|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
8-372 |
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: 625.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 88 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 168 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 247
Cdd:cd01372 151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 248 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372 228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 291167760 328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372 297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
15-371 |
4.34e-140 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 435.08 E-value: 4.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 88 GQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKHIaiknglpaPDFKVNAQFLELYNEEVLDLFDTTrdid 167
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 168 aKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIdadn 247
Cdd:pfam00225 143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 248 atdnkiisesaqmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 326
Cdd:pfam00225 218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 291167760 327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225 282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
9-378 |
5.49e-138 |
|
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: 429.68 E-value: 5.49e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYN 81
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 82 ATVFAYGQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDLFD 161
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 162 ttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcP 241
Cdd:smart00129 147 --------PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITV------E 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 242 QIDADNATDnkiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 321
Cdd:smart00129 213 QKIKNSSSG-------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760 322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:smart00129 279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
9-369 |
5.05e-121 |
|
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: 383.14 E-value: 5.05e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 9 SVRVAVRIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:cd00106 1 NVRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 83 TVFAYGQTGAGKTYTMGTGFDvniveEELGIISRAVKHLFKSIEEKKhiaikngLPAPDFKVNAQFLELYNEEVLDLFDt 162
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRK-------ETKSSFSVSASYLEIYNEKIYDLLS- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 163 trdidaKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpq 242
Cdd:cd00106 147 ------PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV-------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 243 idadnatDNKIISESAQMnefeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVP 322
Cdd:cd00106 213 -------KQRNREKSGES----VTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN--KHIP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 291167760 323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd00106 280 YRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
9-371 |
5.78e-104 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 335.97 E-value: 5.78e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGY 80
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 81 NATVFAYGQTGAGKTYTMGtGFDVNivEEELGIISRAVKHLFKSIEEKKHIAiknglpapDFKVNAQFLELYNEEVldlf 160
Cdd:cd01371 82 NGTIFAYGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHIARSQNNQ--------QFLVRVSYLEIYNEEI---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 161 dttRDIDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV-Cqtrv 239
Cdd:cd01371 147 ---RDLLGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeC---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 240 cpqidadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskRAT 319
Cdd:cd01371 220 ---------------SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KST 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 291167760 320 HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01371 283 HIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
9-371 |
2.46e-102 |
|
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: 331.62 E-value: 2.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFDIDSQQEQIYI 66
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 67 QCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVN 145
Cdd:cd01370 81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLKD--------EKEFEVS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 146 AQFLELYNEEVLDLFDTTrdidakSKKSNIRihEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSR 225
Cdd:cd01370 146 MSYLEIYNETIRDLLNPS------SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 226 SHAIFTIHVCQTrvcpqidadnatdnkiiSESAQMNEfETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALG 305
Cdd:cd01370 218 SHAVLQITVRQQ-----------------DKTASINQ-QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALG 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760 306 NVISALGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01370 280 NCINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
10-373 |
5.06e-102 |
|
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: 330.33 E-value: 5.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 10 VRVAVRIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFDIDSQQEQIYIQcIEKLIEGCFEGYNATVF 85
Cdd:cd01366 4 IRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 86 AYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIEEKKHIAIKnglpapdFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01366 83 AYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIRDLLAPGN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 165 didAKSKKSNIRiHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHvcqtrvcpqid 244
Cdd:cd01366 149 ---APQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILH----------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 245 adnatdnkIISESAQMNEfeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKratHVPYR 324
Cdd:cd01366 214 --------ISGRNLQTGE--ISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS---HIPYR 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 291167760 325 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 373
Cdd:cd01366 281 NSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
8-378 |
4.17e-97 |
|
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: 317.37 E-value: 4.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 8 SSVRVAVRIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVFD-IDSQ------QEQIYiQC 68
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYWsHDSEdpnyasQEQVY-ED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 69 I-EKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDvniveEELGIISRAVKHLFKSIEEKKHIAIKnglpapdFKVNAQ 147
Cdd:cd01365 80 LgEELLQHAFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 148 FLELYNEEVLDLFDTtrdiDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSH 227
Cdd:cd01365 147 YMEIYNEKVRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 228 AIFTIhvcqtrVCPQIDADNATDNKiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNV 307
Cdd:cd01365 223 AVFTI------VLTQKRHDAETNLT-----------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKV 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760 308 ISALGD-----KSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:cd01365 286 ISALADmssgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
7-371 |
6.14e-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: 6.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATV 84
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 85 FAYGQTGAGKTYTMgtgFDVNIVEEELGIISRAVKHLFKSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01369 81 FAYGQTSSGKTYTM---EGKLGDPESMGIIPRIVQDIFETIYSMDENL--------EFHVKVSYFEIYMEKIRDLLDVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 165 DidakskksNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQtrvcpqid 244
Cdd:cd01369 150 T--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 245 aDNATDNKIisesaqmnefetLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYR 324
Cdd:cd01369 214 -ENVETEKK------------KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYR 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 291167760 325 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01369 279 DSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
7-380 |
1.47e-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: 306.94 E-value: 1.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFE 78
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 79 GYNATVFAYGQTGAGKTYTM----GTGFDVNIVEEEL-GIISRAVKHLFKSIEEKKHiaiknglpapDFKVNAQFLELYN 153
Cdd:cd01364 81 GYNCTIFAYGQTGTGKTYTMegdrSPNEEYTWELDPLaGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIYN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 154 EEVLDLFDttrdiDAKSKKSNIRIHEDS--TGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFT 231
Cdd:cd01364 151 EELFDLLS-----PSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 232 IHVcqtrvcpqidadnatdnkIISESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL 311
Cdd:cd01364 226 ITI------------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291167760 312 GDKSKratHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01364 288 VERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
44-511 |
1.19e-90 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 306.67 E-value: 1.19e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 44 GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLF 122
Cdd:COG5059 53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 123 KSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMM 202
Cdd:COG5059 126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 203 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqidadnatdnkiisesaQMNEFETLTAKFHFVDLAGSERLK 282
Cdd:COG5059 190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK---------------------NKVSGTSETSKLSLVDLAGSERAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 283 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059 249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 363 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQtennNLRVRIKA 441
Cdd:COG5059 328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQ----SLKKETET 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 442 MQETVDALRSRITQLVSDQANHVLARaGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 511
Cdd:COG5059 399 LKSRIDLIMKSIISGTFERKKLLKEE-GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
10-380 |
2.00e-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: 297.88 E-value: 2.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 10 VRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYG 88
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 89 QTGAGKTYTM--GTGFDVNIVEEELGIISRAVKHLFKSI--EEKKHIAIKNglpapdFKVNAQFLELYNEEVLDLFDTTr 164
Cdd:cd01373 83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIqrEKEKAGEGKS------FLCKCSFLEIYNEQIYDLLDPA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 165 didakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqid 244
Cdd:cd01373 156 -------SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 245 adnatdnkIISESAQMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-RATHVP 322
Cdd:cd01373 217 --------TIESWEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVC 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 291167760 323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01373 289 YRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
9-371 |
4.53e-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: 4.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 9 SVRVAVRIRPQLAKEKIEGCHICTSVTPG----EPQVFlgkdKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATV 84
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEIDNDtiylVEPPS----TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 85 FAYGQTGAGKTYTMGTGfdvnivEEELGIISRAVKHLFKSIEEKkhiaiknglPAPDFKVNAQFLELYNEEVLDLFDTTr 164
Cdd:cd01374 77 FAYGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDT---------PDREFLLRVSYLEIYNEKINDLLSPT- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 165 didakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqid 244
Cdd:cd01374 141 -------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRI------------ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 245 adnatdnkIISESAQMNEFE--TLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDkSKRATHVP 322
Cdd:cd01374 202 --------TIESSERGELEEgtVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIP 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 291167760 323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01374 273 YRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
10-369 |
3.25e-73 |
|
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: 247.42 E-value: 3.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 10 VRVAVRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNAT 83
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 84 VFAYGQTGAGKTYTMGTGFdvniveEELGIISRAVKHLFKSIEEKkhiaiknglpAPDFKVNAQFLELYNEEVLDLFDtt 163
Cdd:cd01376 81 VFAYGSTGAGKTFTMLGSP------EQPGLMPLTVMDLLQMTRKE----------AWALSFTMSYLEIYQEKILDLLE-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 164 rdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqi 243
Cdd:cd01376 143 ------PASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 244 dadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKRATHVPY 323
Cdd:cd01376 208 -----------DQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPY 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 291167760 324 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd01376 274 RDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
10-367 |
1.66e-70 |
|
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: 239.89 E-value: 1.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 10 VRVAVRIRPQLAKEKIEG-CHICTSVTPGEPQVFLGKDK----------AFTFDYVFDIDSQQEQIYIQCIEKLIEGCFE 78
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKeIDVVSVPSKLTLIVHEPKLKvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 79 GYNATVFAYGQTGAGKTYTMGTGFDVNivEEELGIISRAVKHLFksiEEKKHIAIKNGLpapdfKVNAQFLELYNEEVLD 158
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGGDFSGQ--EESKGIYALAARDVF---RLLNKLPYKDNL-----GVTVSFFEIYGGKVFD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 159 LFdttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFtihvcqtr 238
Cdd:cd01367 152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAIL-------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 239 vcpQIDADNATDNKiisesaqmnefetLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDKSkr 317
Cdd:cd01367 215 ---QIILRDRGTNK-------------LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-- 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 291167760 318 aTHVPYRDSKLTRLLQDSL-GGNSQTIMIACVSPSDRDFMETLNTLKYANR 367
Cdd:cd01367 277 -AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
46-369 |
5.19e-67 |
|
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: 230.16 E-value: 5.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 46 DKAFTFDYVFDiDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNIVEEelGIISRAVKHLFKSI 125
Cdd:cd01375 47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENYKHR--GIIPRALQQVFRMI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 126 EEKkhiaiknglPAPDFKVNAQFLELYNEEVLDLFDTTRDIDAKSKKsnIRIHEDSTGGIYTVGVTTRTVNTESEMMQCL 205
Cdd:cd01375 123 EER---------PTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 206 KLGALSRTTASTQMNVQSSRSHAIFTIHVCqtrvcpqidadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTG 285
Cdd:cd01375 192 FLGETNRIIASHTMNKNSSRSHCIFTIHLE-------------------AHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 286 ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01375 253 VEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330
|
....
