|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
8-372 |
0e+00 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 623.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 8 SSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 87
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 88 GQTGAGKTYTMGTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFDTTRDid 167
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPETD-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 168 aknKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaen 247
Cdd:cd01372 151 ---KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 248 atdnklisESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSK 327
Cdd:cd01372 225 --------PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSK 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 157823695 328 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 372
Cdd:cd01372 297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
15-371 |
1.84e-140 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 435.08 E-value: 1.84e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 15 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 87
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 88 GQTGAGKTYTMGTGfdvnimEEEQGIISRAVRHLFKSIDEKKTSaiknglppPEFKVNAQFLELYNEEVLDLFDTTrdid 167
Cdd:pfam00225 81 GQTGSGKTYTMEGS------DEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 168 aKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTdaen 247
Cdd:pfam00225 143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 248 atdnklisesspmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 326
Cdd:pfam00225 218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 157823695 327 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:pfam00225 282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
9-378 |
3.46e-139 |
|
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: 432.00 E-value: 3.46e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYN 81
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 82 ATVFAYGQTGAGKTYTMGtGFdvnimEEEQGIISRAVRHLFKSIDEKKtsaiknglPPPEFKVNAQFLELYNEEVLDLFD 161
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMI-GT-----PDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 162 TTrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCP 241
Cdd:smart00129 147 PS--------SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 242 QTDaenatdnklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHV 321
Cdd:smart00129 219 SSG-------------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHI 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 157823695 322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:smart00129 279 PYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
9-369 |
2.91e-122 |
|
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: 385.84 E-value: 2.91e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 9 SVRVAVRIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNA 82
Cdd:cd00106 1 NVRVAVRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 83 TVFAYGQTGAGKTYTMGTGFDvnimeEEQGIISRAVRHLFKSIDEKKTsaiknglPPPEFKVNAQFLELYNEEVLDLFDt 162
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRKE-------TKSSFSVSASYLEIYNEKIYDLLS- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 163 trdidaKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRvcPQ 242
Cdd:cd00106 147 ------PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRN--RE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 243 TDAENATDNKLisesspmnefetltakfHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVP 322
Cdd:cd00106 219 KSGESVTSSKL-----------------NLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN--KHIP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 157823695 323 YRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd00106 280 YRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
9-371 |
3.28e-106 |
|
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: 341.75 E-value: 3.28e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGY 80
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 81 NATVFAYGQTGAGKTYTMGtGFDVNimEEEQGIISRAVRHLFKSIdeKKTSAIKNglpppeFKVNAQFLELYNEEVldlf 160
Cdd:cd01371 82 NGTIFAYGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHI--ARSQNNQQ------FLVRVSYLEIYNEEI---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 161 dttRDIDAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV-Cqtrv 239
Cdd:cd01371 147 ---RDLLGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeC---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 240 cpqtdaenatdnkliSESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskRAT 319
Cdd:cd01371 220 ---------------SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KST 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 157823695 320 HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01371 283 HIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
10-373 |
2.47e-102 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 330.71 E-value: 2.47e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 10 VRVAVRIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFDIDSQQEQIYTQcIEKLIEGCFEGYNATVF 85
Cdd:cd01366 4 IRVFCRVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 86 AYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIDEKKTSAIKnglpppeFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01366 83 AYGQTGSGKTYTMeGP-------PESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIRDLLAPGN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 165 didAKNKKSNIRiHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtD 244
Cdd:cd01366 149 ---APQKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI---------S 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 245 AENATDNklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKratHVPYR 324
Cdd:cd01366 216 GRNLQTG------------EISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS---HIPYR 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 157823695 325 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 373
Cdd:cd01366 281 NSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
9-371 |
2.52e-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: 2.52e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 9 SVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFDIDSQQEQIYT 66
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 67 QCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIDEKKTSAiknglpppEFKVN 145
Cdd:cd01370 81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLKDEK--------EFEVS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 146 AQFLELYNEEVLDLFDTTrdidakNKKSNIRihEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSR 225
Cdd:cd01370 146 MSYLEIYNETIRDLLNPS------SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 226 SHAIFTIHVCQTrvcpqtdaenatdNKLISESSpmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALG 305
Cdd:cd01370 218 SHAVLQITVRQQ-------------DKTASINQ-----QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALG 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823695 306 NVISALGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01370 280 NCINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
8-378 |
1.55e-99 |
|
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: 324.31 E-value: 1.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 8 SSVRVAVRIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVFD-IDSQ------QEQIYTQC 68
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYWsHDSEdpnyasQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 69 IEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDvnimeEEQGIISRAVRHLFKSIDEKKTSAIKnglpppeFKVNAQF 148
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVSY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 149 LELYNEEVLDLFDTtrdiDAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHA 228
Cdd:cd01365 148 MEIYNEKVRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 229 IFTIHVCQTRVCPQTDAEnatdnklisesspmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVI 308
Cdd:cd01365 224 VFTIVLTQKRHDAETNLT-----------------TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVI 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157823695 309 SALGD-----KSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:cd01365 287 SALADmssgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
7-371 |
2.39e-98 |
|
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: 319.28 E-value: 2.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATV 84
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 85 FAYGQTGAGKTYTMgtgFDVNIMEEEQGIISRAVRHLFKSIdEKKTSAIknglpppEFKVNAQFLELYNEEVLDLFDTTR 164
Cdd:cd01369 81 FAYGQTSSGKTYTM---EGKLGDPESMGIIPRIVQDIFETI-YSMDENL-------EFHVKVSYFEIYMEKIRDLLDVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 165 DidaknkksNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQtrvcpqtd 244
Cdd:cd01369 150 T--------NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 245 aENATDNKLisesspmnefetLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYR 324
Cdd:cd01369 214 -ENVETEKK------------KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYR 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 157823695 325 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01369 279 DSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
7-380 |
3.06e-96 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 314.65 E-value: 3.06e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 7 ESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFE 78
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 79 GYNATVFAYGQTGAGKTYTMgTGFDVNIME------EEQGIISRAVRHLFKSIDEKKTsaiknglpppEFKVNAQFLELY 152
Cdd:cd01364 81 GYNCTIFAYGQTGTGKTYTM-EGDRSPNEEytweldPLAGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 153 NEEVLDLFDttrdiDAKNKKSNIRIHEDS--TGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIF 230
Cdd:cd01364 150 NEELFDLLS-----PSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 231 TIHVcqtrvcpqtdaenatdnkLISESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISA 310
Cdd:cd01364 225 SITI------------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITA 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 311 LGDKSKratHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01364 287 LVERAP---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
44-511 |
5.92e-92 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 310.13 E-value: 5.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 44 GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLF 122
Cdd:COG5059 53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 123 KSIDEKKTSAiknglpppEFKVNAQFLELYNEEVLDLFDttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 202
Cdd:COG5059 126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 203 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTrvcpqtdaenatdNKLISESSpmnefetlTAKFHFVDLAGSERLK 282
Cdd:COG5059 190 DLLRKGEKNRTTASTEINDESSRSHSIFQIELASK-------------NKVSGTSE--------TSKLSLVDLAGSERAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 283 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 362
Cdd:COG5059 249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 363 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQT---ENNNLRVR 438
