|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
23-380 |
0e+00 |
|
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: 610.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGK 102
Cdd:cd01372 8 RVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 103 TYTMGTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTRDidaknKKSN 182
Cdd:cd01372 88 TYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPETD-----KKPT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 183 IRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaenatdnkli 262
Cdd:cd01372 155 ISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA---------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 263 sESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSKLTRLLQD 342
Cdd:cd01372 225 -PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQD 303
|
330 340 350
....*....|....*....|....*....|....*...
gi 1039748264 343 SLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 380
Cdd:cd01372 304 SLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
23-379 |
2.86e-140 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 435.85 E-value: 2.86e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 95
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 96 GQTGAGKTYTMGTGfdvnimEEEQGIISRAVRHLFKSIDEKKTSaiknglppPEFKVNAQFLELYNEEVLDLFDTTrdid 175
Cdd:pfam00225 81 GQTGSGKTYTMEGS------DEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 176 aKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTdaen 255
Cdd:pfam00225 143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 256 atdnklisesspmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 334
Cdd:pfam00225 218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1039748264 335 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 379
Cdd:pfam00225 282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
23-386 |
3.54e-135 |
|
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: 422.37 E-value: 3.54e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 95
Cdd:smart00129 7 RVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNATIFAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 96 GQTGAGKTYTMGtGFdvnimEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTrdid 175
Cdd:smart00129 87 GQTGSGKTYTMI-GT-----PDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLNPS---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 176 aknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaen 255
Cdd:smart00129 149 ----SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSG--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 256 atdnklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHVPYRDSK 335
Cdd:smart00129 222 ----------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSK 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1039748264 336 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 386
Cdd:smart00129 285 LTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
23-377 |
1.66e-118 |
|
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: 376.21 E-value: 1.66e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYG 96
Cdd:cd00106 7 RVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGTIFAYG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 97 QTGAGKTYTMGTGFDvnimeEEQGIISRAVRHLFKSIDEKKTsaiknglPPPEFKVNAQFLELYNEEVLDLFDttrdida 176
Cdd:cd00106 86 QTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRKE-------TKSSFSVSASYLEIYNEKIYDLLS------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 177 KNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtDAENA 256
Cdd:cd00106 147 PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV---------KQRNR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 257 TDNKLISESSpmnefetltaKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKL 336
Cdd:cd00106 218 EKSGESVTSS----------KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN--KHIPYRDSKL 285
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039748264 337 TRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 377
Cdd:cd00106 286 TRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
23-379 |
2.33e-103 |
|
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: 334.04 E-value: 2.33e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFA 94
Cdd:cd01371 8 RCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYNGTIFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 95 YGQTGAGKTYTMGtGFDVNimEEEQGIISRAVRHLFKSIdeKKTSAIKNglpppeFKVNAQFLELYNEEVldlfdttRDI 174
Cdd:cd01371 88 YGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHI--ARSQNNQQ------FLVRVSYLEIYNEEI-------RDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 175 DAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV-Cqtrvcpqtda 253
Cdd:cd01371 150 LGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeC---------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 254 enatdnkliSESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskRATHVPYRD 333
Cdd:cd01371 220 ---------SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRD 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1039748264 334 SKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 379
Cdd:cd01371 289 SKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
11-381 |
1.59e-101 |
|
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: 328.78 E-value: 1.59e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 11 GCWRVrsydpWSRIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFDIDSQQEQIYTQcIEKLIEGCFE 86
Cdd:cd01366 2 GNIRV-----FCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 87 GYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIDEKKTSAIKnglpppeFKVNAQFLELYNEEVL 165
Cdd:cd01366 76 GYNVCIFAYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 166 DLFDTTRdidAKNKKSNIRiHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqt 245
Cdd:cd01366 142 DLLAPGN---APQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 246 rvcpqtDAENATDNklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKr 325
Cdd:cd01366 215 ------SGRNLQTG------------EISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS- 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039748264 326 atHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 381
Cdd:cd01366 276 --HIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
23-379 |
1.56e-99 |
|
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: 323.91 E-value: 1.56e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFDIDSQQEQIYTQCIEKL 80
Cdd:cd01370 7 RVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYEETTKPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 81 IEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIDEKKTSAiknglpppEFKVNAQFLEL 159
Cdd:cd01370 87 VDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLKDEK--------EFEVSMSYLEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 160 YNEEVLDLFDTTrdidakNKKSNIRihEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFT 239
Cdd:cd01370 152 YNETIRDLLNPS------SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 240 IHVCQTrvcpqtdaenatdNKLISESSpmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL 319
Cdd:cd01370 224 ITVRQQ-------------DKTASINQ-----QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINAL 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 320 GDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 379
Cdd:cd01370 286 ADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
23-379 |
6.45e-96 |
|
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: 312.73 E-value: 6.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGA 100
Cdd:cd01369 9 RFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFAYGQTSS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 101 GKTYTMgtgFDVNIMEEEQGIISRAVRHLFKSIdEKKTSAIknglpppEFKVNAQFLELYNEEVLDLFDTTRDidaknkk 180
Cdd:cd01369 89 GKTYTM---EGKLGDPESMGIIPRIVQDIFETI-YSMDENL-------EFHVKVSYFEIYMEKIRDLLDVSKT------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 181 sNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQtrvcpqtdaENATDNK 260
Cdd:cd01369 151 -NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ---------ENVETEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 261 LisesspmnefetLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLL 340
Cdd:cd01369 221 K------------KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRIL 286
|
330 340 350
....*....|....*....|....*....|....*....
gi 1039748264 341 QDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 379
Cdd:cd01369 287 QDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
23-386 |
1.12e-95 |
|
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: 313.52 E-value: 1.12e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVFD-IDSQ------QEQIYTQCIEKLIEG 83
Cdd:cd01365 8 RVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYWsHDSEdpnyasQEQVYEDLGEELLQH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 84 CFEGYNATVFAYGQTGAGKTYTMgTGFDvnimeEEQGIISRAVRHLFKSIDEKKTSAIKnglpppeFKVNAQFLELYNEE 163
Cdd:cd01365 88 AFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVSYMEIYNEK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 164 VLDLFDTtrdiDAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVC 243
Cdd:cd01365 155 VRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 244 QTRVCPQTDAEnatdnklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD-- 321
Cdd:cd01365 231 QKRHDAETNLT-----------------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADms 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264 322 ---KSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 386
Cdd:cd01365 294 sgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
23-388 |
1.19e-93 |
|
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: 307.33 E-value: 1.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFA 94
Cdd:cd01364 9 RCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYNCTIFA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 95 YGQTGAGKTYTMgTGFDVNIME------EEQGIISRAVRHLFKSIDEKKTsaiknglpppEFKVNAQFLELYNEEVLDLF 168
Cdd:cd01364 89 YGQTGTGKTYTM-EGDRSPNEEytweldPLAGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIYNEELFDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 169 DttrdiDAKNKKSNIRIHEDS--TGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtr 246
Cdd:cd01364 158 S-----PSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITI---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 247 vcpqtdaenatdnkLISESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKra 326
Cdd:cd01364 229 --------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAP-- 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039748264 327 tHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 388
Cdd:cd01364 293 -HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
52-519 |
1.67e-92 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 312.06 E-value: 1.67e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 52 GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLF 130
Cdd:COG5059 53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 131 KSIDEKKTSAiknglpppEFKVNAQFLELYNEEVLDLFDttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 210
Cdd:COG5059 126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 211 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqtdaenatdNKLISESSpmnefetlTAKFHFVDLAGSERLK 290
Cdd:COG5059 190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK-------------NKVSGTSE--------TSKLSLVDLAGSERAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 291 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 370
Cdd:COG5059 249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 371 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQT---ENNNLRVR 446
Cdd:COG5059 328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQSlkkETETLKSR 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039748264 447 IK-AMQETVDALRARITQLVSEqanqvlaraGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 519
Cdd:COG5059 403 IDlIMKSIISGTFERKKLLKEE---------GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
23-388 |
7.71e-90 |
|
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: 296.34 E-value: 7.71e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAG 101
Cdd:cd01373 8 RIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYGQTGSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 102 KTYTM--GTGFDVNIMEEEQGIISRAVRHLFKSIDEKKTSAIKNglppPEFKVNAQFLELYNEEVLDLFDTTrdidaknk 179
Cdd:cd01373 88 KTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIQREKEKAGEG----KSFLCKCSFLEIYNEQIYDLLDPA-------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 180 KSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqtdaenatdn 259
Cdd:cd01373 156 SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC------------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 260 kLISESSPMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-RATHVPYRDSKLT 337
Cdd:cd01373 217 -TIESWEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYRDSKLT 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1039748264 338 RLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 388
Cdd:cd01373 296 FLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
55-379 |
4.07e-89 |
|
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: 293.08 E-value: 4.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 55 KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGfdvnimEEEQGIISRAVRHLFKSID 134
Cdd:cd01374 39 TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 135 EKKTSaiknglpppEFKVNAQFLELYNEEVLDLFDTTrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLK 214
Cdd:cd01374 113 DTPDR---------EFLLRVSYLEIYNEKINDLLSPT--------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 215 LGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtdaenatdnklisESSPMNEFETLTAKF---HFVDLAGSERLKR 291
Cdd:cd01374 176 RGEKNRHVGETDMNERSSRSHTIFRITI---------------------ESSERGELEEGTVRVstlNLIDLAGSERAAQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 292 TGATGERAKEGISINCGLLALGNVISALGDkSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLK 371
Cdd:cd01374 235 TGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLK 313
|
....*...