gi 291167760 366 NRAR 369
Cdd:cd01375 331 SRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
10-365 |
4.17e-65 |
|
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: 224.97 E-value: 4.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 10 VRVAVRIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFDIDSQQEQIYIQCIEKLIE 74
Cdd:cd01368 3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 75 GCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIeekkhiaiknglpaPDFKVNAQFLELYN 153
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMqGS-------PGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 154 EEVLDLFDTTRDIDAKSKKSnIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIH 233
Cdd:cd01368 142 EYIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 234 VCQtrvcpqidADNATDNKIISESAQMNefetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD 313
Cdd:cd01368 221 LVQ--------APGDSDGDVDQDKDQIT-----VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 291167760 314 KSKRAT--HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01368 288 NQLQGTnkMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3-404 |
2.63e-63 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 238.30 E-value: 2.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 3 GAPDeSSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 82
Cdd:PLN03188 94 GVSD-SGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 83 TVFAYGQTGAGKTYTM----GTGFDVNIVEEELGIISRAVKHLFKSIEEKKhiaIKNGLPAPDFKVNAQFLELYNEEVLD 158
Cdd:PLN03188 168 SVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 159 LFDTTrdidakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtr 238
Cdd:PLN03188 245 LLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV---- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 239 vcpqidadnatDNKIISESAQMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-- 316
Cdd:PLN03188 313 -----------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtg 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 317 RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRL 396
Cdd:PLN03188 380 KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQL 458
|
....*...
gi 291167760 397 QMELMEYK 404
Cdd:PLN03188 459 RDELQRVK 466
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1302-1615 |
1.14e-60 |
|
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: 210.27 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1302 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1378
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1379 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1457
Cdd:cd00200 81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1458 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1535
Cdd:cd00200 138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1536 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1613
Cdd:cd00200 209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287
|
..
gi 291167760 1614 WK 1615
Cdd:cd00200 288 WD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1301-1618 |
6.52e-48 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 177.03 E-value: 6.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1301 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsvkycnyTSLVFT------VSTSY 1372
Cdd:COG2319 111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1373 ---IKVWDIrDSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1448
Cdd:COG2319 183 dgtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1449 GKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTI--QGDNLFSGSRDN 1526
Cdd:COG2319 240 RTLTGHSGSVRSVA---FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1527 GIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFT 1604
Cdd:COG2319 311 TVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDGRTLAS 389
|
330
....*....|....
gi 291167760 1605 AADDRTVRIWKARN 1618
Cdd:COG2319 390 GSADGTVRLWDLAT 403
|
|
| Rcc_KIF21A |
cd22263 |
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ... |
923-1004 |
8.39e-46 |
|
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: 159.32 E-value: 8.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 923 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1002
Cdd:cd22263 1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80
|
..
gi 291167760 1003 AK 1004
Cdd:cd22263 81 AK 82
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1301-1575 |
1.03e-36 |
|
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: 140.93 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1301 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWD 1377
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1378 IRdSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLG 1456
Cdd:cd00200 164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1457 PVMCLTVDQissgqdliitgskDHYIkmfdvtegalgtvspthnfepphydgiealtiqgdnLFSGSRDNGIKKWDLTQK 1536
Cdd:cd00200 221 GVNSVAFSP-------------DGYL------------------------------------LASGSEDGTIRVWDLRTG 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 291167760 1537 DLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1575
Cdd:cd00200 252 ECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1407-1627 |
1.19e-34 |
|
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: 135.16 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1407 TVAIPSGENQINQIALNPTGTFLYAASGNA-VRMWDLKRFQSTGKLTGHLGPVmcLTVDQISSGQdLIITGSKDHYIKMF 1485
Cdd:cd00200 2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGELLRTLKGHTGPV--RDVAASADGT-YLASGSSDKTIRLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1486 DvtegaLGTVSPTHNFEPpHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLL 1563
Cdd:cd00200 79 D-----LETGECVRTLTG-HTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLT-TLRGHTDWVNSVAFSPDGTFVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760 1564 SGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIWkarNLQDGQISDT 1627
Cdd:cd00200 152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFspDGEKLLSSSSDGTIKLW---DLSTGKCLGT 214
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
923-1004 |
9.40e-30 |
|
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: 113.45 E-value: 9.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 923 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEgDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1002
Cdd:cd22248 1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKD-ESVLRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79
|
..
gi 291167760 1003 AK 1004
Cdd:cd22248 80 SK 81
|
|
| Rcc_KIF21B |
cd22262 |
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ... |
923-1004 |
2.88e-29 |
|
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: 112.21 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 923 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 1002
Cdd:cd22262 1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80
|
..
gi 291167760 1003 AK 1004
Cdd:cd22262 81 TK 82
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
9-159 |
2.68e-21 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 91.51 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 9 SVRVAVRIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYiQCIEKLIEGCFEGYNATVFAYG 88
Cdd:pfam16796 21 NIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291167760 89 QTGAGKTYTMgtgfdvniveeelgiISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDL 159
Cdd:pfam16796 96 QTGSGSNDGM---------------IPRAREQIFRFISSLK--------KGWKYTIELQFVEIYNESSQDL 143
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1300-1441 |
1.85e-18 |
|
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: 87.78 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1300 LQCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVW 1376
Cdd:cd00200 167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760 1377 DIRdSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWD 1441
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 ... |
12-310 |
7.34e-13 |
|
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: 68.14 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 12 VAVRIRPQLAKEKIEGCHIctsvtpgepqvflgkdkaFTFDYVFDIDSQQEQIYIQCiEKLIEGCFEGYN-ATVFAYGQT 90
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKI------------------IVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 91 GAGKTYTMgtgfdvniveeeLGIISRAVKHLFKSIEEKKhiaiknglpapdfkvnaqflelyneevldlfdttrdidaks 170
Cdd:cd01363 62 GAGKTETM------------KGVIPYLASVAFNGINKGE----------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 171 kksnirihEDStggiyTVGVTTRTVNTESEMMQCLKLGALSRtTASTQMNVQSSRSHAIFTIhvcqtrvcpqidadnatd 250
Cdd:cd01363 89 --------TEG-----WVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------ 136
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 251 nkiisesaqmnefetltakfhFVDLAGSERlkrtgatgerakegisINCGLLALGNVISA 310
Cdd:cd01363 137 ---------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
627-847 |
3.09e-11 |
|
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: 67.10 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 706
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 707 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 777
Cdd:COG4942 101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167760 778 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQ 847
Cdd:COG4942 181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1516-1623 |
2.49e-10 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 64.55 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1516 GDNLFSGSRDNGIKKWDLTQKDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAI 1595
Cdd:COG2319 48 GARLAAGAGDLTLLLLDAAAGALLATLL-GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSV 126
|
90 100 110
....*....|....*....|....*....|
gi 291167760 1596 CV--NSTHIFTAADDRTVRIWkarNLQDGQ 1623
Cdd:COG2319 127 AFspDGKTLASGSADGTVRLW---DLATGK 153
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
389-1025 |
4.41e-10 |
|
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: 64.74 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 389 LRSEITRLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRSRITQLvsdqaNHVLA 466
Cdd:pfam05483 204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL-----EEKTK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 467 RAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArapyfsgsstfspTILSSDKETIEIIDLAKKDLE 546
Cdd:pfam05483 279 LQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK-------------TICQLTEEKEAQMEELNKAKA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 547 KLKRKEKRKKKSVAGKEDNTDTDQEKKEEkgvSERENNELEVEESQEVSDhedeeeeeeeeeddidggessdeSDSESDE 626
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLEK---NEDQLKIITMELQKKSSE-----------------------LEEMTKF 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVRS 706
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 707 EYEKKlQAMNKEL-QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 783
Cdd:pfam05483 479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 784 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLSSSDApAQDTGSSAAAVET 858
Cdd:pfam05483 558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEELHQENK-ALKKKGSAENKQL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 859 DASRTGAqQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 938
Cdd:pfam05483 632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 939 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYindSISDCQANIM----QMEEAKEEGETLDVTA 1014
Cdd:pfam05483 700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776
|
650
....*....|.
gi 291167760 1015 VINACTLTEAR 1025
Cdd:pfam05483 777 KENTAILKDKK 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
627-1010 |
1.16e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 703
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 704 VRSEYEKKLQAMNKELQRLQaaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 781
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIE---EEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 782 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAA---- 854
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkg 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 855 ---AVETDASRTGAQQKMRIPVAR-VQALPTPATNGNRKKYQR-----KGLTGRVFISKTARMKW-------QLLERRVT 918
Cdd:PRK03918 540 eikSLKKELEKLEELKKKLAELEKkLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYlelkdaeKELEREEK 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 919 DIIMQKMTISNMEADMNRLLKQREELTKRREKLSKR-----REKIVKENGEGDKNVANINEEMESLTANIDYINDSISDC 993
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
410
....*....|....*..
gi 291167760 994 QANIMQMEEAKEEGETL 1010
Cdd:PRK03918 700 KEELEEREKAKKELEKL 716
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
630-833 |
2.89e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 630 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYE 709
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 710 KKLQAMNkelQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---RE 781
Cdd:TIGR02168 365 AELEELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAE 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 291167760 782 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 833
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
632-1018 |
6.00e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 632 ADLANITCEIAIKQKLIDELENSQKRLQTLKKQyEEKLMMLQHKIRDTQlerdqvlqnlGSVESYSEEKAKKVRSEYEKK 711
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYE----------GYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 712 LQAMNKELQ----RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQmkeeqekarltesrrnrEIAQLKK 787
Cdd:TIGR02169 246 LASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA-----------------EIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 788 DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQ 867
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 868 KmripvARVQALptpatngnrKKYQRKgltgRVFISKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLKQREELTKR 947
Cdd:TIGR02169 388 K-----DYREKL---------EKLKRE----INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760 948 REKLSKRREKIVKEngegdknVANINEEMESLTANIDYINDSISDCQANIMQMEEAK-----EEGETLDVTAVINA 1018
Cdd:TIGR02169 450 IKKQEWKLEQLAAD-------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKA 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
471-1157 |
2.93e-08 |
|
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: 58.98 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 471 GNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArapyfsgssTFSPTILSSDKETIEIIDLAKKDLEKLKR 550
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVI---------DLQTKLQEMQMERDAMADIRRRESQSQED 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 551 KEKRKKKSV-------AGKED-----NTDTDQEKK----EEKGVSERENNELEVEES--QEVSDHEDEEEEEEEEEDDID 612
Cdd:pfam15921 143 LRNQLQNTVheleaakCLKEDmledsNTQIEQLRKmmlsHEGVLQEIRSILVDFEEAsgKKIYEHDSMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 613 GGEssdesdsesdekanyqadLANITCEIAIKQKLIDELENsqkRLQTLKKQYEEK--LMMLQHKIRDTQLERDQVLQNL 690
Cdd:pfam15921 223 SKI------------------LRELDTEISYLKGRIFPVED---QLEALKSESQNKieLLLQQHQDRIEQLISEHEVEIT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 691 GSVesyseEKAKKVRSEyekkLQAMNKELQRLQaaqkEHARllkNQ-SQYEKQLKKLQQDVMEMkKTKVRLMKQMK---- 765
Cdd:pfam15921 282 GLT-----EKASSARSQ----ANSIQSQLEIIQ----EQAR---NQnSMYMRQLSDLESTVSQL-RSELREAKRMYedki 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 766 EEQEK------ARLTESRRNREiaQLKKDQRKRDHQLRLLEA--QKRNQEVVLRRKTEEvtalRRQVRPMSDKVA-GKVT 836
Cdd:pfam15921 345 EELEKqlvlanSELTEARTERD--QFSQESGNLDDQLQKLLAdlHKREKELSLEKEQNK----RLWDRDTGNSITiDHLR 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 837 RKLSSSDAPAQDTGSSAAAVETDasrtgAQQKMRIPVARVQAlptpatnGNRKKYQRKGLTGRVFISKtarmkwQLLERR 916
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSE-----CQGQMERQMAAIQG-------KNESLEKVSSLTAQLESTK------EMLRKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 917 VTDIIMQKMTISNME---ADMNRLLKQRE--------ELTKRREKLSKRREKIVKENGEGDkNVANINEEMESLTAN--- 982
Cdd:pfam15921 481 VEELTAKKMTLESSErtvSDLTASLQEKEraieatnaEITKLRSRVDLKLQELQHLKNEGD-HLRNVQTECEALKLQmae 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 983 ----IDYINDSISDCQ---------ANIMQMEEAKEEGETLDvtaviNACTLTEARYLLDhflsmginkglqaaQKEAQI 1049
Cdd:pfam15921 560 kdkvIEILRQQIENMTqlvgqhgrtAGAMQVEKAQLEKEIND-----RRLELQEFKILKD--------------KKDAKI 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1050 KVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLghalqENVEDSTDEdapLNSpgsegstLSSDLMKLCGEVKP 1129
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL-----NEVKTSRNE---LNS-------LSEDYEVLKRNFRN 685
|
730 740
....*....|....*....|....*....
