|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
4-368 |
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: 625.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 4 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 83
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 84 GQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVNAQFLELYNEEVLDLFDTTRDid 163
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKD--------TFEFQLKVSFLEIYNEEIRDLLDPETD-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 164 aksKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADN 243
Cdd:cd01372 151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 244 AtdnkiisesaqMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 323
Cdd:cd01372 228 A-----------DDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 30725047 324 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 368
Cdd:cd01372 297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-367 |
7.48e-140 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 434.69 E-value: 7.48e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 11 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAY 83
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 84 GQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKHIaiknglpaPDFKVNAQFLELYNEEVLDLFDTTrdid 163
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 164 aKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIdadn 243
Cdd:pfam00225 143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 244 atdnkiisesaqmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 322
Cdd:pfam00225 218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 30725047 323 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 367
Cdd:pfam00225 282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
5-374 |
8.84e-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: 429.30 E-value: 8.84e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 5 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYN 77
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 78 ATVFAYGQTGAGKTYTMGTgfdvniVEEELGIISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDLFD 157
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 158 ttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcP 237
Cdd:smart00129 147 --------PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITV------E 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 238 QIDADNATDnkiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 317
Cdd:smart00129 213 QKIKNSSSG-------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 30725047 318 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 374
Cdd:smart00129 279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
5-365 |
8.25e-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: 382.76 E-value: 8.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 5 SVRVAVRIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNA 78
Cdd:cd00106 1 NVRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 79 TVFAYGQTGAGKTYTMGTGFDvniveEELGIISRAVKHLFKSIEEKKhiaikngLPAPDFKVNAQFLELYNEEVLDLFDt 158
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRK-------ETKSSFSVSASYLEIYNEKIYDLLS- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 159 trdidaKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpq 238
Cdd:cd00106 147 ------PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHV-------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 239 idadnatDNKIISESAQMnefeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVP 318
Cdd:cd00106 213 -------KQRNREKSGES----VTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN--KHIP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 30725047 319 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 365
Cdd:cd00106 280 YRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
5-367 |
6.75e-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: 335.58 E-value: 6.75e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 5 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGY 76
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 77 NATVFAYGQTGAGKTYTMGtGFDVNivEEELGIISRAVKHLFKSIEEKKHIAiknglpapDFKVNAQFLELYNEEVldlf 156
Cdd:cd01371 82 NGTIFAYGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHIARSQNNQ--------QFLVRVSYLEIYNEEI---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 157 dttRDIDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV-Cqtrv 235
Cdd:cd01371 147 ---RDLLGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeC---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 236 cpqidadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskRAT 315
Cdd:cd01371 220 ---------------SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KST 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 30725047 316 HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 367
Cdd:cd01371 283 HIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
5-367 |
3.59e-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: 331.23 E-value: 3.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 5 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFDIDSQQEQIYI 62
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 63 QCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIEEKKHiaiknglpAPDFKVN 141
Cdd:cd01370 81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLKD--------EKEFEVS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 142 AQFLELYNEEVLDLFDTTrdidakSKKSNIRihEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSR 221
Cdd:cd01370 146 MSYLEIYNETIRDLLNPS------SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 222 SHAIFTIHVCQTrvcpqidadnatdnkiiSESAQMNEfETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALG 301
Cdd:cd01370 218 SHAVLQITVRQQ-----------------DKTASINQ-QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALG 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30725047 302 NVISALGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 367
Cdd:cd01370 280 NCINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
6-369 |
6.60e-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: 329.94 E-value: 6.60e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 6 VRVAVRIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFDIDSQQEQIYIQcIEKLIEGCFEGYNATVF 81
Cdd:cd01366 4 IRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 82 AYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIEEKKHIAIKnglpapdFKVNAQFLELYNEEVLDLFDTTR 160
Cdd:cd01366 83 AYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIRDLLAPGN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 161 didAKSKKSNIRiHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHvcqtrvcpqid 240
Cdd:cd01366 149 ---APQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILH----------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 241 adnatdnkIISESAQMNEfeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKratHVPYR 320
Cdd:cd01366 214 --------ISGRNLQTGE--ISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS---HIPYR 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 30725047 321 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 369
Cdd:cd01366 281 NSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
4-374 |
5.60e-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: 5.60e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 4 SSVRVAVRIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVFD-IDSQ------QEQIYiQC 64
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYWsHDSEdpnyasQEQVY-ED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 65 I-EKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDvniveEELGIISRAVKHLFKSIEEKKHIAIKnglpapdFKVNAQ 143
Cdd:cd01365 80 LgEELLQHAFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 144 FLELYNEEVLDLFDTtrdiDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSH 223
Cdd:cd01365 147 YMEIYNEKVRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 224 AIFTIhvcqtrVCPQIDADNATDNKiisesaqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNV 303
Cdd:cd01365 223 AVFTI------VLTQKRHDAETNLT-----------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKV 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30725047 304 ISALGD-----KSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 374
Cdd:cd01365 286 ISALADmssgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
3-367 |
7.67e-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: 7.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 3 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATV 80
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 81 FAYGQTGAGKTYTMgtgFDVNIVEEELGIISRAVKHLFKSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDTTR 160
Cdd:cd01369 81 FAYGQTSSGKTYTM---EGKLGDPESMGIIPRIVQDIFETIYSMDENL--------EFHVKVSYFEIYMEKIRDLLDVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 161 DidakskksNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQtrvcpqid 240
Cdd:cd01369 150 T--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 241 aDNATDNKIisesaqmnefetLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYR 320
Cdd:cd01369 214 -ENVETEKK------------KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYR 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 30725047 321 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 367
Cdd:cd01369 279 DSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
3-376 |
1.84e-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: 1.84e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 3 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFE 74
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 75 GYNATVFAYGQTGAGKTYTM----GTGFDVNIVEEEL-GIISRAVKHLFKSIEEKKHiaiknglpapDFKVNAQFLELYN 149
Cdd:cd01364 81 GYNCTIFAYGQTGTGKTYTMegdrSPNEEYTWELDPLaGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIYN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 150 EEVLDLFDttrdiDAKSKKSNIRIHEDS--TGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFT 227
Cdd:cd01364 151 EELFDLLS-----PSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 228 IHVcqtrvcpqidadnatdnkIISESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISAL 307
Cdd:cd01364 226 ITI------------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30725047 308 GDKSKratHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 376
Cdd:cd01364 288 VERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
40-507 |
1.74e-90 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 306.28 E-value: 1.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 40 GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLF 118
Cdd:COG5059 53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 119 KSIEEKKHIAiknglpapDFKVNAQFLELYNEEVLDLFDttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMM 198
Cdd:COG5059 126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 199 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqidadnatdnkiisesaQMNEFETLTAKFHFVDLAGSERLK 278
Cdd:COG5059 190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK---------------------NKVSGTSETSKLSLVDLAGSERAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 279 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 358
Cdd:COG5059 249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 359 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQtennNLRVRIKA 437
Cdd:COG5059 328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQ----SLKKETET 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 438 MQETVDALRSRITQLVSDQANHVLARaGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 507
Cdd:COG5059 399 LKSRIDLIMKSIISGTFERKKLLKEE-GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
6-376 |
2.91e-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: 297.50 E-value: 2.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 6 VRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYG 84
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 85 QTGAGKTYTM--GTGFDVNIVEEELGIISRAVKHLFKSI--EEKKHIAIKNglpapdFKVNAQFLELYNEEVLDLFDTTr 160
Cdd:cd01373 83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIqrEKEKAGEGKS------FLCKCSFLEIYNEQIYDLLDPA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 161 didakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqid 240
Cdd:cd01373 156 -------SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 241 adnatdnkIISESAQMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-RATHVP 318
Cdd:cd01373 217 --------TIESWEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVC 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 30725047 319 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 376
Cdd:cd01373 289 YRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
5-367 |
6.61e-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: 292.70 E-value: 6.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 5 SVRVAVRIRPQLAKEKIEGCHICTSVTPG----EPQVFlgkdKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATV 80
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEIDNDtiylVEPPS----TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 81 FAYGQTGAGKTYTMGTGfdvnivEEELGIISRAVKHLFKSIEEKkhiaiknglPAPDFKVNAQFLELYNEEVLDLFDTTr 160
Cdd:cd01374 77 FAYGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDT---------PDREFLLRVSYLEIYNEKINDLLSPT- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 161 didakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqid 240
Cdd:cd01374 141 -------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRI------------ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 241 adnatdnkIISESAQMNEFE--TLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDkSKRATHVP 318
Cdd:cd01374 202 --------TIESSERGELEEgtVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIP 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 30725047 319 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 367
Cdd:cd01374 273 YRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
6-365 |
3.97e-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: 3.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 6 VRVAVRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNAT 79
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 80 VFAYGQTGAGKTYTMGTGFdvniveEELGIISRAVKHLFKSIEEKkhiaiknglpAPDFKVNAQFLELYNEEVLDLFDtt 159
Cdd:cd01376 81 VFAYGSTGAGKTFTMLGSP------EQPGLMPLTVMDLLQMTRKE----------AWALSFTMSYLEIYQEKILDLLE-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 160 rdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqi 239
Cdd:cd01376 143 ------PASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 240 dadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKRATHVPY 319
Cdd:cd01376 208 -----------DQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPY 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 30725047 320 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 365
Cdd:cd01376 274 RDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
6-363 |
1.93e-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: 1.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 6 VRVAVRIRPQLAKEKIEG-CHICTSVTPGEPQVFLGKDK----------AFTFDYVFDIDSQQEQIYIQCIEKLIEGCFE 74
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKeIDVVSVPSKLTLIVHEPKLKvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 75 GYNATVFAYGQTGAGKTYTMGTGFDVNivEEELGIISRAVKHLFksiEEKKHIAIKNGLpapdfKVNAQFLELYNEEVLD 154
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGGDFSGQ--EESKGIYALAARDVF---RLLNKLPYKDNL-----GVTVSFFEIYGGKVFD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 155 LFdttrdidakSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFtihvcqtr 234
Cdd:cd01367 152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAIL-------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 235 vcpQIDADNATDNKiisesaqmnefetLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDKSkr 313
Cdd:cd01367 215 ---QIILRDRGTNK-------------LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-- 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 30725047 314 aTHVPYRDSKLTRLLQDSL-GGNSQTIMIACVSPSDRDFMETLNTLKYANR 363
Cdd:cd01367 277 -AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
42-365 |
6.08e-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: 6.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 42 DKAFTFDYVFDiDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNIVEEelGIISRAVKHLFKSI 121
Cdd:cd01375 47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENYKHR--GIIPRALQQVFRMI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 122 EEKkhiaiknglPAPDFKVNAQFLELYNEEVLDLFDTTRDIDAKSKKsnIRIHEDSTGGIYTVGVTTRTVNTESEMMQCL 201
Cdd:cd01375 123 EER---------PTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 202 KLGALSRTTASTQMNVQSSRSHAIFTIHVCqtrvcpqidadnatdnkiiSESAQMNEFETLTAKFHFVDLAGSERLKRTG 281
Cdd:cd01375 192 FLGETNRIIASHTMNKNSSRSHCIFTIHLE-------------------AHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 282 ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 361
Cdd:cd01375 253 VEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330
|
....