gi 1039748264 372 YANRARNI 379
Cdd:cd01374 314 FASRAKKI 321
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
56-375 |
1.02e-69 |
|
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: 237.58 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 56 AFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGFDVNimEEEQGIISRAVRHLFKSIde 135
Cdd:cd01367 51 TFRFDYVFDESSSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQ--EESKGIYALAARDVFRLL-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 136 kKTSAIKNGLpppefKVNAQFLELYNEEVLDLFdttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKL 215
Cdd:cd01367 127 -NKLPYKDNL-----GVTVSFFEIYGGKVFDLL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIES 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 216 GALSRTTASTQMNVQSSRSHAIFTIhVCQTRvcpqtdaenatdnklisesspmnEFETLTAKFHFVDLAGSER-LKRTGA 294
Cdd:cd01367 192 GSSLRTTGQTSANSQSSRSHAILQI-ILRDR-----------------------GTNKLHGKLSFVDLAGSERgADTSSA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 295 TGERAKEGISINCGLLALGNVISALGDKSkraTHVPYRDSKLTRLLQDSL-GGNSQTIMIACVSPSDRDFMETLNTLKYA 373
Cdd:cd01367 248 DRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYA 324
|
..
gi 1039748264 374 NR 375
Cdd:cd01367 325 DR 326
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
14-377 |
4.53e-69 |
|
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: 235.47 E-value: 4.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 14 RVRSYdpwSRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEG 87
Cdd:cd01376 1 NVRVA---VRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 88 YNATVFAYGQTGAGKTYTMGTGFdvnimeEEQGIISRAVRHLFkSIDEKKTSAiknglpppeFKVNAQFLELYNEEVLDL 167
Cdd:cd01376 77 QNATVFAYGSTGAGKTFTMLGSP------EQPGLMPLTVMDLL-QMTRKEAWA---------LSFTMSYLEIYQEKILDL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 168 FDTtrdidaknKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrv 247
Cdd:cd01376 141 LEP--------ASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 248 cpqtdaenatdnkliSESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKRAT 327
Cdd:cd01376 208 ---------------DQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLP 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1039748264 328 HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 377
Cdd:cd01376 270 RIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
54-377 |
6.16e-69 |
|
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: 235.55 E-value: 6.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 54 DKAFTFDYVFDiDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNImeEEQGIISRAVRHLFKSI 133
Cdd:cd01375 47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENY--KHRGIIPRALQQVFRMI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 134 DEKKTSAIKnglpppefkVNAQFLELYNEEVLDLFDTTRDIDAKNKKsnIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCL 213
Cdd:cd01375 123 EERPTKAYT---------VHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 214 KLGALSRTTASTQMNVQSSRSHAIFTIHvcqtrvcpqtdaenatdnkLISESSPMNEFETLTAKFHFVDLAGSERLKRTG 293
Cdd:cd01375 192 FLGETNRIIASHTMNKNSSRSHCIFTIH-------------------LEAHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 294 ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 373
Cdd:cd01375 253 VEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330
|
....
gi 1039748264 374 NRAR 377
Cdd:cd01375 331 SRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
23-373 |
1.26e-64 |
|
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: 223.81 E-value: 1.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEG 87
Cdd:cd01368 8 RVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQDLLHG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 88 YNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIdekktsaiknglppPEFKVNAQFLELYNEEVLD 166
Cdd:cd01368 88 KNGLLFTYGVTNSGKTYTMqGS-------PGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYNEYIYD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 167 LFDTTRDIDAKNKKSnIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTR 246
Cdd:cd01368 147 LLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 247 VCPQTDAENATDNKLISESSpmnefetltakfhFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRA 326
Cdd:cd01368 226 GDSDGDVDQDKDQITVSQLS-------------LVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQG 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039748264 327 T--HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 373
Cdd:cd01368 293 TnkMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
55-412 |
3.10e-63 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 237.91 E-value: 3.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 55 KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM----GTGFDVNIMEEEQGIISRAVRHLF 130
Cdd:PLN03188 132 QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 131 KSIDEKKtsaIKNGLPPPEFKVNAQFLELYNEEVLDLFDTTrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 210
Cdd:PLN03188 212 ARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITDLLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVT 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 211 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtdaenatDNKLISESSPMNEFETltAKFHFVDLAGSERLK 290
Cdd:PLN03188 281 QLLIKGLSNRRTGATSINAESSRSHSVFTCVV---------------ESRCKSVADGLSSFKT--SRINLVDLAGSERQK 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 291 RTGATGERAKEGISINCGLLALGNVISALGDKSK--RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLN 368
Cdd:PLN03188 344 LTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFS 423
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1039748264 369 TLKYANRARNIKNKVMVNQDrASQQINALRSEITRLQMELMEYK 412
Cdd:PLN03188 424 TLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLRDELQRVK 466
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1314-1627 |
1.24e-58 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 204.49 E-value: 1.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1314 CVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1390
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1391 rESAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1469
Cdd:cd00200 81 -ETGECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1470 VMCLTVDQisnGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALAIQGDN--LFSGSRDNGIKKWDLAQ 1547
Cdd:cd00200 138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1548 KGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRI 1625
Cdd:cd00200 209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287
|
..
gi 1039748264 1626 WK 1627
Cdd:cd00200 288 WD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1308-1630 |
7.06e-47 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 174.33 E-value: 7.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1308 RASPLQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT------ 1379
Cdd:COG2319 106 DLATGLLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkll 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1380 VSTSY---IKVWDIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLK 1455
Cdd:COG2319 178 ASGSDdgtVRLWDLA-TGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1456 RFQSTGKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAI--QGDNLFS 1533
Cdd:COG2319 235 TGKLLRTLTGHSGSVRSVAFS--PDGR-LLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLAS 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1534 GSRDNGIKKWDLAQkGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NS 1611
Cdd:COG2319 306 GSDDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDG 384
|
330
....*....|....*....
gi 1039748264 1612 THVFTAADDRTVRIWKAHN 1630
Cdd:COG2319 385 RTLASGSADGTVRLWDLAT 403
|
|
| Rcc_KIF21A |
cd22263 |
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ... |
946-1027 |
4.84e-44 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410204 [Multi-domain] Cd Length: 82 Bit Score: 154.32 E-value: 4.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 946 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1025
Cdd:cd22263 1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80
|
..
gi 1039748264 1026 AK 1027
Cdd:cd22263 81 AK 82
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1307-1639 |
6.76e-44 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 165.47 E-value: 6.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1307 VRASPLQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT----- 1379
Cdd:COG2319 63 LDAAAGALLATLLGHTAAVLSVAFSPDgrLLASASADGTVRLWDLATGLLLRTLTGHTGAV--------RSVAFSpdgkt 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1380 -VSTSY---IKVWDIrESAKCIRTLTssgqvtlgeacsastsrtvaipSGESQINQIALNPTGTFLYAASG-NAVRMWDL 1454
Cdd:COG2319 135 lASGSAdgtVRLWDL-ATGKLLRTLT----------------------GHSGAVTSVAFSPDGKLLASGSDdGTVRLWDL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1455 KRFQSTGKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAIQGDN--LF 1532
Cdd:COG2319 192 ATGKLLRTLTGHTGAVRSVAFS--PDGK-LLASGSADGTVRLWDLATGKLLRTLTGHS------GSVRSVAFSPDGrlLA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1533 SGSRDNGIKKWDLaQKGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--N 1610
Cdd:COG2319 263 SGSADGTVRLWDL-ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspD 341
|
330 340
....*....|....*....|....*....
gi 1039748264 1611 STHVFTAADDRTVRIWkahNLQDGQLSDT 1639
Cdd:COG2319 342 GKTLASGSDDGTVRLW---DLATGELLRT 367
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1313-1544 |
1.30e-35 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 137.85 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1313 QCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWD 1389
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1390 IReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLG 1468
Cdd:cd00200 164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264 1469 PVMCLTVdqiSNGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAIQGDN--LFSGSRDNGIKKWD 1544
Cdd:cd00200 221 GVNSVAF---SPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT------NSVTSLAWSPDGkrLASGSADGTIRIWD 289
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
946-1027 |
1.48e-28 |
|
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410202 [Multi-domain] Cd Length: 81 Bit Score: 109.99 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 946 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKEsGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1025
Cdd:cd22248 1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDE-GKDESVLRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79
|
..
gi 1039748264 1026 AK 1027
Cdd:cd22248 80 SK 81
|
|
| Rcc_KIF21B |
cd22262 |
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ... |
946-1027 |
2.46e-28 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to a conserved region of KIF21B, which shows high sequence similarity to the regulatory coiled-coil domain of KIF21A.