Cdd:COG5059 328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQSlkkETETLKSR 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823695 439 IK-AMQETVDALRARITQLVSEqanqvlaraGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 511
Cdd:COG5059 403 IDlIMKSIISGTFERKKLLKEE---------GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
10-380 |
9.45e-92 |
|
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: 301.73 E-value: 9.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 10 VRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYG 88
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 89 QTGAGKTYTM--GTGFDVNIMEEEQGIISRAVRHLFKSIDEKKTSAIKNglppPEFKVNAQFLELYNEEVLDLFDTTrdi 166
Cdd:cd01373 83 QTGSGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIQREKEKAGEG----KSFLCKCSFLEIYNEQIYDLLDPA--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 167 daknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhvcqtrvcpqtdae 246
Cdd:cd01373 156 -----SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC-------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 247 natdnkLISESSPMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-RATHVPYR 324
Cdd:cd01373 217 ------TIESWEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYR 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 157823695 325 DSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 380
Cdd:cd01373 291 DSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
9-371 |
3.00e-90 |
|
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: 296.17 E-value: 3.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 9 SVRVAVRIRPQLAKEKIEGCHICTSVTPG----EPQVFlgkdKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATV 84
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEIDNDtiylVEPPS----TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 85 FAYGQTGAGKTYTMGTGfdvnimEEEQGIISRAVRHLFKSIDEKKTSaiknglpppEFKVNAQFLELYNEEVLDLFDTTr 164
Cdd:cd01374 77 FAYGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDTPDR---------EFLLRVSYLEIYNEKINDLLSPT- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 165 didaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtd 244
Cdd:cd01374 141 -------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI---------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 245 aenatdnklisESSPMNEFETLTAKF---HFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDkSKRATHV 321
Cdd:cd01374 204 -----------ESSERGELEEGTVRVstlNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHI 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 157823695 322 PYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 371
Cdd:cd01374 272 PYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
10-369 |
3.44e-72 |
|
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: 244.33 E-value: 3.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 10 VRVAVRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNAT 83
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 84 VFAYGQTGAGKTYTMGTGFdvnimeEEQGIISRAVRHLFkSIDEKKTSAiknglpppeFKVNAQFLELYNEEVLDLFDTt 163
Cdd:cd01376 81 VFAYGSTGAGKTFTMLGSP------EQPGLMPLTVMDLL-QMTRKEAWA---------LSFTMSYLEIYQEKILDLLEP- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 164 rdidaknKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqt 243
Cdd:cd01376 144 -------ASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 244 daenatdnkliSESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKRATHVPY 323
Cdd:cd01376 208 -----------DQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPY 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 157823695 324 RDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 369
Cdd:cd01376 274 RDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
10-367 |
1.51e-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: 1.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 10 VRVAVRIRPQLAKEKIEG-CHICTSVTPGEPQVFLGKDK----------AFTFDYVFDIDSQQEQIYTQCIEKLIEGCFE 78
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKeIDVVSVPSKLTLIVHEPKLKvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 79 GYNATVFAYGQTGAGKTYTMGTGFDVNimEEEQGIISRAVRHLFKSIdekKTSAIKNGLpppefKVNAQFLELYNEEVLD 158
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGGDFSGQ--EESKGIYALAARDVFRLL---NKLPYKDNL-----GVTVSFFEIYGGKVFD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 159 LFdttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIhVCQTR 238
Cdd:cd01367 152 LL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI-ILRDR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 239 vcpqtdaenatdnklisesspmnEFETLTAKFHFVDLAGSER-LKRTGATGERAKEGISINCGLLALGNVISALGDKSkr 317
Cdd:cd01367 222 -----------------------GTNKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-- 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 157823695 318 aTHVPYRDSKLTRLLQDSL-GGNSQTIMIACVSPSDRDFMETLNTLKYANR 367
Cdd:cd01367 277 -AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
46-369 |
1.03e-68 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 235.17 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 46 DKAFTFDYVFDiDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNImeEEQGIISRAVRHLFKSI 125
Cdd:cd01375 47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENY--KHRGIIPRALQQVFRMI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 126 DEKKTSAIKnglpppefkVNAQFLELYNEEVLDLFDTTRDIDAKNKKsnIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCL 205
Cdd:cd01375 123 EERPTKAYT---------VHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 206 KLGALSRTTASTQMNVQSSRSHAIFTIHvcqtrvcpqtdaenatdnkLISESSPMNEFETLTAKFHFVDLAGSERLKRTG 285
Cdd:cd01375 192 FLGETNRIIASHTMNKNSSRSHCIFTIH-------------------LEAHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 286 ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01375 253 VEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330
|
....
gi 157823695 366 NRAR 369
Cdd:cd01375 331 SRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
10-365 |
8.46e-66 |
|
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: 226.89 E-value: 8.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 10 VRVAVRIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFDIDSQQEQIYTQCIEKLIE 74
Cdd:cd01368 3 VKVYLRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 75 GCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVRHLFKSIdekktsaiknglppPEFKVNAQFLELYN 153
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMqGS-------PGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 154 EEVLDLFDTTRDIDAKNKKSnIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIH 233
Cdd:cd01368 142 EYIYDLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 234 VCQTRVCPQTDAENATDNKLISESSpmnefetltakfhFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD 313
Cdd:cd01368 221 LVQAPGDSDGDVDQDKDQITVSQLS-------------LVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 157823695 314 KSKRAT--HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 365
Cdd:cd01368 288 NQLQGTnkMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
7-404 |
4.72e-65 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 243.69 E-value: 4.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 7 ESSVRVAVRIRPQLAKEkiEGCHICTSVTPGEPQVflgKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFA 86
Cdd:PLN03188 97 DSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTI---NGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 87 YGQTGAGKTYTM----GTGFDVNIMEEEQGIISRAVRHLFKSIDEKKtsaIKNGLPPPEFKVNAQFLELYNEEVLDLFDT 162
Cdd:PLN03188 172 YGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLFARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITDLLDP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 163 TrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpq 242
Cdd:PLN03188 249 S--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV-------- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 243 tdaenatDNKLISESSPMNEFETltAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK--RATH 320
Cdd:PLN03188 313 -------ESRCKSVADGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRH 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 321 VPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDrASQQINALRSEITRLQMEL 400
Cdd:PLN03188 384 IPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLRDEL 462
|
....
gi 157823695 401 MEYK 404
Cdd:PLN03188 463 QRVK 466
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1238-1551 |
1.18e-58 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 204.49 E-value: 1.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1238 CVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1314
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1315 rESAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1393
Cdd:cd00200 81 -ETGECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1394 VMCLTVDQisnGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALAIQGDN--LFSGSRDNGIKKWDLAQ 1471
Cdd:cd00200 138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1472 KGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRI 1549
Cdd:cd00200 209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287
|
..
gi 157823695 1550 WK 1551
Cdd:cd00200 288 WD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1232-1554 |
6.66e-47 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 174.33 E-value: 6.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1232 RASPLQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT------ 1303
Cdd:COG2319 106 DLATGLLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkll 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1304 VSTSY---IKVWDIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLK 1379
Cdd:COG2319 178 ASGSDdgtVRLWDLA-TGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1380 RFQSTGKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAI--QGDNLFS 1457
Cdd:COG2319 235 TGKLLRTLTGHSGSVRSVAFS--PDGR-LLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLAS 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1458 GSRDNGIKKWDLAQkGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--NS 1535
Cdd:COG2319 306 GSDDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFspDG 384
|
330
....*....|....*....
gi 157823695 1536 THVFTAADDRTVRIWKAHN 1554
Cdd:COG2319 385 RTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1231-1563 |
6.37e-44 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 165.47 E-value: 6.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1231 VRASPLQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT----- 1303
Cdd:COG2319 63 LDAAAGALLATLLGHTAAVLSVAFSPDgrLLASASADGTVRLWDLATGLLLRTLTGHTGAV--------RSVAFSpdgkt 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1304 -VSTSY---IKVWDIrESAKCIRTLTssgqvtlgeacsastsrtvaipSGESQINQIALNPTGTFLYAASG-NAVRMWDL 1378
Cdd:COG2319 135 lASGSAdgtVRLWDL-ATGKLLRTLT----------------------GHSGAVTSVAFSPDGKLLASGSDdGTVRLWDL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1379 KRFQSTGKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAIQGDN--LF 1456
Cdd:COG2319 192 ATGKLLRTLTGHTGAVRSVAFS--PDGK-LLASGSADGTVRLWDLATGKLLRTLTGHS------GSVRSVAFSPDGrlLA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1457 SGSRDNGIKKWDLaQKGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICV--N 1534
Cdd:COG2319 263 SGSADGTVRLWDL-ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspD 341
|
330 340
....*....|....*....|....*....