gi 30725047 362 NRAR 365
Cdd:cd01375 331 SRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
6-361 |
4.84e-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: 4.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 6 VRVAVRIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFDIDSQQEQIYIQCIEKLIE 70
Cdd:cd01368 3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 71 GCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnivEEELGIISRAVKHLFKSIeekkhiaiknglpaPDFKVNAQFLELYN 149
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMqGS-------PGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 150 EEVLDLFDTTRDIDAKSKKSnIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIH 229
Cdd:cd01368 142 EYIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 230 VCQtrvcpqidADNATDNKIISESAQMNefetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD 309
Cdd:cd01368 221 LVQ--------APGDSDGDVDQDKDQIT-----VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 30725047 310 KSKRAT--HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 361
Cdd:cd01368 288 NQLQGTnkMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3-400 |
3.93e-63 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 237.53 E-value: 3.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 3 ESSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFA 82
Cdd:PLN03188 97 DSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 83 YGQTGAGKTYTM----GTGFDVNIVEEELGIISRAVKHLFKSIEEKKhiaIKNGLPAPDFKVNAQFLELYNEEVLDLFDT 158
Cdd:PLN03188 172 YGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITDLLDP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 159 TrdidakskKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpq 238
Cdd:PLN03188 249 S--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV-------- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 239 idadnatDNKIISESAQMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK--RATH 316
Cdd:PLN03188 313 -------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRH 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 317 VPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRLQMEL 396
Cdd:PLN03188 384 IPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLRDEL 462
|
....
gi 30725047 397 MEYK 400
Cdd:PLN03188 463 QRVK 466
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1322-1635 |
1.15e-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: 1.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1322 CIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1398
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1399 RDSaKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1477
Cdd:cd00200 81 ETG-ECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1478 VMCLTVDQissGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQ 1555
Cdd:cd00200 138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1556 KDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRI 1633
Cdd:cd00200 209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287
|
..
gi 30725047 1634 WK 1635
Cdd:cd00200 288 WD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1321-1638 |
6.62e-48 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 177.03 E-value: 6.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1321 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsvkycnyTSLVFT------VSTSY 1392
Cdd:COG2319 111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1393 ---IKVWDIrDSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1468
Cdd:COG2319 183 dgtVRLWDL-ATGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1469 GKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTI--QGDNLFSGSRDN 1546
Cdd:COG2319 240 RTLTGHSGSVRSVA---FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1547 GIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFT 1624
Cdd:COG2319 311 TVRLWDLATGKLLR-TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDGRTLAS 389
|
330
....*....|....
gi 30725047 1625 AADDRTVRIWKARN 1638
Cdd:COG2319 390 GSADGTVRLWDLAT 403
|
|
| Rcc_KIF21A |
cd22263 |
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ... |
919-1000 |
9.18e-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: 9.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 919 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 998
Cdd:cd22263 1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80
|
..
gi 30725047 999 AK 1000
Cdd:cd22263 81 AK 82
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1321-1647 |
3.22e-44 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 166.24 E-value: 3.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1321 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVvsvkycnyTSLVFT------VSTSY 1392
Cdd:COG2319 69 ALLATLLGHTAAVLSVAFSPDgrLLASASADGTVRLWDLATGLLLRTLTGHTGAV--------RSVAFSpdgktlASGSA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1393 ---IKVWDIrDSAKCIRTLTSsgqvtlgdacsastsrtvaipsGENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1468
Cdd:COG2319 141 dgtVRLWDL-ATGKLLRTLTG----------------------HSGAVTSVAFSPDGKLLASGSDdGTVRLWDLATGKLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1469 GKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTIQGDN--LFSGSRDN 1546
Cdd:COG2319 198 RTLTGHTGAVRSVA---FSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS------GSVRSVAFSPDGrlLASGSADG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1547 GIKKWDLTQKDLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFT 1624
Cdd:COG2319 269 TVRLWDLATGELLRTLT-GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKTLAS 347
|
330 340
....*....|....*....|...
gi 30725047 1625 AADDRTVRIWkarNLQDGQISDT 1647
Cdd:COG2319 348 GSDDGTVRLW---DLATGELLRT 367
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1321-1595 |
1.05e-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: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1321 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVWD 1397
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1398 IRdSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLG 1476
Cdd:cd00200 164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1477 PVMCLTVDQissgqdliitgskDHYIkmfdvtegalgtvspthnfepphydgiealtiqgdnLFSGSRDNGIKKWDLTQK 1556
Cdd:cd00200 221 GVNSVAFSP-------------DGYL------------------------------------LASGSEDGTIRVWDLRTG 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 30725047 1557 DLLQQVPnAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1595
Cdd:cd00200 252 ECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1311-1643 |
1.20e-34 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 138.12 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1311 ASKGIRAFPLQCIHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKY-CNYTSLVFT 1387
Cdd:COG2319 17 ALALLAAALGALLLLLLGLAAAVASLAasPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFsPDGRLLASA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1388 VSTSYIKVWDIrDSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWDLKRFQ 1466
Cdd:COG2319 97 SADGTVRLWDL-ATGLLLRTLTGH----------------------TGAVRSVAFSPDGKTLASGSAdGTVRLWDLATGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1467 STGKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALTI--QGDNLFSGSR 1544
Cdd:COG2319 154 LLRTLTGHSGAVTSVA---FSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT------GAVRSVAFspDGKLLASGSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1545 DNGIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHI 1622
Cdd:COG2319 225 DGTVRLWDLATGKLLR-TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFspDGKLL 303
|
330 340
....*....|....*....|.
gi 30725047 1623 FTAADDRTVRIWkarNLQDGQ 1643
Cdd:COG2319 304 ASGSDDGTVRLW---DLATGK 321
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1427-1647 |
1.21e-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: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1427 TVAIPSGENQINQIALNPTGTFLYAASGNA-VRMWDLKRFQSTGKLTGHLGPVmcLTVDQISSGQdLIITGSKDHYIKMF 1505
Cdd:cd00200 2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGELLRTLKGHTGPV--RDVAASADGT-YLASGSSDKTIRLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1506 DvtegaLGTVSPTHNFEPpHYDGIEALTIQGDN--LFSGSRDNGIKKWDLTQKDLLQqVPNAHKDWVCALGVVPDHPVLL 1583
Cdd:cd00200 79 D-----LETGECVRTLTG-HTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLT-TLRGHTDWVNSVAFSPDGTFVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30725047 1584 SGCRGGILKVWNMDTFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIWkarNLQDGQISDT 1647
Cdd:cd00200 152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFspDGEKLLSSSSDGTIKLW---DLSTGKCLGT 214
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
919-1000 |
9.25e-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: 9.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 919 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEgDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 998
Cdd:cd22248 1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDEGKD-ESVLRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79
|
..
gi 30725047 999 AK 1000
Cdd:cd22248 80 SK 81
|
|
| Rcc_KIF21B |
cd22262 |
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ... |
919-1000 |
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 30725047 919 QKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEE 998
Cdd:cd22262 1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80
|
..
gi 30725047 999 AK 1000
Cdd:cd22262 81 TK 82
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
5-155 |
2.74e-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: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 5 SVRVAVRIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYiQCIEKLIEGCFEGYNATVFAYG 84
Cdd:pfam16796 21 NIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30725047 85 QTGAGKTYTMgtgfdvniveeelgiISRAVKHLFKSIEEKKhiaiknglPAPDFKVNAQFLELYNEEVLDL 155
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 ... |
1320-1461 |
1.88e-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: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1320 LQCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVST-SYIKVW 1396
Cdd:cd00200 167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30725047 1397 DIRdSAKCIRTLTSSgqvtlgdacsastsrtvaipsgENQINQIALNPTGTFLYAASG-NAVRMWD 1461
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 ... |
8-306 |
7.44e-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: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 8 VAVRIRPQLAKEKIEGCHIctsvtpgepqvflgkdkaFTFDYVFDIDSQQEQIYIQCiEKLIEGCFEGYN-ATVFAYGQT 86
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKI------------------IVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 87 GAGKTYTMgtgfdvniveeeLGIISRAVKHLFKSIEEKKhiaiknglpapdfkvnaqflelyneevldlfdttrdidaks 166
Cdd:cd01363 62 GAGKTETM------------KGVIPYLASVAFNGINKGE----------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 167 kksnirihEDStggiyTVGVTTRTVNTESEMMQCLKLGALSRtTASTQMNVQSSRSHAIFTIhvcqtrvcpqidadnatd 246
Cdd:cd01363 89 --------TEG-----WVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------ 136
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 247 nkiisesaqmnefetltakfhFVDLAGSERlkrtgatgerakegisINCGLLALGNVISA 306
Cdd:cd01363 137 ---------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
623-843 |
2.81e-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: 67.48 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 623 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRS 702
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 703 EYEKKLQAMNKELQRLQAA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 773
Cdd:COG4942 101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30725047 774 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQ 843
Cdd:COG4942 181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
385-1021 |
3.08e-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: 65.13 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 385 LRSEITRLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRSRITQLvsdqaNHVLA 462
Cdd:pfam05483 204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL-----EEKTK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 463 RAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArapyfsgsstfspTILSSDKETIEIIDLAKKDLE 542
Cdd:pfam05483 279 LQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK-------------TICQLTEEKEAQMEELNKAKA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 543 KLKRKEKRKKKSVAGKEDNTDTDQEKKEEkgvSERENNELEVEESQEVSDhedeeeeeeeeeddidggessdeSDSESDE 622
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLEK---NEDQLKIITMELQKKSSE-----------------------LEEMTKF 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 623 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVRS 702
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 703 EYEKKlQAMNKEL-QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 779
Cdd:pfam05483 479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 780 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLSSSDApAQDTGSSAAAVET 854
Cdd:pfam05483 558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEELHQENK-ALKKKGSAENKQL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 855 DASRTGAqQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERrvtdIIMQKmtisnmEADMnRLL 934
Cdd:pfam05483 632 NAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK-RCQ 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 935 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYindSISDCQANIM----QMEEAKEEGETLDVTA 1010
Cdd:pfam05483 700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKLKMEA 776
|
650
....*....|.