Pssm-ID: 410203 [Multi-domain] Cd Length: 82 Bit Score: 109.51 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 946 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1025
Cdd:cd22262 1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80
|
..
gi 1039748264 1026 AK 1027
Cdd:cd22262 81 TK 82
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
23-167 |
8.00e-19 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 84.58 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 23 RIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYtQCIEKLIEGCFEGYNATVFAYGQTGAGK 102
Cdd:pfam16796 27 RVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYGQTGSGS 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039748264 103 TYTMgtgfdvnimeeeqgiISRAVRHLFKSIDEKKTSaiknglppPEFKVNAQFLELYNEEVLDL 167
Cdd:pfam16796 102 NDGM---------------IPRAREQIFRFISSLKKG--------WKYTIELQFVEIYNESSQDL 143
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1312-1453 |
3.07e-17 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 83.92 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1312 LQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVW 1388
Cdd:cd00200 167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039748264 1389 DIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWD 1453
Cdd:cd00200 247 DLR-TGECVQTLSGH----------------------TNSVTSLAWSPDGKRLASGSAdGTIRIWD 289
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
54-318 |
1.01e-12 |
|
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: 67.76 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 54 DKAFTFDYVFDIDSQQEQIYTQCiEKLIEGCFEGYN-ATVFAYGQTGAGKTYTMgtgfdvnimeeeQGIISRAVRHLFKS 132
Cdd:cd01363 17 SKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM------------KGVIPYLASVAFNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 133 IDEKKTSAiknglpppefkvnaqflelyneevldlfdttrdidaknkksnirihedstggiyTVGVTTRTVNTEPEMMQC 212
Cdd:cd01363 84 INKGETEG------------------------------------------------------WVYLTEITVTLEDQILQA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 213 LKLGALSRtTASTQMNVQSSRSHAIFTIhvcqtrvcpqtdaenatdnklisesspmnefetltakfhFVDLAGSERlkrt 292
Cdd:cd01363 110 NPILEAFG-NAKTTRNENSSRFGKFIEI---------------------------------------LLDIAGFEI---- 145
|
250 260
....*....|....*....|....*.
gi 1039748264 293 gatgerakegisINCGLLALGNVISA 318
Cdd:cd01363 146 ------------INESLNTLMNVLRA 159
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1523-1639 |
1.06e-11 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 68.78 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1523 ALAIQGDNLFSGSRDNGIKKWDLAQKGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDS 1602
Cdd:COG2319 43 AASPDGARLAAGAGDLTLLLLDAAAGALLATLL-GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTG 121
|
90 100 110
....*....|....*....|....*....|....*....
gi 1039748264 1603 PINAICV--NSTHVFTAADDRTVRIWkahNLQDGQLSDT 1639
Cdd:COG2319 122 AVRSVAFspDGKTLASGSADGTVRLW---DLATGKLLRT 157
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
650-865 |
2.73e-10 |
|
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: 64.40 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKC 729
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 730 EYEKKLHAMNKELQRLQTA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 800
Cdd:COG4942 101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264 801 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSS 865
Cdd:COG4942 181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
673-976 |
1.18e-09 |
|
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: 63.53 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 673 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQTAQKEH 752
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 753 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 831
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 832 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSESPAPdtgSSAASGEADTSRPGTQQKMR-IPVARVQALPTPTTNGT 910
Cdd:TIGR00606 846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR---RQQFEEQLVELSTEVQSLIReIKDAKEQDSPLETFLEK 920
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264 911 RKKYQRKGFTGRVFTSKTARMKWQLLERRVTDIIMQKMTISNM------------EADMNRLLRQREELTKRREKLSK 976
Cdd:TIGR00606 921 DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkddylkqkETELNTVNAQLEECEKHQEKINE 998
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
650-1033 |
1.36e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 726
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 727 VKCEYEKKLHAMNKelqRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 804
Cdd:PRK03918 385 TPEKLEKELEELEK---AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 805 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLrRKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEA 881
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 882 DTSR--------PGTQQKMRIPVARVQALPTPTTNgTRKKYQRKGFT------GRVFTSKTARMKW-------QLLERRV 940
Cdd:PRK03918 540 EIKSlkkeleklEELKKKLAELEKKLDELEEELAE-LLKELEELGFEsveeleERLKELEPFYNEYlelkdaeKELEREE 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 941 TDIIMQKMTISNMEADMNRLLRQREELTKRREKLSKR-----REKIVKESGEGDKSVANIIEEMESLTANIDYINDSIAD 1015
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
410
....*....|....*...
gi 1039748264 1016 CQANIMQMEEAKEEGETL 1033
Cdd:PRK03918 699 LKEELEEREKAKKELEKL 716
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
650-1048 |
2.41e-09 |
|
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: 62.43 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVKC 729
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 730 EYEKKlHAMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 806
Cdd:pfam05483 479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 807 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLsSSESPAPDTGSSAASGEA 881
Cdd:pfam05483 558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEEL-HQENKALKKKGSAENKQL 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 882 DTSRPGTqQKMRIPVARVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 961
Cdd:pfam05483 632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 962 RQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYindSIADCQANIM----QMEEAKEEGETLDVTA 1037
Cdd:pfam05483 700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776
|
410
....*....|.
gi 1039748264 1038 VINACTLTEAR 1048
Cdd:pfam05483 777 KENTAILKDKK 787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
655-1041 |
8.82e-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: 57.39 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 655 ADLANITCEIAIKQKLIDELENSQKRLQTlkkqyeeklmmlqhkirdtqlERDQvlqnlgsVESYSEEKAKKVKCEYEKK 734
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRR---------------------EREK-------AERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 735 LHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE--EQEKARLTESRRN--REIAQLKK 810
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGEleAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 811 DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSEspapdtgssaasgeadtsrpgtqQ 890
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEYAELK-----------------------E 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 891 KMRIPVARVQALPTP--TTNGTRKKYQRK--GFTGRVFTSKTARMKWQLLERRVTdiimqkMTISNMEADMNRLLRQREE 966
Cdd:TIGR02169 365 ELEDLRAELEEVDKEfaETRDELKDYREKleKLKREINELKRELDRLQEELQRLS------EELADLNAAIAGIEAKINE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 967 LTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAK-----EEGETLDVTAVINA 1041
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKA 518
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
650-890 |
1.59e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 650 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL---GSVESYSEE--KA 724
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVllGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 725 KKvkceyekkLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 804
Cdd:COG3883 112 ES--------FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 805 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTS 884
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
|
....*.
gi 1039748264 885 RPGTQQ 890
Cdd:COG3883 264 AAGAAA 269
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
652-855 |
4.01e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 652 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAKKVK 728
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 729 CEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-ARLTESRRN----- 802
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEEleeli 868
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264 803 ----REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 855
Cdd:TIGR02168 869 eeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
590-856 |
5.16e-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: 54.68 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 590 DQEKKEEKGVS-------EKENNELDVEENQEVSDHEDeeeeEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITC 662
Cdd:TIGR02168 220 AELRELELALLvlrleelREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 663 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNkel 742
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELEAELEELE--- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 743 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---REIAQLKKDQRK 814
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAELEELEEELEE 451
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1039748264 815 RDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 856
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1313-1348 |
1.13e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 46.57 E-value: 1.13e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1039748264 1313 QCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1348
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
372-846 |
2.32e-06 |
|
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: 52.52 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 372 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 445
Cdd:pfam10174 280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 446 RIKAMQETVDALRARITQLVSEQANQvlaragegNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 515
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTL--------AGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 516 trataRSPYFSASSAFSPTILSSDKETieiidLAKKDleklkrkekkkkkrlqKLEESGREERSVAGKDDNADTDQEKKE 595
Cdd:pfam10174 423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKE----------------RIIERLKEQREREDRERLEELESLKKE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 596 EKG-----------VSEKENNELDVEENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEI 664
Cdd:pfam10174 477 NKDlkekvsalqpeLTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEI 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 665 AIKQKLIdELENSQKRLQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSeekAKKVKCEYEK--KLHAMNKE 741
Cdd:pfam10174 557 NDRIRLL-EQEVARYKEESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLT---LRQMKEQNKKvaNIKHGQQE 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 742 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrd 816
Cdd:pfam10174 630 MKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-- 701
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1039748264 817 hqlRLLEAQKRNQEVVL------------------RRKT--EEVTALRRQ 846
Cdd:pfam10174 702 ---QLEEILEMKQEALLaaisekdaniallelsssKKKKtqEEVMALKRE 748
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
663-1027 |
2.74e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 663 EIAIKQKL-IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQlerdQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKE 741
Cdd:PRK03918 148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREIN-EISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 742 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNR--EIAQLKKDQRKRDHQL 819
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 820 RLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA--GKVTRKLSssespapdtgssaasgeadtsrpgtqqkmripva 897
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErlEELKKKLK---------------------------------- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 898 rvqalptpttnGTRKKYQRkgFTGRVftsktarmkwQLLERrvtdiIMQKMTisnmeadmnrllrQREELTKRREKLSKr 977
Cdd:PRK03918 349 -----------ELEKRLEE--LEERH----------ELYEE-----AKAKKE-------------ELERLKKRLTGLTP- 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1039748264 978 rEKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAK 1027
Cdd:PRK03918 387 -EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1311-1348 |
3.69e-06 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 45.00 E-value: 3.69e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1039748264 1311 PLQCVHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1348
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
722-848 |
3.99e-06 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 47.61 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 722 EKAKKVKCEYEKKLHamnkelqrlqtaqkeharllknqsQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRR 801
Cdd:pfam20492 2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264 802 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 848
Cdd:pfam20492 58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
654-848 |
5.72e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 654 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRD-TQLERDQVLQNLGSvesySEEKAKKVKCEYE 732
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQA----ELSKLEEEVSRIE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 733 KKLHAMNKELQRL----QTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRnreiAQL 808
Cdd:TIGR02169 812 ARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDL 887
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039748264 809 KKDQRKRDHQLRllEAQKRNQEVVLRRKTEEVTALRRQVR 848
Cdd:TIGR02169 888 KKERDELEAQLR--ELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
548-1102 |
5.98e-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: 51.51 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 548 LAKKDLEKLKRKEKKKKKRLQKLEESGREERSVAGKDDNADTDQEKKEEKgvSEKENNELDVEENQEVSDHEDEEEEEED 627
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE--KLAQVLKENKEEEKEKKLQEEELKLLAK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 628 EEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRL--QTLKKQYEEKLMMLQHKIRDTQLE 705
Cdd:pfam02463 294 EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELeiKREAEEEEEEELEKLQEKLEQLEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 706 RDQVLQNLGSVESYSEEKakkvkcEYEKKLHAMNKELQRLQTAQKeharlLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK 785
Cdd:pfam02463 374 ELLAKKKLESERLSSAAK------LKEEELELKSEEEKEAQLLLE-----LARQLEDLLKEEKKEELEILEEEEESIELK 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 786 QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRR-KTEEVTALRRQVRPMSDK----VAGKVTR 860
Cdd:pfam02463 443 QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRqKLEERSQKESKARSGLKVllalIKDGVGG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 861 KLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIpvarVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERRV 940
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT----ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 941 TDIIMQKMTI--SNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANidyINDSIADCQA 1018
Cdd:pfam02463 599 IDPILNLAQLdkATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVK---ASLSELTKEL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1019 NIMQMEEAKEEGETLdvtavinacTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLK 1098
Cdd:pfam02463 676 LEIQELQEKAESELA---------KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
....