gi 157823695 1535 STHVFTAADDRTVRIWkahNLQDGQLSDT 1563
Cdd:COG2319 342 GKTLASGSDDGTVRLW---DLATGELLRT 367
|
|
| Rcc_KIF21A |
cd22263 |
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ... |
925-1006 |
9.10e-44 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410204 [Multi-domain] Cd Length: 82 Bit Score: 153.54 E-value: 9.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 925 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1004
Cdd:cd22263 1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80
|
..
gi 157823695 1005 AK 1006
Cdd:cd22263 81 AK 82
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1237-1468 |
1.23e-35 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 137.85 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1237 QCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWD 1313
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1314 IReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLG 1392
Cdd:cd00200 164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823695 1393 PVMCLTVdqiSNGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAIQGDN--LFSGSRDNGIKKWD 1468
Cdd:cd00200 221 GVNSVAF---SPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT------NSVTSLAWSPDGkrLASGSADGTIRIWD 289
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
925-1006 |
2.69e-28 |
|
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410202 [Multi-domain] Cd Length: 81 Bit Score: 109.22 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 925 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKEsGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1004
Cdd:cd22248 1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRERALDE-GKDESVLRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79
|
..
gi 157823695 1005 AK 1006
Cdd:cd22248 80 SK 81
|
|
| Rcc_KIF21B |
cd22262 |
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ... |
925-1006 |
4.32e-28 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to a conserved region of KIF21B, which shows high sequence similarity to the regulatory coiled-coil domain of KIF21A.
Pssm-ID: 410203 [Multi-domain] Cd Length: 82 Bit Score: 108.74 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 925 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEE 1004
Cdd:cd22262 1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80
|
..
gi 157823695 1005 AK 1006
Cdd:cd22262 81 TK 82
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
9-159 |
1.76e-20 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 89.20 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 9 SVRVAVRIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYtQCIEKLIEGCFEGYNATVFAYG 88
Cdd:pfam16796 21 NIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823695 89 QTGAGKTYTMgtgfdvnimeeeqgiISRAVRHLFKSIDEKKTSaiknglppPEFKVNAQFLELYNEEVLDL 159
Cdd:pfam16796 96 QTGSGSNDGM---------------IPRAREQIFRFISSLKKG--------WKYTIELQFVEIYNESSQDL 143
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1236-1377 |
2.91e-17 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 83.92 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1236 LQCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVW 1312
Cdd:cd00200 167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823695 1313 DIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWD 1377
Cdd:cd00200 247 DLR-TGECVQTLSGH----------------------TNSVTSLAWSPDGKRLASGSAdGTIRIWD 289
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
12-310 |
6.38e-14 |
|
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: 71.22 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 12 VAVRIRPQLAKEKIEGCHIctsvtpgepqvflgkdkaFTFDYVFDIDSQQEQIYTQCiEKLIEGCFEGYN-ATVFAYGQT 90
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKI------------------IVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGES 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 91 GAGKTYTMgtgfdvnimeeeQGIISRAVRHLFKSIDEKKTSAiknglpppefkvnaqflelyneevldlfdttrdidakn 170
Cdd:cd01363 62 GAGKTETM------------KGVIPYLASVAFNGINKGETEG-------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 171 kksnirihedstggiyTVGVTTRTVNTEPEMMQCLKLGALSRtTASTQMNVQSSRSHAIFTIhvcqtrvcpqtdaenatd 250
Cdd:cd01363 92 ----------------WVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------ 136
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 251 nklisesspmnefetltakfhFVDLAGSERlkrtgatgerakegisINCGLLALGNVISA 310
Cdd:cd01363 137 ---------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1447-1563 |
1.00e-11 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 68.78 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 1447 ALAIQGDNLFSGSRDNGIKKWDLAQKGLLQQVPnAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDS 1526
Cdd:COG2319 43 AASPDGARLAAGAGDLTLLLLDAAAGALLATLL-GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTG 121
|
90 100 110
....*....|....*....|....*....|....*....
gi 157823695 1527 PINAICV--NSTHVFTAADDRTVRIWkahNLQDGQLSDT 1563
Cdd:COG2319 122 AVRSVAFspDGKTLASGSADGTVRLW---DLATGKLLRT 157
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
629-844 |
4.18e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 629 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKC 708
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 709 EYEKKLHAMNKELQRLQTA--------QKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE-EQEKARLTESR 779
Cdd:COG4942 101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823695 780 RN--REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSS 844
Cdd:COG4942 181 AEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
389-1027 |
6.54e-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: 63.97 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 389 LRSEITRLQMELMEYKTGKRI--IDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRARITQLVSEQANQvla 466
Cdd:pfam05483 204 VQAENARLEMHFKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQ--- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 467 raGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATArspyfsassafspTI--LSSDKETIeiIDLAKKD 544
Cdd:pfam05483 281 --DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK-------------TIcqLTEEKEAQ--MEELNKA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 545 LEKLKRKEKKKKKSVAGKDDNADTDQEKKEEkgvSEKENNELDVEENQEVSDhedeeeeeedeeeeddiegeessdeSDS 624
Cdd:pfam05483 344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEK---NEDQLKIITMELQKKSSE-------------------------LEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 625 ESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAK 704
Cdd:pfam05483 396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 705 KVKCEYEKKlHAMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMK--EEQEKARLTESRRN 781
Cdd:pfam05483 475 DLKTELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 782 REIAQLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSdkvagKVTRKLsSSESPAPDTGSSAA 856
Cdd:pfam05483 554 REEFIQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-----KNIEEL-HQENKALKKKGSAE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 857 SGEADTSRPGTqQKMRIPVARVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERrvtdIIMQKmtisnmEADM 936
Cdd:pfam05483 628 NKQLNAYEIKV-NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQK------EIDK 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 937 nRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYindSIADCQANIM----QMEEAKEEGETL 1012
Cdd:pfam05483 697 -RCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI---ELSNIKAELLslkkQLEIEKEEKEKL 772
|
650
....*....|....*
gi 157823695 1013 DVTAVINACTLTEAR 1027
Cdd:pfam05483 773 KMEAKENTAILKDKK 787
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
652-955 |
1.97e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 62.76 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 652 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQTAQKEH 731
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 732 ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 810
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 811 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSESPAPdtgSSAASGEADTSRPGTQQKMR-IPVARVQALPTPTTNGT 889
Cdd:TIGR00606 846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQR---RQQFEEQLVELSTEVQSLIReIKDAKEQDSPLETFLEK 920
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823695 890 RKKYQRKGFTGRVFTSKTARMKWQLLERRVTDIIMQKMTISNM------------EADMNRLLRQREELTKRREKLSK 955
Cdd:TIGR00606 921 DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkddylkqkETELNTVNAQLEECEKHQEKINE 998
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
629-1012 |
2.79e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 629 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 705
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 706 VKCEYEKKLHAMNKelqRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 783
Cdd:PRK03918 385 TPEKLEKELEELEK---AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 784 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLrRKTEEVTALRR---QVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEA 860
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKElaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 861 DTSR--------PGTQQKMRIPVARVQALPTPTTNgTRKKYQRKGFT------GRVFTSKTARMKW-------QLLERRV 919
Cdd:PRK03918 540 EIKSlkkeleklEELKKKLAELEKKLDELEEELAE-LLKELEELGFEsveeleERLKELEPFYNEYlelkdaeKELEREE 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 920 TDIIMQKMTISNMEADMNRLLRQREELTKRREKLSKR-----REKIVKESGEGDKSVANIIEEMESLTANIDYINDSIAD 994
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
410
....*....|....*...
