSMElmklRNKLEAKMKE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 215 VRRRAE------QSQQK-LETLGARVLELEECLGTKERLVQELQTERLQLQE---ERSTLSTQLEEREREFQASEAALSS 284
Cdd:pfam15905 175 VMAKQEgmegklQVTQKnLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEyitELSCVSEQVEKYKLDIAQLEELLKE 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 54312052 285 SRAEVLCLRQKTAAQVTLLAEQ----GDRLYGLEMERRRLHNQLQELKGN 330
Cdd:pfam15905 255 KNDEIESLKQSLEEKEQELSKQikdlNEKCKLLESEKEELLREYEEKEQT 304
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-285 |
1.07e-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: 42.06 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 180 LDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQELQTERLQLQE 259
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
90 100
....*....|....*....|....*.
gi 54312052 260 ERSTLSTQLEEREREFQASEAALSSS 285
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAA 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-327 |
1.10e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 168 EELKQYREKtqtLDRenqgLREQLREVQEQATTLGTERNTLEE--------------------------------ELASV 215
Cdd:TIGR02169 177 EELEEVEEN---IER----LDLIIDEKRQQLERLRREREKAERyqallkekreyegyellkekealerqkeaierQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 216 RRRAEQSQQKLETLGARVLELEECLGTKERLVQEL--------QTERLQLQEERSTLSTQLEEREREFQASE-------A 280
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEerlakleA 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 54312052 281 ALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQEL 327
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
165-332 |
1.11e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLE------EELASVRRRAEQSQQKLETLGARVLELEE 238
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRE 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 239 CLGTK-ER---LVQELQTERLQ-LQEERSTLST----------QLEEREREFQASEAALSSSRAEVLCLRQKTAAqvtlL 303
Cdd:PRK02224 628 RLAEKrERkreLEAEFDEARIEeAREDKERAEEyleqveekldELREERDDLQAEIGAVENELEELEELRERREA----L 703
|
170 180
....*....|....*....|....*....
gi 54312052 304 AEQGDRLYGLEMERRRLHNQLQELKGNIR 332
Cdd:PRK02224 704 ENRVEALEALYDEAEELESMYGDLRAELR 732
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
158-328 |
1.33e-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: 42.08 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLcdlhEELKQYREKTQ----TLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLG--- 230
Cdd:pfam01576 107 DLEEQL----DEEEAARQKLQlekvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSklk 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 231 ----ARVLELEECLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVlclrqkTAAQVTLLAEQ 306
Cdd:pfam01576 183 nkheAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEEL------QAALARLEEET 256
|
170 180
....*....|....*....|..
gi 54312052 307 GDRLYGLEmERRRLHNQLQELK 328
Cdd:pfam01576 257 AQKNNALK-KIRELEAQISELQ 277
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
159-288 |
1.57e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEE 238
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 54312052 239 CLGTKERLVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAE 288
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
180-280 |
1.60e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.84 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 180 LDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRraEQSQQKL------------ETLGARVLELEECLGTKERLV 247
Cdd:pfam15294 138 LKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQK--EQGAKKDvksnlkeisdleEKMAALKSDLEKTLNASTALQ 215
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 54312052 248 QELQT-------ERLQLQEErstLSTQLEEREREFQASEA 280
Cdd:pfam15294 216 KSLEEdlastkhELLKVQEQ---LEMAEKELEKKFQQTAA 252
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
158-326 |
1.72e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQkletlgarvleLE 237
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ-----------FE 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 ECLGTKERLVQELQTERLQLQEERSTLSTQLEererEFQASEAALSSSRAEVlclRQKTAAQVTLLAEQGDRLYGlemER 317
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLE----KDQQEKEELISSKETS---NKKAQDKVNDIKEKVKNIHG---YM 957
|
....*....