gi 1039748264 1099 EKAE 1102
Cdd:pfam02463 747 EEEE 750
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
583-882 |
7.25e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 583 KDDNADTDQEKKEEkgvsEKENNELDVEENQevsdhedeeeeeeDEEEEDDIEGEESSDESDSESDEKANYQADLANITC 662
Cdd:COG1196 233 KLRELEAELEELEA----ELEELEAELEELE-------------AELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 663 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKEL 742
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 743 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLL 822
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 823 EAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEAD 882
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
669-1033 |
1.02e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 669 KLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQR---- 744
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE-QLEEELEQARSELEQleee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 745 -------LQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLM---KQMKEEQEKARLTESRRNREIAQLKKDQRK 814
Cdd:COG4372 82 leelneqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 815 RDHQLRLLEAQKRNQEvvLRRKTEEVTALRRQVRPMSDKVagKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKmri 894
Cdd:COG4372 162 LQEELAALEQELQALS--EAEAEQALDELLKEANRNAEKE--EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 895 pvarVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLRQREELTKRREKL 974
Cdd:COG4372 235 ----LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264 975 SKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAKEEGETL 1033
Cdd:COG4372 311 GALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1590-1627 |
1.15e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 43.84 E-value: 1.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1039748264 1590 TFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRIWK 1627
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
671-825 |
1.20e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 671 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAM--NKELQRLQta 748
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYEALQ-- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264 749 qKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 825
Cdd:COG1579 96 -KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
667-836 |
1.36e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.15 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 667 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsVESYSEEKAKKVKCEYEKKLhAMNKELQRLQ 746
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKA-RQRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 747 TAQKEHARLLKnqsqyEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL---KKDQRKRDHQLRLLE 823
Cdd:pfam13868 242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316
|
170
....*....|...
gi 1039748264 824 AQKRNQEVVLRRK 836
Cdd:pfam13868 317 GERLREEEAERRE 329
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
723-1118 |
2.62e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 723 KAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 798
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 799 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPApdtgSSAAS 878
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE----ELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 879 GEADTSRPGTQQKMripVARVQALPTPTTNgtrkkyQRKGFTGRVftsKTARMKWQLLERRVTDIIMQkmtISNMEADMN 958
Cdd:TIGR02168 325 LEELESKLDELAEE---LAELEEKLEELKE------ELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 959 RLLRQREELTKRREKLSKRREKIvkesgegDKSVANIIEEMESLTANIDY--INDSIADCQANIMQMEEAKEEGETLDVT 1036
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 1037 AVINACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE- 1106
Cdd:TIGR02168 463 LEELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGy 535
|
410
....*....|....*
gi 1039748264 1107 ---LDALLGHALQDL 1118
Cdd:TIGR02168 536 eaaIEAALGGRLQAV 550
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
679-831 |
2.95e-05 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 48.05 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 679 KRLQTLKKQYEEK-------LMMLQHKIR------DTQLERDQVLqnlgsvesysEEKAKKVKCEYEKKlHAMNKELQRL 745
Cdd:pfam02841 155 EERDKLEAKYNQVprkgvkaEEVLQEFLQskeaveEAILQTDQAL----------TAKEKAIEAERAKA-EAAEAEQELL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 746 QTAQKEHARLLKNQ-SQYEKQLKKLQQDvMEMKKtkvrlmKQMKEEQEkaRLTESRRNREIAQLKKDQRKrdhqlrllEA 824
Cdd:pfam02841 224 REKQKEEEQMMEAQeRSYQEHVKQLIEK-MEAER------EQLLAEQE--RMLEHKLQEQEELLKEGFKT--------EA 286
|
....*..
gi 1039748264 825 QKRNQEV 831
Cdd:pfam02841 287 ESLQKEI 293
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
721-866 |
3.06e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 721 EEKAKKVKCEYEKKLHAMNKELQRLQtaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKtKVRLMKQmkEEQEKARLTE-- 798
Cdd:COG2433 394 EPEAEREKEHEERELTEEEEEIRRLE---EQVERLEAEVEELEAELEEKDERIERLER-ELSEARS--EERREIRKDRei 467
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264 799 SRRNREIAQLKKdqrkrdhqlRLLEAQKRNQEvvLRRKTEEVTALRRQVRpMSDKVAGKVTRKLSSSE 866
Cdd:COG2433 468 SRLDREIERLER---------ELEEERERIEE--LKRKLERLKELWKLEH-SGELVPVKVVEKFTKEA 523
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
667-861 |
4.57e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 667 KQKLIDELENSQK-------RLQTLKKQ---YEEKLMMLQHKIR--------DTQLERDQVLQNLGSVESYSEEKAKKVK 728
Cdd:pfam17380 305 KEEKAREVERRRKleeaekaRQAEMDRQaaiYAEQERMAMERERelerirqeERKRELERIRQEEIAMEISRMRELERLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 729 CEYEKKLHAMNKELQ---RLQTAQKEHARLLKNQSQYEKQLKKLQQdvmEMKKTKVRLMKQMKE-EQEKARLTESRRNRE 804
Cdd:pfam17380 385 MERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERArEMERVRLEEQERQQQ 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264 805 IAQLKKDQRKRDHQLRLLEAQKRNQEVV--LRRKTEEVTALRRQVRPMSDKVAGKVTRK 861
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKRAeeQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
686-839 |
4.69e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.61 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 686 KQYEEKLMMLQ-HKIRDTQLERDQVLQNLgsVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQyEK 764
Cdd:pfam13868 9 RELNSKLLAAKcNKERDAQIAEKKRIKAE--EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE-ER 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039748264 765 QLKKlQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEE 839
Cdd:pfam13868 86 EQKR-QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
664-880 |
6.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 664 IAIKQKLIDELEnsqKRLQTLKKQYEEklmmLQhKIRDTQLERDQVLQNLGSVESYSEEKAkkvkcEYEKKLHAMNKELQ 743
Cdd:COG4913 612 LAALEAELAELE---EELAEAEERLEA----LE-AELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 744 RLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKARltesRRNREIAQLKKDQRKRDHQLR 820
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLekeLEQAEEELDELQ----DRLEAAEDLARLELRALLEER 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039748264 821 LLEAQKRNQEVVLRRK-TEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGE 880
Cdd:COG4913 755 FAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1591-1626 |
6.85e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 41.56 E-value: 6.85e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1039748264 1591 FVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRIW 1626
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVW 38
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
663-853 |
8.42e-05 |
|
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: 47.43 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 663 EIAIKQKLIDELEnsqkRLQTLKKQYEEKLMM-----LQHKIRDTQLERDQVLQNLGSVESYSE-EKAKKVKCEYEKKLH 736
Cdd:pfam17380 369 EIAMEISRMRELE----RLQMERQQKNERVRQeleaaRKVKILEEERQRKIQQQKVEMEQIRAEqEEARQREVRRLEEER 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 737 AMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQE----KARLTESRRNREIaqLKKDQ 812
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEleerKQAMIEEERKRKL--LEKEM 522
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039748264 813 RKRdhQLRLLEAQKRNQEVVLRRKTEEVTALRR---QVRPMSDK 853
Cdd:pfam17380 523 EER--QKAIYEEERRREAEEERRKQQEMEERRRiqeQMRKATEE 564
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
666-838 |
9.16e-05 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 45.53 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 666 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSeekakKVKCEYEKKLHAMNKELQRL 745
Cdd:pfam14988 23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFA-----KLKESQEREIQDLEEEKEKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 746 Q-----TAQKEHARLLKNQSQYEKQLKklQQDVMEM---KKTKVRLMKQMKEEQEKARLTESRRN--REIAQLKKDQRKR 815
Cdd:pfam14988 98 RaetaeKDREAHLQFLKEKALLEKQLQ--ELRILELgerATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQL 175
|
170 180
....*....|....*....|...