gi 291167760 1130 KNKARRRTTTQMEL-LYADSSELASDTST 1157
Cdd:pfam15921 686 KSEEMETTTNKLKMqLKSAQSELEQTRNT 714
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
629-832 |
3.70e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 629 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAKKVR 705
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 706 SEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-ARLTESRRN----- 779
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEEleeli 868
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760 780 ----REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 832
Cdd:TIGR02168 869 eeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
656-817 |
4.68e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 656 KRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAmnKELQRLQAAQKEHARLLKN 735
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 736 QSQYEKQLKKLQQDVMEMKKTKVRLMKqmKEEQEKARLTESRRNREiaqlkkDQRKRDHQLRLLEAQKRNQEVVLRRKTE 815
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAK--KAEEDKKKAEEAKKAEE------DEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
..
gi 291167760 816 EV 817
Cdd:PTZ00121 1714 EK 1715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
569-855 |
5.78e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 569 DQEKKEEKGVSERENNELEVEESQevsdhedeeeeeeEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLI 648
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAE-------------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 649 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV---LQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAA 725
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELeeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 726 QKEHARLLKNQSQYEKQLKKLQQdvmeMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRN 805
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEE----AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 291167760 806 QEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAA 855
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
627-867 |
1.23e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL---GSVESYSEE--KA 701
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVllGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 702 KKVrSEYEKKLQAMNkelqRLQAAQKEharLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 781
Cdd:COG3883 112 ESF-SDFLDRLSALS----KIADADAD---LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 782 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDAS 861
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
|
....*.
gi 291167760 862 RTGAQQ 867
Cdd:COG3883 264 AAGAAA 269
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
631-825 |
2.39e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 631 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRD-TQLERDQVLQNLGSvesySEEKAKKVRSEYE 709
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQA----ELSKLEEEVSRIE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 710 KKLQAMNKELQRL----QAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRnreiAQL 785
Cdd:TIGR02169 812 ARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDL 887
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 291167760 786 KKDQRKRDHQLRllEAQKRNQEVVLRRKTEEVTALRRQVR 825
Cdd:TIGR02169 888 KKERDELEAQLR--ELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
364-823 |
2.51e-07 |
|
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: 55.60 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 364 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174 280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 438 RIKAMQETVDALRSRITQLVSDQanhvlaraGEGNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 507
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEK--------STLAGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 508 trataRAPYFSGSSTFSPTILSSDKETieiidLAKKDLEKLKRKEKRKKKSVAGKEDNTDTDQEKKEEKG--------VS 579
Cdd:pfam10174 423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEkvsalqpeLT 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 580 ERENNELEVEE--SQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENSQKR 657
Cdd:pfam10174 493 EKESSLIDLKEhaSSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVARYK 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 658 LQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSEEKAKKvRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQ 736
Cdd:pfam10174 572 EESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLTLRQMKE-QNKKVANIKHGQQEMKKKGAQLLEEARRREDN 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 737 SQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEVVL- 810
Cdd:pfam10174 648 LADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEALLa 716
|
490 500 510
....*....|....*....|....*....|..
gi 291167760 811 -----------------RRKT--EEVTALRRQ 823
Cdd:pfam10174 717 aisekdaniallelsssKKKKtqEEVMALKRE 748
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
631-1163 |
8.82e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 631 QADLANITCEIAIKQKLIDELENsqkRLQTLKKQYEE----KLMMLQHKIRDTQLERDQVLQNLGSVES----------Y 696
Cdd:COG4913 301 RAELARLEAELERLEARLDALRE---ELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEAllaalglplpA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 697 SEEKAKKVRSEYEKKLQAMNKELQRLQAAQkehARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMkeEQEKARLTES 776
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDALAEA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 777 RRNREIA--------QLKKDQRK---------RDHQLRLLEAQKRNQEVV-------LRRK--TEEVTALRRQVRPMSDK 830
Cdd:COG4913 453 LGLDEAElpfvgeliEVRPEEERwrgaiervlGGFALTLLVPPEHYAAALrwvnrlhLRGRlvYERVRTGLPDPERPRLD 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 831 vAGKVTRKLSSSDAPAQD-----TGSSAAAVETDASRTGAQQKMRIpvarvqalpTPA--TNGNRKKYQ---RKGLTGRV 900
Cdd:COG4913 533 -PDSLAGKLDFKPHPFRAwleaeLGRRFDYVCVDSPEELRRHPRAI---------TRAgqVKGNGTRHEkddRRRIRSRY 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 901 FISKTARMKWQLLERRVTDIimqkmtisnmEADMNRLLKQREELTKRREKLSKRREKI--VKENGEGDKNVANINEEMES 978
Cdd:COG4913 603 VLGFDNRAKLAALEAELAEL----------EEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAE 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 979 LTANIDYINDSISDCQANIMQMEEAKEEGETLDvtAVINACTLTEARylldhflsmginKGLQAAQKEAQIKVLEGRLKQ 1058
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELE--EELDELKGEIGR------------LEKELEQAEEELDELQDRLEA 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1059 TEItsatqnqllfhmlKEKAELNPELDALLGHALQENVEDSTDEDaplnspgsegstLSSDLMKLCGEvkpKNKARRRTT 1138
Cdd:COG4913 739 AED-------------LARLELRALLEERFAAALGDAVERELREN------------LEERIDALRAR---LNRAEEELE 790
|
570 580
....*....|....*....|....*
gi 291167760 1139 TQMELLYADSSELASDTSTGDASLP 1163
Cdd:COG4913 791 RAMRAFNREWPAETADLDADLESLP 815
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1301-1336 |
1.12e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 46.57 E-value: 1.12e-06
10 20 30
....*....|....*....|....*....|....*...
gi 291167760 1301 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1336
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
644-824 |
1.26e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.20 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 644 KQKLIDELENSQK-------RLQTLKKQ---YEEKLMMLQHkiRDTQLERDQVlqnlgsvESYSEEKAKKVRSEYEKKLQ 713
Cdd:pfam17380 305 KEEKAREVERRRKleeaekaRQAEMDRQaaiYAEQERMAME--RERELERIRQ-------EERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 714 AMnKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESR-----RNREIAQLKKD 788
Cdd:pfam17380 376 RM-RELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeeRAREMERVRLE 454
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 291167760 789 QRKRDHQLRLL---EAQKRNQEVVL---RRKTEEVTALRRQV 824
Cdd:pfam17380 455 EQERQQQVERLrqqEEERKRKKLELekeKRDRKRAEEQRRKI 496
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
699-825 |
1.64e-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: 48.76 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 699 EKAKKVRSEYEKKLQamnkelqrlqaaqkeharllknqsQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRR 778
Cdd:pfam20492 2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760 779 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 825
Cdd:pfam20492 58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
640-832 |
2.49e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 640 EIAIKQKL-IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEE--KAKKVRSEYEKKLQAMN 716
Cdd:PRK03918 148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 717 KELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARltesrRNREIAQLKKDQRKRDHQL 796
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-----ELKELKEKAEEYIKLSEFY 302
|
170 180 190
....*....|....*....|....*....|....*.
gi 291167760 797 RLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 832
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
640-957 |
3.45e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 640 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESysEEKAKKVRSEYEKKlqamnKEL 719
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKK-----KAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 720 QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRD-HQLRL 798
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 799 LEAQKRNQEvvLRRKTEEV-TALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAV-ETDASRTGAQQKMRIPVARV 876
Cdd:PTZ00121 1374 EEAKKKADA--AKKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkKADEAKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 877 QALPTPATNGNRKKYQRKgltgrvfiSKTARMKWQLLERRVTDIIMQKMTISNMEADMnrlLKQREELTKRREKLSKRRE 956
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEA--------KKADEAKKKAEEAKKADEAKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEE 1520
|
.
gi 291167760 957 K 957
Cdd:PTZ00121 1521 A 1521
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1299-1336 |
3.60e-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: 3.60e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 291167760 1299 PLQCIHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1336
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
479-1058 |
4.40e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 479 IHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARapyfsgsstfsptiLSSDKETIEIIDLAKKDLEKLKRKEKRKKKS 558
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAE--------------LAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 559 VAGKEDNTDTDQEKKEEKgVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANIT 638
Cdd:COG1196 293 LLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 639 CEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKE 718
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-ALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 719 LQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQMKEEQEKARLTESRRNREiAQLKKDQRKRDHQLRL 798
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLLLEAEADYEGFLEGVKA-ALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 799 LeaqkRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQA 878
Cdd:COG1196 529 L----IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 879 LPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTD--IIMQKMTISNMEADMNRLLKQREELTKRREKLSKRRE 956
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 957 KIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDvtavinacTLTEARYLLDHFLSMGI 1036
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE--------ELLEEEELLEEEALEEL 756
|
570 580
....*....|....*....|..
