|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
15-350 |
6.16e-165 |
|
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: 496.47 E-value: 6.16e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYG 94
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 95 QTGSGKTYTMGEASVASLHEDEQGIIPRAMAEAFKLIDE-NDLLDCLVHVSYLELYKEEFRDLLEVGTASR-DIQLREDD 172
Cdd:cd01372 82 QTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKkKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKpTISIREDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 173 RGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPRPAAGHL--LVSKFHF 250
Cdd:cd01372 162 KGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNstFTSKFHF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 251 VDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:cd01372 242 VDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPAD 321
|
330 340
....*....|....*....|
gi 568947410 331 SDFDETLNTLNYASRAQNIR 350
Cdd:cd01372 322 SNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
15-356 |
3.14e-137 |
|
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: 423.14 E-value: 3.14e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERGRIT-------LGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 88 ATVFAYGQTGSGKTYTMGEasvaslHEDEQGIIPRAMAEAFKLIDEN-DLLDCLVHVSYLELYKEEFRDLLevGTASRDI 166
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLL--NPSSKKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 167 QLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRlprpaaGHLLVS 246
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS------GSGKAS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRgSHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:smart00129 227 KLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSKLTRLLQDSLGGNSKTLMIANV 305
|
330 340 350
....*....|....*....|....*....|
gi 568947410 327 SPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:smart00129 306 SPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
21-349 |
7.73e-134 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 413.51 E-value: 7.73e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 21 RVRPLLPKELLHGHQSCLRVEPERGRITL-------GRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 94 GQTGSGKTYTMGEAsvaslhEDEQGIIPRAMAEAFKLIDEN-DLLDCLVHVSYLELYKEEFRDLLEVGTAS-RDIQLRED 171
Cdd:pfam00225 81 GQTGSGKTYTMEGS------DEQPGIIPRALEDLFDRIQKTkERSEFSVKVSYLEIYNEKIRDLLSPSNKNkRKLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 172 DRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPrpaagHLLVSKFHFV 251
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEE-----SVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 252 DLAGSERVLKTG-STGERLKESIQINSTLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSS 307
|
330
....*....|....*....
gi 568947410 331 SDFDETLNTLNYASRAQNI 349
Cdd:pfam00225 308 SNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
15-347 |
5.03e-123 |
|
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: 384.68 E-value: 5.03e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 15 PVRVALRVRPLLPKELLHGHqSCLRVEPERG-RITLGRDRH-----FGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAK-SVISVDGGKSvVLDPPKNRVappktFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 89 TVFAYGQTGSGKTYTMGEASvaslhEDEQGIIPRAMAEAFKLIDENDLLD--CLVHVSYLELYKEEFRDLLEvGTASRDI 166
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKssFSVSASYLEIYNEKIYDLLS-PVPKKPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 167 QLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprpaAGHLLVS 246
Cdd:cd00106 154 SLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS------GESVTSS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRgsHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd00106 228 KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 568947410 327 SPSSSDFDETLNTLNYASRAQ 347
Cdd:cd00106 306 SPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
16-349 |
4.22e-106 |
|
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: 339.71 E-value: 4.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 16 VRVALRVRPLLPKELLHGHQSCLRV---------EPERGRITL-------------GRDRHFGFHVVLGEDTGQEAVYQA 73
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfdPKDEEDGFFhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 74 CVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDE-NDLLDCLVHVSYLELYKEE 152
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTM------LGTPQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 153 FRDLLEvgTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTP 232
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 233 SRLPRPAAGHLLVskfhfVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKD 312
Cdd:cd01370 234 SINQQVRQGKLSL-----IDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKD 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 568947410 313 SLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01370 309 SLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
16-349 |
7.09e-105 |
|
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: 335.97 E-value: 7.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 16 VRVALRVRPLLPKELLHGHQSCLRVEPERGRITL--GRD------RHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 88 ATVFAYGQTGSGKTYTMGEASVAslhEDEQGIIPRAMAEAFKLID-ENDLLDCLVHVSYLELYKEEFRDLLEVGTASRdI 166
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEGKRED---PELRGIIPNSFAHIFGHIArSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 167 QLRED-DRGNVV--LCGVKEVDVEGLDEVLSLlemGNAARHTGATHFNRLSSRSHTVFTVTLEQrgrtpSRLPRPAAGHL 243
Cdd:cd01371 159 ELKERpDTGVYVkdLSMFVVKNADEMEHVMNL---GNKNRSVGATNMNEDSSRSHAIFTITIEC-----SEKGEDGENHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 244 LVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPqrRGSHIPYRDSKITRILKDSLGGNAKTVMI 323
Cdd:cd01371 231 RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
|
330 340
....*....|....*....|....*.
gi 568947410 324 ACVSPSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01371 309 ANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
16-356 |
7.64e-102 |
|
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: 328.93 E-value: 7.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 16 VRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRH------------FGFHVVL----GED---TGQEAVYQACVQ 76
Cdd:cd01365 3 VKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADknnkatrevpksFSFDYSYwshdSEDpnyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 77 PLLEAFFEGFNATVFAYGQTGSGKTYTMGEAsvaslhEDEQGIIPRAMAEAFKLID--ENDLLDCLVHVSYLELYKEEFR 154
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT------QEQPGIIPRLCEDLFSRIAdtTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 155 DLLEVGTASRDIQL--REDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRgRTP 232
Cdd:cd01365 157 DLLNPKPKKNKGNLkvREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQK-RHD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 233 SRLPRPAAghlLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQR-----RGSHIPYRDSKIT 307
Cdd:cd01365 236 AETNLTTE---KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSVLT 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568947410 308 RILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:cd01365 313 WLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
16-349 |
1.26e-101 |
|
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: 326.60 E-value: 1.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 16 VRVALRVRPLLPKELLHG--------HQSCLRVEPERGRitlgrdrhFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01374 2 ITVTVRVRPLNSREIGINeqvaweidNDTIYLVEPPSTS--------FTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 88 ATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDENDLLDCLVHVSYLELYKEEFRDLLEVGtaSRDIQ 167
Cdd:cd01374 74 GTIFAYGQTSSGKTFTM------SGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 168 LREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPsrlprPAAGHLLVSK 247
Cdd:cd01374 146 IRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGE-----LEEGTVRVST 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 248 FHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGsHIPYRDSKITRILKDSLGGNAKTVMIACVS 327
Cdd:cd01374 221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG-HIPYRDSKLTRILQPSLGGNSRTAIICTIT 299
|
330 340
....*....|....*....|..
gi 568947410 328 PSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01374 300 PAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
16-358 |
1.64e-96 |
|
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: 313.88 E-value: 1.64e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 16 VRVALRVRPLLPKELLHGHQSCLRVEPERGRITL--------GRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 88 ATVFAYGQTGSGKTYTM-GEASVASLHEDEQ----GIIPRAMAEAFKLIDENDLlDCLVHVSYLELYKEEFRDLLEV-GT 161
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMeGDRSPNEEYTWELdplaGIIPRTLHQLFEKLEDNGT-EYSVKVSYLEIYNEELFDLLSPsSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 162 ASRDIQLREDDR--GNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprpa 239
Cdd:cd01364 163 VSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTID------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 240 aGHLLV--SKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDpqrRGSHIPYRDSKITRILKDSLGGN 317
Cdd:cd01364 237 -GEELVkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568947410 318 AKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWR 358
Cdd:cd01364 313 TKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
16-351 |
5.04e-95 |
|
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: 308.75 E-value: 5.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 16 VRVALRVRPLLPKELlHGHQSCLRVEPERG-RITL---GRDRH-FGFHVVLGEDTGQEAVYQAcVQPLLEAFFEGFNATV 90
Cdd:cd01366 4 IRVFCRVRPLLPSEE-NEDTSHITFPDEDGqTIELtsiGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 91 FAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDENDLLDCLVH--VSYLELYKEEFRDLLEVGTASR---D 165
Cdd:cd01366 82 FAYGQTGSGKTYTM------EGPPESPGIIPRALQELFNTIKELKEKGWSYTikASMLEIYNETIRDLLAPGNAPQkklE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 166 IQlREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLeqRGRTPSRlprpaaGHLLV 245
Cdd:cd01366 156 IR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQT------GEISV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGdpqRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01366 227 GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR---QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 568947410 326 VSPSSSDFDETLNTLNYASRAQNIRN 351
Cdd:cd01366 304 ISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
16-349 |
4.99e-93 |
|
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: 303.10 E-value: 4.99e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 16 VRVALRVRPLLPKELLHGHQSCLRVEPERgRITLGRD---RHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFA 92
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPED-TVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 93 YGQTGSGKTYTMgeasVASLHEDE-QGIIPRAMAEAFKLIDEND-LLDCLVHVSYLELYKEEFRDLLEVgtaSRD-IQLR 169
Cdd:cd01369 83 YGQTSSGKTYTM----EGKLGDPEsMGIIPRIVQDIFETIYSMDeNLEFHVKVSYFEIYMEKIRDLLDV---SKTnLSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 170 EDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTpsrlprpaAGHLLVSKFH 249
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVE--------TEKKKSGKLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 250 FVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPS 329
Cdd:cd01369 228 LVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRILQDSLGGNSRTTLIICCSPS 305
|
330 340
....*....|....*....|
gi 568947410 330 SSDFDETLNTLNYASRAQNI 349
Cdd:cd01369 306 SYNESETLSTLRFGQRAKTI 325
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
15-356 |
8.00e-86 |
|
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: 283.63 E-value: 8.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLG-RDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 94 GQTGSGKTYTM-GEAS--VASLHEDeQGIIPRAMAEAFKLID-----ENDLLDCLVHVSYLELYKEEFRDLLEvgTASRD 165
Cdd:cd01373 82 GQTGSGKTYTMwGPSEsdNESPHGL-RGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLLD--PASRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 166 IQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprpaAGHLLV 245
Cdd:cd01373 159 LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKAC------FVNIRT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGD-PQRRGSHIPYRDSKITRILKDSLGGNAKTVMIA 324
Cdd:cd01373 233 SRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340 350
....*....|....*....|....*....|..
gi 568947410 325 CVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
55-356 |
4.88e-85 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 289.33 E-value: 4.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 55 FGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDEN 134
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM------SGTEEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 135 DLLDCL-VHVSYLELYKEEFRDLLEVGTASRDIqlREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRL 213
Cdd:COG5059 132 SMTKDFaVSISYLEIYNEKIYDLLSPNEESLNI--REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 214 SSRSHTVFTVTLEQRGRTPSRLPRpaaghllvSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQ 293
Cdd:COG5059 210 SSRSHSIFQIELASKNKVSGTSET--------SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947410 294 RRGsHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:COG5059 282 KSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
15-347 |
3.50e-79 |
|
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: 265.03 E-value: 3.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 15 PVRVALRVRPLLPKELLHGHQSCLRVE--------PERGRITLGRDR-------HFGFHVVLGEDTGQEAVYQACVQPLL 79
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVInsttvvlhPPKGSAANKSERnggqketKFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 80 EAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLHEDEQGIIPRAMAEAFKLIDENDlldclVHVSYLELYKEEFRDLLEV 159
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTM------QGSPGDGGILPRSLDVIFNSIGGYS-----VFVSYIEIYNEYIYDLLEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 160 GTASRD-----IQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQrgrtpsr 234
Cdd:cd01368 151 SPSSPTkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQ------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 235 LPRPAAGHLL-------VSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRG--SHIPYRDSK 305
Cdd:cd01368 224 APGDSDGDVDqdkdqitVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtnKMVPFRDSK 303
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568947410 306 ITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQ 347
Cdd:cd01368 304 LTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
15-345 |
3.54e-78 |
|
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: 261.46 E-value: 3.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 15 PVRVALRVRPLLPKELLHGHQ--------SCLRVEPERGRITLGR--DRH-FGFHVVLGEDTGQEAVYQACVQPLLEAFF 83
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIdvvsvpskLTLIVHEPKLKVDLTKyiENHtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 84 EGFNATVFAYGQTGSGKTYTMGEASvaSLHEDEQGIIPRAMAEAFKLIDE-NDLLDCLVHVSYLELYKEEFRDLLEVGTa 162
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKlPYKDNLGVTVSFFEIYGGKVFDLLNRKK- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 163 srDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLeqrgrtpsrlpRPAAGH 242
Cdd:cd01367 158 --RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-----------RDRGTN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 243 LLVSKFHFVDLAGSER-VLKTGSTGERLKESIQINSTLLALGNVISALGDPQrrgSHIPYRDSKITRILKDSL-GGNAKT 320
Cdd:cd01367 225 KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSKT 301
|
330 340
....*....|....*....|....*
gi 568947410 321 VMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01367 302 CMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
15-347 |
7.54e-78 |
|
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: 260.13 E-value: 7.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 15 PVRVALRVRPLLPKELLHGHQSCLRVEPERgRITLGRDRHFG------FHVVLGEDTGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSC-SVELADPRNHGetlkyqFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 89 TVFAYGQTGSGKTYTM-GeasvaslHEDEQGIIPRAMAEAFKLIDENDLLDClVHVSYLELYKEEFRDLLEVgtASRDIQ 167
Cdd:cd01376 80 TVFAYGSTGAGKTFTMlG-------SPEQPGLMPLTVMDLLQMTRKEAWALS-FTMSYLEIYQEKILDLLEP--ASKELV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 168 LREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRT-PSRLPRpaaghllvS 246
Cdd:cd01376 150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLaPFRQRT--------G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRgshIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR---IPYRDSKLTRLLQDSLGGGSRCIMVANI 298
|
330 340
....*....|....*....|.
gi 568947410 327 SPSSSDFDETLNTLNYASRAQ 347
Cdd:cd01376 299 APERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
55-345 |
1.82e-72 |
|
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: 245.57 E-value: 1.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 55 FGFHVVLgEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLHedeQGIIPRAMAEAFKLIDEN 134
Cdd:cd01375 50 FKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKH---RGIIPRALQQVFRMIEER 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 135 DLLDCLVHVSYLELYKEEFRDLL----EVGTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHF 210
Cdd:cd01375 126 PTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 211 NRLSSRSHTVFTVTLEQRGRTPSrlprpaAGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALG 290
Cdd:cd01375 206 NKNSSRSHCIFTIHLEAHSRTLS------SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALS 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568947410 291 DPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01375 280 DKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
10-356 |
8.60e-59 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 222.89 E-value: 8.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 10 GAEEAPVRVALRVRPLLPKEllhghQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNAT 89
Cdd:PLN03188 94 GVSDSGVKVIVRMKPLNKGE-----EGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 90 VFAYGQTGSGKTYTM-GEASVAS---LHEDEQGIIPRAMAEAFKLIDENDL------LDCLVHVSYLELYKEEFRDLLEv 159
Cdd:PLN03188 169 VFAYGQTGSGKTYTMwGPANGLLeehLSGDQQGLTPRVFERLFARINEEQIkhadrqLKYQCRCSFLEIYNEQITDLLD- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 160 gTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSrlprPA 239
Cdd:PLN03188 248 -PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVA----DG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 240 AGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGS--HIPYRDSKITRILKDSLGGN 317
Cdd:PLN03188 323 LSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKqrHIPYRDSRLTFLLQESLGGN 402
|
330 340 350
....*....|....*....|....*....|....*....