gi 1039748264 816 DHQLRLLEAQKRNQEvvlRRKTE 838
Cdd:pfam14988 176 IQETQALEAIKSKLE---NRKQR 195
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
693-836 |
1.71e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.70 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 693 MMLQHKIRDTQLERdqvlqnlGSVESYSEEKAKKvKCEYEKKLhaMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQD 772
Cdd:pfam13904 38 LTYARKLEGLKLER-------QPLEAYENWLAAK-QRQRQKEL--QAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQ 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039748264 773 vmemkKTKVRLMKQMKEEQEKARLTESRRNREIAQ-----------LKKDQRKRDHQLRLLEAQKRNQEVVLRRK 836
Cdd:pfam13904 108 -----QTKKREESHKQKAAESASKSLAKPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
663-836 |
1.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 663 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV-LQNLGSVEsyseekakkvkceyekklhamnke 741
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLE------------------------ 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 742 lQRLQTAQKEHARLLKNQSQYEKQLKKL-------QQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRK 814
Cdd:COG4913 345 -REIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
170 180
....*....|....*....|....
gi 1039748264 815 RDHQLRLLEAQKRN--QEVVLRRK 836
Cdd:COG4913 424 LEAEIASLERRKSNipARLLALRD 447
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
312-521 |
1.91e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 312 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 386
Cdd:COG3206 96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 387 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 452
Cdd:COG3206 174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 453 ----------TVDALRARITQLVSEQAnQVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKNLTRATAR 521
Cdd:COG3206 254 dalpellqspVIQQLRAQLAELEAELA-ELSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
696-839 |
2.40e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 696 QHKIRDTQLERDQVLQN-LGSVESYSEEK-------AKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQY----E 763
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039748264 764 KQLKKLQQDVMEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQrKRDHQLRLLEAQKRNQEVVLRRKTEE 839
Cdd:PRK12704 110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
733-853 |
3.07e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 733 KKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNREIAQLKK 810
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1039748264 811 dQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 853
Cdd:COG4717 151 -LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
667-848 |
3.21e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 667 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEEKAKKVKCEYEKKLHAMNKELQRLQ 746
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 747 TAQKEH--ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-----QMKEEqEKARLTESRRNREIAQLKKDQRKRDHQL 819
Cdd:pfam13868 198 DEKAERdeLRAKLYQEEQERKERQKEREEAEKKARQRQELQqareeQIELK-ERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
170 180
....*....|....*....|....*....
gi 1039748264 820 RLLEAQKRNQevvlrRKTEEVTALRRQVR 848
Cdd:pfam13868 277 EQEEAEKRRM-----KRLEHRRELEKQIE 300
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
653-840 |
4.00e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 653 YQADLANITCEIAIKQK----LIDELENSQKRLQTLK---KQYEEKLMMLQHKIRDTQLERDQVLQNLgsvESYSEEKAk 725
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEeledLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKRELDRLQEEL---QRLSEELA- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 726 kvkcEYEKKLHAMNKELQRLQTAQKEHARLLKNQsqyEKQLKKLQQDVmemkktkvrlmkqMKEEQEKARLTEsrrnrEI 805
Cdd:TIGR02169 424 ----DLNAAIAGIEAKINELEEEKEDKALEIKKQ---EWKLEQLAADL-------------SKYEQELYDLKE-----EY 478
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039748264 806 AQLKKDQRKRDHQLRLLEAQKR--NQEVVLRRKTEEV 840
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
654-798 |
4.31e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 654 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQY---------EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 724
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039748264 725 KKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTE 798
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
662-830 |
5.55e-04 |
|
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: 44.28 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 662 CEIAIKQKLidELENSQKRLQTLKKQYEE---KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAK---KVKCEYEKKL 735
Cdd:pfam15742 54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQeksRVADAEEKIL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 736 hamnkELQRlqtaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN------------- 802
Cdd:pfam15742 132 -----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdke 202
|
170 180 190
....*....|....*....|....*....|..
gi 1039748264 803 ----REIAQLKKDQRKRDHQLRLLEAQKRNQE 830
Cdd:pfam15742 203 aqleMTNSQQQLRIQQQEAQLKQLENEKRKSD 234
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
709-846 |
6.10e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.56 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 709 VLQNLGSVESYSEEKAKKVKCEyekKLHAMNKELQRLQTAQKEHARL---LKNQSQYEKqlKKLQQDVME-MKKTKVRLM 784
Cdd:pfam15709 305 VTGNMESEEERSEEDPSKALLE---KREQEKASRDRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMREELE 379
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039748264 785 KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 846
Cdd:pfam15709 380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
668-842 |
6.31e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 668 QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLErdqvLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQT 747
Cdd:pfam05622 310 QQLLEDANRRKNELETQNRLANQRILELQQQVEELQKA----LQEQGSKAEDSSLLKQKLE-EHLEKLHEAQSELQKKKE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 748 AQKEHARllKNQSQYEKQLKKLQqdvmEMKKTKVRLMKQMKEEQ----EKARLT----ESRRNR----EIAQLKKDQRKR 815
Cdd:pfam05622 385 QIEELEP--KQDSNLAQKIDELQ----EALRKKDEDMKAMEERYkkyvEKAKSViktlDPKQNPasppEIQALKNQLLEK 458
|
170 180 190
....*....|....*....|....*....|
gi 1039748264 816 DHQLRLLEAQKrnQEVVLRRKTEE---VTA 842
Cdd:pfam05622 459 DKKIEHLERDF--EKSKLQREQEEkliVTA 486
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
668-810 |
7.44e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 43.33 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 668 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSE----------EKAKKV 727
Cdd:cd16269 123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEailqadqaltEKEKEI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 728 KCEYEKKlHAMNKELQRLQTAQKEHARLLKNQSQ-YEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTESRRNRE 804
Cdd:cd16269 201 EAERAKA-EAAEQERKLLEEQQRELEQKLEDQERsYEEHLRQLKEKMEEERENLLKEQERALESklKEQEALLEEGFKEQ 279
|
....*.
gi 1039748264 805 IAQLKK 810
Cdd:cd16269 280 AELLQE 285
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-614 |
8.13e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 370 LKYANRARNIKNKVMVNQDR-ASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIK 448
Cdd:COG1196 216 RELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEE-----------LRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 449 AMQETVDALRARITQLVSE---------QANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 519
Cdd:COG1196 285 EAQAEEYELLAELARLEQDiarleerrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 520 ARspYFSASSAFSPTILSSDKETIEIIDLAKKDLEKLKRKEKKKKKRLQKLEESGREERSVAGKDDNADTDQEKKEEKGV 599
Cdd:COG1196 365 EA--LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250
....*....|....*
gi 1039748264 600 SEKENNELDVEENQE 614
Cdd:COG1196 443 ALEEAAEEEAELEEE 457
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
707-842 |
8.27e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.59 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 707 DQVLQNLGSVESYSEEKA--KKVKCEYEKKLHAMNKELQR----LQTAQKEHARLLKNQSQYEKqlkklqqDVMEMKKTK 780
Cdd:pfam13851 19 DITRNNLELIKSLKEEIAelKKKEERNEKLMSEIQQENKRltepLQKAQEEVEELRKQLENYEK-------DKQSLKNLK 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039748264 781 VRL------MKQMKEEQE--KARLTESRRNREiaQLKKDQRKrdhqlRLLEAQKR--NQEVVLRRKTEEVTA 842
Cdd:pfam13851 92 ARLkvlekeLKDLKWEHEvlEQRFEKVERERD--ELYDKFEA-----AIQDVQQKtgLKNLLLEKKLQALGE 156
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
661-825 |
8.57e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 42.20 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 661 TCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqHKIRDTQLERDQVLQnlgsveSYSEE------KAKKVKCEY--- 731
Cdd:pfam15619 17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIA------RHNEEvrvlreRLRRLQEKErdl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 732 EKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQlkKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKD 811
Cdd:pfam15619 87 ERKLKEKEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKK 164
|
170
....*....|....