gi 30725047 1011 VINACTLTEAR 1021
Cdd:pfam05483 777 KENTAILKDKK 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
623-1006 |
1.20e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 623 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 699
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 700 VRSEYEKKLQAMNKELQRLQaaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 777
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIE---EEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 778 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAA---- 850
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkg 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 851 ---AVETDASRTGAQQKMRIPVAR-VQALPTPATNGNRKKYQR-----KGLTGRVFISKTARMKW-------QLLERRVT 914
Cdd:PRK03918 540 eikSLKKELEKLEELKKKLAELEKkLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYlelkdaeKELEREEK 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 915 DIIMQKMTISNMEADMNRLLKQREELTKRREKLSKR-----REKIVKENGEGDKNVANINEEMESLTANIDYINDSISDC 989
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
410
....*....|....*..
gi 30725047 990 QANIMQMEEAKEEGETL 1006
Cdd:PRK03918 700 KEELEEREKAKKELEKL 716
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
626-829 |
2.85e-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: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 626 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYE 705
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 706 KKLQAMNkelQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---RE 777
Cdd:TIGR02168 365 AELEELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAE 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30725047 778 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 829
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
628-1014 |
6.19e-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: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 628 ADLANITCEIAIKQKLIDELENSQKRLQTLKKQyEEKLMMLQHKIRDTQlerdqvlqnlGSVESYSEEKAKKVRSEYEKK 707
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYE----------GYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 708 LQAMNKELQ----RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQmkeeqekarltesrrnrEIAQLKK 783
Cdd:TIGR02169 246 LASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA-----------------EIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 784 DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQ 863
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 864 KmripvARVQALptpatngnrKKYQRKgltgRVFISKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLKQREELTKR 943
Cdd:TIGR02169 388 K-----DYREKL---------EKLKRE----INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30725047 944 REKLSKRREKIVKEngegdknVANINEEMESLTANIDYINDSISDCQANIMQMEEAK-----EEGETLDVTAVINA 1014
Cdd:TIGR02169 450 IKKQEWKLEQLAAD-------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKA 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
625-828 |
3.72e-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: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 625 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAKKVR 701
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 702 SEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-ARLTESRRN----- 775
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEEleeli 868
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30725047 776 ----REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 828
Cdd:TIGR02168 869 eeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
652-813 |
4.87e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 652 KRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAmnKELQRLQAAQKEHARLLKN 731
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 732 QSQYEKQLKKLQQDVMEMKKTKVRLMKqmKEEQEKARLTESRRNREiaqlkkDQRKRDHQLRLLEAQKRNQEVVLRRKTE 811
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAK--KAEEDKKKAEEAKKAEE------DEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
..
gi 30725047 812 EV 813
Cdd:PTZ00121 1714 EK 1715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
565-851 |
5.76e-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: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 565 DQEKKEEKGVSERENNELEVEESQevsdhedeeeeeeEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLI 644
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAE-------------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 645 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV---LQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAA 721
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELeeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 722 QKEHARLLKNQSQYEKQLKKLQQdvmeMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRN 801
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEE----AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 30725047 802 QEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAA 851
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
623-863 |
9.39e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 623 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL---GSVESYSEE--KA 697
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVllGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 698 KKVrSEYEKKLQAMNkelqRLQAAQKEharLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 777
Cdd:COG3883 112 ESF-SDFLDRLSALS----KIADADAD---LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 778 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDAS 857
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
|
....*.
gi 30725047 858 RTGAQQ 863
Cdd:COG3883 264 AAGAAA 269
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
467-1160 |
2.22e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 467 GNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArapyfsgssTFSPTILSSDKETIEIIDLAKKDLEKLKR 546
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVI---------DLQTKLQEMQMERDAMADIRRRESQSQED 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 547 KEKRKKKSV-------AGKED-----NTDTDQEKK----EEKGVSERENNELEVEES--QEVSDHEDEEEEEEEEEDDID 608
Cdd:pfam15921 143 LRNQLQNTVheleaakCLKEDmledsNTQIEQLRKmmlsHEGVLQEIRSILVDFEEAsgKKIYEHDSMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 609 GGEssdesdsesdekanyqadLANITCEIAIKQKLIDELENsqkRLQTLKKQYEEK--LMMLQHKIRDTQLERDQVLQNL 686
Cdd:pfam15921 223 SKI------------------LRELDTEISYLKGRIFPVED---QLEALKSESQNKieLLLQQHQDRIEQLISEHEVEIT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 687 GSVesyseEKAKKVRSEyekkLQAMNKELQRLQaaqkEHARllkNQ-SQYEKQLKKLQQDVMEMkKTKVRLMKQMK---- 761
Cdd:pfam15921 282 GLT-----EKASSARSQ----ANSIQSQLEIIQ----EQAR---NQnSMYMRQLSDLESTVSQL-RSELREAKRMYedki 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 762 EEQEK------ARLTESRRNREiaQLKKDQRKRDHQLRLLEA--QKRNQEVVLRRKTEEvtalRRQVRPMSDKVA-GKVT 832
Cdd:pfam15921 345 EELEKqlvlanSELTEARTERD--QFSQESGNLDDQLQKLLAdlHKREKELSLEKEQNK----RLWDRDTGNSITiDHLR 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 833 RKLSSSDAPAQDTGSSAAAVETDasrtgAQQKMRIPVARVQAlptpatnGNRKKYQRKGLTGRVFISKtarmkwQLLERR 912
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSE-----CQGQMERQMAAIQG-------KNESLEKVSSLTAQLESTK------EMLRKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 913 VTDIIMQKMTISNME---ADMNRLLKQRE--------ELTKRREKLSKRREKIVKENGEGDkNVANINEEMESLTAN--- 978
Cdd:pfam15921 481 VEELTAKKMTLESSErtvSDLTASLQEKEraieatnaEITKLRSRVDLKLQELQHLKNEGD-HLRNVQTECEALKLQmae 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 979 ----IDYINDSISDCQ---------ANIMQMEEAKEEGETLDvtaviNACTLTEARYLLDhflsmginkglqaaQKEAQI 1045
Cdd:pfam15921 560 kdkvIEILRQQIENMTqlvgqhgrtAGAMQVEKAQLEKEIND-----RRLELQEFKILKD--------------KKDAKI 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1046 KVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALlghalqdldsvpLENVEDSTDEdapLNSpgsegstLSSDLMK 1125
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL------------LNEVKTSRNE---LNS-------LSEDYEV 678
|
730 740 750
....*....|....*....|....*....|....*.
gi 30725047 1126 LCGEVKPKNKARRRTTTQMEL-LYADSSELASDTST 1160
Cdd:pfam15921 679 LKRNFRNKSEEMETTTNKLKMqLKSAQSELEQTRNT 714
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
627-821 |
2.48e-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: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 627 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRD-TQLERDQVLQNLGSvesySEEKAKKVRSEYE 705
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQA----ELSKLEEEVSRIE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 706 KKLQAMNKELQRL----QAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRnreiAQL 781
Cdd:TIGR02169 812 ARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDL 887
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30725047 782 KKDQRKRDHQLRllEAQKRNQEVVLRRKTEEVTALRRQVR 821
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 ... |
360-819 |
2.63e-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: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 360 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 433
Cdd:pfam10174 280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 434 RIKAMQETVDALRSRITQLVSDQanhvlaraGEGNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 503
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEK--------STLAGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 504 trataRAPYFSGSSTFSPTILSSDKETieiidLAKKDLEKLKRKEKRKKKSVAGKEDNTDTDQEKKEEK--------GVS 575
Cdd:pfam10174 423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKekvsalqpELT 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 576 ERENNELEVEE--SQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENSQKR 653
Cdd:pfam10174 493 EKESSLIDLKEhaSSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVARYK 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 654 LQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSEEKAKKvRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQ 732
Cdd:pfam10174 572 EESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLTLRQMKE-QNKKVANIKHGQQEMKKKGAQLLEEARRREDN 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 733 SQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEVVL- 806
Cdd:pfam10174 648 LADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEALLa 716
|
490 500 510
....*....|....*....|....*....|..
gi 30725047 807 -----------------RRKT--EEVTALRRQ 819
Cdd:pfam10174 717 aisekdaniallelsssKKKKtqEEVMALKRE 748
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1321-1356 |
1.14e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 46.57 E-value: 1.14e-06
10 20 30
....*....|....*....|....*....|....*...
gi 30725047 1321 QCIHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1356
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
640-820 |
1.27e-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: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 640 KQKLIDELENSQK-------RLQTLKKQ---YEEKLMMLQHkiRDTQLERDQVlqnlgsvESYSEEKAKKVRSEYEKKLQ 709
Cdd:pfam17380 305 KEEKAREVERRRKleeaekaRQAEMDRQaaiYAEQERMAME--RERELERIRQ-------EERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 710 AMnKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESR-----RNREIAQLKKD 784
Cdd:pfam17380 376 RM-RELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeeRAREMERVRLE 454
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30725047 785 QRKRDHQLRLL---EAQKRNQEVVL---RRKTEEVTALRRQV 820
Cdd:pfam17380 455 EQERQQQVERLrqqEEERKRKKLELekeKRDRKRAEEQRRKI 496
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
695-821 |
1.48e-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: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 695 EKAKKVRSEYEKKLQamnkelqrlqaaqkeharllknqsQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRR 774
Cdd:pfam20492 2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 30725047 775 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 821
Cdd:pfam20492 58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
636-828 |
2.55e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 636 EIAIKQKL-IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEE--KAKKVRSEYEKKLQAMN 712
Cdd:PRK03918 148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 713 KELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARltesrRNREIAQLKKDQRKRDHQL 792
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-----ELKELKEKAEEYIKLSEFY 302
|
170 180 190
....*....|....*....|....*....|....*.
gi 30725047 793 RLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 828
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
637-853 |
2.55e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 637 IAIKQKLIDELEnsqKRLQTLKKQYEEklmmLQhKIRDTQLERDQVLQNLgsvESYSEEKaKKVRSeYEKKLQAMNKELQ 716
Cdd:COG4913 612 LAALEAELAELE---EELAEAEERLEA----LE-AELDALQERREALQRL---AEYSWDE-IDVAS-AEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 717 RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKARltesRRNREIAQLKKDQRKRDHQLR 793
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLekeLEQAEEELDELQ----DRLEAAEDLARLELRALLEER 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30725047 794 LLEAQKRNQEVVLRRK-TEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVE 853
Cdd:COG4913 755 FAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
636-953 |
3.62e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 636 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESysEEKAKKVRSEYEKKlqamnKEL 715
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKK-----KAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 716 QRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRD-HQLRL 794
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 795 LEAQKRNQEvvLRRKTEEV-TALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAV-ETDASRTGAQQKMRIPVARV 872
Cdd:PTZ00121 1374 EEAKKKADA--AKKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkKADEAKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 873 QALPTPATNGNRKKYQRKgltgrvfiSKTARMKWQLLERRVTDIIMQKMTISNMEADMnrlLKQREELTKRREKLSKRRE 952
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEA--------KKADEAKKKAEEAKKADEAKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEE 1520
|
.