gi 568947410 318 AKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:PLN03188 403 AKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
706-1202 |
4.43e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 706 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQ----EAERVRAELCEGQRQLRELEGREPQDA 781
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 782 SERSRLQEFRKRVAAAQSQVQVLKEK-KQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEM 860
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAElAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 861 NKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEEL-GEE 939
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELlEEL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 940 LRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEksgQLRQGSAQNQQQIRGEIDTLRQEKD 1019
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA---ALEAALAAALQNIVVEDDEVAAAAI 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1020 SLLKQ----RLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM--NLMAKLS 1093
Cdd:COG1196 564 EYLKAakagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAalRRAVTLA 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1094 YLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQ 1173
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
490 500
....*....|....*....|....*....
gi 568947410 1174 QGRDHLGEGLADSKRQYEARIHALEKELG 1202
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
743-1214 |
3.23e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 743 RQHSQRIRELEQEAERVRAELCEGQRQLRELEGREpqdASERSRLQEFRKRVAAAQSQVQVLKEKKQATE----RLVSLS 818
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEqdiaRLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 819 AQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSG 898
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 899 SNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKtglESKRLRSSQALNEDIVRV 978
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE---EAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 979 SSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKL-RQGSLLSPEEERTLFQLDEAIEALD 1057
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLaGAVAVLIGVEAAYEAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1058 AAIEYKNE--AITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSE-------- 1127
Cdd:COG1196 549 QNIVVEDDevAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllgrtlv 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1128 ---LEMQLEEQQRLVY-WLEVALERQRLEMDRQLTLQQKEH--------EQNVQLLLQQGRDHLGEGLADSKRQYEARIH 1195
Cdd:COG1196 629 aarLEAALRRAVTLAGrLREVTLEGEGGSAGGSLTGGSRREllaalleaEAELEELAERLAEEELELEEALLAEEEEERE 708
|
490
....*....|....*....
gi 568947410 1196 ALEKELGRHMWINQELKQK 1214
Cdd:COG1196 709 LAEAEEERLEEELEEEALE 727
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
729-1066 |
2.08e-14 |
|
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: 78.56 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 729 GELVRTG---------KAAQALNRQhsQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASE----RSRLQEFRKRVA 795
Cdd:TIGR02168 652 GDLVRPGgvitggsakTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 796 AAQSQVQVLKEKkqaTERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHE 875
Cdd:TIGR02168 730 ALRKDLARLEAE---VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 876 QQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQ 955
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 956 EKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgsaQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQG 1035
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE----LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENK 962
|
330 340 350
....*....|....*....|....*....|....*..
gi 568947410 1036 SLLSPEE-ERTLFQLDEAIEA-----LDAAIEYKNEA 1066
Cdd:TIGR02168 963 IEDDEEEaRRRLKRLENKIKElgpvnLAAIEEYEELK 999
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
711-1134 |
7.64e-12 |
|
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: 70.05 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 711 QQKIREL-AINIRMKEELIGELVRTGKAAQALNRQHSQrIRELEQEAERVRAELCEGQRQL-------RELEGREPQDAS 782
Cdd:TIGR04523 217 ESQISELkKQNNQLKDNIEKKQQEINEKTTEISNTQTQ-LNQLKDEQNKIKKQLSEKQKELeqnnkkiKELEKQLNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 783 ERSRL-----QEFRKRVaaaQSQVQVLKEKKQATERLVSlsaQSETRLQELERNVQLMRrqqgqlqrrlreetEQKRRLE 857
Cdd:TIGR04523 296 EISDLnnqkeQDWNKEL---KSELKNQEKKLEEIQNQIS---QNNKIISQLNEQISQLK--------------KELTNSE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 858 TEMNKRQhrvKELElkhEQQQKILKIKTEEIAAFQRKRRSGSNGSvvSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEEL 936
Cdd:TIGR04523 356 SENSEKQ---RELE---EKQNEIEKLKKENQSYKQEIKNLESQIN--DLESKiQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 937 GEELRKrEVILAKKE--ALMQEKTGLES-----KRLRSSQ-----ALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQ 1004
Cdd:TIGR04523 428 IERLKE-TIIKNNSEikDLTNQDSVKELiiknlDNTRESLetqlkVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1005 QqIRGEIDTLRQEKDSLL-------KQRLEIDSKLRQ--GSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITcrqrvlr 1075
Cdd:TIGR04523 507 E-LEEKVKDLTKKISSLKekiekleSEKKEKESKISDleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK------- 578
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568947410 1076 asaSLLSqcemnlmaklsylSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1134
Cdd:TIGR04523 579 ---SLKK-------------KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
18-288 |
2.01e-11 |
|
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: 63.90 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 18 VALRVRPLLpkellhghqsclRVEPERGRITLGRDRHFGFHvvlgedTGQEAVYqACVQPLLEAFFEGFN-ATVFAYGQT 96
Cdd:cd01363 1 VLVRVNPFK------------ELPIYRDSKIIVFYRGFRRS------ESQPHVF-AIADPAYQSMLDGYNnQSIFAYGES 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 97 GSGKTYTMgeasvaslhedeQGIIPRAMAEAFklidendlldclvhvSYLELYKEEFRDLLEvgtasrdiqlreddrgnv 176
Cdd:cd01363 62 GAGKTETM------------KGVIPYLASVAF---------------NGINKGETEGWVYLT------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 177 vlcgvkEVDVEGLDEVLSLLEMGNAARhTGATHFNRLSSRSHTVFTVtleqrgrtpsrlprpaaghllvskfhFVDLAGS 256
Cdd:cd01363 97 ------EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI--------------------------LLDIAGF 143
|
250 260 270
....*....|....*....|....*....|..
gi 568947410 257 ERvlktgstgerlkesiqINSTLLALGNVISA 288
Cdd:cd01363 144 EI----------------INESLNTLMNVLRA 159
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
704-1215 |
2.04e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 704 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQ------ALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGRE 777
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 778 PQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETR-LQELERNVQLMRRQQGQLQRRLREETEQKRRL 856
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 857 ETEMNKRQHRVKEL------------ELKHEQQQKILKIKTEEIAafqrkrrsgsngsvvsleqqqKIEEQKKWLDQEME 924
Cdd:PRK03918 418 KKEIKELKKAIEELkkakgkcpvcgrELTEEHRKELLEEYTAELK---------------------RIEKELKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 925 KVlqqRRALEELGEELRKREVILAKKEALMQektgLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLR--QGSAQ 1002
Cdd:PRK03918 477 KL---RKELRELEKVLKKESELIKLKELAEQ----LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKslKKELE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1003 NQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEertlfqLDEAIEALDAAIEYKNEAITCRQRvLRASASLLS 1082
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE------LEERLKELEPFYNEYLELKDAEKE-LEREEKELK 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1083 QCEMNLMAKLSYLSSSETRallckyfdkVVTLREEQHQQQIAFSElemqlEEQQRlvywlevaLERQRLEMDRQLTLQQK 1162
Cdd:PRK03918 623 KLEEELDKAFEELAETEKR---------LEELRKELEELEKKYSE-----EEYEE--------LREEYLELSRELAGLRA 680
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 568947410 1163 EHEQnvqllLQQGRDHLGEGLADSKRQYEARIHALE--KELGRHMWINQELKQKL 1215
Cdd:PRK03918 681 ELEE-----LEKRREEIKKTLEKLKEELEEREKAKKelEKLEKALERVEELREKV 730
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
747-1061 |
2.75e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 747 QRIRELEQEAERVR--AELcegQRQLRELEGREpqdasersRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETR 824
Cdd:COG1196 200 RQLEPLERQAEKAEryREL---KEELKELEAEL--------LLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 825 LQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvv 904
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE------- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 905 slEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALnEDIVRVSSRLEH 984
Cdd:COG1196 342 --LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE-EAEEALLERLER 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568947410 985 LEKELSEKsgqlrqgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1061
Cdd:COG1196 419 LEEELEEL--------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
707-1034 |
4.50e-11 |
|
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: 67.35 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 707 LAQAQQKIRELAINIRMKEELIGELvrtgkaaqalNRQHSQ---RIRELEQEAERVRAELCEGQRQLRELEgREPQdase 783
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL----------NEQISQlkkELTNSESENSEKQRELEEKQNEIEKLK-KENQ---- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 784 rSRLQEFRKrvaaAQSQVQVLKEKKQATERLvslSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKR 863
Cdd:TIGR04523 381 -SYKQEIKN----LESQINDLESKIQNQEKL---NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 864 QHRVKELELKHEQQQKILKIKTEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKwldQEMEKVLQQRRALEELGEELRKR 943
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQN-----------LEQKQKELKSKE---KELKKLNEEKKELEEKVKDLTKK 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 944 -EVILAKKEALMQEKTGLESKrLRSsqaLNEDIVRVSSRL--EHLEKELSEKsgqlrqgsaqNQqqirgEIDTLRQEKDS 1020
Cdd:TIGR04523 519 iSSLKEKIEKLESEKKEKESK-ISD---LEDELNKDDFELkkENLEKEIDEK----------NK-----EIEELKQTQKS 579
|
330
....*....|....
gi 568947410 1021 LLKQRLEIDSKLRQ 1034
Cdd:TIGR04523 580 LKKKQEEKQELIDQ 593
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
799-1083 |
7.23e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 799 SQVQVLKEKKQATERLVSLSAQSETRLQELE-RNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQ 877
Cdd:COG1196 200 RQLEPLERQAEKAERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 878 QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRAL-EELGEELRKREVILAKKEALMQE 956
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 957 KTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQlrqgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGS 1036
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-----AAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568947410 1037 LLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1083
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
747-1083 |
9.79e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 747 QRIRELEQEAERVRAELCEGQRQLRELEgrepQDASERSRLQEFRKRVAAAQSQVQV--LKEKKQATERLVSLSAQSETR 824
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLE----RQAEKAERYKELKAELRELELALLVlrLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 825 LQELERnvqlmrrqqgqlqrrlreeteQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVV 904
Cdd:TIGR02168 255 LEELTA---------------------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 905 SLEQQQKIEEQkkwLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEH 984
Cdd:TIGR02168 314 LERQLEELEAQ---LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 985 LEKELSEKSGQLRQGSAQnQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLlsPEEERTLFQLDEAIEALDAAIEYKN 1064
Cdd:TIGR02168 391 LELQIASLNNEIERLEAR-LERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEELQEELERLEEALEELR 467
|
330
....*....|....*....
gi 568947410 1065 EAITCRQRVLRASASLLSQ 1083
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQ 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
715-1061 |
1.65e-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: 65.86 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 715 RELAINIRMKEeLIGELVRTGKAAQALNRQHSQRI---RELEQEAERVRAELCEGQRQLrelegrepqdASERSRLQEFR 791
Cdd:TIGR02169 633 RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGIlfsRSEPAELQRLRERLEGLKREL----------SSLQSELRRIE 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 792 KRVAAAQSQVQVlkekkqATERLVSLSAQSETRLQELERNVQLMRRQQgqlqRRLREETEQKRRLETEMNKRQHRVKELE 871
Cdd:TIGR02169 702 NRLDELSQELSD------ASRKIGEIEKEIEQLEQEEEKLKERLEELE----EDLSSLEQEIENVKSELKELEARIEELE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 872 LK-HEQQQKILKIKT-------EEIAA---FQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEE 939
Cdd:TIGR02169 772 EDlHKLEEALNDLEArlshsriPEIQAelsKLEEEVSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 940 LRKR-EVILAKKEALMQEktgLESKRLRSSQalnedivrVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLR--- 1015
Cdd:TIGR02169 852 IEKEiENLNGKKEELEEE---LEELEAALRD--------LESRLGDLKKERDELEAQLRE-LERKIEELEAQIEKKRkrl 919
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568947410 1016 ---QEKDSLLKQRL-EIDSKLRQGSlLSPEEERTLFQLDEAIEALDAAIE 1061
Cdd:TIGR02169 920 selKAKLEALEEELsEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIR 968
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
848-1227 |
3.63e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 848 EETEQKRRlETEMN-----------KRQhrVKELELKHEQQQKILKIKTEEiaafQRKRRSGSNGSVVSL-EQQQKIEEQ 915
Cdd:TIGR02168 175 KETERKLE-RTRENldrledilnelERQ--LKSLERQAEKAERYKELKAEL----RELELALLVLRLEELrEELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 916 KKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLrssQALNEDIVRVSSRLEHLEKELSEKSGQ 995
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 996 LRQGSAQNQQQIRgEIDTLRQEKDSLLKQRLEIDSKLrqgsllsPEEERTLFQLDEAIEALDAAIEYKNEAItcrqrvlr 1075
Cdd:TIGR02168 325 LEELESKLDELAE-ELAELEEKLEELKEELESLEAEL-------EELEAELEELESRLEELEEQLETLRSKV-------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1076 asASLLSQcEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERqrleMDR 1155
Cdd:TIGR02168 389 --AQLELQ-IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER----LEE 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947410 1156 QLTLQQKEHEQNVQLLLQQGRDHlgegladskRQYEARIHALEKELGRHMWINQELKQKLSAGSTAGQSRGC 1227
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
707-1215 |
3.99e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 707 LAQAQQKIRELAINIRMKEELI-------GELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQ 779
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLeelrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 780 DASERSRLQEFRKRVAAAQSQVQV-LKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLET 858
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 859 EMNKRQHRVKEL-ELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQ-QQKIEEQKKWLDQEMEKVLQQRRALEEL 936
Cdd:TIGR02168 408 RLERLEDRRERLqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERlEEALEELREELEEAEQALDAAERELAQL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 937 GEELRKREVILAKKEALMQEKTGLESKRLRSSQALNE--DIVRVSSRLEH-LEKELSEKSGQLrqgSAQNQQQIRGEIDT 1013
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlsELISVDEGYEAaIEAALGGRLQAV---VVENLNAAKKAIAF 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1014 LRQE---KDSLLKQRLEIDSKLRQGSLLSPEEER----TLFQLDEAIEALDAAIEY--------KNEAITCRQRV-LRAS 1077
Cdd:TIGR02168 565 LKQNelgRVTFLPLDSIKGTEIQGNDREILKNIEgflgVAKDLVKFDPKLRKALSYllggvlvvDDLDNALELAKkLRPG 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1078 ASLLSQcEMNLMAK--LSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLE---VALERQRLE 1152
Cdd:TIGR02168 645 YRIVTL-DGDLVRPggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeelEQLRKELEE 723
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947410 1153 MDRQLTLQQKE---HEQNVQLLLQQGRDHLGE--GLADSKRQYEARIHALEKELGRHMWINQELKQKL 1215
Cdd:TIGR02168 724 LSRQISALRKDlarLEAEVEQLEERIAQLSKEltELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
708-1033 |
5.01e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 708 AQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASE---- 783
Cdd:TIGR02168 207 RQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEieel 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 784 RSRLQEFRKRVAAAQSQVQVLKEKKqatERLVSLSAQSETRLQELERnvqlmrrqqgqlqrrlreeteQKRRLETEMNKR 863
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERL---ANLERQLEELEAQLEELES---------------------KLDELAEELAEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 864 QHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELrkr 943
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLE----------ELEEQLETLRSKVAQLELQIASLNNEIERLEARL--- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 944 EVILAKKEALMQEKTGLESKRLRSsqalneDIVRVSSRLEHLEKELSEKSGQLRQGSAQnQQQIRGEIDTLRQEKDSLLK 1023
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEA------ELKELQAELEELEEELEELQEELERLEEA-LEELREELEEAEQALDAAER 482
|
330
....*....|
gi 568947410 1024 QRLEIDSKLR 1033
Cdd:TIGR02168 483 ELAQLQARLD 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
706-1021 |
1.00e-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: 63.54 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 706 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRE-------LEQEAERVRAELCEGQRQLREL----E 774
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdlarLEAEVEQLEERIAQLSKELTELeaeiE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 775 GREPQDASERSRLQEFRKRVAAAQSQVQVLK-EKKQATERLVSLSAQsetrLQELERNVQLMRRQQGQLQRRLREETEQK 853
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELRAE----LTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 854 RRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRAL 933
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-------LEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 934 EELGEELRKrevilaKKEALMQEKTGLESKRLRSSQALNEdivRVSSRLEHLEKELSEKSGQlrqgsaqnQQQIRGEIDT 1013
Cdd:TIGR02168 914 RRELEELRE------KLAQLELRLEGLEVRIDNLQERLSE---EYSLTLEEAEALENKIEDD--------EEEARRRLKR 976
|
....*...