gi 54312052 318 RRLHNQLQE 326
Cdd:TIGR00606 958 KDIENKIQD 966
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
173-286 |
1.79e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 173 YREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQELQT 252
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
90 100 110
....*....|....*....|....*....|....
gi 54312052 253 ERLQLQEERSTLSTQLEEREREFQASEAALSSSR 286
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
159-262 |
2.15e-03 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEEL----KQYREKTQTLDR----------ENQGLREQLRE----VQEQATTLGTERNTLEEELASVR--RR 218
Cdd:pfam09738 126 LKDKLEEMEESLaelqRELREKNKELERlkrnlrrlqfQLAELKEQLKQrdelIEKHGLVIVPDENTNGEEENSPAdaKR 205
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 54312052 219 AEQSQ---QKLETLGARVLE--LEECLGTKERLVQELQTERLQLQEERS 262
Cdd:pfam09738 206 ALVSVeaaEVLESAGEGSLDvrLKKLADEKEELLDEVRKLKLQLEEEKS 254
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
160-290 |
2.32e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 160 KGQLCDLHEELKQYREKTQTLDRENQGLRE----------QLREVQEQATTLGTERNTLEEELASVRRRAEQSQ-----Q 224
Cdd:pfam17045 102 RKQLKEAREEAKSREEDRSELSRLNGKLEEfrqksleweqQRLQYQQQVASLEAQRKALAEQSSLIQSAAYQVQlegrkQ 181
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54312052 225 KLETLGARVLELEECLGTKER--LVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVL 290
Cdd:pfam17045 182 CLEASQSEIQRLRSKLERAQDslCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQVL 249
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-274 |
2.63e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 158 DLKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 54312052 238 ECLG------------------------------------------TKERLvQELQTERLQLQEERSTLSTQLEERERE 274
Cdd:TIGR02169 938 DPKGedeeipeeelsledvqaelqrveeeiralepvnmlaiqeyeeVLKRL-DELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
189-331 |
3.00e-03 |
|
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: 40.88 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 189 EQL-REVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQElQTERLQL-QEERSTLST 266
Cdd:pfam05557 12 SQLqNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALRE-QAELNRLkKKYLEALNK 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54312052 267 QLEERE-REFQASEAalsssraeVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQELKGNI 331
Cdd:pfam05557 91 KLNEKEsQLADAREV--------ISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
162-334 |
3.18e-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: 40.65 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETlgARvLELEECLG 241
Cdd:pfam07888 210 QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ--AR-LQAAQLTL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 242 TKERLVQELQTERLQLQEERSTLSTQLE-ERER------EFQASEAALSSSRAEvlclRQKtaAQVTLLAEQGDRLYGLE 314
Cdd:pfam07888 287 QLADASLALREGRARWAQERETLQQSAEaDKDRieklsaELQRLEERLQEERME----REK--LEVELGREKDCNRVQLS 360
|
170 180
....*....|....*....|
gi 54312052 315 MERRrlhnQLQELKGNIRVF 334
Cdd:pfam07888 361 ESRR----ELQELKASLRVA 376
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
189-277 |
3.44e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.05 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 189 EQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGArVLELEEclgtKERLVQELQTERLQLQEERSTLSTQL 268
Cdd:COG2825 36 QESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAA-TLSEEE----RQKKERELQKKQQELQRKQQEAQQDL 110
|
....*....
gi 54312052 269 EEREREFQA 277
Cdd:COG2825 111 QKRQQELLQ 119
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
165-312 |
3.65e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLE-EELASVRRRAEQSQQ----KLETLGARVLELEEC 239
Cdd:PRK02224 603 DAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEqveeKLDELREERDDLQAE 682
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 54312052 240 LGTKERLVQELQT---ERLQLQEERSTLSTQLEERErEFQASEAALsssRAEvlcLRQKTAAQV-TLLAEQGDRLYG 312
Cdd:PRK02224 683 IGAVENELEELEElreRREALENRVEALEALYDEAE-ELESMYGDL---RAE---LRQRNVETLeRMLNETFDLVYQ 752
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-264 |
3.68e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGA---RVL-ELEEclg 241
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnlLAIeEYEE--- 792
|
90 100
....*....|....*....|...