gi 30725047 953 K 953
Cdd:PTZ00121 1521 A 1521
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1319-1356 |
3.64e-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: 3.64e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 30725047 1319 PLQCIHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1356
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
475-1054 |
4.46e-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: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 475 IHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARapyfsgsstfsptiLSSDKETIEIIDLAKKDLEKLKRKEKRKKKS 554
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAE--------------LAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 555 VAGKEDNTDTDQEKKEEKgVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANIT 634
Cdd:COG1196 293 LLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 635 CEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKE 714
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-ALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 715 LQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQMKEEQEKARLTESRRNREiAQLKKDQRKRDHQLRL 794
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLLLEAEADYEGFLEGVKA-ALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 795 LeaqkRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQA 874
Cdd:COG1196 529 L----IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 875 LPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTD--IIMQKMTISNMEADMNRLLKQREELTKRREKLSKRRE 952
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 953 KIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDvtavinacTLTEARYLLDHFLSMGI 1032
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE--------ELLEEEELLEEEALEEL 756
|
570 580
....*....|....*....|..
gi 30725047 1033 NKGLQAAQKEAQIKVLEGRLKQ 1054
Cdd:COG1196 757 PEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-1091 |
4.83e-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: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 696 KAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 771
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 772 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEvvlRRKTEEVTALRRQVRPMSDKVAGKvtRKLSSSDAPAQDTgssaaA 851
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQK--QILRERLANLERQ-----L 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 852 VETDASRTGAQQKMRIPVARVQALptpATNGNRKKYQRKGLTGRVfisKTARMKWQLLERRVTDIIMQkmtISNMEADMN 931
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 932 RLLKQREELTKRREKLSKRREKIVKENgegDKNVANINEEMESLTANidYINDSISDCQANIMQMEEAKEEGETLDVTAV 1011
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1012 INACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE--- 1079
Cdd:TIGR02168 465 ELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGyea 537
|
410
....*....|...
gi 30725047 1080 -LDALLGHALQDL 1091
Cdd:TIGR02168 538 aIEAALGGRLQAV 550
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1598-1635 |
6.82e-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: 6.82e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 30725047 1598 TFMPVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIWK 1635
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
640-809 |
7.54e-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: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 640 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsVESYSEEKAKKVRSEYEKKLQaMNKELQRLQ 719
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKAR-QRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 720 AAQKEHARLLKnqsqyEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL---KKDQRKRDHQLRLLE 796
Cdd:pfam13868 242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316
|
170
....*....|...
gi 30725047 797 AQKRNQEVVLRRK 809
Cdd:pfam13868 317 GERLREEEAERRE 329
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
646-828 |
9.86e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 646 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVE---SYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQ 722
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAReelEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 723 KEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLM---KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 799
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170 180
....*....|....*....|....*....
gi 30725047 800 RNQEvvLRRKTEEVTALRRQVRPMSDKVA 828
Cdd:COG4372 174 QALS--EAEAEQALDELLKEANRNAEKEE 200
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
678-838 |
1.22e-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: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 678 ERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAaqkeHARLLKNQsqyekqLKKLQQDVMEMKKtKVRLM 757
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA----EVEELEAE------LEEKDERIERLER-ELSEA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 758 KQmkEEQEKARLTE--SRRNREIAQLKKdqrkrdhqlRLLEAQKRNQEvvLRRKTEEVTALRRQVRpMSDKVAGKVTRKL 835
Cdd:COG2433 454 RS--EERREIRKDReiSRLDREIERLER---------ELEEERERIEE--LKRKLERLKELWKLEH-SGELVPVKVVEKF 519
|
...
gi 30725047 836 SSS 838
Cdd:COG2433 520 TKE 522
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
671-986 |
1.54e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 671 KIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMK 750
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 751 K---TKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV 827
Cdd:COG4372 87 EqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 828 AGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQ 907
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 908 LLE------RRVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDY 981
Cdd:COG4372 247 DKEelleevILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
....*
gi 30725047 982 INDSI 986
Cdd:COG4372 327 KLELA 331
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
666-809 |
1.81e-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: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 666 MMLQHKIRDTQLERdqvlqnlGSVESYSEEKAKKVRsEYEKKLQAMnKELQRLQAAQKEhARLLKNQSQYEKQLKKLQQD 745
Cdd:pfam13904 38 LTYARKLEGLKLER-------QPLEAYENWLAAKQR-QRQKELQAQ-KEEREKEEQEAE-LRKRLAKEKYQEWLQRKARQ 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30725047 746 vmemkKTKVRLMKQMKEEQEKARLTESRRNREIAQ-----------LKKDQRKRDHQLRLLEAQKRNQEVVLRRK 809
Cdd:pfam13904 108 -----QTKKREESHKQKAAESASKSLAKPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
627-812 |
3.38e-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: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 627 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYE------EKLMMLQHKIRdtQLERDQVLQnlgsvesysEEKAKKV 700
Cdd:pfam17380 326 QAEMDRQAAIYAEQERMAMERERELERIRQEERKRElerirqEEIAMEISRMR--ELERLQMER---------QQKNERV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 701 RSEyekkLQAMNKelQRLQaaQKEHARLLKNQSQYEKQLKKLQQdvmEMKKTKVRLMKQMKE-EQEKARLTESRRNREIA 779
Cdd:pfam17380 395 RQE----LEAARK--VKIL--EEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERArEMERVRLEEQERQQQVE 463
|
170 180 190
....*....|....*....|....*....|....*
gi 30725047 780 QLKKDQRKRDHQLRLLEAQKRNQEVV--LRRKTEE 812
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAeeQRRKILE 498
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
639-811 |
3.68e-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: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 639 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKvrseyEKKLQAMNKELQRL 718
Cdd:pfam14988 23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQ-----EREIQDLEEEKEKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 719 QAA-----QKEHARLLKNQSQYEKQLKklQQDVMEM---KKTKVRLMKQMKEEQEKARLTESRRN--REIAQLKKDQRKR 788
Cdd:pfam14988 98 RAEtaekdREAHLQFLKEKALLEKQLQ--ELRILELgerATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQL 175
|
170 180
....*....|....*....|...
gi 30725047 789 DHQLRLLEAQKRNQEvvlRRKTE 811
Cdd:pfam14988 176 IQETQALEAIKSKLE---NRKQR 195
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
652-804 |
3.74e-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: 47.67 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 652 KRLQTLKKQYEEK-------LMMLQHKIR------DTQLERDQVLqnlgsvesysEEKAKKVRSEYEKKlQAMNKELQRL 718
Cdd:pfam02841 155 EERDKLEAKYNQVprkgvkaEEVLQEFLQskeaveEAILQTDQAL----------TAKEKAIEAERAKA-EAAEAEQELL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 719 QAAQKEHARLLKNQ-SQYEKQLKKLQQDvMEMKKtkvrlmKQMKEEQEkaRLTESRRNREIAQLKKDQRKrdhqlrllEA 797
Cdd:pfam02841 224 REKQKEEEQMMEAQeRSYQEHVKQLIEK-MEAER------EQLLAEQE--RMLEHKLQEQEELLKEGFKT--------EA 286
|
....*..
gi 30725047 798 QKRNQEV 804
Cdd:pfam02841 287 ESLQKEI 293
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1601-1634 |
3.97e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 42.33 E-value: 3.97e-05
10 20 30
....*....|....*....|....*....|....*.
gi 30725047 1601 PVGEMKGHDSPINAICV--NSTHIFTAADDRTVRIW 1634
Cdd:pfam00400 3 LLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVW 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
636-821 |
4.04e-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: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 636 EIAIKQKLIDELENSQKRLQTLKKQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYE 705
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 706 KKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkVRLMKQMKEE--QEKARLTES-RRNREIAQLK 782
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREwpAETADLDADlESLPEYLALL 821
|
170 180 190
....*....|....*....|....*....|....*....
gi 30725047 783 KDQRKRDhqlrLLEAQKRNQEVVLRRKTEEVTALRRQVR 821
Cdd:COG4913 822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
644-798 |
4.25e-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: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 644 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAM--NKELQrlqAA 721
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYE---AL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30725047 722 QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 798
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
627-1022 |
4.90e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 627 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQY---------EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 697
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 698 KKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 777
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 778 IA-----QLKKDQRKRDHQLRLLEAQ-------------KRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSD 839
Cdd:COG4717 254 IAaallaLLGLGGSLLSLILTIAGVLflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 840 APAQDTGSS----AAAVETDASRTGAQQKMRIPV--ARVQALPTPATNGNRKKYQRKGLTGRVFISKTARmkWQLLERRV 913
Cdd:COG4717 334 LSPEELLELldriEELQELLREAEELEEELQLEEleQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE--LEELEEQL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 914 TDI------IMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENG--EGDKNVANINEEMESLTANIDYINDS 985
Cdd:COG4717 412 EELlgeleeLLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEE 491
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 30725047 986 ISDCQANIMQMEEAKEEGETLDVTAVINA-----CTLTEARY 1022
Cdd:COG4717 492 WAALKLALELLEEAREEYREERLPPVLERaseyfSRLTDGRY 533
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
644-882 |
5.17e-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: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 644 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesyseEKAKKVRSEYEKKLQAMNKELQRLQAAQK 723
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------EALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 724 EHARLLKNQSQYEKQLKKL---------------QQDVMEMKKTKVRLMKQMKEEQEKArltESRRNREIAQLKKDQRKR 788
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 789 DHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIP 868
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250
....*....|....
gi 30725047 869 VARVQALPTPATNG 882
Cdd:COG3883 247 AGAGAAGAAGAAAG 260
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-724 |
5.27e-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: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 362 NRARNIKNkvmvnqdrASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 441
Cdd:TIGR02168 674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 442 VDALRSRITQLVSDqanhvLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARapyfsgsstfsp 521
Cdd:TIGR02168 735 LARLEAEVEQLEER-----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE------------ 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 522 tiLSSDKETI-----EIIDLAKKDLEKLKRKEKRKKKSVAGKEDNTDTDQEKKEEKGvsERENNELEVEESQEvsdhede 596
Cdd:TIGR02168 798 --LKALREALdelraELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE--DIESLAAEIEELEE------- 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 597 eeeeeeeeddiDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQ 676
Cdd:TIGR02168 867 -----------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 30725047 677 LERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 724
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
662-809 |
5.30e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 662 EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQA----AQKEHARLLKNQSQYEK 737
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEReierLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 738 QLKKL-------QQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRN--QEVVLRR 808
Cdd:COG4913 367 LLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNipARLLALR 446
|
.