gi 1039748264 812 QRKRDHQLRLLEAQ 825
Cdd:pfam15619 165 HKEAQEEVKILQEE 178
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
663-848 |
8.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 663 EIAIKQKLIDELENSQKRLQTLKKQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYE 732
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 733 KKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkVRLMKQMKEE--QEKARLTES-RRNREIAQLK 809
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREwpAETADLDADlESLPEYLALL 821
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039748264 810 KDQRKRDhqlrLLEAQKRNQEVVLRRKTEEVTALRRQVR 848
Cdd:COG4913 822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
373-1028 |
1.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 373 ANRARNIKNKVMVNQDRASQQINALR-SEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRiKAMQ 451
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 452 ETVDALRARITQLVSEQANQV--LARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNEnLRKNLTRATARSPyfsass 529
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKAD------ 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 530 afsptilSSDKETIEiidlaKKDLEKLKRKEKKKKKRLQKLEESGREERSVAGKDDNADTDQEKKEEKGVSEKENNELDV 609
Cdd:PTZ00121 1333 -------AAKKKAEE-----AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 610 EENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYE 689
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 690 E--KLMMLQHKIRDTQLERDQVLQNLGSVESYSE----EKAKKV----KCEYEKKLHAMNKELQRLQTAQKEHARLLKNQ 759
Cdd:PTZ00121 1481 EakKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkaEEAKKAdeakKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 760 SQYEK-QLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTESRRNREIAQLKK--DQRKRDHQLRLLEAQKRNQEVVLR 834
Cdd:PTZ00121 1561 EEKKKaEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKaeEAKIKAEELKKAEEEKKKVEQLKK 1640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 835 RKTEEVTAlRRQVRPMSDKVAGKvTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVAR-VQALPTPTTNGTRKK 913
Cdd:PTZ00121 1641 KEAEEKKK-AEELKKAEEENKIK-AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKKKA 1718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 914 YQ-RKGFTGRVFTSKTARMKWQLLERRVTDIIMQkmtisnmEADMNRLLRQREELTKRREKLSKRREKIVKE-------- 984
Cdd:PTZ00121 1719 EElKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-------EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeldeedek 1791
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264 985 -SGEGDKSVANIIEEMESL----TANIDYINDS----------IADCQAniMQMEEAKE 1028
Cdd:PTZ00121 1792 rRMEVDKKIKDIFDNFANIieggKEGNLVINDSkemedsaikeVADSKN--MQLEEADA 1848
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
664-847 |
1.24e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 664 IAIKQKLIDELENSQKRL-QTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvESYSEEKAKKVKCEYEKKL---HAMN 739
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLdEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQIEEREQKRQEEYEEKLqerEQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 740 KELQRLQTAQKEharllknqsQYEKQLKK---LQQDVMEMKKTKVRLMKQMKEEQEKarltESRRNREiAQLKKDQRKrd 816
Cdd:pfam13868 105 EIVERIQEEDQA---------EAEEKLEKqrqLREEIDEFNEEQAEWKELEKEEERE----EDERILE-YLKEKAERE-- 168
|
170 180 190
....*....|....*....|....*....|.
gi 1039748264 817 hqlrllEAQKRNQEVVLRRKTEEVTALRRQV 847
Cdd:pfam13868 169 ------EEREAEREEIEEEKEREIARLRAQQ 193
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
659-861 |
1.32e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 659 NITCEIAIKQKLIDELENSQK-RLQTLKKQYEEKL-MMLQHKIRDTQLErDQVLQNLGSVESYSEEKAK--------KVK 728
Cdd:PHA02562 192 HIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVeEAKTIKAEIEELT-DELLNLVMDIEDPSAALNKlntaaakiKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 729 CEYEKKLHAMNKE-------LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEkarltesrR 801
Cdd:PHA02562 271 IEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE--------L 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 802 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRK 861
Cdd:PHA02562 343 KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
663-866 |
1.32e-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: 43.47 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 663 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLErdqvLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKEL 742
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI----IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 743 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL-----------------MKQMKEEQEKARLTESRR--NR 803
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLesekkekeskisdledeLNKDDFELKKENLEKEIDekNK 568
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039748264 804 EIAQLKKDQRKrdhqlrLLEAQKRNQEvVLRRKTEEVTALRRQVRpMSDKVAGKVTRKLSSSE 866
Cdd:TIGR04523 569 EIEELKQTQKS------LKKKQEEKQE-LIDQKEKEKKDLIKEIE-EKEKKISSLEKELEKAK 623
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
680-848 |
1.33e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 680 RLQTLKKQYEEkLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQ 759
Cdd:COG4913 226 AADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 760 SQYEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTesrrnREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKT 837
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLE-----REIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170
....*....|.
gi 1039748264 838 EEVTALRRQVR 848
Cdd:COG4913 380 EEFAALRAEAA 390
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
678-842 |
1.39e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.40 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 678 QKRLQTLKKQYEEKLmmlqhkirDTQLERDQvlqnlgsvESYSEE-KAKKVKCEYEKKLHAMNKELQRLQ-TAQKEHARL 755
Cdd:pfam15709 360 QRRLQQEQLERAEKM--------REELELEQ--------QRRFEEiRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 756 lkNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQlrlLEAQKRNQEVVLRR 835
Cdd:pfam15709 424 --QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ---EAEEKARLEAEERR 498
|
....*..
gi 1039748264 836 KTEEVTA 842
Cdd:pfam15709 499 QKEEEAA 505
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
745-871 |
1.42e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 745 LQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKqmkeEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEA 824
Cdd:pfam07888 310 QQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1039748264 825 QKrnQEV-----VLRRKTEEVTALRRQVRPMSDKvaGKVTRKLSSSESPAPD 871
Cdd:pfam07888 386 EK--QELleyirQLEQRLETVADAKWSEAALTST--ERPDSPLSDSEDENPE 433
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
666-891 |
1.48e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 43.13 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 666 IKQKLIDELENSQKRLQTLKKQYEEKLM--MLQHKIRDtqlERDQVLQNLGSVESYSE-EKAKKVKCEYEKKLHAMNKEL 742
Cdd:pfam04747 12 IRQQLTNRRKNLGRVAKSQRNQFRQWLLtaVLPNSIND---QRKEAFASLELTEQPQQvEKVKKSEKKKAQKQIAKDHEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 743 QRLQTAQKEHArllKNQSQYEKQLKKlqqdvmemKKTKVRLMKQMKEEQEKarltesrrnreiaqLKKDQRKRDHQLRLL 822
Cdd:pfam04747 89 EQKVNAKKAAE---KEARRAEAEAKK--------RAAQEEEHKQWKAEQER--------------IQKEQEKKEADLKKL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039748264 823 EAQKRNQEVVLRRKTEEVTALRRQVRPM---SDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQK 891
Cdd:pfam04747 144 QAEKKKEKAVKAEKAEKAEKTKKASTPApveEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKK 215
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
672-846 |
1.55e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 672 DELENSQKRLQTLKKQyeeklmmlqHKIRDTQLERDQVLQNLGSVES-YSEEKAKKVkcEYEKKLHAMNKELQRLQTAQK 750
Cdd:COG3206 189 KELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESqLAEARAELA--EAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 751 EH------ARLLKNQSQYEKQLKKLQQ-------DVMEMKKTKVRLMKQMKEEQEKArLTESRRNREIAQLKKD---QRK 814
Cdd:COG3206 258 ELlqspviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRI-LASLEAELEALQAREAslqAQL 336
|
170 180 190
....*....|....*....|....*....|..
gi 1039748264 815 RDHQLRLLEAQKRNQEvvLRRKTEEVTALRRQ 846
Cdd:COG3206 337 AQLEARLAELPELEAE--LRRLEREVEVAREL 366
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
720-827 |
1.55e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 41.21 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 720 SEEKAK------KVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKlqqdvmeMKKTKVRLMKQMKEEQEK 793
Cdd:pfam11600 10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEK-------ELKEKERREKKEKDEKEK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039748264 794 A---RLTESRRNREIAQLK---KDQRKRDHQLRLLEAQKR 827
Cdd:pfam11600 83 AeklRLKEEKRKEKQEALEaklEEKRKKEEEKRLKEEEKR 122
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
734-848 |
1.58e-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: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 734 KLHAMNKELQRLQTAQKEH----ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-----ARLTESRRNR- 803
Cdd:COG1579 11 DLQELDSELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeEQLGNVRNNKe 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1039748264 804 ------EIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 848
Cdd:COG1579 91 yealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1457-1498 |
1.64e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 1.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1039748264 1457 FQSTGKLTGHLGPVMCLTvdqISNGQDLIITGSKDHYIKMFD 1498
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLA---FSPDGKLLASGSDDGTVKVWD 39
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
681-847 |
1.80e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.57 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 681 LQTLKKQYEEKLmmlQHKIRDTqleRDQVLQNLGSVESYSEEKAKKVKCE-----YEK-KLHAMNK-ELQRLQTAQKEha 753
Cdd:pfam15665 16 IQALKEAHEEEI---QQILAET---REKILQYKSKIGEELDLKRRIQTLEesleqHERmKRQALTEfEQYKRRVEERE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 754 rlLKNQSQYEKQLKKLQQDVMEMKKT---KVR----LMKQMKEEQEKArLTESRR--NREIAQLKKDQRKR-----DHQL 819
Cdd:pfam15665 88 --LKAEAEHRQRVVELSREVEEAKRAfeeKLEsfeqLQAQFEQEKRKA-LEELRAkhRQEIQELLTTQRAQsasslAEQE 164
|
170 180
....*....|....*....|....*....
gi 1039748264 820 RLLEAQKrnQEVV-LRRKTEEVTALRRQV 847
Cdd:pfam15665 165 KLEELHK--AELEsLRKEVEDLRKEKKKL 191
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
671-910 |
1.86e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 671 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsveSYSEEKAKKVkceyEKKLHAMNKELQRLQTAQK 750
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----EALQAEIDKL----QAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 751 EHARLLKNQSQYEKQLKKL---------------QQDVMEMKKTKVRLMKQMKEEQEKArltESRRNREIAQLKKDQRKR 815
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 816 DHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIP 895
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250
....*....|....*
gi 1039748264 896 VARVQALPTPTTNGT 910
Cdd:COG3883 247 AGAGAAGAAGAAAGS 261
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
667-826 |
2.17e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.40 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 667 KQKLidELENSQKRLQtLKKQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVESYSE----EKAKKVKC 729
Cdd:pfam03528 24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSEntkqEAIDEVKS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 730 EYEKK---LHAMNKELQRLQTAQKeHARLLKNQSQYEKQLKKLQQDVMEMKKtkvRL------------MKQMKEEQEKA 794
Cdd:pfam03528 101 QWQEEvasLQAIMKETVREYEVQF-HRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAEKL 176
|
170 180 190
....*....|....*....|....*....|..