gi 291167760 1037 NKGLQAAQKEAQIKVLEGRLKQ 1058
Cdd:COG1196 757 PEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
700-1104 |
5.09e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 700 KAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 775
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 776 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEvvlRRKTEEVTALRRQVRPMSDKVAGKvtRKLSSSDAPAQDTgssaaA 855
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQK--QILRERLANLERQ-----L 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 856 VETDASRTGAQQKMRIPVARVQALptpATNGNRKKYQRKGLTGRVfisKTARMKWQLLERRVTDIIMQkmtISNMEADMN 935
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 936 RLLKQREELTKRREKLSKRREKIVKENgegDKNVANINEEMESLTANidYINDSISDCQANIMQMEEAKEEGETLDVTAV 1015
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1016 INACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE--- 1083
Cdd:TIGR02168 465 ELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGyea 537
|
410 420
....*....|....*....|..
gi 291167760 1084 -LDALLGHALQeNVEDSTDEDA 1104
Cdd:TIGR02168 538 aIEAALGGRLQ-AVVVENLNAA 558
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1578-1615 |
6.74e-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: 44.23 E-value: 6.74e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 291167760 1578 TFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIWK 1615
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
644-813 |
7.84e-06 |
|
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: 49.92 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 644 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsVESYSEEKAKKVRSEYEKKLQaMNKELQRLQ 723
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKAR-QRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 724 AAQKEHARLLKnqsqyEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL---KKDQRKRDHQLRLLE 800
Cdd:pfam13868 242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316
|
170
....*....|...
gi 291167760 801 AQKRNQEVVLRRK 813
Cdd:pfam13868 317 GERLREEEAERRE 329
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
650-832 |
1.04e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 650 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVE---SYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQ 726
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAReelEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 727 KEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLM---KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 803
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170 180
....*....|....*....|....*....
gi 291167760 804 RNQEvvLRRKTEEVTALRRQVRPMSDKVA 832
Cdd:COG4372 174 QALS--EAEAEQALDELLKEANRNAEKEE 200
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
682-842 |
1.15e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.24 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 682 ERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAaqkeHARLLKNQsqyekqLKKLQQDVMEMKKtKVRLM 761
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA----EVEELEAE------LEEKDERIERLER-ELSEA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 762 KQmkEEQEKARLTE--SRRNREIAQLKKdqrkrdhqlRLLEAQKRNQEvvLRRKTEEVTALRRQVRpMSDKVAGKVTRKL 839
Cdd:COG2433 454 RS--EERREIRKDReiSRLDREIERLER---------ELEEERERIEE--LKRKLERLKELWKLEH-SGELVPVKVVEKF 519
|
...
gi 291167760 840 SSS 842
Cdd:COG2433 520 TKE 522
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
675-990 |
1.66e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 675 KIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMK 754
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 755 K---TKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV 831
Cdd:COG4372 87 EqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 832 AGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQ 911
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 912 LLE------RRVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDY 985
Cdd:COG4372 247 DKEelleevILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
....*
gi 291167760 986 INDSI 990
Cdd:COG4372 327 KLELA 331
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
670-813 |
1.73e-05 |
|
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: 47.78 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 670 MMLQHKIRDTQLERdqvlqnlGSVESYSEEKAKKVRsEYEKKLQAMnKELQRLQAAQKEhARLLKNQSQYEKQLKKLQQD 749
Cdd:pfam13904 38 LTYARKLEGLKLER-------QPLEAYENWLAAKQR-QRQKELQAQ-KEEREKEEQEAE-LRKRLAKEKYQEWLQRKARQ 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291167760 750 vmemkKTKVRLMKQMKEEQEKARLTESRRNREIAQ-----------LKKDQRKRDHQLRLLEAQKRNQEVVLRRK 813
Cdd:pfam13904 108 -----QTKKREESHKQKAAESASKSLAKPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
631-816 |
3.34e-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: 48.58 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 631 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYE------EKLMMLQHKIRdtQLERDQVLQnlgsvesysEEKAKKV 704
Cdd:pfam17380 326 QAEMDRQAAIYAEQERMAMERERELERIRQEERKRElerirqEEIAMEISRMR--ELERLQMER---------QQKNERV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 705 RSEyekkLQAMNKelQRLQaaQKEHARLLKNQSQYEKQLKKLQQdvmEMKKTKVRLMKQMKE-EQEKARLTESRRNREIA 783
Cdd:pfam17380 395 RQE----LEAARK--VKIL--EEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERArEMERVRLEEQERQQQVE 463
|
170 180 190
....*....|....*....|....*....|....*
gi 291167760 784 QLKKDQRKRDHQLRLLEAQKRNQEVV--LRRKTEE 816
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAeeQRRKILE 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
640-825 |
3.70e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 640 EIAIKQKLIDELENSQKRLQTLKKQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYE 709
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 710 KKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkVRLMKQMKEE--QEKARLTES-RRNREIAQLK 786
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREwpAETADLDADlESLPEYLALL 821
|
170 180 190
....*....|....*....|....*....|....*....
gi 291167760 787 KDQRKRDhqlrLLEAQKRNQEVVLRRKTEEVTALRRQVR 825
Cdd:COG4913 822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
643-815 |
3.91e-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: 46.68 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 643 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKvrseyEKKLQAMNKELQRL 722
Cdd:pfam14988 23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQ-----EREIQDLEEEKEKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 723 QAA-----QKEHARLLKNQSQYEKQLKklQQDVMEM---KKTKVRLMKQMKEEQEKARLTESRRN--REIAQLKKDQRKR 792
Cdd:pfam14988 98 RAEtaekdREAHLQFLKEKALLEKQLQ--ELRILELgerATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQL 175
|
170 180
....*....|....*....|...
gi 291167760 793 DHQLRLLEAQKRNQEvvlRRKTE 815
Cdd:pfam14988 176 IQETQALEAIKSKLE---NRKQR 195
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1581-1614 |
3.92e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 42.33 E-value: 3.92e-05
10 20 30
....*....|....*....|....*....|....*.
gi 291167760 1581 PVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIW 1614
Cdd:pfam00400 3 LLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVW 38
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
656-808 |
4.22e-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: 47.28 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 656 KRLQTLKKQYEEK-------LMMLQHKIR------DTQLERDQVLqnlgsvesysEEKAKKVRSEYEKKlQAMNKELQRL 722
Cdd:pfam02841 155 EERDKLEAKYNQVprkgvkaEEVLQEFLQskeaveEAILQTDQAL----------TAKEKAIEAERAKA-EAAEAEQELL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 723 QAAQKEHARLLKNQ-SQYEKQLKKLQQDvMEMKKtkvrlmKQMKEEQEkaRLTESRRNREIAQLKKDQRKrdhqlrllEA 801
Cdd:pfam02841 224 REKQKEEEQMMEAQeRSYQEHVKQLIEK-MEAER------EQLLAEQE--RMLEHKLQEQEELLKEGFKT--------EA 286
|
....*..
gi 291167760 802 QKRNQEV 808
Cdd:pfam02841 287 ESLQKEI 293
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
648-802 |
4.24e-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: 46.84 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 648 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAM--NKELQrlqAA 725
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYE---AL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760 726 QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 802
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
631-1026 |
4.84e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 631 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQY---------EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 701
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 702 KKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 781
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 782 IA-----QLKKDQRKRDHQLRLLEAQ-------------KRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSD 843
Cdd:COG4717 254 IAaallaLLGLGGSLLSLILTIAGVLflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 844 APAQDTGSS----AAAVETDASRTGAQQKMRIPV--ARVQALPTPATNGNRKKYQRKGLTGRVFISKTARmkWQLLERRV 917
Cdd:COG4717 334 LSPEELLELldriEELQELLREAEELEEELQLEEleQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE--LEELEEQL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 918 TDI------IMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENG--EGDKNVANINEEMESLTANIDYINDS 989
Cdd:COG4717 412 EELlgeleeLLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEE 491
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 291167760 990 ISDCQANIMQMEEAKEEGETLDVTAVINA-----CTLTEARY 1026
Cdd:COG4717 492 WAALKLALELLEEAREEYREERLPPVLERaseyfSRLTDGRY 533
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
682-1011 |
5.22e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 682 ERDQVLQNLGSvesyseekAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQyekqlkKLQQDVMEMKKTKVRLM 761
Cdd:pfam12128 605 RLDKAEEALQS--------AREKQAAAEEQLVQANGELEKASREETFARTALKNARL------DLRRLFDEKQSEKDKKN 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 762 KQMKEEQEKArltesrrNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrkTEEVTALRRQVRPMSDKVAgkvtrklss 841
Cdd:pfam12128 671 KALAERKDSA-------NERLNSLEAQLKQLDKKHQAWLEEQKEQKREAR--TEKQAYWQVVEGALDAQLA--------- 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 842 sdapAQDTGSSAAAVETDASRTGAQQKMRIPVArvqALPTPATNGNRKKYQRKGLTGRvfISKTARMKWQLLERRVtdiI 921
Cdd:pfam12128 733 ----LLKAAIAARRSGAKAELKALETWYKRDLA---SLGVDPDVIAKLKREIRTLERK--IERIAVRRQEVLRYFD---W 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 922 MQ----------KMTISNMEADMNRLlkqREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSIS 991
Cdd:pfam12128 801 YQetwlqrrprlATQLSNIERAISEL---QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
|
330 340
....*....|....*....|
gi 291167760 992 DCQANimqmEEAKEEGETLD 1011
Cdd:pfam12128 878 DANSE----QAQGSIGERLA 893
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-728 |
5.42e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 366 NRARNIKNkvmvnqdrASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 445
Cdd:TIGR02168 674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 446 VDALRSRITQLVSDqanhvLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARapyfsgsstfsp 525
Cdd:TIGR02168 735 LARLEAEVEQLEER-----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE------------ 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 526 tiLSSDKETI-----EIIDLAKKDLEKLKRKEKRKKKSVAGKEDNTDTDQEKKEEKGvsERENNELEVEESQEvsdhede 600
Cdd:TIGR02168 798 --LKALREALdelraELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE--DIESLAAEIEELEE------- 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 601 eeeeeeeeddiDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQ 680
Cdd:TIGR02168 867 -----------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 291167760 681 LERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 728
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
645-776 |
5.73e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 645 QKLIDELENSQKRLQTLKKQYEEklmmlQH-KIRDTQLERDQVLQNLgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQ 723
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 291167760 724 AAQKEHARLLKNQSQYEKQLKKLQQDVmemkKTKVRLMKQMKEEQEKARLTES 776
Cdd:COG3206 334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
648-886 |
6.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 648 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesyseEKAKKVRSEYEKKLQAMNKELQRLQAAQK 727
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------EALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 728 EHARLLKNQSQYEKQLKKL---------------QQDVMEMKKTKVRLMKQMKEEQEKArltESRRNREIAQLKKDQRKR 792
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 793 DHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIP 872
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250
....*....|....