gi 30725047 809 K 809
Cdd:COG4913 447 D 447
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
678-1007 |
5.57e-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: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 678 ERDQVLQNLGSvesyseekAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQyekqlkKLQQDVMEMKKTKVRLM 757
Cdd:pfam12128 605 RLDKAEEALQS--------AREKQAAAEEQLVQANGELEKASREETFARTALKNARL------DLRRLFDEKQSEKDKKN 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 758 KQMKEEQEKArltesrrNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrkTEEVTALRRQVRPMSDKVAgkvtrklss 837
Cdd:pfam12128 671 KALAERKDSA-------NERLNSLEAQLKQLDKKHQAWLEEQKEQKREAR--TEKQAYWQVVEGALDAQLA--------- 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 838 sdapAQDTGSSAAAVETDASRTGAQQKMRIPVArvqALPTPATNGNRKKYQRKGLTGRvfISKTARMKWQLLERRVtdiI 917
Cdd:pfam12128 733 ----LLKAAIAARRSGAKAELKALETWYKRDLA---SLGVDPDVIAKLKREIRTLERK--IERIAVRRQEVLRYFD---W 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 918 MQ----------KMTISNMEADMNRLlkqREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSIS 987
Cdd:pfam12128 801 YQetwlqrrprlATQLSNIERAISEL---QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
|
330 340
....*....|....*....|
gi 30725047 988 DCQANimqmEEAKEEGETLD 1007
Cdd:pfam12128 878 DANSE----QAQGSIGERLA 893
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
641-772 |
6.38e-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: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 641 QKLIDELENSQKRLQTLKKQYEEklmmlQH-KIRDTQLERDQVLQNLgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQ 719
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30725047 720 AAQKEHARLLKNQSQYEKQLKKLQQDVmemkKTKVRLMKQMKEEQEKARLTES 772
Cdd:COG3206 334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
669-812 |
6.58e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 669 QHKIRDTQLERDQVLQN-LGSVESYSEEK-------AKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQY----E 736
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30725047 737 KQLKKLQQDVMEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQrKRDHQLRLLEAQKRNQEVVLRRKTEE 812
Cdd:PRK12704 110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
691-1054 |
8.97e-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: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 691 SYSEEKAKKVRSEYEKKLQAMNKELQRLQA----AQKEHARLLKNQSQYEKQLKKLQQDVMEMKktkvRLMKQMKEEQEK 766
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEkiaeLEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 767 ARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSDAPAQDTG 846
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-ALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 847 SSAAAVETDASRTGAQQKMripvarvqalptpatngnrkkyqrkgltgrvfisktarmkwqlLERRVTDIIMQkmtISNM 926
Cdd:TIGR02168 817 EEAANLRERLESLERRIAA-------------------------------------------TERRLEDLEEQ---IEEL 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 927 EADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIM----QMEEAKEE 1002
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEelreKLAQLELR 930
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 30725047 1003 GETLDVTAVINACTLTE-ARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1054
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
645-819 |
1.12e-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: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 645 DELENSQKRLQTLKKQyeeklmmlqHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 724
Cdd:COG3206 189 KELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELES-QLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 725 H------ARLLKNQSQYEKQLKKLQQ-------DVMEMKKTKVRLMKQMKEEQEKArLTESRRNREIAQLKKD---QRKR 788
Cdd:COG3206 259 LlqspviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRI-LASLEAELEALQAREAslqAQLA 337
|
170 180 190
....*....|....*....|....*....|.
gi 30725047 789 DHQLRLLEAQKRNQEvvLRRKTEEVTALRRQ 819
Cdd:COG3206 338 QLEARLAELPELEAE--LRRLEREVEVAREL 366
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
469-813 |
1.22e-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: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 469 EEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARApyfsgsstfsptilssDKETIEIIDLAKKDLEKLKRKE 548
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI----------------KDLGEEEQLRVKEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 549 KRKKKSVAGKEDNTDtDQEKKEEKGVSERENNELEVEESQEvsdhedeeeeeeeeeddidggessdesdsesdEKANYQA 628
Cdd:TIGR02169 304 ASLERSIAEKERELE-DAEERLAKLEAEIDKLLAEIEELER--------------------------------EIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 629 DLANITCEIAIKQK----LIDELENSQKRLQTLK---KQYEEKLMMLQHKIRDTQLERDQVLqnlgsvesyseEKAKKVR 701
Cdd:TIGR02169 351 RRDKLTEEYAELKEeledLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKRELDRLQ-----------EELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 702 SEyekkLQAMNKELQRLQAAQKE-HARLLKNQSQYEKQLKKLQQDVMEMKktkvrlmkqmKEEQEKARLTEsrrnrEIAQ 780
Cdd:TIGR02169 420 EE----LADLNAAIAGIEAKINElEEEKEDKALEIKKQEWKLEQLAADLS----------KYEQELYDLKE-----EYDR 480
|
330 340 350
....*....|....*....|....*....|....*
gi 30725047 781 LKKDQRKRDHQLRLLEAQKR--NQEVVLRRKTEEV 813
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
651-815 |
1.25e-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: 46.48 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 651 QKRLQTLKKQYEEKLmmlqhkirDTQLERDQvlqnlgsvESYSEE-KAKKVRSEYEKKLQAMNKELQRLQ-AAQKEHARL 728
Cdd:pfam15709 360 QRRLQQEQLERAEKM--------REELELEQ--------QRRFEEiRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 729 lkNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQlrlLEAQKRNQEVVLRR 808
Cdd:pfam15709 424 --QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ---EAEEKARLEAEERR 498
|
....*..
gi 30725047 809 KTEEVTA 815
Cdd:pfam15709 499 QKEEEAA 505
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
706-826 |
1.35e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 706 KKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNREIAQLKK 783
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 30725047 784 dQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 826
Cdd:COG4717 151 -LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
640-821 |
1.43e-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: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 640 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQ 719
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 720 AAQKEH--ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-----QMKEEqEKARLTESRRNREIAQLKKDQRKRDHQL 792
Cdd:pfam13868 198 DEKAERdeLRAKLYQEEQERKERQKEREEAEKKARQRQELQqareeQIELK-ERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
170 180
....*....|....*....|....*....
gi 30725047 793 RLLEAQKRNQevvlrRKTEEVTALRRQVR 821
Cdd:pfam13868 277 EQEEAEKRRM-----KRLEHRRELEKQIE 300
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
639-778 |
1.90e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 639 IKQKLiDELENSQKRLQtlkkQYEEklmMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVRSEYEKKLQAMNKELQRL 718
Cdd:PRK12704 77 LRERR-NELQKLEKRLL----QKEE---NLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIEEQLQELERI 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 719 QAAQKEHARllknqsqyEKQLKKLQqdvmemKKTKVRLMKQMKEEQEKARLTESRRNREI 778
Cdd:PRK12704 148 SGLTAEEAK--------EILLEKVE------EEARHEAAVLIKEIEEEAKEEADKKAKEI 193
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
640-799 |
2.36e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.87 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 640 KQKLidELENSQKRLQtLKKQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVESYSEEKAKKVRSEYEK 706
Cdd:pfam03528 24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSENTKQEAIDEVKS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 707 KLQamnKELQRLQAAQKE---------HARLLKNQSQYEKQLKKLQQDVMEMKKtkvRL------------MKQMKEEQE 765
Cdd:pfam03528 101 QWQ---EEVASLQAIMKEtvreyevqfHRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAE 174
|
170 180 190
....*....|....*....|....*....|....
gi 30725047 766 KARLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 799
Cdd:pfam03528 175 KLRSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
|
|
| mS26_PET12 |
cd23703 |
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ... |
700-794 |
3.18e-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: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 700 VRSEYEKKLQAMNKELQRLQAAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkqmkEEQEKARLTESRRN 775
Cdd:cd23703 67 LRELEERKLKTEELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT-----DPEREERAAKRRAN 138
|
90
....*....|....*....
gi 30725047 776 REIAQLKKDQRKRDHQLRL 794
Cdd:cd23703 139 REAKELAKKEARADALHEL 157
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
682-819 |
3.77e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 682 VLQNLGSVESYSEEKAKKVRSEyekKLQAMNKELQRLQAAQKEHARL---LKNQSQYEKqlKKLQQDVME-MKKTKVRLM 757
Cdd:pfam15709 305 VTGNMESEEERSEEDPSKALLE---KREQEKASRDRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMREELE 379
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30725047 758 KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 819
Cdd:pfam15709 380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
642-809 |
4.12e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 642 KLIDELENSQKRLQTLKKQYEEKL------MMLQHKIRDTQL----ERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAM 711
Cdd:PRK11637 103 KQIDELNASIAKLEQQQAAQERLLaaqldaAFRQGEHTGLQLilsgEESQRGERILAYFGYLNQARQETIAELKQTREEL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 712 NKELQRLQAAQKEHARLLKNQSQyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNR-----EIAQLKKDQR 786
Cdd:PRK11637 183 AAQKAELEEKQSQQKTLLYEQQA---QQQKLEQARNERKKTLTGLESSLQKDQ--QQLSELRANEsrlrdSIARAEREAK 257
|
170 180
....*....|....*....|....*
gi 30725047 787 KR-DHQLRllEAQK-RNQEVVLRRK 809
Cdd:PRK11637 258 ARaEREAR--EAARvRDKQKQAKRK 280
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
629-826 |
4.71e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 629 DLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEE-KAKKVRSEYEKK 707
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKENLEKE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 708 LQAMNKELQRLQAAQKEharLLKNQSQYEKQLKKLQQDVMEMKKtkvrlmkqmkeEQEKARLTESRRNREIAQLKKDQRK 787
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKS---LKKKQEEKQELIDQKEKEKKDLIK-----------EIEEKEKKISSLEKELEKAKKENEK 628
|
170 180 190
....*....|....*....|....*....|....*....
gi 30725047 788 rdhqlrlLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 826
Cdd:TIGR04523 629 -------LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
645-778 |
4.89e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 645 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVlqnlgsvesysEEKAKKVRSEYEKKLQAMNKELQ-RLQAAQK 723
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 30725047 724 EHARLLKNQSQYEKQLKKLQ--QDVMEMKKtkvrLMKQMKEEQEKARLTESRRNREI 778
Cdd:PRK00409 585 EADEIIKELRQLQKGGYASVkaHELIEARK----RLNKANEKKEKKKKKQKEKQEEL 637
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
646-1062 |
5.03e-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: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 646 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRsEYEKKLQAMNKELQRLQAAQKEH 725
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 726 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 804
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 805 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSDAPAQdtgssaaavetdasRTGAQQKMRIPVARVQALptpatngnr 884
Cdd:TIGR00606 846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR--------------RQQFEEQLVELSTEVQSL--------- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 885 kkyqrkgltgrvfisktarmkwqllerrVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENgegDKN 964
Cdd:TIGR00606 901 ----------------------------IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI---KEK 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 965 VANINEEMESLTANI-----DYINDSISDCQANIMQMEEAKEEGETLD-----VTAVINACTLTEaRYLLDHFLSMGINK 1034
Cdd:TIGR00606 950 VKNIHGYMKDIENKIqdgkdDYLKQKETELNTVNAQLEECEKHQEKINedmrlMRQDIDTQKIQE-RWLQDNLTLRKREN 1028
|
410 420
....*....|....*....|....*...