gi 568947410 1014 LRQEKDSL 1021
Cdd:TIGR02168 977 LENKIKEL 984
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
16-157 |
1.89e-09 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 57.62 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 16 VRVALRVRPLLPKELlhghqsclRVEPERGRITLGRDRH----FGFHVVLGEDTGQEAVYQACVQpLLEAFFEGFNATVF 91
Cdd:pfam16796 22 IRVFARVRPELLSEA--------QIDYPDETSSDGKIGSknksFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVCIF 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568947410 92 AYGQTGSGKTYTMgeasvaslhedeqgiIPRAMAEAFKLIDENDLLDCL-VHVSYLELYKEEFRDLL 157
Cdd:pfam16796 93 AYGQTGSGSNDGM---------------IPRAREQIFRFISSLKKGWKYtIELQFVEIYNESSQDLL 144
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
795-1040 |
5.33e-09 |
|
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: 59.78 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 795 AAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKH 874
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 875 EQQQKILKIKTEEIAAFQRKR-RSGSNGSVVSLEQQQKIEEQKKWLdQEMEKVLQQRRA-LEELGEELRKREVILAKKEA 952
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREqAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 953 LMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKL 1032
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*...
gi 568947410 1033 RQGSLLSP 1040
Cdd:COG4942 251 LKGKLPWP 258
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
702-1033 |
1.44e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 702 ASEWRLAQAQQKIRELAiniRMKEELIGELVRTGKAAQALNR--QHSQRIRELEQEAERVRAELCEGQRQLRELEgrEPQ 779
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEA---KKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 780 DASERSRLQEFRK--RVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRrlreETEQKRRLE 857
Cdd:PTZ00121 1541 KAEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM----KAEEAKKAE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 858 TEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKW--LDQEMEKVLQQRRALEE 935
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKK 1696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 936 LGEELRKREViLAKKEALMQEKtgleSKRLRSSQALNEDIVRVSSRLEHLEKELSE----------KSGQLRQGSAQNQQ 1005
Cdd:PTZ00121 1697 EAEEAKKAEE-LKKKEAEEKKK----AEELKKAEEENKIKAEEAKKEAEEDKKKAEeakkdeeekkKIAHLKKEEEKKAE 1771
|
330 340 350
....*....|....*....|....*....|
gi 568947410 1006 QIRGEIDTLRQE--KDSLLKQRLEIDSKLR 1033
Cdd:PTZ00121 1772 EIRKEKEAVIEEelDEEDEKRRMEVDKKIK 1801
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
706-1083 |
1.66e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 706 RLAQAQQKIRELAINIRMKEELIGELVRTGK---AAQALNRQHSQRIRELEQ--EAERVRAELCEGQRQLRELEGREPQD 780
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEeleELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 781 ASERSRLQEFRKRVAAAQSQVQVLKEkkQATERLVSLSAQSETRLQELERNVQlmrrqqgQLQRRLREETEQKRRLETEM 860
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELE-------ELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 861 NKRQHRVKELELKHEQQQKILKIKTEEIAAF------------------------------------------QRKRRSG 898
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflllarEKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 899 SNGSVVSLEQQQKIEEQK-------------------KWLDQEMEKVLQQRRALEELGEELRkREVILAKKEALMQEKTG 959
Cdd:COG4717 303 EAEELQALPALEELEEEEleellaalglppdlspeelLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 960 LESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQ--------QQIRGEIDTLRQEKDSLLKQRLEIDSK 1031
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleeelEELEEELEELEEELEELREELAELEAE 461
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 568947410 1032 LRQgsllsPEEERTLFQLDEAIEALDAAIEYKNEAItcrqRVLRASASLLSQ 1083
Cdd:COG4717 462 LEQ-----LEEDGELAELLQELEELKAELRELAEEW----AALKLALELLEE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
702-1018 |
1.89e-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: 59.31 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 702 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELCEGQRQLRELEGREp 778
Cdd:TIGR02169 210 AERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKlteEISELEKRLEEIEQLLEELNKKIKDLGEEE- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 779 qDASERSRLQEFRKRVAAAQSQVqvlKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLET 858
Cdd:TIGR02169 289 -QLRVKEKIGELEAEIASLERSI---AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 859 EMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGE 938
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 939 ELRKRevILAKKEALMQEKTGLESKRlrssqalnEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEK 1018
Cdd:TIGR02169 445 DKALE--IKKQEWKLEQLAADLSKYE--------QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
749-1134 |
2.05e-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: 58.93 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 749 IRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQefrkrvaaaqsqvqvlKEKKQATERLVSLSAQSETRLQEL 828
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR----------------REREKAERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 829 ERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQ-QQKILKIKTEEIAAFQRKRRSGSnGSVVSLE 907
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELE-AEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 908 --------QQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKRevilakKEALMQEktgleskrLRSSQALNEDIVrvs 979
Cdd:TIGR02169 308 rsiaekerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR------RDKLTEE--------YAELKEELEDLR--- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 980 SRLEhlekELSEKSGQLRQGSAQNQQqirgEIDTLRQEKDSLLKQRLEIDSKLRqgsllspeeertlfQLDEAIEALDAA 1059
Cdd:TIGR02169 371 AELE----EVDKEFAETRDELKDYRE----KLEKLKREINELKRELDRLQEELQ--------------RLSEELADLNAA 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568947410 1060 IEYKNEAITCRQRVLRASASLLSQCEMNLMaklsylsssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1134
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLE---------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
696-893 |
3.04e-08 |
|
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: 57.47 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 696 QAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEg 775
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 776 repqdASERSRLQEFRKRVAAAQ-----SQVQVL---KEKKQATERLVSLSAQSETR----------LQELERNVQLMRR 837
Cdd:COG4942 97 -----AELEAQKEELAELLRALYrlgrqPPLALLlspEDFLDAVRRLQYLKYLAPARreqaeelradLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568947410 838 QQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQR 893
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
723-1002 |
3.14e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 723 MKEELIGELVRTGKAAQAlnrQHSQRIRELEQEAERVRAELCEGQRQLRELEGRepqdaseRSRLQEFRKRVAAAQSQVQ 802
Cdd:PRK03918 186 KRTENIEELIKEKEKELE---EVLREINEISSELPELREELEKLEKEVKELEEL-------KEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 803 VLKEKKQATERLVslsAQSETRLQELERNVQlmrrqqgqLQRRLREETEQKRRLETEMNKRQHRVKELElkheqqqKILK 882
Cdd:PRK03918 256 KLEEKIRELEERI---EELKKEIEELEEKVK--------ELKELKEKAEEYIKLSEFYEEYLDELREIE-------KRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 883 IKTEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLES 962
Cdd:PRK03918 318 RLEEEINGIEER-----------IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568947410 963 KRlrssqaLNEDIVRVSSRLEHLEKELSE---KSGQLRQGSAQ 1002
Cdd:PRK03918 387 EK------LEKELEELEKAKEEIEEEISKitaRIGELKKEIKE 423
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
704-1202 |
8.04e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 704 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELCEGQRQLRELEGREPQD 780
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 781 ASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLEtem 860
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE--- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 861 nkrqhrvkELELKHEQQQKILKIKTEeiaaFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEE 939
Cdd:PRK03918 356 --------ELEERHELYEEAKAKKEE----LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 940 LRK----------------REVILAKKEALMQEKTgLESKRLRSSQALNEDIVR-VSSRLEHLEKELSEKSGQLRqgsaq 1002
Cdd:PRK03918 424 LKKaieelkkakgkcpvcgRELTEEHRKELLEEYT-AELKRIEKELKEIEEKERkLRKELRELEKVLKKESELIK----- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1003 nQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQ----------GSLLSPEEErtLFQLDEAIEALDAAIEYKNEAITCRQR 1072
Cdd:PRK03918 498 -LKELAEQLKELEEKLKKYNLEELEKKAEEYEklkekliklkGEIKSLKKE--LEKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1073 VLRASASLLSQCEMNLMAKLSYLSSSETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywLEVALERQRLE 1152
Cdd:PRK03918 575 LLKELEELGFESVEELEERLKELEPFYNEYLELK--DAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEELRKE 648
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 568947410 1153 MDR-QLTLQQKEHEQNVQLLLQQGRDHLG-----EGLADSKRQYEARIHALEKELG 1202
Cdd:PRK03918 649 LEElEKKYSEEEYEELREEYLELSRELAGlraelEELEKRREEIKKTLEKLKEELE 704
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
931-1235 |
8.22e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 931 RALEELGEELRKREvilaKKEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGE 1010
Cdd:TIGR02169 668 FSRSEPAELQRLRE----RLEGLKRELSSLQSELRRIENRLDE----LSQELSDASRKIGEIEKEIEQ-LEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1011 IDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAA--------IEYKNEAITCRQRVLRASASLLS 1082
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1083 QCEMNLMAKLSYLSSS----ETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLE---VALERQRLEMDR 1155
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEiqelQEQRIDLK--EQIKSIEKEIENLNGKKEELEEELEELEAALRDLEsrlGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1156 QLT-LQQKEHEQNVQllLQQGRDHLGEgLADSKRQYEARIHALEKELGRHMWINQELkqkLSAGSTAGQSRGCERRSLCL 1234
Cdd:TIGR02169 897 QLReLERKIEELEAQ--IEKKRKRLSE-LKAKLEALEEELSEIEDPKGEDEEIPEEE---LSLEDVQAELQRVEEEIRAL 970
|
.
gi 568947410 1235 E 1235
Cdd:TIGR02169 971 E 971
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
589-1067 |
8.62e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 589 VSSEQVVSGKEV-KAEVLAQADKLRSASSTTSEEEGEEEEEEEeeeeeppRRTLYLRRNGISNWSQRAGLSPGSPPDRKG 667
Cdd:PTZ00121 1272 IKAEEARKADELkKAEEKKKADEAKKAEEKKKADEAKKKAEEA-------KKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 668 PEVCPEEPAAAIPAPQAVGSGKVPVQTRQAPAAMASEWRLAQAQQK-----IRELAINIRMKEELIGELVRTGKAAQALN 742
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkadeAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 743 R--QHSQRIRELEQEAERVR-----AELCEGQRQLREL-----EGREPQD----ASERSRLQEFRKRVAAAQSQVQVLKE 806
Cdd:PTZ00121 1425 KkaEEKKKADEAKKKAEEAKkadeaKKKAEEAKKAEEAkkkaeEAKKADEakkkAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 807 KKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLEtEMNKRQHRVKELELKHEQQQKILKIKTE 886
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 887 EIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLD-----QEMEKVLQQRRALEEL----------GEELRKREVILAKKE 951
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLkkkeaeekkkAEELKKAEEENKIKA 1663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 952 ALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKElSEKSGQLRQGSAQNQ---QQIRGEiDTLRQEKDSLLKQRLEI 1028
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKkkaEELKKA-EEENKIKAEEAKKEAEE 1741
|
490 500 510
....*....|....*....|....*....|....*....
gi 568947410 1029 DSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAI 1067
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
812-1191 |
9.92e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.90 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 812 ERLVSLSAQSETRLQEL--ERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRqhrvKELELKhEQQQKILKIKTEEIA 889
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKkkEALKKLIEETENLAELIIDLEELKLQELKLKEQAK----KALEYY-QLKEKLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 890 AFQRKRrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQ 969
Cdd:pfam02463 229 LDYLKL----------NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 970 ALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKD-SLLKQRLEIDSKLRQGSLLSPEEERTLFQ 1048
Cdd:pfam02463 299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1049 LDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLS--------------YLSSSETRALLCKYFDKVVTL 1114
Cdd:pfam02463 379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEekkeeleileeeeeSIELKQGKLTEEKEELEKQEL 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568947410 1115 REEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRDHLGEGLADSKRQYE 1191
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
926-1191 |
1.17e-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: 56.60 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 926 VLQQRRALEELGEELrkrEVILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQ 1005
Cdd:TIGR02168 672 ILERRREIEELEEKI---EELEEKIAELEKALAELRKEL----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1006 ------QIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASAS 1079
Cdd:TIGR02168 745 leeriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1080 LLSQCEMNLMAKLSYLSssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTL 1159
Cdd:TIGR02168 825 RLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-ELSE 901
|
250 260 270
....*....|....*....|....*....|..