gi 291167760 873 VARVQALPTPATNG 886
Cdd:COG3883 247 AGAGAAGAAGAAAG 260
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
673-816 |
6.55e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 673 QHKIRDTQLERDQVLQN-LGSVESYSEEK-------AKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQY----E 740
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760 741 KQLKKLQQDVMEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQrKRDHQLRLLEAQKRNQEVVLRRKTEE 816
Cdd:PRK12704 110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
695-1058 |
9.07e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 695 SYSEEKAKKVRSEYEKKLQAMNKELQRLQA----AQKEHARLLKNQSQYEKQLKKLQQDVMEMKktkvRLMKQMKEEQEK 770
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEkiaeLEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 771 ARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSDAPAQDTG 850
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-ALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 851 SSAAAVETDASRTGAQQKMripvarvqalptpatngnrkkyqrkgltgrvfisktarmkwqlLERRVTDIIMQkmtISNM 930
Cdd:TIGR02168 817 EEAANLRERLESLERRIAA-------------------------------------------TERRLEDLEEQ---IEEL 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 931 EADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIM----QMEEAKEE 1006
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEelreKLAQLELR 930
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 291167760 1007 GETLDVTAVINACTLTE-ARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1058
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
649-823 |
1.03e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 649 DELENSQKRLQTLKKQyeeklmmlqHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 728
Cdd:COG3206 189 KELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELES-QLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 729 H------ARLLKNQSQYEKQLKKLQQ-------DVMEMKKTKVRLMKQMKEEQEKArLTESRRNREIAQLKKD---QRKR 792
Cdd:COG3206 259 LlqspviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRI-LASLEAELEALQAREAslqAQLA 337
|
170 180 190
....*....|....*....|....*....|.
gi 291167760 793 DHQLRLLEAQKRNQEvvLRRKTEEVTALRRQ 823
Cdd:COG3206 338 QLEARLAELPELEAE--LRRLEREVEVAREL 366
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
655-819 |
1.13e-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: 46.87 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 655 QKRLQTLKKQYEEKLmmlqhkirDTQLERDQvlqnlgsvESYSEE-KAKKVRSEYEKKLQAMNKELQRLQ-AAQKEHARL 732
Cdd:pfam15709 360 QRRLQQEQLERAEKM--------REELELEQ--------QRRFEEiRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 733 lkNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQlrlLEAQKRNQEVVLRR 812
Cdd:pfam15709 424 --QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ---EAEEKARLEAEERR 498
|
....*..
gi 291167760 813 KTEEVTA 819
Cdd:pfam15709 499 QKEEEAA 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
473-817 |
1.18e-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: 46.98 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 473 EEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARApyfsgsstfsptilssDKETIEIIDLAKKDLEKLKRKE 552
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI----------------KDLGEEEQLRVKEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 553 KRKKKSVAGKEDNTDtDQEKKEEKGVSERENNELEVEESQEvsdhedeeeeeeeeeddidggessdesdsesdEKANYQA 632
Cdd:TIGR02169 304 ASLERSIAEKERELE-DAEERLAKLEAEIDKLLAEIEELER--------------------------------EIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 633 DLANITCEIAIKQK----LIDELENSQKRLQTLK---KQYEEKLMMLQHKIRDTQLERDQVLqnlgsvesyseEKAKKVR 705
Cdd:TIGR02169 351 RRDKLTEEYAELKEeledLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKRELDRLQ-----------EELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 706 SEyekkLQAMNKELQRLQAAQKE-HARLLKNQSQYEKQLKKLQQDVMEMKktkvrlmkqmKEEQEKARLTEsrrnrEIAQ 784
Cdd:TIGR02169 420 EE----LADLNAAIAGIEAKINElEEEKEDKALEIKKQEWKLEQLAADLS----------KYEQELYDLKE-----EYDR 480
|
330 340 350
....*....|....*....|....*....|....*
gi 291167760 785 LKKDQRKRDHQLRLLEAQKR--NQEVVLRRKTEEV 817
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
710-830 |
1.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 710 KKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNREIAQLKK 787
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 291167760 788 dQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 830
Cdd:COG4717 151 -LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
644-825 |
1.44e-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: 46.07 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 644 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQ 723
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 724 AAQKEH--ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-----QMKEEqEKARLTESRRNREIAQLKKDQRKRDHQL 796
Cdd:pfam13868 198 DEKAERdeLRAKLYQEEQERKERQKEREEAEKKARQRQELQqareeQIELK-ERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
170 180
....*....|....*....|....*....
gi 291167760 797 RLLEAQKRNQevvlrRKTEEVTALRRQVR 825
Cdd:pfam13868 277 EQEEAEKRRM-----KRLEHRRELEKQIE 300
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
643-782 |
1.89e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 643 IKQKLiDELENSQKRLQtlkkQYEEklmMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKELQRL 722
Cdd:PRK12704 77 LRERR-NELQKLEKRLL----QKEE---NLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIEEQLQELERI 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 723 QAAQKEHARllknqsqyEKQLKKLQqdvmemKKTKVRLMKQMKEEQEKARLTESRRNREI 782
Cdd:PRK12704 148 SGLTAEEAK--------EILLEKVE------EEARHEAAVLIKEIEEEAKEEADKKAKEI 193
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
644-803 |
2.04e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.87 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 644 KQKLidELENSQKRLQtLKKQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVESYSEEKAKKVRSEYEK 710
Cdd:pfam03528 24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSENTKQEAIDEVKS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 711 KLQamnKELQRLQAAQKE---------HARLLKNQSQYEKQLKKLQQDVMEMKKtkvRL------------MKQMKEEQE 769
Cdd:pfam03528 101 QWQ---EEVASLQAIMKEtvreyevqfHRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAE 174
|
170 180 190
....*....|....*....|....*....|....
gi 291167760 770 KARLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 803
Cdd:pfam03528 175 KLRSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
|
|
| mS26_PET12 |
cd23703 |
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ... |
704-798 |
2.83e-04 |
|
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: 43.31 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 704 VRSEYEKKLQAMNKELQRLQAAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkqmkEEQEKARLTESRRN 779
Cdd:cd23703 67 LRELEERKLKTEELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT-----DPEREERAAKRRAN 138
|
90
....*....|....*....
gi 291167760 780 REIAQLKKDQRKRDHQLRL 798
Cdd:cd23703 139 REAKELAKKEARADALHEL 157
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
686-823 |
3.41e-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: 45.33 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 686 VLQNLGSVESYSEEKAKKVRSEyekKLQAMNKELQRLQAAQKEHARL---LKNQSQYEKqlKKLQQDVME-MKKTKVRLM 761
Cdd:pfam15709 305 VTGNMESEEERSEEDPSKALLE---KREQEKASRDRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMREELE 379
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167760 762 KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 823
Cdd:pfam15709 380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
646-813 |
4.18e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 646 KLIDELENSQKRLQTLKKQYEEKL------MMLQHKIRDTQL----ERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAM 715
Cdd:PRK11637 103 KQIDELNASIAKLEQQQAAQERLLaaqldaAFRQGEHTGLQLilsgEESQRGERILAYFGYLNQARQETIAELKQTREEL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 716 NKELQRLQAAQKEHARLLKNQSQyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNR-----EIAQLKKDQR 790
Cdd:PRK11637 183 AAQKAELEEKQSQQKTLLYEQQA---QQQKLEQARNERKKTLTGLESSLQKDQ--QQLSELRANEsrlrdSIARAEREAK 257
|
170 180
....*....|....*....|....*
gi 291167760 791 KR-DHQLRllEAQK-RNQEVVLRRK 813
Cdd:PRK11637 258 ARaEREAR--EAARvRDKQKQAKRK 280
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
650-1066 |
4.75e-04 |
|
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: 45.04 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 650 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAMNKELQRLQAAQKEH 729
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 730 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 808
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 809 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSDAPAQdtgssaaavetdasRTGAQQKMRIPVARVQALptpatngnr 888
Cdd:TIGR00606 846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR--------------RQQFEEQLVELSTEVQSL--------- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 889 kkyqrkgltgrvfisktarmkwqllerrVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENgegDKN 968
Cdd:TIGR00606 901 ----------------------------IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI---KEK 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 969 VANINEEMESLTANI-----DYINDSISDCQANIMQMEEAKEEGETLD-----VTAVINACTLTEaRYLLDHFLSMGINK 1038
Cdd:TIGR00606 950 VKNIHGYMKDIENKIqdgkdDYLKQKETELNTVNAQLEECEKHQEKINedmrlMRQDIDTQKIQE-RWLQDNLTLRKREN 1028
|
410 420
....*....|....*....|....*...
gi 291167760 1039 GLQAAQKEaqIKVLEGRLKQTEITSATQ 1066
Cdd:TIGR00606 1029 ELKEVEEE--LKQHLKEMGQMQVLQMKQ 1054
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
649-782 |
4.87e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 649 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVlqnlgsvesysEEKAKKVRSEYEKKLQAMNKELQ-RLQAAQK 727
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760 728 EHARLLKNQSQYEKQLKKLQ--QDVMEMKKtkvrLMKQMKEEQEKARLTESRRNREI 782
Cdd:PRK00409 585 EADEIIKELRQLQKGGYASVkaHELIEARK----RLNKANEKKEKKKKKQKEKQEEL 637
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
633-830 |
4.97e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 633 DLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEE-KAKKVRSEYEKK 711
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKENLEKE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 712 LQAMNKELQRLQAAQKEharLLKNQSQYEKQLKKLQQDVMEMKKtkvrlmkqmkeEQEKARLTESRRNREIAQLKKDQRK 791
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKS---LKKKQEEKQELIDQKEKEKKDLIK-----------EIEEKEKKISSLEKELEKAKKENEK 628
|
170 180 190
....*....|....*....|....*....|....*....
gi 291167760 792 rdhqlrlLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 830
Cdd:TIGR04523 629 -------LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
697-804 |
5.74e-04 |
|
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: 42.37 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 697 SEEKAK------KVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKlqqdvmeMKKTKVRLMKQMKEEQEK 770
Cdd:pfam11600 10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEK-------ELKEKERREKKEKDEKEK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 291167760 771 A---RLTESRRNREIAQLK---KDQRKRDHQLRLLEAQKR 804
Cdd:pfam11600 83 AeklRLKEEKRKEKQEALEaklEEKRKKEEEKRLKEEEKR 122
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
645-961 |
5.88e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 645 QKLIDEL---ENSQKRL----QTLKKQYEEKLmmlqhKIRDTQLE--RDQVLQNLGSVESYSEEKaKKVRSEY---EKKL 712
Cdd:pfam01576 702 EELEDELqatEDAKLRLevnmQALKAQFERDL-----QARDEQGEekRRQLVKQVRELEAELEDE-RKQRAQAvaaKKKL 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 713 QAMNKELQ-RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrrnrEIAQLKKD--- 788
Cdd:pfam01576 776 ELDLKELEaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA----ELLQLQEDlaa 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 789 ---QRKRDHQLR---------------LLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVagkvtRKLSSSdapaqdtg 850
Cdd:pfam01576 852 serARRQAQQERdeladeiasgasgksALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL-----RKSTLQ-------- 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 851 SSAAAVETDASRTGAQQkmripvarvqalptpaTNGNRKKYQRKgltgrvfiSKTARMKWQLLERRVTDiiMQKMTISNM 930
Cdd:pfam01576 919 VEQLTTELAAERSTSQK----------------SESARQQLERQ--------NKELKAKLQEMEGTVKS--KFKSSIAAL 972
|
330 340 350
....*....|....*....|....*....|....