gi 157823695 995 CQANIMQMEEAKEEGETL 1012
Cdd:PRK03918 699 LKEELEEREKAKKELEKL 716
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
634-1020 |
1.55e-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: 56.61 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 634 ADLANITCEIAIKQKLIDELENSQKRLQTlkkqyeeklmmlqhkirdtqlERDQvlqnlgsVESYSEEKAKKVKCEYEKK 713
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRR---------------------EREK-------AERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 714 LHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKE--EQEKARLTESRRN--REIAQLKK 789
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGEleAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 790 DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSEspapdtgssaasgeadtsrpgtqQ 869
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEYAELK-----------------------E 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 870 KMRIPVARVQALPTP--TTNGTRKKYQRK--GFTGRVFTSKTARMKWQLLERRVTdiimqkMTISNMEADMNRLLRQREE 945
Cdd:TIGR02169 365 ELEDLRAELEEVDKEfaETRDELKDYREKleKLKREINELKRELDRLQEELQRLS------EELADLNAAIAGIEAKINE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 946 LTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAK-----EEGETLDVTAVINA 1020
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKA 518
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
629-869 |
2.83e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 629 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL---GSVESYSEE--KA 703
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVllGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 704 KKvkceyekkLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNRE 783
Cdd:COG3883 112 ES--------FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 784 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTS 863
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
|
....*.
gi 157823695 864 RPGTQQ 869
Cdd:COG3883 264 AAGAAA 269
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
631-834 |
5.79e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 631 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAKKVK 707
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 708 CEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-ARLTESRRN----- 781
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEEleeli 868
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157823695 782 ----REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 834
Cdd:TIGR02168 869 eeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
569-835 |
7.09e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 569 DQEKKEEKGVS-------EKENNELDVEENQEVSDHEDeeeeEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITC 641
Cdd:TIGR02168 220 AELRELELALLvlrleelREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 642 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNkel 721
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELEAELEELE--- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 722 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---REIAQLKKDQRK 793
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAELEELEEELEE 451
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 157823695 794 RDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 835
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1237-1272 |
1.08e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 46.57 E-value: 1.08e-06
10 20 30
....*....|....*....|....*....|....*...
gi 157823695 1237 QCVHIAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1272
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
364-825 |
1.13e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 53.29 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 364 YANRARNIKNKVmvnqDRASQQINALRSEITRLQMEL----MEYKTGKRIIDeegV--ESINDMFHENAMLQTENNNLRV 437
Cdd:pfam10174 280 YKSHSKFMKNKI----DQLKQELSKKESELLALQTKLetltNQNSDCKQHIE---VlkESLTAKEQRAAILQTEVDALRL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 438 RIKAMQETVDALRARITQLVSEQANQvlaragegNEEISNM----------IHSYIKEIEDLRAKLLESEAVNENLRKnl 507
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTL--------AGEIRDLkdmldvkerkINVLQKKIENLQEQLRDKDKQLAGLKE-- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 508 trataRSPYFSASSAFSPTILSSDKETieiidLAKKDLEKLKRKEKKKKKSVAGKDDNADTDQEKKEEK--------GVS 579
Cdd:pfam10174 423 -----RVKSLQTDSSNTDTALTTLEEA-----LSEKERIIERLKEQREREDRERLEELESLKKENKDLKekvsalqpELT 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 580 EKENNELDVEENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIdELENSQKR 659
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-EQEVARYK 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 660 LQTLKKQYE-EKLMMLqhkIRDTQLERDQVLQNLGSVESYSeekAKKVKCEYEK--KLHAMNKELQRLQTAQKEHARLLK 736
Cdd:pfam10174 572 EESGKAQAEvERLLGI---LREVENEKNDKDKKIAELESLT---LRQMKEQNKKvaNIKHGQQEMKKKGAQLLEEARRRE 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 737 NQSQYEKQLKKLQQDVMEMKKTKVRLmkqmkeEQEKARLTESR-----RNREIAQLKKDQRKrdhqlRLLEAQKRNQEVV 811
Cdd:pfam10174 646 DNLADNSQQLQLEELMGALEKTRQEL------DATKARLSSTQqslaeKDGHLTNLRAERRK-----QLEEILEMKQEAL 714
|
490 500 510
....*....|....*....|....*....|....
gi 157823695 812 L------------------RRKT--EEVTALRRQ 825
Cdd:pfam10174 715 LaaisekdaniallelsssKKKKtqEEVMALKRE 748
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1235-1272 |
3.52e-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: 3.52e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 157823695 1235 PLQCVHIAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1272
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
349-956 |
3.59e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 349 SPSDRDFMETL-NTLKYANRARNIKNKVMVNqdrASQQINALRSEITRLQMELMEYKT---------GKRIIDEEGVES- 417
Cdd:pfam15921 137 SQSQEDLRNQLqNTVHELEAAKCLKEDMLED---SNTQIEQLRKMMLSHEGVLQEIRSilvdfeeasGKKIYEHDSMSTm 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 418 --------INDMFHEnamLQTENNNLRVRIKAMQETVDALRA---------------RITQLVSEQANQV--LARAGEGN 472
Cdd:pfam15921 214 hfrslgsaISKILRE---LDTEISYLKGRIFPVEDQLEALKSesqnkielllqqhqdRIEQLISEHEVEItgLTEKASSA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 473 EEISNMIHSYIKeiedlrakLLESEAVNEN---LRK----NLTRATARSPYFSASSAFSPTILSSDKETIeiidLAKKDL 545
Cdd:pfam15921 291 RSQANSIQSQLE--------IIQEQARNQNsmyMRQlsdlESTVSQLRSELREAKRMYEDKIEELEKQLV----LANSEL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 546 EKLKRKEKKKKKSVAGKDDNAD---TDQEKKEEKGVSEKENNE--LDVEENQEVS-DHEDEEEEEEDEEEEDDIEGEESS 619
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQkllADLHKREKELSLEKEQNKrlWDRDTGNSITiDHLRRELDDRNMEVQRLEALLKAM 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 620 desdsesdeKANYQADLANITCEIAIKQK-------LIDELENSQKRLQTLKKQYEEKLMMLQHKIRdtqlerdqVLQNL 692
Cdd:pfam15921 439 ---------KSECQGQMERQMAAIQGKNEslekvssLTAQLESTKEMLRKVVEELTAKKMTLESSER--------TVSDL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 693 GSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEK-QLKKLQQD-VMEMKKTKVRLMKQMKEEQ 770
Cdd:pfam15921 502 TASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlKLQMAEKDkVIEILRQQIENMTQLVGQH 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 771 ---------EKARLTESRRNR--EIAQLKKDQRKRDHQLRLLEA---------------------------QKRNQ---E 809
Cdd:pfam15921 582 grtagamqvEKAQLEKEINDRrlELQEFKILKDKKDAKIRELEArvsdlelekvklvnagserlravkdikQERDQllnE 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 810 VVLRRK-----TEEVTALRRQVRPMSDKV---AGKVTRKLSSSESPAPDTGSS-----AASGEADTSRPGTQQKMRIPVA 876
Cdd:pfam15921 662 VKTSRNelnslSEDYEVLKRNFRNKSEEMettTNKLKMQLKSAQSELEQTRNTlksmeGSDGHAMKVAMGMQKQITAKRG 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 877 RVQALPT-------PTTNGTRKKY----QRKGFTGRVFTSKTARMKW----QLL---ERRVtdiimqKMTISNMEADMNR 938
Cdd:pfam15921 742 QIDALQSkiqfleeAMTNANKEKHflkeEKNKLSQELSTVATEKNKMagelEVLrsqERRL------KEKVANMEVALDK 815
|
730 740
....*....|....*....|.