gi 568947410 1160 QQKEHEQNVQlLLQQGRDHLGEGLADSKRQYE 1191
Cdd:TIGR02168 902 ELRELESKRS-ELRRELEELREKLAQLELRLE 932
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
739-1200 |
1.22e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 739 QALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLS 818
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 819 AQSEtRLQELERNVQlmrrqqgqlqrRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSG 898
Cdd:COG4717 129 PLYQ-ELEALEAELA-----------ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 899 SNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGL----ESKRLRSSQALNE 973
Cdd:COG4717 197 LAEELEELQQRlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallgLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 974 DIVRVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLrqgsllSPEEERTLFQLDEAI 1053
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLG-KEAEELQALPALEELEEEELEELLAALGLPPDL------SPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1054 EALDAAIEYKNEAITcRQRVLRASASLLSQCEMnlmaklsylSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLE 1133
Cdd:COG4717 350 QELLREAEELEEELQ-LEELEQEIAALLAEAGV---------EDEEELRAALEQAEEYQELKEE-------LEELEEQLE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947410 1134 E-----QQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNV-------QLLLQQGRDHLGEGLADSKRQYEARIHALEKE 1200
Cdd:COG4717 413 EllgelEELLEALDEEELEEELEELEEELEELEEELEELReelaeleAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
693-1065 |
3.45e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 693 QTRQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRE 772
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 773 LEGREPQDASE----RSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLRE 848
Cdd:COG1196 426 LEEALAELEEEeeeeEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 849 ETEQKRRLETEMNKR----------------------------QHRVKELELKHEQQQKILKIKTEEIAAF--------- 891
Cdd:COG1196 506 FLEGVKAALLLAGLRglagavavligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkirar 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 892 ---QRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSS 968
Cdd:COG1196 586 aalAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 969 QALNEDivrvSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQ 1048
Cdd:COG1196 666 SRRELL----AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
410
....*....|....*..
gi 568947410 1049 LDEAIEALDAAIEYKNE 1065
Cdd:COG1196 742 LEEEELLEEEALEELPE 758
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
707-1177 |
4.85e-07 |
|
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: 54.74 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 707 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAERVRAElCEGQ--RQLRELEGREPQDA 781
Cdd:pfam15921 383 LADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmeVQRLEALLKAMKSE-CQGQmeRQMAAIQGKNESLE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 782 SERSRLQEFRKRVAAAQSQVQVLKEKK---QATERLVSlsaQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLET 858
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKmtlESSERTVS---DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 859 EMNKRQHRVKE---LELKHEQQQKILKIKTEEIAAFQRkrRSGSNGSVVSLEQQQKIEEQKKWLDQEMEkvLQQRRALEE 935
Cdd:pfam15921 539 EGDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQ--LVGQHGRTAGAMQVEKAQLEKEINDRRLE--LQEFKILKD 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 936 lGEELRKREvILAKKEALMQEKTGL---ESKRLRS--------SQALNE------DIVRVSSRLEHLEKELSEKSGQLRQ 998
Cdd:pfam15921 615 -KKDAKIRE-LEARVSDLELEKVKLvnaGSERLRAvkdikqerDQLLNEvktsrnELNSLSEDYEVLKRNFRNKSEEMET 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 999 GSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDeaieALDAAIEYKNEAITC---RQRVLR 1075
Cdd:pfam15921 693 TTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID----ALQSKIQFLEEAMTNankEKHFLK 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1076 ASASLLSQcemnlmaKLSYLSSSETRALlckyfdkvvtlreeqhqqqiafSELEMQLEEQQRL---VYWLEVALERQRLE 1152
Cdd:pfam15921 769 EEKNKLSQ-------ELSTVATEKNKMA----------------------GELEVLRSQERRLkekVANMEVALDKASLQ 819
|
490 500
....*....|....*....|....*
gi 568947410 1153 MDRQLTLQQKEHEQNVQLLLQQGRD 1177
Cdd:pfam15921 820 FAECQDIIQRQEQESVRLKLQHTLD 844
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
699-1220 |
5.00e-07 |
|
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: 54.36 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 699 AAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAERVRAELCEGQRQL----- 770
Cdd:pfam05557 35 KASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYleaLNKKLNEKESQLADAREVISCLknels 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 771 ---RELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLmRRQQGQLQRRLR 847
Cdd:pfam05557 115 elrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS-QEQDSEIVKNSK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 848 EETEQKRRLETEMNKRQHRVKELelkHEQQQKILKIKtEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVL 927
Cdd:pfam05557 194 SELARIPELEKELERLREHNKHL---NENIENKLLLK-EEVEDLKRK-----------LEREEKYREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 928 QQRRALEELG----------EELRKREVILAKKE-ALMQEKTGLES--KRLRSSQALNEDIVRV-SSRLEHLEKELSEKS 993
Cdd:pfam05557 259 QELQSWVKLAqdtglnlrspEDLSRRIEQLQQREiVLKEENSSLTSsaRQLEKARRELEQELAQyLKKIEDLNKKLKRHK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 994 GQLRQgsaqNQQQIRgeidTLRQEKDsLLKQRLE-IDSKLRqgsllspEEERTLFQLDEAIEALDAAIEYKNEAITCRQR 1072
Cdd:pfam05557 339 ALVRR----LQRRVL----LLTKERD-GYRAILEsYDKELT-------MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1073 V---LRASASLLSQCEMnLMAKLSYLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVALERQ 1149
Cdd:pfam05557 403 LsvaEEELGGYKQQAQT-LERELQALRQQESLADPSYSKEEVDSLRRK-------LETLELERQRLREQKNELEMELERR 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947410 1150 rlemdrqlTLQQKEHEQNVQLLlqqgrdHLGEG-LADSKRQYEARIHALEKELGRHMWINQELKQKLSAGST 1220
Cdd:pfam05557 475 --------CLQGDYDPKKTKVL------HLSMNpAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLR 532
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-1201 |
6.60e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 704 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR--EPQDA 781
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 782 SE--RSRLQEFRKRVAAAQSQVQVLKEKKQATE-RLVSLSAQSETRLQELERN-VQLMRRQQGQLQRRLREETEQKRRLE 857
Cdd:TIGR02168 381 LEtlRSKVAQLELQIASLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 858 TEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR--SGSNGSVVSLEQQQK------------IEEQKKWlDQEM 923
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSglsgilgvlselISVDEGY-EAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 924 EKVL-------------QQRRALEELGEELRKREVILA---KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---- 983
Cdd:TIGR02168 540 EAALggrlqavvvenlnAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkals 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 984 ----------------HLEKELSE-------------KSGQLRQGSAQNQQQI---RGEIDTLRQEK------------- 1018
Cdd:TIGR02168 620 yllggvlvvddldnalELAKKLRPgyrivtldgdlvrPGGVITGGSAKTNSSIlerRREIEELEEKIeeleekiaeleka 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1019 -DSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEykneaiTCRQRVLRASASLLSQcEMNLMAKLSYLSS 1097
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLSKELTEL-EAEIEELEERLEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1098 SETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTLQQKEHEQNVQLLLQQGRD 1177
Cdd:TIGR02168 773 AEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEE 849
|
570 580
....*....|....*....|....*.
gi 568947410 1178 --HLGEGLADSKRQYEARIHALEKEL 1201
Cdd:TIGR02168 850 lsEDIESLAAEIEELEELIEELESEL 875
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
706-994 |
6.92e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 706 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR--EPQDASE 783
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 784 RSRLQEFRKRVAAAQSQVQ----VLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETE 859
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSrieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 860 MNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgSNGSVVSLEQQQK-IEEQKKWLDQEMEKVLQQRRALEELGE 938
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-LEAQIEKKRKRLSeLKAKLEALEEELSEIEDPKGEDEEIPE 948
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568947410 939 ELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSG 994
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
695-955 |
7.00e-07 |
|
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: 53.97 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 695 RQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTgkaAQALNRQHSQRIR--ELEQEAERVRA-ELCEGQRQLR 771
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---RQEERKRELERIRqeEIAMEISRMRElERLQMERQQK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 772 ELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATE-RLVSLSAQSETRLQELERnVQLMRRQQGQLQRRLREET 850
Cdd:pfam17380 391 NERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEERAREMER-VRLEEQERQQQVERLRQQE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 851 EQKRRLETEMNKRQHRVKELElkhEQQQKILKIKTEE----IAAFQRKRR-----SGSNGSVVSLEQQQKIEEQKKWLDQ 921
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAE---EQRRKILEKELEErkqaMIEEERKRKllekeMEERQKAIYEEERRREAEEERRKQQ 546
|
250 260 270
....*....|....*....|....*....|....
gi 568947410 922 EMEKVLQQRRALEELGEELRKREVILAKKEALMQ 955
Cdd:pfam17380 547 EMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
741-1204 |
7.69e-07 |
|
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: 53.82 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 741 LNRQHS--QRIRELEQEAERVRAE---LCEGQRQLRELEGR-EPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERL 814
Cdd:TIGR00618 371 SCQQHTltQHIHTLQQQKTTLTQKlqsLCKELDILQREQATiDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 815 VSLSAQSETRLQELERNVQlmrrqqgqlqrrlrEETEQKRRLETeMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRK 894
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLK--------------EREQQLQTKEQ-IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 895 RRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQrraleelGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNED 974
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ-------LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 975 IVRVSSRLEHLEKELSEKSGQLRQgsAQNQQQIRGEIDTLRQEKDSLLKQrleIDSKLRQGSLLSPEEERTLFQLDEAIE 1054
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLAC--EQHALLRKLQPEQDLQDVRLHLQQ---CSQELALKLTALHALQLTLTQERVREH 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1055 ALdAAIEYKNEAITCRQRVLRASASLLSQCEMN---LMAKLSYLSSSETrallckyfdKVVTLREEQHQQQIAFSELEMQ 1131
Cdd:TIGR00618 664 AL-SIRVLPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELET---------HIEEYDREFNEIENASSSLGSD 733
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568947410 1132 LEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRD--HLGEGLADSKRQYEARIHALEKELGRH 1204
Cdd:TIGR00618 734 LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAElsHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
747-1057 |
9.98e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.44 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 747 QRIRELEQEAE---RVRAELCEGQRQLRELEGREpqdaSERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSET 823
Cdd:pfam02463 173 EALKKLIEETEnlaELIIDLEELKLQELKLKEQA----KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 824 RLQELERNVQLMRRQqgqlqrrlrEETEQKRRLETEMNKRQHRVKELELKheqqQKILKIKTEEIAAFQRKRRSGSNGSV 903
Cdd:pfam02463 249 EQEEIESSKQEIEKE---------EEKLAQVLKENKEEEKEKKLQEEELK----LLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 904 VSLEQ-------------QQKIEEQKKWLD------QEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTG----- 959
Cdd:pfam02463 316 LKESEkekkkaekelkkeKEEIEELEKELKeleikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAklkee 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 960 LESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSG-----QLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQ 1034
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEileeeEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340
....*....|....*....|...
gi 568947410 1035 GSLLSPEEERTLFQLDEAIEALD 1057
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEER 498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
601-1191 |
1.07e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 601 KAEVLAQADKLRSASST----TSEEEGEEEEEEEEEEEEPPRRTLYLRR----NGISNWSQRAGLSPGSPPDRKGPEVCP 672
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDArkaeAARKAEEERKAEEARKAEDAKKAEAVKKaeeaKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 673 EEPAAAIPAPQAVGSGKVPVQTRQAPAAMASEWRLAQAQQKIREL---AINIRMKEELIGELVRTGKAAQALNRQHSQR- 748
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAkkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAk 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 749 ----IRELEQEAERVRAELCEGQRQLRELEGREP--------QDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVS 816
Cdd:PTZ00121 1343 kaaeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkadaakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 817 LSAQSE--TRLQELERNVQlmrrqQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKI----LKIKTEEI-- 888
Cdd:PTZ00121 1423 AKKKAEekKKADEAKKKAE-----EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkadeAKKKAEEAkk 1497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 889 AAFQRKRRSGSNGSVVSL---EQQQKIEEQKKWLD----QEMEKVLQQRRAlEEL--GEELRKREVILAKKEALMQEKTG 959
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAkkaEEAKKADEAKKAEEakkaDEAKKAEEKKKA-DELkkAEELKKAEEKKKAEEAKKAEEDK 1576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 960 LESKRlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLS 1039
Cdd:PTZ00121 1577 NMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1040 PEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKlsylsssETRALLCKYFDKVVTLREEQH 1119
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-------ELKKKEAEEKKKAEELKKAEE 1726
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947410 1120 QQQIAFSELEMQLEEQQRlvywlevALERQRLEMDRQLTLQQ--KEHEQNVQLLLQQGRDHLGEGL--ADSKRQYE 1191
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKK-------KAEEAKKDEEEKKKIAHlkKEEEKKAEEIRKEKEAVIEEELdeEDEKRRME 1795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
748-1217 |
1.14e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 748 RIRELEQEAERVraelcegQRQLRELEGREPQDASERSRLQEFRKRVAAaqsqvqvLKEKKQATERLVSLSAQSETRLQE 827
Cdd:PRK03918 194 LIKEKEKELEEV-------LREINEISSELPELREELEKLEKEVKELEE-------LKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 828 LERNVQlmrrqqgqlqrrlrEETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEeiaafqrkrrsgsngsvvSLE 907
Cdd:PRK03918 260 KIRELE--------------ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE------------------YLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 908 QQQKIEEqkkwldqEMEKVLQQRRALEELGEELRKREvilAKKEALMQEKTGLESK--RLRSSQALNEDIVRVSSRLEHL 985
Cdd:PRK03918 308 ELREIEK-------RLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRleELEERHELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 986 EKELSEKSgqlrqgsaqnQQQIRGEIDTLRQEKDSLLKQRLEIDSKLrqGSLLSPEEERtlfqlDEAIEALDAAieyKNE 1065
Cdd:PRK03918 378 KKRLTGLT----------PEKLEKELEELEKAKEEIEEEISKITARI--GELKKEIKEL-----KKAIEELKKA---KGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1066 AITCRqrvlrasASLLSQCEMNLMAKLSyLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVA 1145
Cdd:PRK03918 438 CPVCG-------RELTEEHRKELLEEYT-AELKRIEKELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKELA 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947410 1146 LERQRLEmdrqltlqQKEHEQNVQLLLQQGRDHlgEGLADSKRQYEARIHALEKELGRhmwiNQELKQKLSA 1217
Cdd:PRK03918 503 EQLKELE--------EKLKKYNLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAE 560
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
720-1047 |
1.29e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 720 NIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELegrepqdaseRSRLQEFRKRVAAAQS 799
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKEL----------REEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 800 QVQVLKEKKQAterlvsLSAQSETRLQELERnvqlmrrqqgqlqrrLREETEQKRRLETEMNKRQHRVKELELKheQQQK 879
Cdd:COG1340 72 KVKELKEERDE------LNEKLNELREELDE---------------LRKELAELNKAGGSIDKLRKEIERLEWR--QQTE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 880 ILKIKtEEIAAFQRKRRSGSngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRK-REVILAKKEALMQEKT 958
Cdd:COG1340 129 VLSPE-EEKELVEKIKELEK-----ELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQELHEEMIELYK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 959 GLESKRlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgsaQNQQQIRGEIDTLR-----QEKDSLLKQRLEIDSKLR 1033
Cdd:COG1340 203 EADELR-KEADELHKEIVEAQEKADELHEEIIELQKELR----ELRKELKKLRKKQRalkreKEKEELEEKAEEIFEKLK 277
|
330
....*....|....