gi 291167760 931 EADMNRLLKQREELTKRRE---KLSKRREKIVKE 961
Cdd:pfam01576 973 EAKIAQLEEQLEQESRERQaanKLVRRTEKKLKE 1006
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
645-825 |
6.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 645 QKLIDELENSQKRLQTLKKQYEeklmMLQHkIRDTQLERDQVLQNLGSVESYSE----EKAKKVRSEYEKKLQAMNKELQ 720
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIE----LLEP-IRELAERYAAARERLAELEYLRAalrlWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 721 RLQAAQKEHARLLKNQSQYEKQLKKLQQDVmemkktKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLE 800
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180
....*....|....*....|....*.
gi 291167760 801 AQ-KRNQEVVLRRKtEEVTALRRQVR 825
Cdd:COG4913 380 EEfAALRAEAAALL-EALEEELEALE 404
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
639-807 |
7.01e-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: 43.90 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 639 CEIAIKQKLidELENSQKRLQTLKKQYEE---KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAK---KVRSEYEKKL 712
Cdd:pfam15742 54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQeksRVADAEEKIL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 713 qamnkELQRlqaaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN------------- 779
Cdd:pfam15742 132 -----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdke 202
|
170 180 190
....*....|....*....|....*....|..
gi 291167760 780 ----REIAQLKKDQRKRDHQLRLLEAQKRNQE 807
Cdd:pfam15742 203 aqleMTNSQQQLRIQQQEAQLKQLENEKRKSD 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
424-792 |
8.15e-04 |
|
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: 44.28 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 424 ENAMLQTENN--NLRVRIKAMQETVDALRSRITQLVSDQanhvlaragegnEEISNMIHSYIKEIEDLRAKLLESEAVNE 501
Cdd:TIGR02168 669 NSSILERRREieELEEKIEELEEKIAELEKALAELRKEL------------EELEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 502 NLRKNLTRATARAPYFSGSSTFSPTILSSDKETIEIIDLAKKDLEklkrkekrkkksvAGKEDNTDTDQEKKEEKGVSER 581
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-------------AEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 582 ENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKAnyQADLANITCEIAIKQKLIDELENSQKRLQTL 661
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL--SEDIESLAAEIEELEELIEELESELEALLNE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 662 KKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYEKKLQAMNKELQRLQAAQKEHARL-----LKNQ 736
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLtleeaEALE 960
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291167760 737 SQYEKQLKKLQQDVMEMKKTKVRL----------MKQMKE-----EQEKARLTESRRNRE--IAQLKKDQRKR 792
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELgpvnlaaieeYEELKErydflTAQKEDLTEAKETLEeaIEEIDREARER 1033
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1445-1486 |
1.05e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.10 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 291167760 1445 FQSTGKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFD 1486
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLA---FSPDGKLLASGSDDGTVKVWD 39
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
638-802 |
1.30e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 41.81 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 638 TCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqHKIRDTQLERDQVLQnlgsveSYSEE------KAKKVRSEY--- 708
Cdd:pfam15619 17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIA------RHNEEvrvlreRLRRLQEKErdl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 709 EKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQlkKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKD 788
Cdd:pfam15619 87 ERKLKEKEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKK 164
|
170
....*....|....
gi 291167760 789 QRKRDHQLRLLEAQ 802
Cdd:pfam15619 165 HKEAQEEVKILQEE 178
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
627-754 |
1.45e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 627 KANYQADLANItceiaikQKLIDELENSQKRLQT-------LKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsvESYSE- 698
Cdd:PRK00409 508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEAE--KEAQQa 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 699 -EKAKKVRSEYEKKLQAMNKELQRLQAAQK---EHARLLKNQSQYEKQLKKLQQDVMEMK 754
Cdd:PRK00409 579 iKEAKKEADEIIKELRQLQKGGYASVKAHElieARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
629-808 |
1.49e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 629 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQleRDQVLQNLGSVESYSEEKAKKVRSEY 708
Cdd:pfam12128 351 SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKI--REARDRQLAVAEDDLQALESELREQL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 709 EKKLQAMNKELQRLQAAQKEhARLLKNQSQYEKQLKklqqdvmEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKK- 787
Cdd:pfam12128 429 EAGKLEFNEEEYRLKSRLGE-LKLRLNQATATPELL-------LQLENFDERIERAREEQEAANAEVERLQSELRQARKr 500
|
170 180
....*....|....*....|....*
gi 291167760 788 ----DQRKRDHQLRLLEAQKRNQEV 808
Cdd:pfam12128 501 rdqaSEALRQASRRLEERQSALDEL 525
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
942-1034 |
1.53e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 942 EELTKRREKLSKRREKIVKENgegdKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEgetldvtavINACTL 1021
Cdd:smart00787 204 TELDRAKEKLKKLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ---------CRGFTF 270
|
90
....*....|...
gi 291167760 1022 TEARYLLDHFLSM 1034
Cdd:smart00787 271 KEIEKLKEQLKLL 283
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
657-825 |
1.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 657 RLQTLKKQYEEkLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQ 736
Cdd:COG4913 226 AADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 737 SQYEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTesrrnREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKT 814
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLE-----REIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170
....*....|.
gi 291167760 815 EEVTALRRQVR 825
Cdd:COG4913 380 EEFAALRAEAA 390
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1544-1575 |
1.59e-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: 37.68 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|..
gi 291167760 1544 NAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1575
Cdd:smart00320 9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
627-818 |
1.67e-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: 42.96 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQ---LERDQVLQNLGSVE---SYSEEK 700
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeAENEALLEELRSLQerlNASERK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 701 AKKVRSE---------------YEKKLQAMNKELQ---------------------RLQAAQKEHARLLKNQSQYEKQLK 744
Cdd:pfam07888 253 VEGLGEElssmaaqrdrtqaelHQARLQAAQLTLQladaslalregrarwaqeretLQQSAEADKDRIEKLSAELQRLEE 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291167760 745 KLQQDVMEMKKTKVRLMKqmkeEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKrnQEV-----VLRRKTEEVT 818
Cdd:pfam07888 333 RLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK--QELleyirQLEQRLETVA 405
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
684-819 |
1.70e-03 |
|
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: 41.43 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 684 DQVLQNLGSVESYSEEKA--KKVRSEYEKKLQAMNKELQR----LQAAQKEHARLLKNQSQYEKqlkklqqDVMEMKKTK 757
Cdd:pfam13851 19 DITRNNLELIKSLKEEIAelKKKEERNEKLMSEIQQENKRltepLQKAQEEVEELRKQLENYEK-------DKQSLKNLK 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167760 758 VRL------MKQMKEEQE--KARLTESRRNREiaQLKKDQRKrdhqlRLLEAQKR--NQEVVLRRKTEEVTA 819
Cdd:pfam13851 92 ARLkvlekeLKDLKWEHEvlEQRFEKVERERD--ELYDKFEA-----AIQDVQQKtgLKNLLLEKKLQALGE 156
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
658-824 |
1.79e-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: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 658 LQTLKKQYEEKLmmlQHKIRDTqleRDQVLQNLGSVESYSEEK-----AKKVRSEYEK-KLQAMNK-ELQRLQAAQKEha 730
Cdd:pfam15665 16 IQALKEAHEEEI---QQILAET---REKILQYKSKIGEELDLKrriqtLEESLEQHERmKRQALTEfEQYKRRVEERE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 731 rlLKNQSQYEKQLKKLQQDVMEMKKT---KVR----LMKQMKEEQEKArLTESRR--NREIAQLKKDQRKR-----DHQL 796
Cdd:pfam15665 88 --LKAEAEHRQRVVELSREVEEAKRAfeeKLEsfeqLQAQFEQEKRKA-LEELRAkhRQEIQELLTTQRAQsasslAEQE 164
|
170 180
....*....|....*....|....*....
gi 291167760 797 RLLEAQKrnQEVV-LRRKTEEVTALRRQV 824
Cdd:pfam15665 165 KLEELHK--AELEsLRKEVEDLRKEKKKL 191
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
645-808 |
1.82e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.18 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 645 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSEE--KAKKVRSEYEKKL 712
Cdd:cd16269 123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEAilQADQALTEKEKEI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 713 QAMNKELQRLQAAQKEharllknqsqYEKQLKKLQQDVMEMKKTKVRLMKQMKEE-QEKARLTESRRNREIAQLKKDQRK 791
Cdd:cd16269 201 EAERAKAEAAEQERKL----------LEEQQRELEQKLEDQERSYEEHLRQLKEKmEEERENLLKEQERALESKLKEQEA 270
|
170
....*....|....*..
gi 291167760 792 RDHQLRLLEAQKRNQEV 808
Cdd:cd16269 271 LLEEGFKEQAELLQEEI 287
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
643-884 |
1.96e-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: 42.74 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 643 IKQKLIDELENSQKRLQTLKKQYEEKLM--MLQHKIRDTQ------LERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQA 714
Cdd:pfam04747 12 IRQQLTNRRKNLGRVAKSQRNQFRQWLLtaVLPNSINDQRkeafasLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 715 MNKELQRLQAAQKEHARLLKNQSQYEKQlkklqqdvmemkktkvrlmKQMKEEQEKarltesrrnreiaqLKKDQRKRDH 794
Cdd:pfam04747 92 VNAKKAAEKEARRAEAEAKKRAAQEEEH-------------------KQWKAEQER--------------IQKEQEKKEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 795 QLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPM---SDKVAGKVTRKLSSSDAPAQDTGSSAAA--VETDASRTGAQQKM 869
Cdd:pfam04747 139 DLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPApveEEIVVKKVANDRSAAPAPEPKTPTNTPAepAEQVQEITGKKNKK 218
|
250
....*....|....*
gi 291167760 870 RIPVARVQALPTPAT 884
Cdd:pfam04747 219 NKKKSESEATAAPAS 233
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1539-1575 |
1.98e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.98e-03
10 20 30
....*....|....*....|....*....|....*..