gi 30725047 1035 GLQAAQKEaqIKVLEGRLKQTEITSATQ 1062
Cdd:TIGR00606 1029 ELKEVEEE--LKQHLKEMGQMQVLQMKQ 1054
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
641-957 |
5.67e-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: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 641 QKLIDEL---ENSQKRL----QTLKKQYEEKLmmlqhKIRDTQLE--RDQVLQNLGSVESYSEEKaKKVRSEY---EKKL 708
Cdd:pfam01576 702 EELEDELqatEDAKLRLevnmQALKAQFERDL-----QARDEQGEekRRQLVKQVRELEAELEDE-RKQRAQAvaaKKKL 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 709 QAMNKELQ-RLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrrnrEIAQLKKD--- 784
Cdd:pfam01576 776 ELDLKELEaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA----ELLQLQEDlaa 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 785 ---QRKRDHQLR---------------LLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVagkvtRKLSSSdapaqdtg 846
Cdd:pfam01576 852 serARRQAQQERdeladeiasgasgksALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL-----RKSTLQ-------- 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 847 SSAAAVETDASRTGAQQkmripvarvqalptpaTNGNRKKYQRKgltgrvfiSKTARMKWQLLERRVTDiiMQKMTISNM 926
Cdd:pfam01576 919 VEQLTTELAAERSTSQK----------------SESARQQLERQ--------NKELKAKLQEMEGTVKS--KFKSSIAAL 972
|
330 340 350
....*....|....*....|....*....|....
gi 30725047 927 EADMNRLLKQREELTKRRE---KLSKRREKIVKE 957
Cdd:pfam01576 973 EAKIAQLEEQLEQESRERQaanKLVRRTEKKLKE 1006
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
693-800 |
5.81e-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: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 693 SEEKAK------KVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKlqqdvmeMKKTKVRLMKQMKEEQEK 766
Cdd:pfam11600 10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEK-------ELKEKERREKKEKDEKEK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 30725047 767 A---RLTESRRNREIAQLK---KDQRKRDHQLRLLEAQKR 800
Cdd:pfam11600 83 AeklRLKEEKRKEKQEALEaklEEKRKKEEEKRLKEEEKR 122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
641-821 |
6.68e-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: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 641 QKLIDELENSQKRLQTLKKQYEeklmMLQHkIRDTQLERDQVLQNLGSVESYSE----EKAKKVRSEYEKKLQAMNKELQ 716
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIE----LLEP-IRELAERYAAARERLAELEYLRAalrlWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 717 RLQAAQKEHARLLKNQSQYEKQLKKLQQDVmemkktKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLE 796
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180
....*....|....*....|....*.
gi 30725047 797 AQ-KRNQEVVLRRKtEEVTALRRQVR 821
Cdd:COG4913 380 EEfAALRAEAAALL-EALEEELEALE 404
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
635-803 |
7.23e-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: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 635 CEIAIKQKLidELENSQKRLQTLKKQYEE---KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAK---KVRSEYEKKL 708
Cdd:pfam15742 54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQeksRVADAEEKIL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 709 qamnkELQRlqaaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN------------- 775
Cdd:pfam15742 132 -----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdke 202
|
170 180 190
....*....|....*....|....*....|..
gi 30725047 776 ----REIAQLKKDQRKRDHQLRLLEAQKRNQE 803
Cdd:pfam15742 203 aqleMTNSQQQLRIQQQEAQLKQLENEKRKSD 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
420-788 |
7.98e-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: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 420 ENAMLQTENN--NLRVRIKAMQETVDALRSRITQLVSDQanhvlaragegnEEISNMIHSYIKEIEDLRAKLLESEAVNE 497
Cdd:TIGR02168 669 NSSILERRREieELEEKIEELEEKIAELEKALAELRKEL------------EELEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 498 NLRKNLTRATARAPYFSGSSTFSPTILSSDKETIEIIDLAKKDLEklkrkekrkkksvAGKEDNTDTDQEKKEEKGVSER 577
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-------------AEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 578 ENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKAnyQADLANITCEIAIKQKLIDELENSQKRLQTL 657
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL--SEDIESLAAEIEELEELIEELESELEALLNE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 658 KKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVrSEYEKKLQAMNKELQRLQAAQKEHARL-----LKNQ 732
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLtleeaEALE 960
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30725047 733 SQYEKQLKKLQQDVMEMKKTKVRL----------MKQMKE-----EQEKARLTESRRNRE--IAQLKKDQRKR 788
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELgpvnlaaieeYEELKErydflTAQKEDLTEAKETLEeaIEEIDREARER 1033
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1465-1506 |
1.06e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.10 E-value: 1.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 30725047 1465 FQSTGKLTGHLGPVMCLTvdqISSGQDLIITGSKDHYIKMFD 1506
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLA---FSPDGKLLASGSDDGTVKVWD 39
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
634-798 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 634 TCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqHKIRDTQLERDQVLQnlgsveSYSEE------KAKKVRSEY--- 704
Cdd:pfam15619 17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIA------RHNEEvrvlreRLRRLQEKErdl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 705 EKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQlkKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKD 784
Cdd:pfam15619 87 ERKLKEKEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKK 164
|
170
....*....|....
gi 30725047 785 QRKRDHQLRLLEAQ 798
Cdd:pfam15619 165 HKEAQEEVKILQEE 178
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
705-1096 |
1.48e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 705 EKKLQAMNKELQRLQAAQKEharllknqsqYEKQLKKLQQDV----------MEMKKTKVRLMKQmkeEQEKARLTESRR 774
Cdd:COG1196 178 ERKLEATEENLERLEDILGE----------LERQLEPLERQAekaeryrelkEELKELEAELLLL---KLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 775 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRpmsdkVAGKVTRKLSSSDAPAQDTGSSAAAVET 854
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY-----ELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 855 DASRTGAQQKMRIpvarvqalptpatngnrkkyqrkgltgrvfISKTARmkwqlLERRVTDIIMQKMTISNMEADMNRLL 934
Cdd:COG1196 320 ELEEELAELEEEL------------------------------EELEEE-----LEELEEELEEAEEELEEAEAELAEAE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 935 KQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINA 1014
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 1015 CTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLGHALQDLDSV 1094
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
..
gi 30725047 1095 PL 1096
Cdd:COG1196 525 AV 526
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
623-750 |
1.48e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 623 KANYQADLANItceiaikQKLIDELENSQKRLQT-------LKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsvESYSE- 694
Cdd:PRK00409 508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEAE--KEAQQa 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 695 -EKAKKVRSEYEKKLQAMNKELQRLQAAQK---EHARLLKNQSQYEKQLKKLQQDVMEMK 750
Cdd:PRK00409 579 iKEAKKEADEIIKELRQLQKGGYASVKAHElieARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
625-804 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 625 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQleRDQVLQNLGSVESYSEEKAKKVRSEY 704
Cdd:pfam12128 351 SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKI--REARDRQLAVAEDDLQALESELREQL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 705 EKKLQAMNKELQRLQAAQKEhARLLKNQSQYEKQLKklqqdvmEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKK- 783
Cdd:pfam12128 429 EAGKLEFNEEEYRLKSRLGE-LKLRLNQATATPELL-------LQLENFDERIERAREEQEAANAEVERLQSELRQARKr 500
|
170 180
....*....|....*....|....*
gi 30725047 784 ----DQRKRDHQLRLLEAQKRNQEV 804
Cdd:pfam12128 501 rdqaSEALRQASRRLEERQSALDEL 525
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
938-1030 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 938 EELTKRREKLSKRREKIVKENgegdKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEgetldvtavINACTL 1017
Cdd:smart00787 204 TELDRAKEKLKKLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ---------CRGFTF 270
|
90
....*....|...
gi 30725047 1018 TEARYLLDHFLSM 1030
Cdd:smart00787 271 KEIEKLKEQLKLL 283
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
641-804 |
1.57e-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: 42.56 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 641 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSEE--KAKKVRSEYEKKL 708
Cdd:cd16269 123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEAilQADQALTEKEKEI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 709 QAMNKELQRLQAAQKEharllknqsqYEKQLKKLQQDVMEMKKTKVRLMKQMKEE-QEKARLTESRRNREIAQLKKDQRK 787
Cdd:cd16269 201 EAERAKAEAAEQERKL----------LEEQQRELEQKLEDQERSYEEHLRQLKEKmEEERENLLKEQERALESKLKEQEA 270
|
170
....*....|....*..
gi 30725047 788 RDHQLRLLEAQKRNQEV 804
Cdd:cd16269 271 LLEEGFKEQAELLQEEI 287
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1564-1595 |
1.61e-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: 1.61e-03
10 20 30
....*....|....*....|....*....|..
gi 30725047 1564 NAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1595
Cdd:smart00320 9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
680-815 |
1.62e-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: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 680 DQVLQNLGSVESYSEEKA--KKVRSEYEKKLQAMNKELQR----LQAAQKEHARLLKNQSQYEKqlkklqqDVMEMKKTK 753
Cdd:pfam13851 19 DITRNNLELIKSLKEEIAelKKKEERNEKLMSEIQQENKRltepLQKAQEEVEELRKQLENYEK-------DKQSLKNLK 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30725047 754 VRL------MKQMKEEQE--KARLTESRRNREiaQLKKDQRKrdhqlRLLEAQKR--NQEVVLRRKTEEVTA 815
Cdd:pfam13851 92 ARLkvlekeLKDLKWEHEvlEQRFEKVERERD--ELYDKFEA-----AIQDVQQKtgLKNLLLEKKLQALGE 156
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
653-821 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 653 RLQTLKKQYEEkLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQ 732
Cdd:COG4913 226 AADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 733 SQYEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTesrrnREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKT 810
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLE-----REIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170
....*....|.
gi 30725047 811 EEVTALRRQVR 821
Cdd:COG4913 380 EEFAALRAEAA 390
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
654-820 |
1.74e-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: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 654 LQTLKKQYEEKLmmlQHKIRDTqleRDQVLQNLGSVESYSEEK-----AKKVRSEYEK-KLQAMNK-ELQRLQAAQKEha 726
Cdd:pfam15665 16 IQALKEAHEEEI---QQILAET---REKILQYKSKIGEELDLKrriqtLEESLEQHERmKRQALTEfEQYKRRVEERE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 727 rlLKNQSQYEKQLKKLQQDVMEMKKT---KVR----LMKQMKEEQEKArLTESRR--NREIAQLKKDQRKR-----DHQL 792
Cdd:pfam15665 88 --LKAEAEHRQRVVELSREVEEAKRAfeeKLEsfeqLQAQFEQEKRKA-LEELRAkhRQEIQELLTTQRAQsasslAEQE 164
|
170 180
....*....|....*....|....*....