gi 568947410 1034 QGSLLSPEEERTLF 1047
Cdd:COG1340 278 KGEKLTTEELKLLQ 291
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
707-1034 |
1.39e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 707 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQE----AERVRAELCEGQRQLRELE---GREPQ 779
Cdd:pfam02463 671 LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKqkiDEEEE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 780 DASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETE 859
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 860 MNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKR---RSGSNGSVVSLEQQQKIEEQKKWLDQEME-KVLQQRRALEE 935
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEellQELLLKEEELEEQKLKDELESKEEKEKEEkKELEEESQKLN 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 936 LGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNED---------IVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQ 1006
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEkeennkeeeEERNKRLLLAKEELGKVNLMAIEEFEEKEERY 990
|
330 340 350
....*....|....*....|....*....|
gi 568947410 1007 --IRGEIDTLRQEKDSLLKQRLEIDSKLRQ 1034
Cdd:pfam02463 991 nkDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
727-1166 |
1.58e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.80 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 727 LIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELcegQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKE 806
Cdd:pfam05483 350 VVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL---QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 807 KKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKEL------------ELKH 874
Cdd:pfam05483 427 FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdklllenkELTQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 875 EQQQKILKIKTEEIAAFQRKRRSGSngsvvSLEQQQKIEEQKKWLDQEMEKVlqqRRALEELGEELRKReviLAKKEALM 954
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEER-----MLKQIENLEEKEMNLRDELESV---REEFIQKGDEVKCK---LDKSEENA 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 955 QEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK---ELSEKSGQL-RQGSAQNQQQIRGEIDTLRQEKD-SLLKQRLE-- 1027
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALkKKGSAENKQLNAYEIKVNKLELElASAKQKFEei 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1028 IDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA-ITCRQRVLRASAsllsqcemnLMAKLSYlsssetrallck 1106
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIdKRCQHKIAEMVA---------LMEKHKH------------ 714
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568947410 1107 YFDKVVtlrEEQHQQQIAFSELEmqlEEQQRLVYWLEVALERQRLEM---DRQLTLQQKEHEQ 1166
Cdd:pfam05483 715 QYDKII---EERDSELGLYKNKE---QEQSSAKAALEIELSNIKAELlslKKQLEIEKEEKEK 771
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
733-1033 |
1.69e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.92 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 733 RTGKAAQALNRQHSqRIRELEQEAERVRAELCEGQRQLrELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATE 812
Cdd:pfam12128 605 RLDKAEEALQSARE-KQAAAEEQLVQANGELEKASREE-TFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 813 RLVSLSAQsetrLQELERNVQLMrrqqgqlqrrLREETEQKRRLETEMNKrqhrvKELELKHEQQQKILKIKtEEIAAfq 892
Cdd:pfam12128 683 RLNSLEAQ----LKQLDKKHQAW----------LEEQKEQKREARTEKQA-----YWQVVEGALDAQLALLK-AAIAA-- 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 893 rkRRSGSNGSVVSLEQQQKIEEQKKWLDQE-MEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLrssqal 971
Cdd:pfam12128 741 --RRSGAKAELKALETWYKRDLASLGVDPDvIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRL------ 812
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568947410 972 nedivrvSSRLEHLEKELSEKSGQLrqgsAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLR 1033
Cdd:pfam12128 813 -------ATQLSNIERAISELQQQL----ARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
707-1027 |
1.91e-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: 52.43 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 707 LAQAQQKIRELAINIRMKEELIGELVRTGkaaqalNRQHSQRIRELEQEAERVRAELCEGQRQLRElegrepqdasersR 786
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQ------NSMYMRQLSDLESTVSQLRSELREAKRMYED-------------K 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 787 LQEFRKRVAAAQSQvqvLKEKKQATERLVSLSAQSETRLQELERNVQlmrrqqgqlqrrlreETEQKRRLETEMNKR--- 863
Cdd:pfam15921 344 IEELEKQLVLANSE---LTEARTERDQFSQESGNLDDQLQKLLADLH---------------KREKELSLEKEQNKRlwd 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 864 ---------QHRVKELELKHEQQQK---ILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLqqrr 931
Cdd:pfam15921 406 rdtgnsitiDHLRRELDDRNMEVQRleaLLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV---- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 932 aleelgEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELseksgQLRQGSAQNQQQIRGEI 1011
Cdd:pfam15921 482 ------EELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL-----QHLKNEGDHLRNVQTEC 550
|
330 340
....*....|....*....|..
gi 568947410 1012 DTLR---QEKD---SLLKQRLE 1027
Cdd:pfam15921 551 EALKlqmAEKDkviEILRQQIE 572
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
694-1068 |
2.54e-06 |
|
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: 52.28 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 694 TRQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKA-AQALNRQHSQRI----RELEQEAERVRAELCEG-Q 767
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvLARLLELQEEPCplcgSCIHPNPARQDIDNPGPlT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 768 RQLRELEGREPQDASE----RSRLQEFRKRVAAAQSQVQVLKEKKQA-TERLVSLSAQSETRLQELERNVQLMRRQQGQL 842
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSeedvYHQLTSERKQRASLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 843 QRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQ------------QQ 910
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmQS 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 911 KIE---------EQKKWLDQEMEKVL--------QQRRALEELGEELRKREVILAK--KEALMQEKTGLESKRL---RSS 968
Cdd:TIGR00618 688 EKEqltywkemlAQCQTLLRELETHIeeydrefnEIENASSSLGSDLAAREDALNQslKELMHQARTVLKARTEahfNNN 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 969 QALNEDIVRvSSRLEHLE-------KELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPE 1041
Cdd:TIGR00618 768 EEVTAALQT-GAELSHLAaeiqffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
410 420
....*....|....*....|....*..
gi 568947410 1042 EERTLFQLDEAIEALDAAIEYKNEAIT 1068
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
724-1058 |
7.15e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 724 KEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSR-----------LQEFRK 792
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDElrereaeleatLRTARE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 793 RVAAAQ------------------SQVQVLKEKKQATERLVSLSAQSETRLQELERNVqlmrrqqgqlqrrlrEETEQKR 854
Cdd:PRK02224 441 RVEEAEalleagkcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERL---------------ERAEDLV 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 855 RLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE 934
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELK 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 935 ELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---HLEKELS----EKSGQLRQGSAQNQQQI 1007
Cdd:PRK02224 586 ERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRErkrELEAEFDeariEEAREDKERAEEYLEQV 665
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568947410 1008 RGEIDTLRQEKDSLLKQRLEIDSKLRQgsLLSPEEERTlfQLDEAIEALDA 1058
Cdd:PRK02224 666 EEKLDELREERDDLQAEIGAVENELEE--LEELRERRE--ALENRVEALEA 712
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
702-943 |
7.86e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 702 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELE------- 774
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEseleall 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 775 ----GREPQDASERSRLQEFRKRVAAAQSQVQvlkEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREET 850
Cdd:TIGR02168 880 neraSLEEALALLRSELEELSEELRELESKRS---ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 851 EQK-RRLETEMNKRQHRVKELElkheqqqkilkiktEEIAAFqrkrrsgsnGSV--VSLEQQQKIEEQKKWLDQEMEKVL 927
Cdd:TIGR02168 957 EALeNKIEDDEEEARRRLKRLE--------------NKIKEL---------GPVnlAAIEEYEELKERYDFLTAQKEDLT 1013
|
250
....*....|....*.
gi 568947410 928 QQRRALEELGEELRKR 943
Cdd:TIGR02168 1014 EAKETLEEAIEEIDRE 1029
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
711-1183 |
8.62e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.36 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 711 QQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRE--LEQEAERVRAELCEGQR--QLRELEGREPQDASERSR 786
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeeKEKKLQEEELKLLAKEEeeLKSELLKLERRKVDDEEK 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 787 LQEFRKRVAAAQSQVQvlKEKKQATERLVSLSAQSETRLQELERNVQLMRRQqgqlqrrlrEETEQKR-------RLETE 859
Cdd:pfam02463 316 LKESEKEKKKAEKELK--KEKEEIEELEKELKELEIKREAEEEEEEELEKLQ---------EKLEQLEeellakkKLESE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 860 MNKRQHRVKE--LELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELG 937
Cdd:pfam02463 385 RLSSAAKLKEeeLELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 938 EELRKREVILAKKE---ALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEID-- 1012
Cdd:pfam02463 465 LELKKSEDLLKETQlvkLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKva 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1013 --TLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCR-----QRVLRASASLLSQCE 1085
Cdd:pfam02463 545 isTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNlaqldKATLEADEDDKRAKV 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1086 MNLMAKLSYLSSSETRALlckyfDKVVTLREEQHQQQIAFSELEMQ---LEEQQRLVYWLEVALERQRLEMDRQLTLQQK 1162
Cdd:pfam02463 625 VEGILKDTELTKLKESAK-----AKESGLRKGVSLEEGLAEKSEVKaslSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
490 500
....*....|....*....|.
gi 568947410 1163 EHEQNVQLLLQQGRDHLGEGL 1183
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAE 720
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
777-1034 |
9.19e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 777 EPQDASER-SRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQK-R 854
Cdd:COG4913 219 EEPDTFEAaDALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAElE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 855 RLETEMNKRQHRVKELELKHEQQQkilkiktEEIAAFQRKRRSgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE 934
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALR-------EELDELEAQIRG------NGGDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 935 ELGEELrkrevilakKEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKELSEKSGQLRQGsaqnqqqiRGEIDTL 1014
Cdd:COG4913 366 ALLAAL---------GLPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDL--------RRELREL 424
|
250 260
....*....|....*....|
gi 568947410 1015 RQEKDSLLKQRLEIDSKLRQ 1034
Cdd:COG4913 425 EAEIASLERRKSNIPARLLA 444
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
834-1066 |
9.61e-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: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 834 LMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvslEQQQKIE 913
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR----------ALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 914 EQKKWLDQEMEKVLQQRRALEELGEELRKREVILAK-------KEALMQEKTGLESKRLRSSQALN-------EDIVRVS 979
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAparreqaEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 980 SRLEHLEKELSEKSGQLRQGSAQNQQQiRGEIDTLRQEKDSLLKQrLEIDSKLRQGSLLSPEEERTlfQLDEAIEALDAA 1059
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEE-RAALEALKAERQKLLAR-LEKELAELAAELAELQQEAE--ELEALIARLEAE 235
|
....*..
gi 568947410 1060 IEYKNEA 1066
Cdd:COG4942 236 AAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
921-1061 |
1.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 921 QEMEKVLQQRRALE---ELGEELRKREVILAKKEALM--------QEKTGLESKRLRSSQA----LNEDIVRVSSRLEHL 985
Cdd:COG4913 242 EALEDAREQIELLEpirELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAelarLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947410 986 EKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1061
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
706-833 |
3.38e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 706 RLAQAQQKIRELAINIRMKEELIGELVRTGkAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERS 785
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568947410 786 R-LQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQ 833
Cdd:COG3206 313 RiLASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
851-1217 |
3.79e-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: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 851 EQKRRLETEMNKRQhrvKELELKHEQQQKILK--IKTEEIAAFQRKRRSGSNGSVVSLEQQQKI-EEQKKWLDQEMEKVL 927
Cdd:TIGR04523 117 EQKNKLEVELNKLE---KQKKENKKNIDKFLTeiKKKEKELEKLNNKYNDLKKQKEELENELNLlEKEKLNIQKNIDKIK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 928 QQRRALEEL-----------------GEELRKREVILAK-KEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKEL 989
Cdd:TIGR04523 194 NKLLKLELLlsnlkkkiqknkslesqISELKKQNNQLKDnIEKKQQEINEKTTEISNTQTQLNQ----LKDEQNKIKKQL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 990 SEKSGQLRQGSAQ-----NQ-QQIRGEIDTLRQEK----DSLLKQRLE-IDSKLRQGSLLSPEEERTLFQLDEAIEALDA 1058
Cdd:TIGR04523 270 SEKQKELEQNNKKikeleKQlNQLKSEISDLNNQKeqdwNKELKSELKnQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1059 AIEYKNEAITCRQRVLRASASLLSQCEMNlmaKLSYLSSSetrallckyfdkvvtlreEQHQQQIafSELEMQLEEQqrl 1138
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEI------------------KNLESQI--NDLESKIQNQ--- 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1139 vywlevalERQRLEMDRQLTLQQKEH---EQNVQLLLQQGRDhlgegLADSKRQYEARIHALEKELGRHMWINQELKQKL 1215
Cdd:TIGR04523 404 --------EKLNQQKDEQIKKLQQEKellEKEIERLKETIIK-----NNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
..
gi 568947410 1216 SA 1217
Cdd:TIGR04523 471 KV 472
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
743-1072 |
4.39e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.03 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 743 RQHSQRIRELEQEAERVRAELCEGQRQLRELEgrepqDASERSRLQEFRKRVAAAQSQVQVLKEKKQATErlvslsaqse 822
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEKIAEYT-----KSIDIKKATESLEEQLAAAEAEQELEESKRETE---------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 823 TRLQELERNVQLMRRQQGQLQRRLREETEQ------KRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR 896
Cdd:COG5185 336 TGIQNLTAEIEQGQESLTENLEAIKEEIENivgeveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 897 SgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEEL-RKREVILAKKEALMQEKTGLESKRLRSSqalNEDI 975
Cdd:COG5185 416 K---------AADRQIEELQRQIEQATSSNEEVSKLLNELISELnKVMREADEESQSRLEEAYDEINRSVRSK---KEDL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 976 vrvSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLlkqrleiDSKLRQGSLLSPEEERTLFQLDEAIEA 1055
Cdd:COG5185 484 ---NEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESL-------KDFMRARGYAHILALENLIPASELIQA 553
|
330
....*....|....*..