gi 291167760 1539 LQQVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1575
Cdd:pfam00400 3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
763-1087 |
2.22e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 763 QMKEEQEKAR--LTESRRNREIA---------QLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV 831
Cdd:TIGR02169 167 EFDRKKEKALeeLEEVEENIERLdliidekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 832 AGKvTRKLSSSDAPAQDTGSSAAAVEtdasrtgaqQKMRIPVARVQALptpaTNGNRKKYQRKGLTGRVFISKTAR---- 907
Cdd:TIGR02169 247 ASL-EEELEKLTEEISELEKRLEEIE---------QLLEELNKKIKDL----GEEEQLRVKEKIGELEAEIASLERsiae 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 908 ----MKwQLLERR---VTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLT 980
Cdd:TIGR02169 313 kereLE-DAEERLaklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 981 ANIDYINDSISDCQANIMQMEEAKEE--GETLDVTAVINActltearylldhfLSMGINKgLQAAQKEAQ--IKVLEGRL 1056
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRlsEELADLNAAIAG-------------IEAKINE-LEEEKEDKAleIKKQEWKL 457
|
330 340 350
....*....|....*....|....*....|.
gi 291167760 1057 KQTEITSATQNQLLFHMLKEKAELNPELDAL 1087
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
365-1016 |
2.41e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 365 ANRARNIKNKVMVNQDRASQQINALR-SEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRiKAMQ 443
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 444 ETVDALRSRITQLVSDQANHV--LARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNEnLRKNLTRATARAPYFSGSS 521
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKA 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 522 TFSPTILSSDKETIEIidlAKKDLEKLKRKEKRKKKSVAGKEDNTDTDQEKKEEKgvseRENNEL--EVEESQEVSDHED 599
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK----KKADEAkkKAEEDKKKADELK 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 600 EEEEEEEEEDDIDGGESSDESDSESDEKAN--YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIR 677
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 678 dtqlerdqvlqnlgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEK--QLKKLQQ--DVMEM 753
Cdd:PTZ00121 1492 --------------------AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadEAKKAEEkkKADEL 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 754 KKTKVRLMKQMKEEQEKARLTESRRN---REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 830
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 831 vaGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKgltgrvfISKTARMKW 910
Cdd:PTZ00121 1632 --KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-------LKKEAEEAK 1702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 911 QLLERRVTDIIMQKMTISNMEADMNRLLKQrEELTKRREKLSKRREKIVKENGEGDKnVANINEEMESLTANIDYINDSI 990
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKA-EEAKKEAEEDKKKAEEAKKDEEEKKK-IAHLKKEEEKKAEEIRKEKEAV 1780
|
650 660 670
....*....|....*....|....*....|
gi 291167760 991 ----SDCQANIMQMEEAKEEGETLDVTAVI 1016
Cdd:PTZ00121 1781 ieeeLDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
645-870 |
2.45e-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: 42.85 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 645 QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIR-DTQL----------------ERDQVLQNLGSVESYSEEKAKKVRSE 707
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQaETELcaeaeemrarlaarkqELEEILHELESRLEEEEERSQQLQNE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 708 yEKKLQAMNKELQRlQAAQKEHARllkNQSQYEK-----QLKKLQQDVMEMKKTKVRLMK--------------QMKEEQ 768
Cdd:pfam01576 98 -KKKMQQHIQDLEE-QLDEEEAAR---QKLQLEKvtteaKIKKLEEDILLLEDQNSKLSKerklleeriseftsNLAEEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 769 EKARLTESRRNREIAQLKkdqrkrDHQLRLLEAQKRNQEVV-LRRKTE-EVTALRRQVRPMSDKVAgKVTRKLSSSDAPA 846
Cdd:pfam01576 173 EKAKSLSKLKNKHEAMIS------DLEERLKKEEKGRQELEkAKRKLEgESTDLQEQIAELQAQIA-ELRAQLAKKEEEL 245
|
250 260
....*....|....*....|....
gi 291167760 847 QDTgsSAAAVETDASRTGAQQKMR 870
Cdd:pfam01576 246 QAA--LARLEEETAQKNNALKKIR 267
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
709-1104 |
2.46e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 709 EKKLQAMNKELQRLQAAQKEharllknqsqYEKQLKKLQQDV----------MEMKKTKVRLMKQmkeEQEKARLTESRR 778
Cdd:COG1196 178 ERKLEATEENLERLEDILGE----------LERQLEPLERQAekaeryrelkEELKELEAELLLL---KLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 779 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRpmsdkVAGKVTRKLSSSDAPAQDTGSSAAAVET 858
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY-----ELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 859 DASRTGAQQKMRIpVARVQALPTPATNGNRKKYQRKGLTgrvfisKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLL 938
Cdd:COG1196 320 ELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 939 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINA 1018
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 1019 CTLTEARYLLDHFLSMGINKG--LQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLGHALQENV 1096
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLllLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
....*...
gi 291167760 1097 EDsTDEDA 1104
Cdd:COG1196 553 VE-DDEVA 559
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
698-772 |
2.50e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 40.59 E-value: 2.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760 698 EEKAKKVRSEYEKKLQAMNKELQRLQAA-QKEhaRLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKAR 772
Cdd:COG2825 45 QKKLEKEFKKRQAELQKLEKELQALQEKlQKE--AATLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQELL 118
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
684-791 |
2.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 684 DQVLQNLGSVESYSEEKAKKV---RSEYEKKLQAMNKELQRLQaaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL 760
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQ--EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
|
90 100 110
....*....|....*....|....*....|.
gi 291167760 761 MKQMKEEQEKARLTESRRNREIAQLKKDQRK 791
Cdd:PRK00409 597 QKGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
649-784 |
2.65e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 39.57 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 649 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSvesyseekakkvrSEYEKKLQAMNKELQRLQAAQKE 728
Cdd:pfam02050 1 DEAARELAEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISA-------------AELRNYQAFISQLDEAIAQQQQE 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 291167760 729 HARLLKNQSQYEKQLKKLQQDVMEMKKTKVRlmkQMKEEQEKARLTESRRNREIAQ 784
Cdd:pfam02050 68 LAQAEAQVEKAREEWQEARQERKSLEKLRER---EKKEERKEQNRREQKQLDELAA 120
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
649-826 |
3.16e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 649 DELENsQKRLQTLKKQYEEKlmmlqhKIRDTQLERDQVLQNLGSvesysEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 728
Cdd:pfam17380 454 EEQER-QQQVERLRQQEEER------KRKKLELEKEKRDRKRAE-----EQRRKILEKELEERKQAMIEEERKRKLLEKE 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 729 HARllKNQSQYEKQlkklQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNReiaqLKKDQRKRDHQLRLLEAQKRNQEV 808
Cdd:pfam17380 522 MEE--RQKAIYEEE----RRREAEEERRKQQEMEERRRIQEQMRKATEERSR----LEAMEREREMMRQIVESEKARAEY 591
|
170
....*....|....*...
gi 291167760 809 vlrRKTEEVTALRRQVRP 826
Cdd:pfam17380 592 ---EATTPITTIKPIYRP 606
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1445-1486 |
3.23e-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: 3.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 291167760 1445 FQSTGKLTGHLGPVMCLtvdQISSGQDLIITGSKDHYIKMFD 1486
Cdd:smart00320 2 GELLKTLKGHTGPVTSV---AFSPDGKYLASGSDDGTIKLWD 40
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
653-786 |
3.53e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 39.50 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 653 NSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYseekakkvRSEYEKKLQAMNKE-------------L 719
Cdd:COG2882 2 KRSFRLQTLLDLAEKEEDEAARELGQAQQALEQAEEQLEQLEQY--------REEYEQRLQQKLQQglsaaqlrnyqqfI 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291167760 720 QRLQAAQKEHARLLKN-QSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 786
Cdd:COG2882 74 ARLDEAIEQQQQQVAQaEQQVEQARQAWLEARQERKALEKLKERRREEERQEENRREQKELDELASRR 141
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
304-513 |
3.84e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 304 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:COG3206 96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 379 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 444
Cdd:COG3206 174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 445 ----------TVDALRSRITQLVSDQANhVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKNLTRATAR 513
Cdd:COG3206 254 dalpellqspVIQQLRAQLAELEAELAE-LSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
695-849 |
4.06e-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: 40.52 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 695 SYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHArllknqSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLT 774
Cdd:pfam14988 7 EYLAKKTEEKQKKIEKLWNQYVQECEEIERRRQELA------SRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760 775 ESrRNREIAQLKKDQRK--RDHQLRLLEAQKRnqevVLRRKteevTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDT 849
Cdd:pfam14988 81 ES-QEREIQDLEEEKEKvrAETAEKDREAHLQ----FLKEK----ALLEKQLQELRILELGERATRELKRKAQALKL 148
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
384-979 |
4.40e-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: 41.93 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 384 QQINALRSEITRLQMELMEyktGKRIIDEEGVESINDMfHENAMLQTENNNLRVRIKAMQETVDALRSRITQLVS--DQA 461
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKE---NKKNIDKFLTEIKKKE-KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKniDKI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 462 NHVLARAgegNEEISNmIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARapyFSGSSTfspTILSSDKETIEIIDLA 541
Cdd:TIGR04523 193 KNKLLKL---ELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE---INEKTT---EISNTQTQLNQLKDEQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 542 KKDLEKLKRKEkrkkksvagKEDNTDTDQEKKEEKGVSEREnNELEVEESQEVSDHEDEEEEEEeeeddidggessdesd 621
Cdd:TIGR04523 263 NKIKKQLSEKQ---------KELEQNNKKIKELEKQLNQLK-SEISDLNNQKEQDWNKELKSEL---------------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 622 sesdekANYQADLANITCEIAIKQKLIDELENSQKRL-----------QTLKKQYEEKlmmlQHKIRDTQLERDQVLQNL 690
Cdd:TIGR04523 317 ------KNQEKKLEEIQNQISQNNKIISQLNEQISQLkkeltnsesenSEKQRELEEK----QNEIEKLKKENQSYKQEI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 691 GSVESYSE------EKAKKVRSEYEKKLQAMNKELQRLqaaQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQM 764
Cdd:TIGR04523 387 KNLESQINdleskiQNQEKLNQQKDEQIKKLQQEKELL---EKEIERLKETIIKNNSEIKDLTNQDSV-KELIIKNLDNT 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 765 KEEQEKarltesrrnrEIAQLKKDQRKRDHQLrlleaQKRNQEvvLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSda 844