gi 30725047 793 RLLEAQKrnQEVV-LRRKTEEVTALRRQV 820
Cdd:pfam15665 165 KLEELHK--AELEsLRKEVEDLRKEKKKL 191
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
623-814 |
1.78e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 623 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQ---LERDQVLQNLGSVE---SYSEEK 696
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeAENEALLEELRSLQerlNASERK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 697 AKKVRSE---------------YEKKLQAMNKELQ---------------------RLQAAQKEHARLLKNQSQYEKQLK 740
Cdd:pfam07888 253 VEGLGEElssmaaqrdrtqaelHQARLQAAQLTLQladaslalregrarwaqeretLQQSAEADKDRIEKLSAELQRLEE 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30725047 741 KLQQDVMEMKKTKVRLMKqmkeEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKrnQEV-----VLRRKTEEVT 814
Cdd:pfam07888 333 RLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK--QELleyirQLEQRLETVA 405
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
639-880 |
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 30725047 639 IKQKLIDELENSQKRLQTLKKQYEEKLM--MLQHKIRDTQ------LERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQA 710
Cdd:pfam04747 12 IRQQLTNRRKNLGRVAKSQRNQFRQWLLtaVLPNSINDQRkeafasLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 711 MNKELQRLQAAQKEHARLLKNQSQYEKQlkklqqdvmemkktkvrlmKQMKEEQEKarltesrrnreiaqLKKDQRKRDH 790
Cdd:pfam04747 92 VNAKKAAEKEARRAEAEAKKRAAQEEEH-------------------KQWKAEQER--------------IQKEQEKKEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 791 QLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPM---SDKVAGKVTRKLSSSDAPAQDTGSSAAA--VETDASRTGAQQKM 865
Cdd:pfam04747 139 DLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPApveEEIVVKKVANDRSAAPAPEPKTPTNTPAepAEQVQEITGKKNKK 218
|
250
....*....|....*
gi 30725047 866 RIPVARVQALPTPAT 880
Cdd:pfam04747 219 NKKKSESEATAAPAS 233
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1559-1595 |
2.01e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 2.01e-03
10 20 30
....*....|....*....|....*....|....*..
gi 30725047 1559 LQQVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWN 1595
Cdd:pfam00400 3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
759-1083 |
2.25e-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: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 759 QMKEEQEKAR--LTESRRNREIA---------QLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV 827
Cdd:TIGR02169 167 EFDRKKEKALeeLEEVEENIERLdliidekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 828 AGKvTRKLSSSDAPAQDTGSSAAAVEtdasrtgaqQKMRIPVARVQALptpaTNGNRKKYQRKGLTGRVFISKTAR---- 903
Cdd:TIGR02169 247 ASL-EEELEKLTEEISELEKRLEEIE---------QLLEELNKKIKDL----GEEEQLRVKEKIGELEAEIASLERsiae 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 904 ----MKwQLLERR---VTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLT 976
Cdd:TIGR02169 313 kereLE-DAEERLaklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 977 ANIDYINDSISDCQANIMQMEEAKEE--GETLDVTAVINActltearylldhfLSMGINKgLQAAQKEAQ--IKVLEGRL 1052
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRlsEELADLNAAIAG-------------IEAKINE-LEEEKEDKAleIKKQEWKL 457
|
330 340 350
....*....|....*....|....*....|.
gi 30725047 1053 KQTEITSATQNQLLFHMLKEKAELNPELDAL 1083
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
641-866 |
2.40e-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: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 641 QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIR-DTQL----------------ERDQVLQNLGSVESYSEEKAKKVRSE 703
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQaETELcaeaeemrarlaarkqELEEILHELESRLEEEEERSQQLQNE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 704 yEKKLQAMNKELQRlQAAQKEHARllkNQSQYEK-----QLKKLQQDVMEMKKTKVRLMK--------------QMKEEQ 764
Cdd:pfam01576 98 -KKKMQQHIQDLEE-QLDEEEAAR---QKLQLEKvtteaKIKKLEEDILLLEDQNSKLSKerklleeriseftsNLAEEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 765 EKARLTESRRNREIAQLKkdqrkrDHQLRLLEAQKRNQEVV-LRRKTE-EVTALRRQVRPMSDKVAgKVTRKLSSSDAPA 842
Cdd:pfam01576 173 EKAKSLSKLKNKHEAMIS------DLEERLKKEEKGRQELEkAKRKLEgESTDLQEQIAELQAQIA-ELRAQLAKKEEEL 245
|
250 260
....*....|....*....|....
gi 30725047 843 QDTgsSAAAVETDASRTGAQQKMR 866
Cdd:pfam01576 246 QAA--LARLEEETAQKNNALKKIR 267
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
694-768 |
2.46e-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: 2.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30725047 694 EEKAKKVRSEYEKKLQAMNKELQRLQAA-QKEhaRLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKAR 768
Cdd:COG2825 45 QKKLEKEFKKRQAELQKLEKELQALQEKlQKE--AATLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQELL 118
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
645-780 |
2.49e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 39.57 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 645 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSvesyseekakkvrSEYEKKLQAMNKELQRLQAAQKE 724
Cdd:pfam02050 1 DEAARELAEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISA-------------AELRNYQAFISQLDEAIAQQQQE 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 30725047 725 HARLLKNQSQYEKQLKKLQQDVMEMKKTKVRlmkQMKEEQEKARLTESRRNREIAQ 780
Cdd:pfam02050 68 LAQAEAQVEKAREEWQEARQERKSLEKLRER---EKKEERKEQNRREQKQLDELAA 120
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
680-787 |
2.55e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 680 DQVLQNLGSVESYSEEKAKKV---RSEYEKKLQAMNKELQRLQaaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL 756
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQ--EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
|
90 100 110
....*....|....*....|....*....|.
gi 30725047 757 MKQMKEEQEKARLTESRRNREIAQLKKDQRK 787
Cdd:PRK00409 597 QKGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
623-818 |
2.63e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 623 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDqvlqnlgSVESYSEEKAKKVRS 702
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-------AEELKKAEEENKIKA 1663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 703 EYEKKLQAMNK----ELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK----------QMKEEQ---- 764
Cdd:PTZ00121 1664 AEEAKKAEEDKkkaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKaeeenkikaeEAKKEAeedk 1743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30725047 765 ---EKARLTESRRNReIAQLKKDQRKRDHQLRlleaqkRNQEVVLRRKTEEVTALRR 818
Cdd:PTZ00121 1744 kkaEEAKKDEEEKKK-IAHLKKEEEKKAEEIR------KEKEAVIEEELDEEDEKRR 1793
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-1012 |
2.77e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 361 ANRARNIKNKVMVNQDRASQQINALR-SEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRiKAMQ 439
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 440 ETVDALRSRITQLVSDQANHV--LARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNEnLRKNLTRATARAPYFSGSS 517
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKA 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 518 TFSPTILSSDKETIEIidlAKKDLEKLKRKEKRKKKSVAGKEDNTDTDQEKKEEKgvseRENNEL--EVEESQEVSDHED 595
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK----KKADEAkkKAEEDKKKADELK 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 596 EEEEEEEEEDDIDGGESSDESDSESDEKAN--YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIR 673
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 674 dtqlerdqvlqnlgsvesysEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEK--QLKKLQQ--DVMEM 749
Cdd:PTZ00121 1492 --------------------AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadEAKKAEEkkKADEL 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 750 KKTKVRLMKQMKEEQEKARLTESRRN---REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 826
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 827 vaGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKgltgrvfISKTARMKW 906
Cdd:PTZ00121 1632 --KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-------LKKEAEEAK 1702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 907 QLLERRVTDIIMQKMTISNMEADMNRLLKQrEELTKRREKLSKRREKIVKENGEGDKnVANINEEMESLTANIDYINDSI 986
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKA-EEAKKEAEEDKKKAEEAKKDEEEKKK-IAHLKKEEEKKAEEIRKEKEAV 1780
|
650 660 670
....*....|....*....|....*....|
gi 30725047 987 ----SDCQANIMQMEEAKEEGETLDVTAVI 1012
Cdd:PTZ00121 1781 ieeeLDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1465-1506 |
3.27e-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: 3.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 30725047 1465 FQSTGKLTGHLGPVMCLtvdQISSGQDLIITGSKDHYIKMFD 1506
Cdd:smart00320 2 GELLKTLKGHTGPVTSV---AFSPDGKYLASGSDDGTIKLWD 40
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
645-822 |
3.34e-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: 42.03 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 645 DELENsQKRLQTLKKQYEEKlmmlqhKIRDTQLERDQVLQNLGSvesysEEKAKKVRSEYEKKLQAMNKELQRLQAAQKE 724
Cdd:pfam17380 454 EEQER-QQQVERLRQQEEER------KRKKLELEKEKRDRKRAE-----EQRRKILEKELEERKQAMIEEERKRKLLEKE 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 725 HARllKNQSQYEKQlkklQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNReiaqLKKDQRKRDHQLRLLEAQKRNQEV 804
Cdd:pfam17380 522 MEE--RQKAIYEEE----RRREAEEERRKQQEMEERRRIQEQMRKATEERSR----LEAMEREREMMRQIVESEKARAEY 591
|
170
....*....|....*...