gi 568947410 1056 LDAAIEYKNEAITCRQR 1072
Cdd:COG5185 554 SNAKTDGQAANLRTAVI 570
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
708-1181 |
4.62e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 708 AQAQQKIRElaINIRMKEELIGELVRTGKAAQALNRQHSQRiRELEQEAERVR------AELCEGQRQLR-ELEGREPQD 780
Cdd:TIGR00606 545 MDKDEQIRK--IKSRHSDELTSLLGYFPNKKQLEDWLHSKS-KEINQTRDRLAklnkelASLEQNKNHINnELESKEEQL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 781 AS-------------ERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSA--------------QSETRLQELERNVQ 833
Cdd:TIGR00606 622 SSyedklfdvcgsqdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdenqsccpvcqrvfQTEAELQEFISDLQ 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 834 LMRRQQgqlqrrlreETEQKRrLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVvslEQQQKIE 913
Cdd:TIGR00606 702 SKLRLA---------PDKLKS-TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ---RLKNDIE 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 914 EQKKWL-----DQEMEKVLQQR-RALEELGEELRKREVILAKKEALMQEKTGleskrLRSSQALNEdivRVSSRLEHLEK 987
Cdd:TIGR00606 769 EQETLLgtimpEEESAKVCLTDvTIMERFQMELKDVERKIAQQAAKLQGSDL-----DRTVQQVNQ---EKQEKQHELDT 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 988 ELSEksGQLRQGSAQNQQQirgEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAI 1067
Cdd:TIGR00606 841 VVSK--IELNRKLIQDQQE---QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1068 TCRQRVLRASASLLSQCEM-NLMAKLSYLSSSETRALLCKY----FDKVVTLREEQ-HQQQIAFSELEMQLEEQQRLVYW 1141
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETsNKKAQDKVNDIKEKVKNIHGYmkdiENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEK 995
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 568947410 1142 LEVALERQRLEMDRQltlQQKEHEQNVQLLLQQGRDHLGE 1181
Cdd:TIGR00606 996 INEDMRLMRQDIDTQ---KIQERWLQDNLTLRKRENELKE 1032
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
702-955 |
4.64e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 702 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDA 781
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 782 SERSRLqefrkrVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETE----QKRRLE 857
Cdd:pfam15921 632 LEKVKL------VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKSAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 858 TEMNKRQHRVKELELK--HEQQ-----QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQR 930
Cdd:pfam15921 706 SELEQTRNTLKSMEGSdgHAMKvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
250 260
....*....|....*....|....*
gi 568947410 931 RALEELGEELRKREVILAKKEALMQ 955
Cdd:pfam15921 786 NKMAGELEVLRSQERRLKEKVANME 810
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
724-1066 |
1.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 724 KEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAelCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQsqvqv 803
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK----- 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 804 lkeKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETemnkrQHRVKELELKHEQQQKILKI 883
Cdd:PTZ00121 1177 ---KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA-----VKKAEEAKKDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 884 KT-EEIAAFQRKRRSgsngSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRAlEELGEELRKREVILAKKEAlMQEKTGLES 962
Cdd:PTZ00121 1249 RNnEEIRKFEEARMA----HFARRQAAIKAEEARK--ADELKKAEEKKKA-DEAKKAEEKKKADEAKKKA-EEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 963 KRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQiRGEIDTLRQE----KDSLLKQRLEIDSKLRQGSLL 1038
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEeakkKADAAKKKAEEKKKADEAKKK 1399
|
330 340
....*....|....*....|....*...
gi 568947410 1039 SPEEERTLFQLDEAIEALDAAIEYKNEA 1066
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
601-1170 |
1.42e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 601 KAEVLAQADKLRSASSTTSEEEGEEEEEEEE----EEEEPPRRTLYLRRNGIsnwSQRAGLSPGSPPDRKGPEVCPEEPA 676
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEARKAEDARKAEEARKaedaKRVEIARKAEDARKAEE---ARKAEDAKKAEAARKAEEVRKAEEL 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 677 AAIPAPQAVGSGKVPVQTRQAPAA-MASEWRLAQAQQKIREL---------AINIRMKEEL-------IGELVRTGKAAQ 739
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEArKAEDAKKAEAVKKAEEAkkdaeeakkAEEERNNEEIrkfeearMAHFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 740 ALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR--EPQDASE-RSRLQEFRKRVAAAQSQVQVLKEKKQATERLVS 816
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaeEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 817 LSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLEtEMNKRQHRVK----ELELKHEQQQKI--LKIKTEEIAA 890
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD-EAKKKAEEDKkkadELKKAAAAKKKAdeAKKKAEEKKK 1432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 891 FQRKRRSGSNGSVVSlEQQQKIEEQKKwlDQEMEKVLQQRRALEEL---GEELRKREVilAKKEALMQEKTGLESKRLRS 967
Cdd:PTZ00121 1433 ADEAKKKAEEAKKAD-EAKKKAEEAKK--AEEAKKKAEEAKKADEAkkkAEEAKKADE--AKKKAEEAKKKADEAKKAAE 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 968 SQALNEDIVRV--SSRLEHLEK-ELSEKSGQLRQGSAQNQQQIRGEIDTLR--QEKDSLLKQRLEIDSK---LRQGSLLS 1039
Cdd:PTZ00121 1508 AKKKADEAKKAeeAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKnmaLRKAEEAK 1587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1040 PEEER---TLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEmnlmaKLSYLSSSETRallckyfdKVVTLRE 1116
Cdd:PTZ00121 1588 KAEEArieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE-----QLKKKEAEEKK--------KAEELKK 1654
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 568947410 1117 EQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRlEMDRQLTLQQKEHEQNVQL 1170
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK-KAAEALKKEAEEAKKAEEL 1707
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
707-1055 |
2.04e-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: 45.94 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 707 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR------EPQD 780
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQlakkeeELQA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 781 A-----SERSRLQEFRKRVAAAQSQVQVLKE--------KKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLR 847
Cdd:pfam01576 248 AlarleEETAQKNNALKKIRELEAQISELQEdleseraaRNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 848 EETEQKRRLETEMNKRQHRVKELELKHEQQQKILkikTEEIAAFQRKRrsgsngsvVSLEQ-QQKIEEQKKWLDQEMeKV 926
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQKHTQALEEL---TEQLEQAKRNK--------ANLEKaKQALESENAELQAEL-RT 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 927 LQQRRALEElgeelRKREvilaKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSE---KSGQLRQGSAQN 1003
Cdd:pfam01576 396 LQQAKQDSE-----HKRK----KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEaegKNIKLSKDVSSL 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 568947410 1004 QQQIRGEIDTLRQEKdsllKQRLEIDSKLRQgsllsPEEERT--LFQLDEAIEA 1055
Cdd:pfam01576 467 ESQLQDTQELLQEET----RQKLNLSTRLRQ-----LEDERNslQEQLEEEEEA 511
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
753-1165 |
2.20e-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: 45.94 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 753 EQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEfrkrvaAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNV 832
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE------QLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 833 QlmrrqqgqlqrrlrEETEQKRRLETEMNKRQHRVKELELKHEqqqkilkiktEEIAAFQRKRRSGsngsvVSLEQQ-QK 911
Cdd:pfam01576 85 E--------------EEEERSQQLQNEKKKMQQHIQDLEEQLD----------EEEAARQKLQLEK-----VTTEAKiKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 912 IEEQKKWLDQEMEKVLQQRRALEE--------LGEELRKR-----------------EVILAKKEALMQEKTGLESKRLR 966
Cdd:pfam01576 136 LEEDILLLEDQNSKLSKERKLLEEriseftsnLAEEEEKAkslsklknkheamisdlEERLKKEEKGRQELEKAKRKLEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 967 SSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDsLLKQRLEIDSKLRQGSLLSPEEERTL 1046
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1047 FQLDEAIEALDAAIEYKNEAiTCRQRVLRasasllSQCEMNLmAKLSYLSSSETRAllckyFDKVVTLREEQHQQqiAFS 1126
Cdd:pfam01576 295 RDLGEELEALKTELEDTLDT-TAAQQELR------SKREQEV-TELKKALEEETRS-----HEAQLQEMRQKHTQ--ALE 359
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568947410 1127 ELEMQLEEQQRLVYWLE---VALERQRLEMDRQL-TLQQKEHE 1165
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEkakQALESENAELQAELrTLQQAKQD 402
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
744-1080 |
2.40e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 744 QHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSR---LQEFRKRVAAAQSQVQ-VLKEKKQATERLVSLSA 819
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLStlsLRQLESRLAQTLDQLQnAQNDLAEYNSQLVSLQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 820 QSE----------TRLQELerNVQLMRRQQGQLQRRLreetEQKRRLETEMnkrqhrvKELELKHEQQQKILKIKTEEIA 889
Cdd:PRK11281 157 QPEraqaalyansQRLQQI--RNLLKGGKVGGKALRP----SQRVLLQAEQ-------ALLNAQNDLQRKSLEGNTQLQD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 890 AFQrKRRSGSNgsvvslEQQQKIEEQKKWLdQEMekVLQQRRAL-EELGEELRKREVI-------LAKKEalMQEKTGLE 961
Cdd:PRK11281 224 LLQ-KQRDYLT------ARIQRLEHQLQLL-QEA--INSKRLTLsEKTVQEAQSQDEAariqanpLVAQE--LEINLQLS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 962 SKRLRSSQALNE---DIVRVSSRLEHL---EKELSEKSGQLrQGSAQ-----NQQQ------------------IRGEID 1012
Cdd:PRK11281 292 QRLLKATEKLNTltqQNLRVKNWLDRLtqsERNIKEQISVL-KGSLLlsrilYQQQqalpsadliegladriadLRLEQF 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1013 TLRQEKDSLLKQRLEIDSKLR-QGSLLSPEEERTLFQ--------LDEAIEALDAAIeykNEAITC---RQRVLRASASL 1080
Cdd:PRK11281 371 EINQQRDALFQPDAYIDKLEAgHKSEVTDEVRDALLQllderrelLDQLNKQLNNQL---NLAINLqlnQQQLLSVSDSL 447
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
849-991 |
2.67e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 849 ETEQKRRLETEMNKRQHRVKELELkhEQQQKILKIKTEEIAAFQRKRRSgsngsvvsLEQQQKIEEQKK-WLDQEMEKVL 927
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNE--------LQKLEKRLLQKEeNLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568947410 928 QQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRvSSRLEHLEKELSE 991
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAK-EILLEKVEEEARH 169
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
848-1066 |
2.93e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 848 EETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKR--RSGSNGSVVSLEQQ-QKIEE--QKKWLDQE 922
Cdd:COG1340 54 ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELaeLNKAGGSIDKLRKEiERLEWrqQTEVLSPE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 923 MEKVLQQRraLEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQaLNEDIvrvssrlehleKELSEKSGQLRqgsaQ 1002
Cdd:COG1340 134 EEKELVEK--IKELEKELEKAKKALEKNEKLKELRAELKELRKEAEE-IHKKI-----------KELAEEAQELH----E 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568947410 1003 NQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQgslLSPEEERTLFQLDEAIEALDAAIEYKNEA 1066
Cdd:COG1340 196 EMIELYKEADELRKEADELHKEIVEAQEKADE---LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
708-1028 |
2.97e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 708 AQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRL 787
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 788 QEFRKRVAAAQsqvqvlkekkqaterlvslsAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRV 867
Cdd:pfam07888 114 SEEKDALLAQR--------------------AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 868 KELELKHEQQQKILKIKTEEiaaFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVIL 947
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKE---FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 948 AKKEALMQEKTGLESKRLRSSQALNEdivrvsSRLE--HLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQR 1025
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRTQAELHQ------ARLQaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLS 324
|
...
gi 568947410 1026 LEI 1028
Cdd:pfam07888 325 AEL 327
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
754-1201 |
3.12e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 754 QEAERVRAELCEGQRQLR-ELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERlVSLSAQSETRLQELERNv 832
Cdd:pfam01576 422 SESERQRAELAEKLSKLQsELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETR-QKLNLSTRLRQLEDERN- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 833 qlmrrqqgQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKI 912
Cdd:pfam01576 500 --------SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 913 EEQKKWLDQEMEKVL----QQRRALEELGEELRKREVILAKKEALmqeKTGLESKRLRSSQALNEDIVRVSSrlehLEKE 988
Cdd:pfam01576 572 EKTKNRLQQELDDLLvdldHQRQLVSNLEKKQKKFDQMLAEEKAI---SARYAEERDRAEAEAREKETRALS----LARA 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 989 LSEKSGQLRQGSAQNQQQiRGEIDTLRQEKDSLLKQRLEIDsKLRQGSLLSPEEERTlfQLDEAIEALDAAIEYKneait 1068
Cdd:pfam01576 645 LEEALEAKEELERTNKQL-RAEMEDLVSSKDDVGKNVHELE-RSKRALEQQVEEMKT--QLEELEDELQATEDAK----- 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1069 crQRVLRASASLLSQCEMNLMAKLSylSSSETRALLCKYFDKVVTLREEQHQQ-----------QIAFSELEMQLE---- 1133
Cdd:pfam01576 716 --LRLEVNMQALKAQFERDLQARDE--QGEEKRRQLVKQVRELEAELEDERKQraqavaakkklELDLKELEAQIDaank 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1134 ------------EQQRLVYWLEvaLERQRLEMDRQLTlQQKEHEQNVQLL--------------------LQQGRDHLGE 1181
Cdd:pfam01576 792 greeavkqlkklQAQMKDLQRE--LEEARASRDEILA-QSKESEKKLKNLeaellqlqedlaaserarrqAQQERDELAD 868
|
490 500 510
....*....|....*....|....*....|
gi 568947410 1182 GLA----------DSKRQYEARIHALEKEL 1201
Cdd:pfam01576 869 EIAsgasgksalqDEKRRLEARIAQLEEEL 898
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
967-1201 |
3.43e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 967 SSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRqgsllspEEERTL 1046
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1047 FQLDEAIEALDAAIEYKNEAItcrQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYF-DKVVTLREEQHQQQIAF 1125
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947410 1126 SELEMQLEEQQRLVYWLEVALERQRlemdRQLTLQQKEHEQNVQLLLQQGRDHLGE--GLADSKRQYEARIHALEKEL 1201
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEER----AALEALKAERQKLLARLEKELAELAAElaELQQEAEELEALIARLEAEA 236
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
788-1080 |
5.36e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 788 QEFRKRVAAAQSQVQVLKEK-KQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHR 866
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 867 VKELELKHEQQQKILKikteeiaafqrkrrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEEL--GEELRKRE 944
Cdd:pfam12128 680 ANERLNSLEAQLKQLD-----------------------KKHQAWLEEQKEQKREARTEKQAYWQVVEGAldAQLALLKA 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 945 VILAKKEALMQEKTGLESKRLRSSQALNEDIVRVsSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQ 1024
Cdd:pfam12128 737 AIAARRSGAKAELKALETWYKRDLASLGVDPDVI-AKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQ 815
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1025 RLEIDSKLR--QGSL--LSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASL 1080
Cdd:pfam12128 816 LSNIERAISelQQQLarLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
948-1201 |
6.20e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 948 AKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELseksgqlrQGSAQNQQQIRGEIDTLRQEKDSLLKQRLE 1027
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQL--------AQAPAKLRQAQAELEALKDDNDEETRETLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1028 IDSkLRQgslLSPEEERTLFQLDEAIEALDaaiEYKNEAITCRQRVLRASASllsqcemnlmaklsyLSSSETRAllcky 1107
Cdd:PRK11281 120 TLS-LRQ---LESRLAQTLDQLQNAQNDLA---EYNSQLVSLQTQPERAQAA---------------LYANSQRL----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1108 fdkvvtlreeqhqQQIAfSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQL--LLQQGRDHLgeglad 1185
Cdd:PRK11281 173 -------------QQIR-NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLqdLLQKQRDYL------ 232
|
250
....*....|....*.