gi 54312052 242 TKERLvQELQTERLQLQEERSTL 264
Cdd:COG1196 793 LEERY-DFLSEQREDLEEARETL 814
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
163-332 |
3.88e-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: 40.72 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 163 LCDLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTErntlEEELASVRRRAEQSQQKLETLGARVL-ELEECLG 241
Cdd:TIGR00618 530 MQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS----FSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSE 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 242 TKERLVQELQTERLQLQEERSTLSTQLEEREreFQASEAalsssraevLCLRQKTAAQVTLLAEQgdrlyglEMERRRLH 321
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQ--CSQELA---------LKLTALHALQLTLTQER-------VREHALSI 667
|
170
....*....|.
gi 54312052 322 NQLQELKGNIR 332
Cdd:TIGR00618 668 RVLPKELLASR 678
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
160-278 |
3.96e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 160 KGQLCDLHEELKQYREKTQTLDRENQGLREQLREVQEQAT----------------------TLGTERNTLEEELASVRR 217
Cdd:pfam00038 3 KEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGaepsrlyslyekeiedlrrqldTLTVERARLQLELDNLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54312052 218 RAEQSQQKLETLGARVLELEECLGTKERLVQELQTERLQLQEERSTLSTQL-------EEREREFQAS 278
Cdd:pfam00038 83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELaflkknhEEEVRELQAQ 150
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
165-250 |
4.10e-03 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 39.61 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKletLGARVLELEECLGTKE 244
Cdd:pfam14932 78 EIREATEDLEAELQELQKTKQLKINRLNKLQAQASSLSQGLRALVAEEEEAAKQLEELQEE---LAALNAKTNNVLQSLQ 154
|
....*.
gi 54312052 245 RLVQEL 250
Cdd:pfam14932 155 SEVKEL 160
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
168-243 |
4.36e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 168 EELKQYREKTQTLDRENQGLREQLREVQEQATTLGTE-------RNTLEEELASVRRRAEQSQQ----KLETLGARVLEL 236
Cdd:smart00787 204 TELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKiedltnkKSELNTEIAEAEKKLEQCRGftfkEIEKLKEQLKLL 283
|
....*..
gi 54312052 237 EECLGTK 243
Cdd:smart00787 284 QSLTGWK 290
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
168-332 |
4.49e-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: 40.34 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 168 EELKQYREKTQTLDRENQGLREQLrevQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLgarvLELEECLGTKERLV 247
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCT---PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL----TQKREAQEEQLKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 248 QELQTERLQLQEERSTLSTQLEERER-EFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEMERRRLHNQLQE 326
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERiNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
....*.
gi 54312052 327 LKGNIR 332
Cdd:TIGR00618 340 IEEQRR 345
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
165-280 |
4.81e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQAttlgterNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKE 244
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEA-------QELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
90 100 110
....*....|....*....|....*....|....*.
gi 54312052 245 RLVQELQTERLQLQEERSTLSTQLEEREREFQASEA 280
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEEL 265
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
207-274 |
4.93e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 36.77 E-value: 4.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54312052 207 TLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKERLVQELQTERLQLQEERSTLSTQLEERERE 274
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEE 68
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
166-331 |
5.65e-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: 39.95 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 166 LHEELKQYREKTQTLDRENQGLREQLREVQEQATTLgTERNTLEEELASVRRRAEQSQQKLETLGARVLELEECLGTKER 245
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL-LELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQ 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 246 LVQELQTERLQLQEERSTLStQLEEREREFQASEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRLYGLEmERRRLHNQLQ 325
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRA-SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE-DMLACEQHAL 617
|
....*.