gi 30725047 805 vlrRKTEEVTALRRQVRP 822
Cdd:pfam17380 592 ---EATTPITTIKPIYRP 606
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
649-782 |
3.44e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 39.50 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 649 NSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYseekakkvRSEYEKKLQAMNKE-------------L 715
Cdd:COG2882 2 KRSFRLQTLLDLAEKEEDEAARELGQAQQALEQAEEQLEQLEQY--------REEYEQRLQQKLQQglsaaqlrnyqqfI 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30725047 716 QRLQAAQKEHARLLKN-QSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 782
Cdd:COG2882 74 ARLDEAIEQQQQQVAQaEQQVEQARQAWLEARQERKALEKLKERRREEERQEENRREQKELDELASRR 141
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
380-975 |
3.64e-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: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 380 QQINALRSEITRLQMELMEyktGKRIIDEEGVESINDMfHENAMLQTENNNLRVRIKAMQETVDALRSRITQLVS--DQA 457
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKE---NKKNIDKFLTEIKKKE-KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKniDKI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 458 NHVLARAgegNEEISNmIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARapyFSGSSTfspTILSSDKETIEIIDLA 537
Cdd:TIGR04523 193 KNKLLKL---ELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE---INEKTT---EISNTQTQLNQLKDEQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 538 KKDLEKLKRKEkrkkksvagKEDNTDTDQEKKEEKGVSEREnNELEVEESQEVSDHEDEEEEEEeeeddidggessdesd 617
Cdd:TIGR04523 263 NKIKKQLSEKQ---------KELEQNNKKIKELEKQLNQLK-SEISDLNNQKEQDWNKELKSEL---------------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 618 sesdekANYQADLANITCEIAIKQKLIDELENSQKRL-----------QTLKKQYEEKlmmlQHKIRDTQLERDQVLQNL 686
Cdd:TIGR04523 317 ------KNQEKKLEEIQNQISQNNKIISQLNEQISQLkkeltnsesenSEKQRELEEK----QNEIEKLKKENQSYKQEI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 687 GSVESYSE------EKAKKVRSEYEKKLQAMNKELQRLqaaQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQM 760
Cdd:TIGR04523 387 KNLESQINdleskiQNQEKLNQQKDEQIKKLQQEKELL---EKEIERLKETIIKNNSEIKDLTNQDSV-KELIIKNLDNT 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 761 KEEQEKarltesrrnrEIAQLKKDQRKRDHQLrlleaQKRNQEvvLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSda 840
Cdd:TIGR04523 463 RESLET----------QLKVLSRSINKIKQNL-----EQKQKE--LKSKEKELKKLNEEKKELEEKVK-DLTKKISSL-- 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 841 paqdtgssaaavetdasrtgaqqkmripVARVQALPTPATNGNRKKYQRKgltgRVFISKTARMKWQLLErrvTDIIMQK 920
Cdd:TIGR04523 523 ----------------------------KEKIEKLESEKKEKESKISDLE----DELNKDDFELKKENLE---KEIDEKN 567
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 30725047 921 MTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESL 975
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
691-845 |
3.86e-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: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 691 SYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHArllknqSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLT 770
Cdd:pfam14988 7 EYLAKKTEEKQKKIEKLWNQYVQECEEIERRRQELA------SRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30725047 771 ESrRNREIAQLKKDQRK--RDHQLRLLEAQKRnqevVLRRKteevTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDT 845
Cdd:pfam14988 81 ES-QEREIQDLEEEKEKvrAETAEKDREAHLQ----FLKEK----ALLEKQLQELRILELGERATRELKRKAQALKL 148
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
300-509 |
4.31e-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: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 300 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 374
Cdd:COG3206 96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 375 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 440
Cdd:COG3206 174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 441 ----------TVDALRSRITQLVSDQANhVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKNLTRATAR 509
Cdd:COG3206 254 dalpellqspVIQQLRAQLAELEAELAE-LSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
623-741 |
4.37e-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: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 623 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMM---------LQHKIRDTQLER----DQVLQNLGSV 689
Cdd:COG1579 40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKRRIsdleDEILELMERI 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 690 ESYSEEKA-------------KKVRSEYEKKLQAMNKELQRLQAAQKEHA-----RLLKnqsQYEKQLKK 741
Cdd:COG1579 120 EELEEELAeleaelaeleaelEEKKAELDEELAELEAELEELEAEREELAakippELLA---LYERIRKR 186
|
|
| Cep57_CLD |
pfam14073 |
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ... |
668-796 |
4.83e-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: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 668 LQHKIRDTQLERDQ-----------------VLQNLGSVESYSEEKAKKVRSEYEKKLQA-------MNKELQR----LQ 719
Cdd:pfam14073 9 LQEKIRRLELERKQaednlkqlsretshykeVLQKENDARDPSRGEVSKQNQELISQLAAaesrcslLEKQLEYmrkmVE 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30725047 720 AAQKEHARLLKNQSQYEKQlkkLQQDVMEMKKtkvRLMKQMKEEQEKARLTESRRNRE--IAQLKKDQRKRDHQLRLLE 796
Cdd:pfam14073 89 NAEKERTAVLEKQASLERE---RSQDSSELQA---QLEKLEKLEQEYLRLTRTQSLAEtkIKELEEKLQEEEHQRKLVQ 161
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
653-782 |
5.18e-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: 39.22 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 653 RLQTLKKQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYE-KKLQAMNKELQRLQAAQKEHARLL- 729
Cdd:TIGR02473 6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30725047 730 KNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 782
Cdd:TIGR02473 86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
|
|
| XRCC4 |
pfam06632 |
DNA double-strand break repair and V(D)J recombination protein XRCC4; This family consists of ... |
686-791 |
5.43e-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: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 686 LGSVESYS-EEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKK-------LQQD-------VMEMK 750
Cdd:pfam06632 112 LGSVKLQKvPEPAEVIRELISYCLDCIAELQAKNEHLQKENERLQRDWNDVTGRLEKcvkakeeLEADlykrfilVLNEK 191
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 30725047 751 KTKVRLMKQMKEEQEKARLTESRRNREIAqlkKDQRKRDHQ 791
Cdd:pfam06632 192 KAKIRSLQKLLNELQESEESTEQKREDPA---TSDRTPDEE 229
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
640-786 |
6.53e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 640 KQKLIDELENSQKRLQTLKKQYEEKlmmlqhkirdtQLERDQVLqnlgsvesySEEKAKKvrseyekklqamnkelQRLQ 719
Cdd:PRK11637 168 RQETIAELKQTREELAAQKAELEEK-----------QSQQKTLL---------YEQQAQQ----------------QKLE 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30725047 720 AAQKEHARLLknqSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQR 786
Cdd:PRK11637 212 QARNERKKTL---TGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQK 275
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
641-761 |
6.56e-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: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 641 QKLIDELENSQKRLQTLKKQYEEklmmlqhkIRDTQ---LER-DQVLQNLGSVE---SYSEEKAKKVRSEYEKKLQAMNK 713
Cdd:pfam10168 578 QSLEEERKSLSERAEKLAEKYEE--------IKDKQeklMRRcKKVLQRLNSQLpvlSDAEREMKKELETINEQLKHLAN 649
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 30725047 714 ELQRLQAAQKEHAR-LLKNQSQY--------EKQLKKLQQDVMEMKKTKVRLMKQMK 761
Cdd:pfam10168 650 AIKQAKKKMNYQRYqIAKSQSIRkksslslsEKQRKTIKEILKQLGSEIDELIKQVK 706
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
638-777 |
6.91e-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: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 638 AIKQKLIDELENSQKRlQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL-----GSVESYSE--EKAKKVRSEYEKKLQA 710
Cdd:pfam01576 303 ALKTELEDTLDTTAAQ-QELRSKREQEVTELKKALEEETRSHEAQLQEMrqkhtQALEELTEqlEQAKRNKANLEKAKQA 381
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30725047 711 MNKELQRLQAaqkeharllknqsqyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNRE 777
Cdd:pfam01576 382 LESENAELQA-----------------ELRTLQQAKQDSEHKRKKLEGQLQELQ--ARLSESERQRA 429
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
644-748 |
7.11e-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: 38.71 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 644 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDtqlERDQVLQNLGSVESYSEEKakkvrseyEKKLQAMNKELQRLQAAQK 723
Cdd:pfam03938 14 SPEGKAAQAQLEKKFKKRQAELEAKQKELQK---LYEELQKDGALLEEEREEK--------EQELQKKEQELQQLQQKAQ 82
|
90 100
....*....|....*....|....*
gi 30725047 724 EharllKNQSQYEKQLKKLQQDVME 748
Cdd:pfam03938 83 Q-----ELQKKQQELLQPIQDKINK 102
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
711-828 |
7.89e-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: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 711 MNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKarltesrRNREIAQLKKDqrkrdh 790
Cdd:pfam03938 7 MQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREE-------KEQELQKKEQE------ 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 30725047 791 qlrLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 828
Cdd:pfam03938 74 ---LQQLQQKAQQELQKKQQELLQPIQDKINKAIKEVA 108
|
|
| F-BAR_Rgd1 |
cd07652 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ... |
695-821 |
8.71e-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: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 695 EKAKKVRSEYEKKLQAMNKELQRLqAAQKEHARllKNQSQYEKQL-KKLQQDVMEMKKTKVRLmKQMKEEQEKARLTESR 773
Cdd:cd07652 75 EKLADNGLRFAKALNEMSDELSSL-AKTVEKSR--KSIKETGKRAeKKVQDAEAAAEKAKARY-DSLADDLERVKTGDPG 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30725047 774 R--------NREIAQLKKD-QRK-----RDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 821
Cdd:cd07652 151 KklkfglkgNKSAAQHEDElLRKvqaadQDYASKVNAAQALRQELLSRHRPEAVKDLFDLIL 212
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
649-775 |
9.19e-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: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 649 NSQKrlqTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesYSEEKAKKVRSEYEKKLQAMNKELQrlqAAQKEHARL 728
Cdd:smart00435 266 NHQR---TVSKTHEKSMEKLQEKIKALKYQLKRLKKMI-----LLFEMISDLKRKLKSKFERDNEKLD---AEVKEKKKE 334
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 30725047 729 LKNQSQYEKQLKKLQQDVMEMKKTkvrlmKQMKEEQEKARLTESRRN 775
Cdd:smart00435 335 KKKEEKKKKQIERLEERIEKLEVQ-----ATDKEENKTVALGTSKIN 376
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
642-821 |
9.27e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 642 KLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV---------LQNlgSVESYSEEKA--KKVRSEYEKKLQA 710
Cdd:pfam00038 72 RLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLdeatlarvdLEA--KIESLKEELAflKKNHEEEVRELQA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 711 MNKELQRL----QAAQKEHARLLKN-QSQYEKQLKKLQQDVMEMKKTKVR-----------LMKQMKEEQEKARLTESRR 774
Cdd:pfam00038 150 QVSDTQVNvemdAARKLDLTSALAEiRAQYEEIAAKNREEAEEWYQSKLEelqqaaarngdALRSAKEEITELRRTIQSL 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 30725047 775 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 821
Cdd:pfam00038 230 EIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
680-808 |
9.49e-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: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30725047 680 DQVLQNLGSVESYSEEKAKkVRSEYEKKLQAMNKELQ-RLQA--AQKE-----------HARLLKNQSQYEKQ-----LK 740
Cdd:cd12923 4 EKLAKKLKEINKEYLDKSR-EYDELYEKYNKLSQEIQlKRQAleAFEEavkmfeeqlrtQEKFQKEAQPHEKQrlmenNE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30725047 741 KLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN---REIAQLkkdQRKRDHQLRLLEAQKRNQEVVLRR 808
Cdd:cd12923 83 LLKSRLKELEESKEQLEEDLRKQVAYNRELEREMNslkPELMQL---RKQKDQYLRWLKRKGVSQEEINQL 150
|
|
| |