gi 157823695 939 LLRQREE---LTKRREKLSKR 956
Cdd:pfam15921 816 ASLQFAEcqdIIQRQEQESVR 836
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
642-1006 |
5.56e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 642 EIAIKQKL-IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQlerdQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKE 720
Cdd:PRK03918 148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREIN-EISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 721 LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNR--EIAQLKKDQRKRDHQL 798
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 799 RLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA--GKVTRKLSssespapdtgssaasgeadtsrpgtqqkmripva 876
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErlEELKKKLK---------------------------------- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 877 rvqalptpttnGTRKKYQRkgFTGRVftsktarmkwQLLERrvtdiIMQKMTisnmeadmnrllrQREELTKRREKLSKr 956
Cdd:PRK03918 349 -----------ELEKRLEE--LEERH----------ELYEE-----AKAKKE-------------ELERLKKRLTGLTP- 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 157823695 957 rEKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAK 1006
Cdd:PRK03918 387 -EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
562-861 |
6.75e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 562 KDDNADTDQEKKEEkgvsEKENNELDVEENQevsdhedeeeeeeDEEEEDDIEGEESSDESDSESDEKANYQADLANITC 641
Cdd:COG1196 233 KLRELEAELEELEA----ELEELEAELEELE-------------AELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 642 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKEL 721
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 722 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLL 801
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 802 EAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEAD 861
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
633-827 |
7.35e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 633 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDT-QLERDQVLQNLGSvesySEEKAKKVKCEYE 711
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQA----ELSKLEEEVSRIE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 712 KKLHAMNKELQRL----QTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRnreiAQL 787
Cdd:TIGR02169 812 ARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDL 887
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 157823695 788 KKDQRKRDHQLRllEAQKRNQEVVLRRKTEEVTALRRQVR 827
Cdd:TIGR02169 888 KKERDELEAQLR--ELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
701-827 |
8.41e-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: 46.45 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 701 EKAKKVKCEYEKKLHamnkelqrlqtaqkeharllknqsQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRR 780
Cdd:pfam20492 2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 157823695 781 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 827
Cdd:pfam20492 58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1514-1551 |
1.10e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 43.84 E-value: 1.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 157823695 1514 TFVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRIWK 1551
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
650-804 |
1.82e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 650 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAM--NKELQRLQta 727
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYEALQ-- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823695 728 qKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 804
Cdd:COG1579 96 -KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
646-815 |
2.77e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.99 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 646 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsVESYSEEKAKKVKCEYEKKLhAMNKELQRLQ 725
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKA-RQRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 726 TAQKEHARLLKnqsqyEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL---KKDQRKRDHQLRLLE 802
Cdd:pfam13868 242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316
|
170
....*....|...
gi 157823695 803 AQKRNQEVVLRRK 815
Cdd:pfam13868 317 GERLREEEAERRE 329
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
648-834 |
2.91e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 648 KLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQR---- 723
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE-QLEEELEQARSELEQleee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 724 -------LQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLM---KQMKEEQEKARLTESRRNREIAQLKKDQRK 793
Cdd:COG4372 82 leelneqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157823695 794 RDHQLRLLEAQKRNQEvvLRRKTEEVTALRRQVRPMSDKVA 834
Cdd:COG4372 162 LQEELAALEQELQALS--EAEAEQALDELLKEANRNAEKEE 200
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
700-845 |
3.35e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 700 EEKAKKVKCEYEKKLHAMNKELQRLQtaqKEHARLLKNQSQYEKQLKKLQQDVMEMKKtKVRLMKQmkEEQEKARLTE-- 777
Cdd:COG2433 394 EPEAEREKEHEERELTEEEEEIRRLE---EQVERLEAEVEELEAELEEKDERIERLER-ELSEARS--EERREIRKDRei 467
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157823695 778 SRRNREIAQLKKdqrkrdhqlRLLEAQKRNQEvvLRRKTEEVTALRRQVRpMSDKVAGKVTRKLSSSE 845
Cdd:COG2433 468 SRLDREIERLER---------ELEEERERIEE--LKRKLERLKELWKLEH-SGELVPVKVVEKFTKEA 523
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
646-840 |
4.33e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 646 KQKLIDELENSQK-------RLQTLKKQ---YEEKLMMLQHKIR--------DTQLERDQVLQNLGSVESYSEEKAKKVK 707
Cdd:pfam17380 305 KEEKAREVERRRKleeaekaRQAEMDRQaaiYAEQERMAMERERelerirqeERKRELERIRQEEIAMEISRMRELERLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 708 CEYEKKLHAMNKELQ---RLQTAQKEHARLLKNQSQYEKQLKKLQQdvmEMKKTKVRLMKQMKE-EQEKARLTESRRNRE 783
Cdd:pfam17380 385 MERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERArEMERVRLEEQERQQQ 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157823695 784 IAQLKKDQRKRDHQLRLLEAQKRNQEVV--LRRKTEEVTALRRQVRPMSDKVAGKVTRK 840
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKRAeeQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
658-810 |
4.99e-05 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 47.28 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 658 KRLQTLKKQYEEK-------LMMLQHKIR------DTQLERDQVLqnlgsvesysEEKAKKVKCEYEKKlHAMNKELQRL 724
Cdd:pfam02841 155 EERDKLEAKYNQVprkgvkaEEVLQEFLQskeaveEAILQTDQAL----------TAKEKAIEAERAKA-EAAEAEQELL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 725 QTAQKEHARLLKNQ-SQYEKQLKKLQQDvMEMKKtkvrlmKQMKEEQEkaRLTESRRNREIAQLKKDQRKrdhqlrllEA 803
Cdd:pfam02841 224 REKQKEEEQMMEAQeRSYQEHVKQLIEK-MEAER------EQLLAEQE--RMLEHKLQEQEELLKEGFKT--------EA 286
|
....*..
gi 157823695 804 QKRNQEV 810
Cdd:pfam02841 287 ESLQKEI 293
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1515-1550 |
6.53e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 41.56 E-value: 6.53e-05
10 20 30
....*....|....*....|....*....|....*...
gi 157823695 1515 FVPVGEMRGHDSPINAICV--NSTHVFTAADDRTVRIW 1550
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVW 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
643-859 |
7.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 643 IAIKQKLIDELEnsqKRLQTLKKQYEEklmmLQhKIRDTQLERDQVLQNLGSVESYSEEKAkkvkcEYEKKLHAMNKELQ 722
Cdd:COG4913 612 LAALEAELAELE---EELAEAEERLEA----LE-AELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 723 RLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRL---MKQMKEEQEKARltesRRNREIAQLKKDQRKRDHQLR 799
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLekeLEQAEEELDELQ----DRLEAAEDLARLELRALLEER 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823695 800 LLEAQKRNQEVVLRRK-TEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGE 859
Cdd:COG4913 755 FAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
665-818 |
8.51e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.45 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 665 KQYEEKLMMLQ-HKIRDTQLERDQVLQNLgsVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQyEK 743
Cdd:pfam13868 9 RELNSKLLAAKcNKERDAQIAEKKRIKAE--EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE-ER 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157823695 744 QLKKlQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEE 818
Cdd:pfam13868 86 EQKR-QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
632-1033 |
9.33e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 632 YQADLANITCEIA--IKQKLIDELENSQKrLQTLKKQYEEKLMMLQHkirdtqLERDQVLQNLGSVESySEEKAKKVKCE 709
Cdd:TIGR01612 669 YEDDIDALYNELSsiVKENAIDNTEDKAK-LDDLKSKIDKEYDKIQN------METATVELHLSNIEN-KKNELLDIIVE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 710 YEKKLHA-----MNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNR 782
Cdd:TIGR01612 741 IKKHIHGeinkdLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNhyNDQINIDNIKDEDAKQNYDKSKEYI 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 783 EIAQLKKDQ-RKRDHQLRLLEAQ---KRNQEVVLRRK-TEEVTALRRQVRPMSDKVAGKVT-RKLSSSESPAPDTGS--- 853
Cdd:TIGR01612 821 KTISIKEDEiFKIINEMKFMKDDflnKVDKFINFENNcKEKIDSEHEQFAELTNKIKAEISdDKLNDYEKKFNDSKSlin 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 854 -SAASGEADTSRPGTQQKmripVARVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMK-WQLLERRVT----------- 920
Cdd:TIGR01612 901 eINKSIEEEYQNINTLKK----VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKeSNLIEKSYKdkfdntlidki 976
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 921 ---DIIMQKMTISNMEADMNRLLRQREELtkrREKLSKRREKIV-KESGEGDKSVANIIEEMESLTANIDYINDSIADCQ 996
Cdd:TIGR01612 977 nelDKAFKDASLNDYEAKNNELIKYFNDL---KANLGKNKENMLyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI 1053
|
410 420 430
....*....|....*....|....*....|....*..