gi 568947410 1186 skrqyEARIHALEKEL 1201
Cdd:PRK11281 233 -----TARIQRLEHQL 243
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
739-1024 |
8.99e-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: 43.66 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 739 QALNRQHSQRIRELEQEAERVRAELCEGQRQL----RELEGREP-------QDASERSRLQEFRKRVAAAQSQVQVLKE- 806
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVsalqPELTEKESslidlkeHASSLASSGLKKDSKLKSLEIAVEQKKEe 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 807 ---------KKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQ 877
Cdd:pfam10174 533 csklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 878 QKILKIKTEEIAAFQRKRRSGSNG----------SVVSLEQQQKIEEqkkwLDQEMEKVLQQrraLEELGEELRKREVIL 947
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKGAQlleearrredNLADNSQQLQLEE----LMGALEKTRQE---LDATKARLSSTQQSL 685
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947410 948 AKKEALmqektgLESKRLRSSQALNEdivRVSSRLEHLEKELSEKSGQ--LRQGSAQNQQQIRGEIDTLRQEKDSLLKQ 1024
Cdd:pfam10174 686 AEKDGH------LTNLRAERRKQLEE---ILEMKQEALLAAISEKDANiaLLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
748-1199 |
1.10e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 748 RIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQ-----------EFRKRVAAAQSQVQVL-KEKKQATERLV 815
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikKLEEDILLLEDQNSKLsKERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 816 SLS---AQSETRLQELE--RNVQLMRRQQGQLQRRLREETEQ-----KRRLETEMNKRQHRVKELELKHEQQQKILKIKT 885
Cdd:pfam01576 163 EFTsnlAEEEEKAKSLSklKNKHEAMISDLEERLKKEEKGRQelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKKE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 886 EEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEME-------KVLQQRRALEELGEELR----------------- 941
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnKAEKQRRDLGEELEALKteledtldttaaqqelr 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 942 -KREVILAK-KEALMQEKTGLESK----RLRSSQALNEdivrVSSRLEHLE--KELSEKSgqlRQGSAQNQQQIRGEIDT 1013
Cdd:pfam01576 323 sKREQEVTElKKALEEETRSHEAQlqemRQKHTQALEE----LTEQLEQAKrnKANLEKA---KQALESENAELQAELRT 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1014 LRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLS 1093
Cdd:pfam01576 396 LQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1094 YLsSSETRALLcKYFDKVVTLREEQhqqqiafSELEMQLEEQQRlvywLEVALERQRLEMDRQLTLQQKEHEQNVQLL-- 1171
Cdd:pfam01576 476 LL-QEETRQKL-NLSTRLRQLEDER-------NSLQEQLEEEEE----AKRNVERQLSTLQAQLSDMKKKLEEDAGTLea 542
|
490 500
....*....|....*....|....*...
gi 568947410 1172 LQQGRDHLGEGLADSKRQYEARIHALEK 1199
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDK 570
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
731-1181 |
1.10e-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: 43.42 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 731 LVRTGKAAQALNRQHSQRIRELEQ--EAERVRAELCEGQRQLRELEGrEPQDASERSRLQEFrkrvaAAQSQVQVLKEKK 808
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEKKELLMNlfPLDQYTQLALMEFAKKKSLHG-KAELLTLRSQLLTL-----CTPCMPDTYHERK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 809 QATERLVslsAQSETRLQELERNvqlmrrqqGQLQRRLREETEQKRRLETEMNKRQHRVKELElkheqqqkilkiktEEI 888
Cdd:TIGR00618 222 QVLEKEL---KHLREALQQTQQS--------HAYLTQKREAQEEQLKKQQLLKQLRARIEELR--------------AQE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 889 AAFQrkrrsgsngsvvslEQQQKIEEQKKWL-----DQEMEKVLQQR-RALEELGEELRKREVILAKKEALMQEKTGLES 962
Cdd:TIGR00618 277 AVLE--------------ETQERINRARKAAplaahIKAVTQIEQQAqRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 963 KRLRSSQALN-EDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPE 1041
Cdd:TIGR00618 343 QRRLLQTLHSqEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1042 EERtLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQ- 1120
Cdd:TIGR00618 423 QGQ-LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQe 501
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568947410 1121 QQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKehEQNVQLLLQQGRDHLGE 1181
Cdd:TIGR00618 502 EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETS--EEDVYHQLTSERKQRAS 560
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
692-1134 |
1.36e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 692 VQTRQAPAAMASEWRlaQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAEL----CEGQ 767
Cdd:PRK02224 233 RETRDEADEVLEEHE--ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 768 RQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKkqaTERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLR 847
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED---ADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 848 EETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSN-----------GSVVSLEQQQKIEEQK 916
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleaGKCPECGQPVEGSPHV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 917 KWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSqalnedivRVSSRLEHLEKELSEKSGQL 996
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE--------DLEELIAERRETIEEKRERA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 997 RQGSAQNQqqirgEIDTLRQEK-DSLLKQRLEIDSKLRQGSLLspeeERTLFQLDEAIEALDAAIEYKNEAITCRQRVLR 1075
Cdd:PRK02224 540 EELRERAA-----ELEAEAEEKrEAAAEAEEEAEEAREEVAEL----NSKLAELKERIESLERIRTLLAAIADAEDEIER 610
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568947410 1076 ASASLLSQCEMNLMAKLSYLSSSETRALLCKYFD--KVVTLREEQHQQQIAFSELEMQLEE 1134
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDeaRIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
706-1240 |
1.39e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 706 RLAQAQQKIRELAINIRMKEELIGELVRTgkaaqalnrqhsqrIRELEQEAERVRAELC----EGQRQLRELEGREPQDA 781
Cdd:pfam10174 220 QLQPDPAKTKALQTVIEMKDTKISSLERN--------------IRDLEDEVQMLKTNGLlhteDREEEIKQMEVYKSHSK 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 782 SERSRLQEFRKRVAAAQSQVQVLKEKkqaterLVSLSAQSETRLQELErnvqlmrrqqgqlqrRLREETEQKrrlETEMN 861
Cdd:pfam10174 286 FMKNKIDQLKQELSKKESELLALQTK------LETLTNQNSDCKQHIE---------------VLKESLTAK---EQRAA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 862 KRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvsleQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELR 941
Cdd:pfam10174 342 ILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKST----------LAGEIRDLKDMLDVKERKINVLQKKIENLQEQLR 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 942 KREVILA-KKEALmqektgleskrlrssQALNEDIVRVSSRLEHLEKELSEKSG---QLRQGSAQNQQQIRGEIDTLRQE 1017
Cdd:pfam10174 412 DKDKQLAgLKERV---------------KSLQTDSSNTDTALTTLEEALSEKERiieRLKEQREREDRERLEELESLKKE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1018 -KDslLKQRLEI--DSKLRQGSLLSPEEERT------LFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMN- 1087
Cdd:pfam10174 477 nKD--LKEKVSAlqPELTEKESSLIDLKEHAsslassGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNp 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1088 -LMAKLSYLSSSETRallckYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQL----TLQQK 1162
Cdd:pfam10174 555 eINDRIRLLEQEVAR-----YKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVanikHGQQE 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1163 EHEQNVQLLLQQGRDHLGEGLADSKRQYEARIHALEKelgrhmwINQEL---KQKLSAGSTAGQSRGCERRSLCLENRQC 1239
Cdd:pfam10174 630 MKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEK-------TRQELdatKARLSSTQQSLAEKDGHLTNLRAERRKQ 702
|
.
gi 568947410 1240 L 1240
Cdd:pfam10174 703 L 703
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
743-964 |
1.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 743 RQHSQRIRELEQEAERVRA-----ELCEGQRQLRELEGREPQDASERSRLQEfrkRVAAAQSQVQVLKEKKQATERlvSL 817
Cdd:COG4913 258 RELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEA---ELERLEARLDALREELDELEA--QI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 818 SAQSETRLQELERnvqlmrrqqgqlqrrlreeteQKRRLETEMNKRQHRVKELelkhEQQQKILKIKT-EEIAAFQRKRR 896
Cdd:COG4913 333 RGNGGDRLEQLER---------------------EIERLERELEERERRRARL----EALLAALGLPLpASAEEFAALRA 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947410 897 sgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEElgeelrkrevilaKKEALMQEKTGLESKR 964
Cdd:COG4913 388 -------EAAALLEALEEELEALEEALAEAEAALRDLRR-------------ELRELEAEIASLERRK 435
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
796-1201 |
1.52e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 796 AAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVkelelkhe 875
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 876 qqqkilkiktEEIAAFqrkrrsgSNGSVVSLEQQQKIEEQKkwldqemEKVLQQRRALEELGEELRKREvilakkealmQ 955
Cdd:pfam05483 394 ----------EEMTKF-------KNNKEVELEELKKILAED-------EKLLDEKKQFEKIAEELKGKE----------Q 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 956 EKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLrqgsaqnqqqirgeidtlrqEKDSLlkQRLEIDSKLRQG 1035
Cdd:pfam05483 440 ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL--------------------EKEKL--KNIELTAHCDKL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1036 SLlspeEERTLFQldeaiEALDAAIEYKNEA---ITCRQRVLRASASL--LSQCEMNLMAKLSYlsssetrallckyfdk 1110
Cdd:pfam05483 498 LL----ENKELTQ-----EASDMTLELKKHQediINCKKQEERMLKQIenLEEKEMNLRDELES---------------- 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1111 vvtLREEQHQQQiafSELEMQL---EEQQRLVYWLEVALERQRLEMDRQ---LTLQQKEHEQNVQLLLQQGRDHLGEGLA 1184
Cdd:pfam05483 553 ---VREEFIQKG---DEVKCKLdksEENARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSA 626
|
410
....*....|....*....
gi 568947410 1185 DSKR--QYEARIHALEKEL 1201
Cdd:pfam05483 627 ENKQlnAYEIKVNKLELEL 645
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
704-991 |
1.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 704 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALnRQHSQRIREL---EQEAERVRAELCEGQRQLRELEgrepqd 780
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYswdEIDVASAEREIAELEAELERLD------ 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 781 aSERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEM 860
Cdd:COG4913 682 -ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 861 NKRQHRVKElELKHEQQQKILKIKTEE------IAAFQRKRRSGSNGSVVSLEQqqkIEEQKKWLDQemekvlQQRRALE 934
Cdd:COG4913 761 DAVERELRE-NLEERIDALRARLNRAEeeleraMRAFNREWPAETADLDADLES---LPEYLALLDR------LEEDGLP 830
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568947410 935 ELGEELRKrevilAKKEALMQEKTGLeskrlrsSQALNEDIVRVSSRLEHLEKELSE 991
Cdd:COG4913 831 EYEERFKE-----LLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDSLKR 875
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
794-956 |
1.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 794 VAAAQSQVQVLKEK-KQATERLVSLSAQSETRLQELERnvqlmrrqqgqlqrrLREETEQ-KRRLETEMNKRQHRVKELE 871
Cdd:PRK00409 504 IEEAKKLIGEDKEKlNELIASLEELERELEQKAEEAEA---------------LLKEAEKlKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 872 LKHEQQ-QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwLDQEMEKV----LQQRRALEEL--GEELR--- 941
Cdd:PRK00409 569 EEAEKEaQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKKekkkKKQKEKQEELkvGDEVKyls 647
|
170 180
....*....|....*....|
gi 568947410 942 ---KREV--ILAKKEALMQE 956
Cdd:PRK00409 648 lgqKGEVlsIPDDKEAIVQA 667
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
861-1054 |
1.63e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 861 NKRQHRVKELELKHEQQQKILKIKTEEIAAFQR------KRRSGSNGSVVSLEQQQKieEQKKWLDQEMEKVLQQRRALE 934
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKnlnkdeEKINNSNNKIKILEQQIK--DLNDKLKKNKDKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 935 ELGEELR-KREVILAKKEalmqektglESKRL-RSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgsaqnqqQIRGEID 1012
Cdd:TIGR04523 107 KINSEIKnDKEQKNKLEV---------ELNKLeKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN--------DLKKQKE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568947410 1013 TLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIE 1054
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ 211
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
747-943 |
1.63e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 747 QRIRELEQEAERVRAELCEGQRQLRELEGREpqdASERSRLQEFRKRVAAAQSQVQVLKEK-KQATERLVSLSAQSEtrL 825
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNKE--Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 826 QELERnvqlmrrqqgqlqrrlrEETEQKRRLEtemnKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvs 905
Cdd:COG1579 92 EALQK-----------------EIESLKRRIS----DLEDEILELMERIEELEEELAELEAELAELEAELE--------- 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 568947410 906 lEQQQKIEEQKKWLDQEMEKVLQQRRALEE-LGEELRKR 943
Cdd:COG1579 142 -EKKAELDEELAELEAELEELEAEREELAAkIPPELLAL 179
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
718-1066 |
2.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 718 AINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQdasERSRLQEFRKRVAAA 797
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE---LNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 798 QSQVQVLKEKKQATERLVslsAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELE---LKH 874
Cdd:COG4372 100 QEELESLQEEAEELQEEL---EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqelQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 875 EQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEEL-GEELRKREVILAKKEAL 953
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALlDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 954 MQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLR 1033
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|...