Cdd:TIGR04523 463 RESLET----------QLKVLSRSINKIKQNL-----EQKQKE--LKSKEKELKKLNEEKKELEEKVK-DLTKKISSL-- 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 845 paqdtgssaaavetdasrtgaqqkmripVARVQALPTPATNGNRKKYQRKgltgRVFISKTARMKWQLLErrvTDIIMQK 924
Cdd:TIGR04523 523 ----------------------------KEKIEKLESEKKEKESKISDLE----DELNKDDFELKKENLE---KEIDEKN 567
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 291167760 925 MTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESL 979
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
627-745 |
4.47e-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: 40.68 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 627 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMM---------LQHKIRDTQLER----DQVLQNLGSV 693
Cdd:COG1579 40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRIsdleDEILELMERI 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 694 ESYSEEKA-------------KKVRSEYEKKLQAMNKELQRLQAAQKEHA-----RLLKnqsQYEKQLKK 745
Cdd:COG1579 120 EELEEELAeleaelaeleaelEEKKAELDEELAELEAELEELEAEREELAakippELLA---LYERIRKR 186
|
|
| Cep57_CLD |
pfam14073 |
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ... |
672-800 |
4.76e-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: 39.92 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 672 LQHKIRDTQLERDQ-----------------VLQNLGSVESYSEEKAKKVRSEYEKKLQA-------MNKELQR----LQ 723
Cdd:pfam14073 9 LQEKIRRLELERKQaednlkqlsretshykeVLQKENDARDPSRGEVSKQNQELISQLAAaesrcslLEKQLEYmrkmVE 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291167760 724 AAQKEHARLLKNQSQYEKQlkkLQQDVMEMKKtkvRLMKQMKEEQEKARLTESRRNRE--IAQLKKDQRKRDHQLRLLE 800
Cdd:pfam14073 89 NAEKERTAVLEKQASLERE---RSQDSSELQA---QLEKLEKLEQEYLRLTRTQSLAEtkIKELEEKLQEEEHQRKLVQ 161
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
700-1105 |
4.84e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 700 KAKKVRSEYEKKLQAMNKELQRLQAAQK----------EHARLLKNQSQYEKQLKKLQQDVMEMKktkVRLmkqmkEEQE 769
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSARESdleqdyqaasDHLNLVQTALRQQEKIERYQEDLEELT---ERL-----EEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 770 KAR--LTESR-RNREIAQLKKDQRKR------DHQLRLLEAQKRN---QEVVLR-RKTEEVTALRrqvrpmsdkvagkvt 836
Cdd:COG3096 368 EVVeeAAEQLaEAEARLEAAEEEVDSlksqlaDYQQALDVQQTRAiqyQQAVQAlEKARALCGLP--------------- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 837 rKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVArvqalptpATNGNRKKYQR-KGLTGRVFIS---KTARmkwQL 912
Cdd:COG3096 433 -DLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA--------ARRQFEKAYELvCKIAGEVERSqawQTAR---EL 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 913 LER---------RVTDIIMQKmtisnmeADMNRLLKQREELTKRREKLSKRREKIVKENGEgdknvanINEEMESLTANI 983
Cdd:COG3096 501 LRRyrsqqalaqRLQQLRAQL-------AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-------LEELLAELEAQL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 984 DYINDSISDCQANIMQM----EEAKEEGETLDVTAVI--------------NACTLTEARYLLDHflsMGinkglQAAQK 1045
Cdd:COG3096 567 EELEEQAAEAVEQRSELrqqlEQLRARIKELAARAPAwlaaqdalerlreqSGEALADSQEVTAA---MQ-----QLLER 638
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291167760 1046 EAQIKVLEGRLKQTEITSATQ-NQLLFHMLKEKAELNPELDALLGHALQENVEDSTDEDAP 1105
Cdd:COG3096 639 EREATVERDELAARKQALESQiERLSQPGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAP 699
|
|
| XRCC4 |
pfam06632 |
DNA double-strand break repair and V(D)J recombination protein XRCC4; This family consists of ... |
690-795 |
5.22e-03 |
|
DNA double-strand break repair and V(D)J recombination protein XRCC4; This family consists of several eukaryotic DNA double-strand break repair and V(D)J recombination protein XRCC4 sequences. In the non-homologous end joining pathway of DNA double-strand break repair, the ligation step is catalyzed by a complex of XRCC4 and DNA ligase IV. It is thought that XRCC4 and ligase IV are essential for alignment-based gap filling, as well as for final ligation of the breaks.
Pssm-ID: 369011 [Multi-domain] Cd Length: 336 Bit Score: 40.86 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 690 LGSVESYS-EEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKK-------LQQD-------VMEMK 754
Cdd:pfam06632 112 LGSVKLQKvPEPAEVIRELISYCLDCIAELQAKNEHLQKENERLQRDWNDVTGRLEKcvkakeeLEADlykrfilVLNEK 191
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 291167760 755 KTKVRLMKQMKEEQEKARLTESRRNREIAqlkKDQRKRDHQ 795
Cdd:pfam06632 192 KAKIRSLQKLLNELQESEESTEQKREDPA---TSDRTPDEE 229
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
657-786 |
5.31e-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: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 657 RLQTLKKQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYE-KKLQAMNKELQRLQAAQKEHARLL- 733
Cdd:TIGR02473 6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 291167760 734 KNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 786
Cdd:TIGR02473 86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
645-765 |
6.37e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.18 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 645 QKLIDELENSQKRLQTLKKQYEEklmmlqhkIRDTQ---LER-DQVLQNLGSVE---SYSEEKAKKVRSEYEKKLQAMNK 717
Cdd:pfam10168 578 QSLEEERKSLSERAEKLAEKYEE--------IKDKQeklMRRcKKVLQRLNSQLpvlSDAEREMKKELETINEQLKHLAN 649
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760 718 ELQRLQAAQKEHAR-LLKNQSQY--------EKQLKKLQQDVMEMKKTKVRLMKQMK 765
Cdd:pfam10168 650 AIKQAKKKMNYQRYqIAKSQSIRkksslslsEKQRKTIKEILKQLGSEIDELIKQVK 706
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
644-790 |
6.61e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 644 KQKLIDELENSQKRLQTLKKQYEEKlmmlqhkirdtQLERDQVLqnlgsvesySEEKAKKvrseyekklqamnkelQRLQ 723
Cdd:PRK11637 168 RQETIAELKQTREELAAQKAELEEK-----------QSQQKTLL---------YEQQAQQ----------------QKLE 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760 724 AAQKEHARLLknqSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQR 790
Cdd:PRK11637 212 QARNERKKTL---TGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQK 275
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
642-781 |
6.93e-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: 41.31 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 642 AIKQKLIDELENSQKRlQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL-----GSVESYSE--EKAKKVRSEYEKKLQA 714
Cdd:pfam01576 303 ALKTELEDTLDTTAAQ-QELRSKREQEVTELKKALEEETRSHEAQLQEMrqkhtQALEELTEqlEQAKRNKANLEKAKQA 381
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291167760 715 MNKELQRLQAaqkeharllknqsqyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNRE 781
Cdd:pfam01576 382 LESENAELQA-----------------ELRTLQQAKQDSEHKRKKLEGQLQELQ--ARLSESERQRA 429
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
648-752 |
7.72e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 648 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDtqlERDQVLQNLGSVESYSEEKakkvrseyEKKLQAMNKELQRLQAAQK 727
Cdd:pfam03938 14 SPEGKAAQAQLEKKFKKRQAELEAKQKELQK---LYEELQKDGALLEEEREEK--------EQELQKKEQELQQLQQKAQ 82
|
90 100
....*....|....*....|....*
gi 291167760 728 EharllKNQSQYEKQLKKLQQDVME 752
Cdd:pfam03938 83 Q-----ELQKKQQELLQPIQDKINK 102
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
715-832 |
8.25e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 715 MNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKarltesrRNREIAQLKKDqrkrdh 794
Cdd:pfam03938 7 MQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREE-------KEQELQKKEQE------ 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 291167760 795 qlrLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 832
Cdd:pfam03938 74 ---LQQLQQKAQQELQKKQQELLQPIQDKINKAIKEVA 108
|
|
| F-BAR_Rgd1 |
cd07652 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ... |
699-825 |
8.44e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153336 [Multi-domain] Cd Length: 234 Bit Score: 39.64 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 699 EKAKKVRSEYEKKLQAMNKELQRLqAAQKEHARllKNQSQYEKQL-KKLQQDVMEMKKTKVRLmKQMKEEQEKARLTESR 777
Cdd:cd07652 75 EKLADNGLRFAKALNEMSDELSSL-AKTVEKSR--KSIKETGKRAeKKVQDAEAAAEKAKARY-DSLADDLERVKTGDPG 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291167760 778 R--------NREIAQLKKD-QRK-----RDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 825
Cdd:cd07652 151 KklkfglkgNKSAAQHEDElLRKvqaadQDYASKVNAAQALRQELLSRHRPEAVKDLFDLIL 212
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
653-779 |
9.07e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 40.41 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 653 NSQKrlqTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesYSEEKAKKVRSEYEKKLQAMNKELQrlqAAQKEHARL 732
Cdd:smart00435 266 NHQR---TVSKTHEKSMEKLQEKIKALKYQLKRLKKMI-----LLFEMISDLKRKLKSKFERDNEKLD---AEVKEKKKE 334
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 291167760 733 LKNQSQYEKQLKKLQQDVMEMKKTkvrlmKQMKEEQEKARLTESRRN 779
Cdd:smart00435 335 KKKEEKKKKQIERLEERIEKLEVQ-----ATDKEENKTVALGTSKIN 376
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
684-812 |
9.37e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 38.36 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 684 DQVLQNLGSVESYSEEKAKkVRSEYEKKLQAMNKELQ-RLQA--AQKE-----------HARLLKNQSQYEKQ-----LK 744
Cdd:cd12923 4 EKLAKKLKEINKEYLDKSR-EYDELYEKYNKLSQEIQlKRQAleAFEEavkmfeeqlrtQEKFQKEAQPHEKQrlmenNE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291167760 745 KLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN---REIAQLkkdQRKRDHQLRLLEAQKRNQEVVLRR 812
Cdd:cd12923 83 LLKSRLKELEESKEQLEEDLRKQVAYNRELEREMNslkPELMQL---RKQKDQYLRWLKRKGVSQEEINQL 150
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
646-825 |
9.39e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 646 KLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV---------LQNlgSVESYSEEKA--KKVRSEYEKKLQA 714
Cdd:pfam00038 72 RLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLdeatlarvdLEA--KIESLKEELAflKKNHEEEVRELQA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 715 MNKELQRL----QAAQKEHARLLKN-QSQYEKQLKKLQQDVMEMKKTKVR-----------LMKQMKEEQEKARLTESRR 778
Cdd:pfam00038 150 QVSDTQVNvemdAARKLDLTSALAEiRAQYEEIAAKNREEAEEWYQSKLEelqqaaarngdALRSAKEEITELRRTIQSL 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 291167760 779 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 825
Cdd:pfam00038 230 EIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
710-825 |
9.72e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 40.41 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291167760 710 KKLQAMNKelQRLQAA-----QKEHARLLKNQSQYEKQLKKLQ-----QDVMEMKKTKVRLMKQMKEEQEKARLTESR-R 778
Cdd:pfam15558 18 KEEQRMRE--LQQQAAlaweeLRRRDQKRQETLERERRLLLQQsqeqwQAEKEQRKARLGREERRRADRREKQVIEKEsR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 291167760 779 NREIAQLKKDQRKRDHQLRLLEAQ--KRNQEVVLRRKTEEVTALRRQVR 825
Cdd:pfam15558 96 WREQAEDQENQRQEKLERARQEAEqrKQCQEQRLKEKEEELQALREQNS 144
|
|
| |