gi 157823695 997 ANIMQmEEAKEEGETLDvtaVINACTLTEARYLLDHF 1033
Cdd:TIGR01612 1054 YNIID-EIEKEIGKNIE---LLNKEILEEAEINITNF 1086
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
702-1062 |
1.07e-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: 46.97 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 702 KAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKN---QSQYEKQLKKLQQDVMEMKKT-KVRLMKQMKEEQEKARLTE 777
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 778 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPApdtgSSAAS 857
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE----ELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 858 GEADTSRPGTQQKMripVARVQALPTPTTNgtrkkyQRKGFTGRVftsKTARMKWQLLERRVTDIIMQkmtISNMEADMN 937
Cdd:TIGR02168 325 LEELESKLDELAEE---LAELEEKLEELKE------ELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 938 RLLRQREELTKRREKLSKRREKIvkesgegDKSVANIIEEMESLTANIDY--INDSIADCQANIMQMEEAKEEGETLDVT 1015
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEA 462
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 157823695 1016 AVINACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE 1062
Cdd:TIGR02168 463 LEELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLE 502
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
645-817 |
1.41e-04 |
|
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: 44.76 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 645 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSeekakKVKCEYEKKLHAMNKELQRL 724
Cdd:pfam14988 23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFA-----KLKESQEREIQDLEEEKEKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 725 Q-----TAQKEHARLLKNQSQYEKQLKklQQDVMEM---KKTKVRLMKQMKEEQEKARLTESRRN--REIAQLKKDQRKR 794
Cdd:pfam14988 98 RaetaeKDREAHLQFLKEKALLEKQLQ--ELRILELgerATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQL 175
|
170 180
....*....|....*....|...
gi 157823695 795 DHQLRLLEAQKRNQEvvlRRKTE 817
Cdd:pfam14988 176 IQETQALEAIKSKLE---NRKQR 195
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
672-815 |
1.57e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.70 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 672 MMLQHKIRDTQLERdqvlqnlGSVESYSEEKAKKvKCEYEKKLhaMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQD 751
Cdd:pfam13904 38 LTYARKLEGLKLER-------QPLEAYENWLAAK-QRQRQKEL--QAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQ 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157823695 752 vmemkKTKVRLMKQMKEEQEKARLTESRRNREIAQ-----------LKKDQRKRDHQLRLLEAQKRNQEVVLRRK 815
Cdd:pfam13904 108 -----QTKKREESHKQKAAESASKSLAKPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
365-1007 |
2.01e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 365 ANRARNIKNKVMVNQDRASQQINALR-SEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRiKAMQ 443
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAEAARkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 444 ETVDALRARITQLVSEQANQV--LARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNEnLRKNLTRATARSPYFSASS 521
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKA 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 522 AFSPTILSSDKETIEIidlAKKDLEKLKRKEKKKKKSVAGKDDNADTDQEKKEEKGVSEKENNEldVEENQEVSDHEDEE 601
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK--AEEDKKKADELKKA 1413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 602 EEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE--KLMMLQHKIR 679
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAE 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 680 DTQLERDQVLQNLGSVESYSE----EKAKKV----KCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEK--QLKKLQ 749
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEakkaEEAKKAdeakKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeEAKKAE 1573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 750 QD-VMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKK--DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTAlRRQV 826
Cdd:PTZ00121 1574 EDkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-AEEL 1652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 827 RPMSDKVAGKvTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVAR-VQALPTPTTNGTRKKYQ-RKGFTGRVFT 904
Cdd:PTZ00121 1653 KKAEEENKIK-AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKKKAEElKKAEEENKIK 1731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 905 SKTARMKWQLLERRVTDIIMQkmtisnmEADMNRLLRQREELTKRREKLSKRREKIVKE---------SGEGDKSVANII 975
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKD-------EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeldeedekrRMEVDKKIKDIF 1804
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 157823695 976 EEMESL----TANIDYINDS----------IADCQAniMQMEEAKE 1007
Cdd:PTZ00121 1805 DNFANIieggKEGNLVINDSkemedsaikeVADSKN--MQLEEADA 1848
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
642-815 |
2.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 642 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV-LQNLGSVEsyseekakkvkceyekklhamnke 720
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLE------------------------ 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 721 lQRLQTAQKEHARLLKNQSQYEKQLKKL-------QQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRK 793
Cdd:COG4913 345 -REIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
170 180
....*....|....*....|....
gi 157823695 794 RDHQLRLLEAQKRN--QEVVLRRK 815
Cdd:COG4913 424 LEAEIASLERRKSNipARLLALRD 447
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
675-818 |
3.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 675 QHKIRDTQLERDQVLQN-LGSVESYSEEK-------AKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQY----E 742
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823695 743 KQLKKLQQDVMEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQrKRDHQLRLLEAQKRNQEVVLRRKTEE 818
Cdd:PRK12704 110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
304-513 |
3.35e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 304 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 378
Cdd:COG3206 96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 379 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 444
Cdd:COG3206 174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 445 ----------TVDALRARITQLVSEQAnQVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKNLTRATAR 513
Cdd:COG3206 254 dalpellqspVIQQLRAQLAELEAELA-ELSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
712-832 |
3.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 712 KKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKK--TKVRLMKQMKEEQEKARLTESRRNREIAQLKK 789
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 157823695 790 dQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 832
Cdd:COG4717 151 -LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
633-777 |
5.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 633 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQY---------EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 703
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823695 704 KKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTE 777
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
688-825 |
6.05e-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: 44.17 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 688 VLQNLGSVESYSEEKAKKVKCEyekKLHAMNKELQRLQTAQKEHARL---LKNQSQYEKqlKKLQQDVME-MKKTKVRLM 763
Cdd:pfam15709 305 VTGNMESEEERSEEDPSKALLE---KREQEKASRDRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMREELE 379
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823695 764 KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 825
Cdd:pfam15709 380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
632-819 |
6.09e-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: 44.67 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 632 YQADLANITCEIAIKQK----LIDELENSQKRLQTLK---KQYEEKLMMLQHKIRDTQLERDQVLQNLgsvESYSEEKAk 704
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEeledLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKRELDRLQEEL---QRLSEELA- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 705 kvkcEYEKKLHAMNKELQRLQTAQKEHARLLKNQsqyEKQLKKLQQDVmemkktkvrlmkqMKEEQEKARLTEsrrnrEI 784
Cdd:TIGR02169 424 ----DLNAAIAGIEAKINELEEEKEDKALEIKKQ---EWKLEQLAADL-------------SKYEQELYDLKE-----EY 478
|
170 180 190
....*....|....*....|....*....|....*..