gi 1039748264 795 RLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 826
Cdd:pfam03528 177 RSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
672-805 |
2.18e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 672 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVlqnlgsvesysEEKAKKVKCEYEKKLHAMNKELQ-RLQTAQK 750
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264 751 EHARLLKNQSQYEKQLKKLQ--QDVMEMKKtkvrLMKQMKEEQEKARLTESRRNREI 805
Cdd:PRK00409 585 EADEIIKELRQLQKGGYASVkaHELIEARK----RLNKANEKKEKKKKKQKEKQEEL 637
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
650-780 |
2.30e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 650 KANYQADLANItceiaikQKLIDELENSQKRLQT-------LKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEE 722
Cdd:PRK00409 508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEA-------EK 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039748264 723 KAKKV----KCEYEKKLHAMNKELQRLQTAQKEHaRLLKNQSQYEKQLKKLQQDVMEMKKTK 780
Cdd:PRK00409 574 EAQQAikeaKKEADEIIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
666-805 |
2.40e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 666 IKQKLiDELENSQKRLQtlkkQYEEklmMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKCEYEKKLHAMNKELQRL 745
Cdd:PRK12704 77 LRERR-NELQKLEKRLL----QKEE---NLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIEEQLQELERI 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 746 QTAQKEHARllknqsqyEKQLKKLQqdvmemKKTKVRLMKQMKEEQEKARLTESRRNREI 805
Cdd:PRK12704 148 SGLTAEEAK--------EILLEKVE------EEARHEAAVLIKEIEEEAKEEADKKAKEI 193
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
672-815 |
2.49e-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: 42.42 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 672 DELENsQKRLQTLKKQYEEKLmmlQHKIRDTQLERDQVL---QNLGSVESYSEEKAKKVkCEYEKKLHAMNKELQRLQTA 748
Cdd:pfam17380 454 EEQER-QQQVERLRQQEEERK---RKKLELEKEKRDRKRaeeQRRKILEKELEERKQAM-IEEERKRKLLEKEMEERQKA 528
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264 749 QKEHARLLKNQSQYEKQLKklqqdvMEMKKtkvRLMKQM-KEEQEKARLTESRRNREIA-QLKKDQRKR 815
Cdd:pfam17380 529 IYEEERRREAEEERRKQQE------MEERR---RIQEQMrKATEERSRLEAMEREREMMrQIVESEKAR 588
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
668-799 |
2.98e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 668 QKLIDELENSQKRLQTLKKQYEEklmmlQH-KIRDTQLERDQVLQNLgsvesysEEKAKKVKCEYEKKLHAMNKELQRLQ 746
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1039748264 747 TAQKEHARLLKNQSQYEKQLKKLQQDVmemkKTKVRLMKQMKEEQEKARLTES 799
Cdd:COG3206 334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
|
|
| mS26_PET12 |
cd23703 |
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ... |
711-821 |
3.15e-03 |
|
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.
Pssm-ID: 467916 [Multi-domain] Cd Length: 179 Bit Score: 40.23 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 711 QNLgsVESYSEEKAKKVKCEyekklhamNKELQRLQTAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkq 786
Cdd:cd23703 61 QNL--REGLRELEERKLKTE--------ELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT--- 124
|
90 100 110
....*....|....*....|....*....|....*
gi 1039748264 787 mkEEQEKARLTESRRNREIAQLKKDQRKRDHQLRL 821
Cdd:cd23703 125 --DPEREERAAKRRANREAKELAKKEARADALHEL 157
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
357-1110 |
3.26e-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: 42.41 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 357 SPSDRDFMETL-NTLKYANRARNIKNKVMVNqdrASQQINALRSEITRLQMELMEYKT---------GKRIIDEEGVES- 425
Cdd:pfam15921 137 SQSQEDLRNQLqNTVHELEAAKCLKEDMLED---SNTQIEQLRKMMLSHEGVLQEIRSilvdfeeasGKKIYEHDSMSTm 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 426 --------INDMFHEnamLQTENNNLRVRIKAMQETVDALRaritqlvSEQANQVLARAGEGNEEISNMIHSYIKEIEDL 497
Cdd:pfam15921 214 hfrslgsaISKILRE---LDTEISYLKGRIFPVEDQLEALK-------SESQNKIELLLQQHQDRIEQLISEHEVEITGL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 498 RAKlleseavnenlrknltratarspyfsASSAFSPTilSSDKETIEIIdlakkdleklkrkekkkkkrlqklEESGREE 577
Cdd:pfam15921 284 TEK--------------------------ASSARSQA--NSIQSQLEII------------------------QEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 578 RSVAGKddnadtdQEKKEEKGVSEkenneLDVEENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADL 657
Cdd:pfam15921 312 NSMYMR-------QLSDLESTVSQ-----LRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 658 anitceiaikQKLIDELENSQKRLqTLKKQYEEKL--------MMLQHKIRDTQlERDQVLQNLGSVesyseEKAKKVKC 729
Cdd:pfam15921 380 ----------QKLLADLHKREKEL-SLEKEQNKRLwdrdtgnsITIDHLRRELD-DRNMEVQRLEAL-----LKAMKSEC 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 730 --EYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrRNREIAQ 807
Cdd:pfam15921 443 qgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA-TNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 808 LkkdqRKRdHQLRLLEAQK-RNQEVVLRRKTEEVTALRRQVRPmSDKVAGKVTRKLSSSESPAPDTGSSAASgeadtsrp 886
Cdd:pfam15921 522 L----RSR-VDLKLQELQHlKNEGDHLRNVQTECEALKLQMAE-KDKVIEILRQQIENMTQLVGQHGRTAGA-------- 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 887 gtqqkMRIPVARVQAlptpTTNGTRKKYQRKgftgRVFTSKTaRMKWQLLERRVTDIIMQKMTISNMEADMNRLLRQree 966
Cdd:pfam15921 588 -----MQVEKAQLEK----EINDRRLELQEF----KILKDKK-DAKIRELEARVSDLELEKVKLVNAGSERLRAVKD--- 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 967 ltkrrekLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANI-MQMEEAKEEGETldvtaviNACTLT 1045
Cdd:pfam15921 651 -------IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkMQLKSAQSELEQ-------TRNTLK 716
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039748264 1046 EARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTE--ITSATQNQllfHMLK-EKAELNPELDAL 1110
Cdd:pfam15921 717 SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeaMTNANKEK---HFLKeEKNKLSQELSTV 781
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1457-1498 |
3.49e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 36.91 E-value: 3.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1039748264 1457 FQSTGKLTGHLGPVMCLtvdQISNGQDLIITGSKDHYIKMFD 1498
Cdd:smart00320 2 GELLKTLKGHTGPVTSV---AFSPDGKYLASGSDDGTIKLWD 40
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
669-836 |
3.56e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 669 KLIDELENSQKRLQTLKKQYEEKL------MMLQHKIRDTQL----ERDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAM 738
Cdd:PRK11637 103 KQIDELNASIAKLEQQQAAQERLLaaqldaAFRQGEHTGLQLilsgEESQRGERILAYFGYLNQARQETIAELKQTREEL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 739 NKELQRLQTAQKEHARLLKNQSQyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNR-----EIAQLKKDQR 813
Cdd:PRK11637 183 AAQKAELEEKQSQQKTLLYEQQA---QQQKLEQARNERKKTLTGLESSLQKDQ--QQLSELRANEsrlrdSIARAEREAK 257
|
170 180
....*....|....*....|....*
gi 1039748264 814 KR-DHQLRllEAQK-RNQEVVLRRK 836
Cdd:PRK11637 258 ARaEREAR--EAARvRDKQKQAKRK 280
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
722-848 |
4.19e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 41.12 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 722 EKAKKVKCEYEKKLHAMNK-ELQRLQ--TAQKEHARLLKNQSQYEKQLKKLQQDVMEmkktkvrlmkqmkEEQEKARLTE 798
Cdd:pfam12037 29 ERAAKAARELESSPHAKKAlELMKKQeqTRQAELQAKIKEYEAAQEQLKIERQRVEY-------------EERRKTLQEE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1039748264 799 SRRNREIAQlKKDQ--RKRdHQLRLLEAQKRNQEVVlrRKTEEVTALRRQVR 848
Cdd:pfam12037 96 TKQKQQRAQ-YQDElaRKR-YQDQLEAQRRRNEELL--RKQEESVAKQEAMR 143
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
668-984 |
4.21e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 668 QKLIDEL---ENSQKRL----QTLKKQYEEKLmmlqhKIRDTQLE--RDQVLQNLGSVESYSEE--KAKKVKCEYEKKLH 736
Cdd:pfam01576 702 EELEDELqatEDAKLRLevnmQALKAQFERDL-----QARDEQGEekRRQLVKQVRELEAELEDerKQRAQAVAAKKKLE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 737 AMNKELQ-RLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrrnrEIAQLKKD---- 811
Cdd:pfam01576 777 LDLKELEaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA----ELLQLQEDlaas 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 812 --QRKRDHQLR---------------LLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVagkvtRKLSSSEspapDTGS 874
Cdd:pfam01576 853 erARRQAQQERdeladeiasgasgksALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL-----RKSTLQV----EQLT 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 875 SAASGEADTSrpgtqQKmripvarvqalptptTNGTRKKYQRKgftgrvftSKTARMKWQLLERRVTDiiMQKMTISNME 954
Cdd:pfam01576 924 TELAAERSTS-----QK---------------SESARQQLERQ--------NKELKAKLQEMEGTVKS--KFKSSIAALE 973
|
330 340 350
....*....|....*....|....*....|...
gi 1039748264 955 ADMNRLLRQREELTKRRE---KLSKRREKIVKE 984
Cdd:pfam01576 974 AKIAQLEEQLEQESRERQaanKLVRRTEKKLKE 1006
|
|
| Cep57_CLD |
pfam14073 |
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ... |
695-823 |
5.32e-03 |
|
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.