gi 54312052 326 ELKGNI 331
Cdd:TIGR00618 618 LRKLQP 623
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
171-274 |
6.20e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 171 KQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGArvLELEEclgTKERLVQEL 250
Cdd:PRK12704 89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG--LTAEE---AKEILLEKV 163
|
90 100
....*....|....*....|....
gi 54312052 251 QTErlqLQEERSTLSTQLEERERE 274
Cdd:PRK12704 164 EEE---ARHEAAVLIKEIEEEAKE 184
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
165-329 |
6.93e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGT---------------ERNTLEEELASVRRR---AEQSQQKL 226
Cdd:COG3096 833 DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEqlqllnkllpqanllADETLADRLEELREEldaAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 227 ETLGARVLELEECLGTKERLVQ---ELQTERLQLQEERSTLSTQLE------EREREFQASEAA--LSSSRAEVLCLRQK 295
Cdd:COG3096 913 QQHGKALAQLEPLVAVLQSDPEqfeQLQADYLQAKEQQRRLKQQIFalsevvQRRPHFSYEDAVglLGENSDLNEKLRAR 992
|
170 180 190
....*....|....*....|....*....|....
gi 54312052 296 TAAQVTLLAEQGDRLYGLEMERRRLHNQLQELKG 329
Cdd:COG3096 993 LEQAEEARREAREQLRQAQAQYSQYNQVLASLKS 1026
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
168-327 |
7.09e-03 |
|
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: 38.82 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 168 EELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASvRRRAEQSQQKLETLGARVLELEECLGTKERLV 247
Cdd:pfam12795 30 DKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILA-SLSLEELEQRLLQTSAQLQELQNQLAQLNSQL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 248 QELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEvlcLRQKTAAQVTLLAEQgdrlygLEMERRRL--HNQLQ 325
Cdd:pfam12795 109 IELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEA---QRWALQAELAALKAQ------IDMLEQELlsNNNRQ 179
|
..
gi 54312052 326 EL 327
Cdd:pfam12795 180 DL 181
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
167-344 |
7.16e-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: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 167 HEELKQYREKTQTLDRENQGLREQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETL-GARVLELEECLGTKER 245
Cdd:pfam17380 339 QERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAArKVKILEEERQRKIQQQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 246 LVQELQTERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVLCLRQKTAAQ----VTLLAEQGDRLYGLEMERRRLH 321
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERkrkkLELEKEKRDRKRAEEQRRKILE 498
|
170 180
....*....|....*....|...
gi 54312052 322 NQLQELKGNIRVFCRVRPVLEGE 344
Cdd:pfam17380 499 KELEERKQAMIEEERKRKLLEKE 521
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
219-288 |
7.33e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 37.89 E-value: 7.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54312052 219 AEQSQQKLETLGA-RVLELEeclgtkeRLVQELQTERLQLQEERSTLS-TQLEEREREFQASEAALSSSRAE 288
Cdd:COG2825 41 GKAAQKKLEKEFKkRQAELQ-------KLEKELQALQEKLQKEAATLSeEERQKKERELQKKQQELQRKQQE 105
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
159-310 |
7.40e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.78 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 159 LKGQLCDLHEELKQYREKTQTLDRENQGLREQLREVqeqATTLGTERNtLEEELASVRRRAEQSQQKLETLGARvLELEE 238
Cdd:PRK10246 549 LRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAV---CASLNITLQ-PQDDIQPWLDAQEEHERQLRLLSQR-HELQG 623
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54312052 239 CLGTKERLV----QELQTERLQLQEERSTLSTQLEERErefqaSEAALSSSRAEVLCLRQKTAAQVTLLAEQGDRL 310
Cdd:PRK10246 624 QIAAHNQQIiqyqQQIEQRQQQLLTALAGYALTLPQED-----EEASWLATRQQEAQSWQQRQNELTALQNRIQQL 694
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
165-327 |
9.35e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 39.29 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKTQTLDRENQGLREQLREVQEQATTLGtERNTLEEE---LASVRRRAEQSQQKLETLGARVLELEECLG 241
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAALQPG-EEEELEEErrrLSNAEKLREALQEALEALSGGEGGALDLLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 242 TKERLVQELQT---------ERL-----QLQEERSTLSTQLEERE---REFQASEAALS----------SSRAEVLCLRQ 294
Cdd:COG0497 248 QALRALERLAEydpslaelaERLesaliELEEAASELRRYLDSLEfdpERLEEVEERLAllrrlarkygVTVEELLAYAE 327
|
170 180 190
....*....|....*....|....*....|...