gi 157823695 785 AQLKKDQRKRDHQLRLLEAQKR--NQEVVLRRKTEEV 819
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
646-827 |
6.75e-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: 43.75 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 646 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEEKAKKVKCEYEKKLHAMNKELQRLQ 725
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 726 TAQKEH--ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMK-----QMKEEqEKARLTESRRNREIAQLKKDQRKRDHQL 798
Cdd:pfam13868 198 DEKAERdeLRAKLYQEEQERKERQKEREEAEKKARQRQELQqareeQIELK-ERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
170 180
....*....|....*....|....*....
gi 157823695 799 RLLEAQKRNQevvlrRKTEEVTALRRQVR 827
Cdd:pfam13868 277 EQEEAEKRRM-----KRLEHRRELEKQIE 300
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
641-809 |
8.33e-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: 43.51 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 641 CEIAIKQKLidELENSQKRLQTLKKQYEE---KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAK---KVKCEYEKKL 714
Cdd:pfam15742 54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQeksRVADAEEKIL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 715 hamnkELQRlqtaQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRN------------- 781
Cdd:pfam15742 132 -----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdke 202
|
170 180 190
....*....|....*....|....*....|..
gi 157823695 782 ----REIAQLKKDQRKRDHQLRLLEAQKRNQE 809
Cdd:pfam15742 203 aqleMTNSQQQLRIQQQEAQLKQLENEKRKSD 234
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
647-821 |
8.43e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.91 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 647 QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLErdqvLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQT 726
Cdd:pfam05622 310 QQLLEDANRRKNELETQNRLANQRILELQQQVEELQKA----LQEQGSKAEDSSLLKQKLE-EHLEKLHEAQSELQKKKE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 727 AQKEHARllKNQSQYEKQLKKLQqdvmEMKKTKVRLMKQMKEEQ----EKARLT----ESRRNR----EIAQLKKDQRKR 794
Cdd:pfam05622 385 QIEELEP--KQDSNLAQKIDELQ----EALRKKDEDMKAMEERYkkyvEKAKSViktlDPKQNPasppEIQALKNQLLEK 458
|
170 180 190
....*....|....*....|....*....|
gi 157823695 795 DHQLRLLEAQKrnQEVVLRRKTEE---VTA 821
Cdd:pfam05622 459 DKKIEHLERDF--EKSKLQREQEEkliVTA 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
642-827 |
9.46e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 642 EIAIKQKLIDELENSQKRLQTLKKQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYE 711
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 712 KKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkVRLMKQMKEE--QEKARLTES-RRNREIAQLK 788
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREwpAETADLDADlESLPEYLALL 821
|
170 180 190
....*....|....*....|....*....|....*....
gi 157823695 789 KDQRKRDhqlrLLEAQKRNQEVVLRRKTEEVTALRRQVR 827
Cdd:COG4913 822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
634-810 |
1.00e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 634 ADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqhkirDTQLERDQVLQNLGSVESYSEEKAKKVKCEYEKK 713
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNI--------DKFLTEIKKKEKELEKLNNKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 714 LHAMNKELQRLQ----TAQKEHARL---LKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQ-EKARLTE--SRRNRE 783
Cdd:TIGR04523 175 LNLLEKEKLNIQknidKIKNKLLKLellLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQqEINEKTTeiSNTQTQ 254
|
170 180
....*....|....*....|....*..
gi 157823695 784 IAQLKKDQRKRDHQLrlleaQKRNQEV 810
Cdd:TIGR04523 255 LNQLKDEQNKIKKQL-----SEKQKEL 276
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
367-846 |
1.18e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 367 RARNIKNKVMVNQDRAS-----------------QQINALRSEITRLQMELMEyktgkriIDEEGVESINDMFHENAMLQ 429
Cdd:TIGR04523 83 QIKDLNDKLKKNKDKINklnsdlskinseikndkEQKNKLEVELNKLEKQKKE-------NKKNIDKFLTEIKKKEKELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 430 TENNNLRVRIKAMQETVDALRARITQLVSEQANQVLARAGEGNEE--ISNmIHSYIKEIEDLRAKLLESEAVNENLRKNL 507
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEllLSN-LKKKIQKNKSLESQISELKKQNNQLKDNI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 508 TRATarspyfSASSAFSPTILSSDKETIEIIDLAKKDLeklkrkekkkkksvagKDDNADTDQEKKEEKGVSEKENN--- 584
Cdd:TIGR04523 235 EKKQ------QEINEKTTEISNTQTQLNQLKDEQNKIK----------------KQLSEKQKELEQNNKKIKELEKQlnq 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 585 ---ELDVEENQEVSDHEDEEEEEEdeeeeddiegeessdesdsesdekANYQADLANITCEIAIKQKLIDELENSQKRL- 660
Cdd:TIGR04523 293 lksEISDLNNQKEQDWNKELKSEL------------------------KNQEKKLEEIQNQISQNNKIISQLNEQISQLk 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 661 ----------QTLKKQYEEKlmmlQHKIRDTQLERDQVLQNLGSVESYSE------EKAKKVKCEYEKKLHAMNKELQRL 724
Cdd:TIGR04523 349 keltnsesenSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINdleskiQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 725 qtaQKEHARLLKNQSQYEKQLKKLQQDVMEmKKTKVRLMKQMKEEQEKarltesrrnrEIAQLKKDQRKRDHQLrlleaQ 804
Cdd:TIGR04523 425 ---EKEIERLKETIIKNNSEIKDLTNQDSV-KELIIKNLDNTRESLET----------QLKVLSRSINKIKQNL-----E 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 157823695 805 KRNQEvvLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSES 846
Cdd:TIGR04523 486 QKQKE--LKSKEKELKKLNEEKKELEEKVK-DLTKKISSLKE 524
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
647-789 |
1.31e-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: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 647 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSE----------EKAKKV 706
Cdd:cd16269 123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEailqadqaltEKEKEI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 707 KCEYEKKlHAMNKELQRLQTAQKEHARLLKNQSQ-YEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTESRRNRE 783
Cdd:cd16269 201 EAERAKA-EAAEQERKLLEEQQRELEQKLEDQERsYEEHLRQLKEKMEEERENLLKEQERALESklKEQEALLEEGFKEQ 279
|
....*.
gi 157823695 784 IAQLKK 789
Cdd:cd16269 280 AELLQE 285
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
640-804 |
1.33e-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: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 640 TCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqHKIRDTQLERDQVLQnlgsveSYSEE------KAKKVKCEY--- 710
Cdd:pfam15619 17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIA------RHNEEvrvlreRLRRLQEKErdl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 711 EKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQlkKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKD 790
Cdd:pfam15619 87 ERKLKEKEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKK 164
|
170
....*....|....
gi 157823695 791 QRKRDHQLRLLEAQ 804
Cdd:pfam15619 165 HKEAQEEVKILQEE 178
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
645-870 |
1.35e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 43.13 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 645 IKQKLIDELENSQKRLQTLKKQYEEKLM--MLQHKIRDtqlERDQVLQNLGSVESYSE-EKAKKVKCEYEKKLHAMNKEL 721
Cdd:pfam04747 12 IRQQLTNRRKNLGRVAKSQRNQFRQWLLtaVLPNSIND---QRKEAFASLELTEQPQQvEKVKKSEKKKAQKQIAKDHEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 722 QRLQTAQKEHArllKNQSQYEKQLKKlqqdvmemKKTKVRLMKQMKEEQEKarltesrrnreiaqLKKDQRKRDHQLRLL 801
Cdd:pfam04747 89 EQKVNAKKAAE---KEARRAEAEAKK--------RAAQEEEHKQWKAEQER--------------IQKEQEKKEADLKKL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823695 802 EAQKRNQEVVLRRKTEEVTALRRQVRPM---SDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQK 870
Cdd:pfam04747 144 QAEKKKEKAVKAEKAEKAEKTKKASTPApveEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKK 215
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
657-821 |
1.40e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 657 QKRLQTLKKQYEEKLmmlqhkirDTQLERDQvlqnlgsvESYSEE-KAKKVKCEYEKKLHAMNKELQRLQ-TAQKEHARL 734
Cdd:pfam15709 360 QRRLQQEQLERAEKM--------REELELEQ--------QRRFEEiRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 735 lkNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQlrlLEAQKRNQEVVLRR 814
Cdd:pfam15709 424 --QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ---EAEEKARLEAEERR 498
|
....*..