gi 568947410 1034 QGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA 1066
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
743-1027 |
2.23e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.97 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 743 RQHSQRIRELEQEAERVRAELCEGQRQLRELE---GREPQDASERSRLQE----FRKRVAAAQSQVQVLKEK-KQAteRL 814
Cdd:pfam15742 65 KQAQQKLLDSTKMCSSLTAEWKHCQQKIRELElevLKQAQSIKSQNSLQEklaqEKSRVADAEEKILELQQKlEHA--HK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 815 VSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMN---------------------KRQHRVKELELK 873
Cdd:pfam15742 143 VCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdkeaqlemtnsQQQLRIQQQEAQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 874 HEQQQKILKIKTEEIAAfqrkrrsgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQ-RRALEELGEELRKRevilakKEA 952
Cdd:pfam15742 223 LKQLENEKRKSDEHLKS------------------NQELSEKLSSLQQEKEALQEElQQVLKQLDVHVRKY------NEK 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568947410 953 LMQEKTGLEskrlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQnQQQIRGEIDTLRQEKDSLLKQRLE 1027
Cdd:pfam15742 279 HHHHKAKLR----RAKDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAF-QKQVTAQNEILLLEKRKLLEQLTE 348
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
906-1200 |
2.69e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 906 LEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREvilAKKEALMQEKTGLESKRLRSSQALNEDIVR------VS 979
Cdd:COG3096 343 LRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAE---ARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqAV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 980 SRLEHLEK-----ELSEKSGQLRQGSAQNQQQirgEIDTLRQEkdslLKQRLEIDSKLRQgsllspeeertlfQLDEAIE 1054
Cdd:COG3096 420 QALEKARAlcglpDLTPENAEDYLAAFRAKEQ---QATEEVLE----LEQKLSVADAARR-------------QFEKAYE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1055 AL---------DAAIEYKNEAItCRQRVLRASASLLSQCEMNLmAKLSYLSSSETRAL-----LCKYFDKVVT----LRE 1116
Cdd:COG3096 480 LVckiageverSQAWQTARELL-RRYRSQQALAQRLQQLRAQL-AELEQRLRQQQNAErlleeFCQRIGQQLDaaeeLEE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1117 EQHQQQIAFSELEMQLEEQQrlvywlEVALE-RQRLEmdrQLTLQQKEHEQ------NVQLLLQQGRDHLGEGLADSKRQ 1189
Cdd:COG3096 558 LLAELEAQLEELEEQAAEAV------EQRSElRQQLE---QLRARIKELAArapawlAAQDALERLREQSGEALADSQEV 628
|
330
....*....|.
gi 568947410 1190 YEARIHALEKE 1200
Cdd:COG3096 629 TAAMQQLLERE 639
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
786-1061 |
2.96e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 786 RLQEFRKRVAAAQSQVQVLKEKKQatERLVSLSAQSE--------TRLQELErnvqlmrrqqgqlqRRLREETEQKRRLE 857
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQR--GSLDQLKAQIEekeekdlhERLNGLE--------------SELAELDEEIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 858 TEMNKRQHRVKELEL---KHEQQQKILKIKTEEIAafqrkrrsgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALE 934
Cdd:PRK02224 227 EQREQARETRDEADEvleEHEERREELETLEAEIE-----------------DLRETIAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 935 ELGEELRKrevilakkealMQEKTGLESKrlrSSQALNEDIVRVSSRLEHLEKELSEKSgqLRQGSAQNQ-QQIRGEIDT 1013
Cdd:PRK02224 290 ELEEERDD-----------LLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECR--VAAQAHNEEaESLREDADD 353
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568947410 1014 LRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1061
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
708-915 |
3.34e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 708 AQAQQKIRELAINIrmkEELIGELvrtgkaaQALNRQHSQRIRELE---QEAERVRAELcegQRQLRELEGREpqdASER 784
Cdd:PRK00409 505 EEAKKLIGEDKEKL---NELIASL-------EELERELEQKAEEAEallKEAEKLKEEL---EEKKEKLQEEE---DKLL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 785 SRL-QEFRKRVAAAqsqvqvlkekKQATERLVSlsaqsetRLQELERnvqlmrrqqgqlqrrlREETEQKRRLETEMNKR 863
Cdd:PRK00409 569 EEAeKEAQQAIKEA----------KKEADEIIK-------ELRQLQK----------------GGYASVKAHELIEARKR 615
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568947410 864 qhrvkeLELKHEQQQKILKIKTEEIAAFQ-----RKRRSGSNGSVVSLEQQQKIEEQ 915
Cdd:PRK00409 616 ------LNKANEKKEKKKKKQKEKQEELKvgdevKYLSLGQKGEVLSIPDDKEAIVQ 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
706-1205 |
4.49e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 706 RLAQAQQKIRELAINIRMKEELIgELVRTGKAAQALNRQHsQRIRELEQEAERVRAELCEGQRQLRELEGREpqDASERS 785
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLR-AALRLWFAQRRLELLE-AELEELRAELARLEAELERLEARLDALREEL--DELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 786 RLQEFRKRVAAAQSQVQVLKEKKQATERLvslSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQH 865
Cdd:COG4913 332 IRGNGGDRLEQLEREIERLERELEERERR---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 866 rvkELELKHEQQQKILKIKTEEIAAFQRkRRSGSNGSVVS----LEQQQKI---------------EEQKKWLDQeMEKV 926
Cdd:COG4913 409 ---EAEAALRDLRRELRELEAEIASLER-RKSNIPARLLAlrdaLAEALGLdeaelpfvgelievrPEEERWRGA-IERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 927 L---------------QQRRALEE--LGEELRKREVILAKKEALMQ--------EKtgLESKR------LRSSQALNEDI 975
Cdd:COG4913 484 LggfaltllvppehyaAALRWVNRlhLRGRLVYERVRTGLPDPERPrldpdslaGK--LDFKPhpfrawLEAELGRRFDY 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 976 VRVSS--RLEHLEKELSeKSGQLRQGSAqnqqqiRGEIDTLRQEKDSLL-----KQRLEIDSKLRQgsllspEEERTLFQ 1048
Cdd:COG4913 562 VCVDSpeELRRHPRAIT-RAGQVKGNGT------RHEKDDRRRIRSRYVlgfdnRAKLAALEAELA------ELEEELAE 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1049 LDEAIEALDAAIEYKNEAITCRQRVLRAS------ASLLSQCEmNLMAKLSYLSSSEtrallckyfDKVVTLREEQHQQQ 1122
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIA-ELEAELERLDASS---------DDLAALEEQLEELE 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 1123 IAFSELEMQLEEQQRLVYWLEVALERQRLEMDR-QLTLQQKEHEQNV-----------QLLLQQGRDHLGEGLADSKRQY 1190
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDElQDRLEAAEDLARLelralleerfaAALGDAVERELRENLEERIDAL 778
|
570
....*....|....*
gi 568947410 1191 EARIHALEKELGRHM 1205
Cdd:COG4913 779 RARLNRAEEELERAM 793
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
708-957 |
7.17e-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: 40.88 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 708 AQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRL 787
Cdd:pfam17380 400 AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 788 QEFRKRVAAAQSQVQVLKEKkqaterlvslsaqsetrlqELERNVQLMrrqqgqlqrrlREETEQKRRLETEMNKRQHRV 867
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKILEK-------------------ELEERKQAM-----------IEEERKRKLLEKEMEERQKAI 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 868 KElelkhEQQQKILkikteeiaafQRKRRsgsngsvvsleQQQKIEEQKKwLDQEMEKVLQQRRALEELGeelRKREVIL 947
Cdd:pfam17380 530 YE-----EERRREA----------EEERR-----------KQQEMEERRR-IQEQMRKATEERSRLEAME---REREMMR 579
|
250
....*....|
gi 568947410 948 AKKEALMQEK 957
Cdd:pfam17380 580 QIVESEKARA 589
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
747-950 |
7.22e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 747 QRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQsqvqvlkEKKQATERLVSLSAQSETRLQ 826
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE-------ELQREEERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 827 ELErnvqlmrrqqgqlqrrlreetEQKRRLETEMNKRQHRVKELELKHEQQQKILKIkteeiaafqrkrrsgsngsVVSL 906
Cdd:PRK12705 99 KLD---------------------NLENQLEEREKALSARELELEELEKQLDNELYR-------------------VAGL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568947410 907 EQQQKIEEQKKWLDQEMEKVLQQR--RALEELGEELRKREVILAKK 950
Cdd:PRK12705 139 TPEQARKLLLKLLDAELEEEKAQRvkKIEEEADLEAERKAQNILAQ 184
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
746-1083 |
7.29e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 746 SQRIRELEQEAERVRAELCEGQRQLRELEgrepqdasersrlqefrkrvAAAQSQVQVLKEKKQatERLVSLSAQSETRL 825
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALK--------------------SESQNKIELLLQQHQ--DRIEQLISEHEVEI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 826 QELERNVQLMRRQQGQLQRRLREETEQKRR-----------LETEMNKRQHRVKE----LELKHEQQQKILKIKTEEIAA 890
Cdd:pfam15921 281 TGLTEKASSARSQANSIQSQLEIIQEQARNqnsmymrqlsdLESTVSQLRSELREakrmYEDKIEELEKQLVLANSELTE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 891 FQRKRRSGSNGSVVSLEQQQKI------EEQKKWLDQEMEKVLQQRR-----ALEELGEELRKREVILAKKEALMQ---- 955
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQKLladlhkREKELSLEKEQNKRLWDRDtgnsiTIDHLRRELDDRNMEVQRLEALLKamks 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 956 EKTGLESKRLRSSQALNEDIVRVSSRLEHLE--KELSEKSGQ---LRQGSAQNQQQIRGEIDTLRQEKD--------SLL 1022
Cdd:pfam15921 441 ECQGQMERQMAAIQGKNESLEKVSSLTAQLEstKEMLRKVVEeltAKKMTLESSERTVSDLTASLQEKEraieatnaEIT 520
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568947410 1023 KQRLEIDSKLRQGSLLSPEEERtLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1083
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
737-969 |
7.48e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.89 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 737 AAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGR-EPQDASERSRLQEFRKrvaaaqsqvQVLKEKKQATERLV 815
Cdd:pfam07111 471 PAPPVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRaREQGEAERQQLSEVAQ---------QLEQELQRAQESLA 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 816 SLSAQSETRLQelernvqlmrrqqgqlqrRLREETEQKRRLETEMNKRQH--------RVKELELKHEQQQKILKIKTEE 887
Cdd:pfam07111 542 SVGQQLEVARQ------------------GQQESTEEAASLRQELTQQQEiygqalqeKVAEVETRLREQLSDTKRRLNE 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 888 IAAFQRKrrsgsngSVVSLEQQQKIEEQKKWLDQEMEKVlqQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRS 967
Cdd:pfam07111 604 ARREQAK-------AVVSLRQIQHRATQEKERNQELRRL--QDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRY 674
|
..
gi 568947410 968 SQ 969
Cdd:pfam07111 675 KQ 676
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
724-1058 |
7.72e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 724 KEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELcegQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQ 800
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKalfELDKLQEELEQLREEL---EQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 801 VQ-VLKEKKQATERLVSLSAQSETRLQELERnvqlMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELElkheqqQK 879
Cdd:COG4372 89 LQaAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE------EQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 880 ILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTG 959
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 960 LESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLS 1039
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330
....*....|....*....
gi 568947410 1040 PEEERTLFQLDEAIEALDA 1058
Cdd:COG4372 319 AALLELAKKLELALAILLA 337
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
914-1065 |
7.78e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 914 EQKKWLDQEMEKVLQQRRALEELGEELRKREVIL--------AKKEALMQEKTGL--ESKRLRSS-QALNEDIVRVSSRL 982
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELneelkelaEKRDELNAQVKELreEAQELREKrDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 983 EHLEKELSEKSGQLRQGSAQNQQQI--RGEIDTLRQEKDSLLKQrleidsklRQGSLLSPEEERTLF----QLDEAIEAL 1056
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNkaGGSIDKLRKEIERLEWR--------QQTEVLSPEEEKELVekikELEKELEKA 152
|
....*....
gi 568947410 1057 DAAIEYKNE 1065
Cdd:COG1340 153 KKALEKNEK 161
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
709-950 |
7.93e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 709 QAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEgrepqdaSERSRLQ 788
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN-------EEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 789 EfrkRVAAAQSQVQVLKEKKQAterLVSLSAQSETRLQELERNVQLMrrqqgqlqrrlrEETEQKRRLETEMNKRQHRVK 868
Cdd:TIGR04523 510 E---KVKDLTKKISSLKEKIEK---LESEKKEKESKISDLEDELNKD------------DFELKKENLEKEIDEKNKEIE 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 869 ELEL-------KHEQQQKILKIKTEEIAAFqRKRRSGSNGSVVSLEQQ--------QKIEEQKKWLDQEMEKVLQQRRAL 933
Cdd:TIGR04523 572 ELKQtqkslkkKQEEKQELIDQKEKEKKDL-IKEIEEKEKKISSLEKElekakkenEKLSSIIKNIKSKKNKLKQEVKQI 650
|
250
....*....|....*..
gi 568947410 934 EELGEELRKREVILAKK 950
Cdd:TIGR04523 651 KETIKEIRNKWPEIIKK 667
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
862-1066 |
9.39e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 862 KRQHRVKELELKhEQQQKILKIKTEEIAAFQRKRRsgsngsvvsLEQQQKIEEQKkwldQEMEKVLQQRRA-LEELGEEL 940
Cdd:PRK12704 26 KKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL---------LEAKEEIHKLR----NEFEKELRERRNeLQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 941 RKREVILAKK-EALMQEKTGLESKRlrssqalnedivrvsSRLEHLEKELSEKsgqlrqgsaqnqqqiRGEIDTLRQEkd 1019
Cdd:PRK12704 92 LQKEENLDRKlELLEKREEELEKKE---------------KELEQKQQELEKK---------------EEELEELIEE-- 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568947410 1020 slLKQRLEIDSKlrqgslLSPEEERTLfQLDEAIEAL--DAAI---EYKNEA 1066
Cdd:PRK12704 140 --QLQELERISG------LTAEEAKEI-LLEKVEEEArhEAAVlikEIEEEA 182
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
698-817 |
9.92e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947410 698 PAAMASEWRLAQAQQKIRELAINIRMKEELIGELvrtgkaaQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGRE 777
Cdd:COG2433 399 REKEHEERELTEEEEEIRRLEEQVERLEAEVEEL-------EAELEEKDERIERLERELSEARSEERREIRKDREISRLD 471
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568947410 778 PQDASERSRLQEFRKRVAAAQSQVQVLKE--KKQATERLVSL 817
Cdd:COG2433 472 REIERLERELEEERERIEELKRKLERLKElwKLEHSGELVPV 513
|
|
| |