gi 54312052 295 KTAAQVTLLAEQGDRLYGLEMERRRLHNQLQEL 327
Cdd:COG0497 328 ELRAELAELENSDERLEELEAELAEAEAELLEA 360
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
189-278 |
9.55e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 37.18 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 189 EQLREVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGArVLELEEclgtKERLVQELQTERLQLQEERSTLSTQL 268
Cdd:smart00935 11 QESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAA-TLSEAA----REKKEKELQKKVQEFQRKQQKLQQDL 85
|
90
....*....|
gi 54312052 269 EEREREFQAS 278
Cdd:smart00935 86 QKRQQEELQK 95
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
165-335 |
9.57e-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: 39.18 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 165 DLHEELKQYREKtqtLDRENQgLREQLREVQEQATTLGTERNTLEEELASVRRraEQSQQKLETLGARVLELEECLGTKE 244
Cdd:TIGR00618 359 DAHEVATSIREI---SCQQHT-LTQHIHTLQQQKTTLTQKLQSLCKELDILQR--EQATIDTRTSAFRDLQGQLAHAKKQ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 245 rlvQELQTERLQLQEERSTLSTQLEE-REREFQASEAALSSsraevlclRQKTAAQVTLLAEQGDRLYGLEMERrrlhnq 323
Cdd:TIGR00618 433 ---QELQQRYAELCAAAITCTAQCEKlEKIHLQESAQSLKE--------REQQLQTKEQIHLQETRKKAVVLAR------ 495
|
170
....*....|..
gi 54312052 324 LQELKGNIRVFC 335
Cdd:TIGR00618 496 LLELQEEPCPLC 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
162-328 |
9.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 162 QLCDLHEELKQYR-EKTQTLDRENQGLREQLREVQEQATTLGTERNTLEE---ELASVRRRAEQSQQKLETLGARVLELE 237
Cdd:PRK03918 504 QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELG 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 238 -ECLGTKERLVQELQT---ERLQLQEERSTLSTQLEER---EREFQASEAALSSSRAEVLCLRQK-TAAQVTLLAEQGDR 309
Cdd:PRK03918 584 fESVEELEERLKELEPfynEYLELKDAEKELEREEKELkklEEELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEE 663
|
170 180
....*....|....*....|...
gi 54312052 310 LYG----LEMERRRLHNQLQELK 328
Cdd:PRK03918 664 LREeyleLSRELAGLRAELEELE 686
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
167-330 |
9.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 167 HEELKQYREKTQTLDREnQGLREQlrEVQEQATTLGTERNTLEEELASVRRRAEQSQQKLETLGA--RVLELEECLGTKE 244
Cdd:COG4717 297 KASLGKEAEELQALPAL-EELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEleEELQLEELEQEIA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54312052 245 RLVQELQT--------------ERLQLQEERSTLSTQLEEREREFQASEAALSSSRAEVlcLRQKTAAQVTLLAEQGDRL 310
Cdd:COG4717 374 ALLAEAGVedeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDEEELEE--ELEELEEELEELEEELEEL 451
|
170 180
....*....|....*....|
gi 54312052 311 YgleMERRRLHNQLQELKGN 330
Cdd:COG4717 452 R---EELAELEAELEQLEED 468
|
|
| |