Pssm-ID: 464080 [Multi-domain] Cd Length: 178 Bit Score: 39.53 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 695 LQHKIRDTQLERDQ-----------------VLQNLGSVESYSEEKAKKVKCEYEKKLHA-------MNKELQR----LQ 746
Cdd:pfam14073 9 LQEKIRRLELERKQaednlkqlsretshykeVLQKENDARDPSRGEVSKQNQELISQLAAaesrcslLEKQLEYmrkmVE 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039748264 747 TAQKEHARLLKNQSQYEKQlkkLQQDVMEMKKtkvRLMKQMKEEQEKARLTESRRNRE--IAQLKKDQRKRDHQLRLLE 823
Cdd:pfam14073 89 NAEKERTAVLEKQASLERE---RSQDSSELQA---QLEKLEKLEQEYLRLTRTQSLAEtkIKELEEKLQEEEHQRKLVQ 161
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
448-1081 |
5.40e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 448 KAMQETVDALRARITQLVSEQANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARspYFSA 527
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE--EYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 528 SSAFSPTILSSDKETIEIIDLAKKdleklkrkekkkkkrlqkLEESGREERSVAGKDDNADTD-QEKKEEKGVSEKENNE 606
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEER------------------LEELEEELAELEEELEELEEElEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 607 LDVEENQEVSDHEDEEEEEEdeeeeddiegeessdesDSESDEKANYQADLANITcEIAIKQKLIDELENSQKRLQTLKK 686
Cdd:COG1196 356 AEAELAEAEEALLEAEAELA-----------------EAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 687 QYEEKLMMLQHKIRDTQLERDQVLQNLgsvesyseekakkvkceyEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQL 766
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEAL------------------EEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 767 KKLQQDVMEmKKTKVRLMKQMKEEQE-----KARLTESRRNREIAQLKKDQRKRDHQLRLLEAQkRNQEVVLRRKTEEVT 841
Cdd:COG1196 480 AELLEELAE-AAARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 842 ALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVARvqalptpttngtrkkYQRKGFTG 921
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR---------------YYVLGDTL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 922 RVFTSKTARMKWQLLERRVTD----IIMQKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIE 997
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAgrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 998 EMESLTANIDYINDSIADCQANIMQMEEAKEEGETLDvtavinacTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEG 1077
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLE--------ELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....
gi 1039748264 1078 RLKQ 1081
Cdd:COG1196 775 EIEA 778
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
748-876 |
5.42e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 39.67 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 748 AQKEHARLLKNQSQYEKQLKKLQQdvmemKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK---------KDQRKRDHQ 818
Cdd:pfam11600 11 EEKEKQRLEKDKERLRRQLKLEAE-----KEEKERLKEEAKAEKERAKEEARRKKEEEKELKekerrekkeKDEKEKAEK 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039748264 819 LRLLEAQKRNQEVVL------RRKTEEVTALRRQVRPMSDKVAGkVTRKLSSSESP-APDTGSSA 876
Cdd:pfam11600 86 LRLKEEKRKEKQEALeakleeKRKKEEEKRLKEEEKRIKAEKAE-ITRFLQKPKTQqAPKTLAGS 149
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
672-807 |
6.17e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 38.42 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 672 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQlerdQVLQNLGSVESYSEEKAkkvkceYEKKLHAMNKELQRLQtaqKE 751
Cdd:pfam02050 1 DEAARELAEAQRELQQAEEKLEELQQYRAEYQ----QQLSGAGQGISAAELRN------YQAFISQLDEAIAQQQ---QE 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039748264 752 HARLLKNQSQYEKQLKKLQQDVMEMKKTKVRlmkQMKEEQEKARLTESRRNREIAQ 807
Cdd:pfam02050 68 LAQAEAQVEKAREEWQEARQERKSLEKLRER---EKKEERKEQNRREQKQLDELAA 120
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
680-809 |
6.41e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 38.84 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 680 RLQTLKKQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYE-KKLHAMNKELQRLQTAQKEHARLL- 756
Cdd:TIGR02473 6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1039748264 757 KNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 809
Cdd:TIGR02473 86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
725-827 |
7.55e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 39.75 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 725 KKVKCEYEKKLHAMNKelQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrRNRE 804
Cdd:pfam14988 10 AKKTEEKQKKIEKLWN--QYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKES-QERE 86
|
90 100
....*....|....*....|....*
gi 1039748264 805 IAQLKKDQRK--RDHQLRLLEAQKR 827
Cdd:pfam14988 87 IQDLEEEKEKvrAETAEKDREAHLQ 111
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
690-913 |
7.79e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 690 EKLMMLQHKIRDTQLERDQvLQNLGSVESYSEEKAK---KVKCEYEKKLHAMNKElQRLQTAQKEHARLLKNQSQYEKQL 766
Cdd:PTZ00108 1102 EKVEKLNAELEKKEKELEK-LKNTTPKDMWLEDLDKfeeALEEQEEVEEKEIAKE-QRLKSKTKGKASKLRKPKLKKKEK 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 767 KKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 846
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDE 1259
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748264 847 VRPMSDKVAGKVTRKLSSSE---------SPAPDTGSSAASGEADTSRPGTQQKMR-IPVARVQALPTPTTNGTRKK 913
Cdd:PTZ00108 1260 FSSDDLSKEGKPKNAPKRVSavqysppppSKRPDGESNGGSKPSSPTKKKVKKRLEgSLAALKKKKKSEKKTARKKK 1336
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
671-853 |
8.67e-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: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 671 IDELENSQKRLQTLKKQYEEKLMMLQHKIrdtqLERDQVLQNlgsvesyseEKAKKVKCEYekklhamNKELQRLQTAQK 750
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDEL----NKDDFELKK---------ENLEKEIDEK-------NKEIEELKQTQK 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 751 EharLLKNQSQYEKQLKKLQQDVMEMKKtkvrlmkqmkeEQEKARLTESRRNREIAQLKKDQRKrdhqlrlLEAQKRNQE 830
Cdd:TIGR04523 579 S---LKKKQEEKQELIDQKEKEKKDLIK-----------EIEEKEKKISSLEKELEKAKKENEK-------LSSIIKNIK 637
|
170 180
....*....|....*....|...
gi 1039748264 831 VVLRRKTEEVTALRRQVRPMSDK 853
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNK 660
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
380-848 |
8.74e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 380 KNKVMVNQDRASQQINALRSEITRLqmELMEYKTGKRIIDEEGVESINDMFHENAMLQTEnnnlrvrIKAMQETVDALRA 459
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKEL--EEKEERLEELKKKLKELEKRLEELEERHELYEE-------AKAKKEELERLKK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 460 RITQLVSEQANQVLARAGEGNEEISnmihsyiKEIEDLRAKLLESEAVNENLRKN---LTRATARSPYFSAS-------- 528
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIE-------EEISKITARIGELKKEIKELKKAieeLKKAKGKCPVCGRElteehrke 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 529 --SAFSPTILSSDKETIEIIDLAKKdleklkrkekkKKKRLQKLEESGREERSVAGKDDNADTDQEKKEEKGVSEKENNE 606
Cdd:PRK03918 453 llEEYTAELKRIEKELKEIEEKERK-----------LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 607 LDVEENQEVSDhedeeeeeedeeeeddiegeessdesdsesdekanyqaDLANITCEIAIKQKLIDELENSQKRLQTLKK 686
Cdd:PRK03918 522 KKAEEYEKLKE--------------------------------------KLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 687 QY---EEKLMMLQHKIRDTQLER-DQVLQNLGSVESYSEE--KAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQS 760
Cdd:PRK03918 564 KLdelEEELAELLKELEELGFESvEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748264 761 QYEKQLKKLQQ--DVMEMKKTKVRLMKQMKE-EQEKARLTESRRNREiaQLKKDQRKRDHQLRLLEAQKRNQEvVLRRKT 837
Cdd:PRK03918 644 ELRKELEELEKkySEEEYEELREEYLELSRElAGLRAELEELEKRRE--EIKKTLEKLKEELEEREKAKKELE-KLEKAL 720
|
490
....*....|.
gi 1039748264 838 EEVTALRRQVR 848
Cdd:PRK03918 721 ERVEELREKVK 731
|
|
| |