gi 157823695 815 KTEEVTA 821
Cdd:pfam15709 499 QKEEEAA 505
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
659-827 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 659 RLQTLKKQYEEkLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQ 738
Cdd:COG4913 226 AADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 739 SQYEKQLKKLQQDVMEMKKTKVRLMKQMKEE--QEKARLTesrrnREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKT 816
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLE-----REIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170
....*....|.
gi 157823695 817 EEVTALRRQVR 827
Cdd:COG4913 380 EEFAALRAEAA 390
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
724-850 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 724 LQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKqmkeEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEA 803
Cdd:pfam07888 310 QQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 157823695 804 QKrnQEV-----VLRRKTEEVTALRRQVRPMSDKvaGKVTRKLSSSESPAPD 850
Cdd:pfam07888 386 EK--QELleyirQLEQRLETVADAKWSEAALTST--ERPDSPLSDSEDENPE 433
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
686-821 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 686 DQVLQNLGSVESYSEEKA--KKVKCEYEKKLHAMNKELQR----LQTAQKEHARLLKNQSQYEKqlkklqqDVMEMKKTK 759
Cdd:pfam13851 19 DITRNNLELIKSLKEEIAelKKKEERNEKLMSEIQQENKRltepLQKAQEEVEELRKQLENYEK-------DKQSLKNLK 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823695 760 VRL------MKQMKEEQE--KARLTESRRNREiaQLKKDQRKrdhqlRLLEAQKR--NQEVVLRRKTEEVTA 821
Cdd:pfam13851 92 ARLkvlekeLKDLKWEHEvlEQRFEKVERERD--ELYDKFEA-----AIQDVQQKtgLKNLLLEKKLQALGE 156
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1381-1422 |
1.57e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 1.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 157823695 1381 FQSTGKLTGHLGPVMCLTvdqISNGQDLIITGSKDHYIKMFD 1422
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLA---FSPDGKLLASGSDDGTVKVWD 39
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
638-840 |
1.73e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 638 NITCEIAIKQKLIDELENSQK-RLQTLKKQYEEKL-MMLQHKIRDTQLErDQVLQNLGSVESYSEEKAK--------KVK 707
Cdd:PHA02562 192 HIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVeEAKTIKAEIEELT-DELLNLVMDIEDPSAALNKlntaaakiKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 708 CEYEKKLHAMNKE-------LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEkarltesrR 780
Cdd:PHA02562 271 IEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE--------L 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 781 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRK 840
Cdd:PHA02562 343 KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-730 |
1.77e-03 |
|
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: 43.12 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 366 NRARNIKNkvmvnqdrASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 445
Cdd:TIGR02168 674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 446 VDALRARItqlvsEQANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARspyfsassafsp 525
Cdd:TIGR02168 735 LARLEAEV-----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE------------ 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 526 tiLSSDKETIEiidlAKKDLEKLKRKEKKKKKSVAGKDDNADTDQEKKEEKGVSEKENNELDVEE-NQEVSDhedeeeee 604
Cdd:TIGR02168 798 --LKALREALD----ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlAAEIEE-------- 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 605 edeeeeDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLE 684
Cdd:TIGR02168 864 ------LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 157823695 685 RDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKE 730
Cdd:TIGR02168 938 IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
713-827 |
2.36e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 713 KLHAMNKELQRLQTAQKEH----ARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEK-----ARLTESRRNR- 782
Cdd:COG1579 11 DLQELDSELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeEQLGNVRNNKe 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 157823695 783 ------EIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 827
Cdd:COG1579 91 yealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
699-806 |
2.37e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 40.44 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 699 SEEKAK------KVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKlqqdvmeMKKTKVRLMKQMKEEQEK 772
Cdd:pfam11600 10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEK-------ELKEKERREKKEKDEKEK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 157823695 773 A---RLTESRRNREIAQLK---KDQRKRDHQLRLLEAQKR 806
Cdd:pfam11600 83 AeklRLKEEKRKEKQEALEaklEEKRKKEEEKRLKEEEKR 122
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
651-794 |
2.38e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 651 DELENsQKRLQTLKKQYEEKLmmlQHKIRDTQLERDQVL---QNLGSVESYSEEKAKKVkCEYEKKLHAMNKELQRLQTA 727
Cdd:pfam17380 454 EEQER-QQQVERLRQQEEERK---RKKLELEKEKRDRKRaeeQRRKILEKELEERKQAM-IEEERKRKLLEKEMEERQKA 528
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823695 728 QKEHARLLKNQSQYEKQLKklqqdvMEMKKtkvRLMKQM-KEEQEKARLTESRRNREIA-QLKKDQRKR 794
Cdd:pfam17380 529 IYEEERRREAEEERRKQQE------MEERR---RIQEQMrKATEERSRLEAMEREREMMrQIVESEKAR 588
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
642-808 |
2.40e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 642 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLErdqvLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKEL 721
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI----IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 722 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVmemkktkvrlmKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLR-- 799
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKI-----------SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKke 557
|
....*....
gi 157823695 800 LLEAQKRNQ 808
Cdd:TIGR04523 558 NLEKEIDEK 566
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
651-784 |
2.43e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 651 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVlqnlgsvesysEEKAKKVKCEYEKKLHAMNKELQ-RLQTAQK 729
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 157823695 730 EHARLLKNQSQYEKQLKKLQ--QDVMEMKKtkvrLMKQMKEEQEKARLTESRRNREI 784
Cdd:PRK00409 585 EADEIIKELRQLQKGGYASVkaHELIEARK----RLNKANEKKEKKKKKQKEKQEEL 637
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
651-825 |
2.51e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 651 DELENSQKRLQTLKKQyeeklmmlqHKIRDTQLERDQVLQNLGSVES-YSEEKAKKVkcEYEKKLHAMNKELQRLQTAQK 729
Cdd:COG3206 189 KELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESqLAEARAELA--EAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 730 EH------ARLLKNQSQYEKQLKKLQQ-------DVMEMKKTKVRLMKQMKEEQEKArLTESRRNREIAQLKKD---QRK 793
Cdd:COG3206 258 ELlqspviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRI-LASLEAELEALQAREAslqAQL 336
|
170 180 190
....*....|....*....|....*....|..
gi 157823695 794 RDHQLRLLEAQKRNQEvvLRRKTEEVTALRRQ 825
Cdd:COG3206 337 AQLEARLAELPELEAE--LRRLEREVEVAREL 366
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
646-805 |
2.67e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.01 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 646 KQKLidELENSQKRLQtLKKQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVESYSE----EKAKKVKC 708
Cdd:pfam03528 24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSEntkqEAIDEVKS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 709 EYEKK---LHAMNKELQRLQTAQKeHARLLKNQSQYEKQLKKLQQDVMEMKKtkvRL------------MKQMKEEQEKA 773
Cdd:pfam03528 101 QWQEEvasLQAIMKETVREYEVQF-HRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAEKL 176
|
170 180 190
....*....|....*....|....*....|..
gi 157823695 774 RLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 805
Cdd:pfam03528 177 RSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
629-759 |
2.76e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 629 KANYQADLANItceiaikQKLIDELENSQKRLQT-------LKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEE 701
Cdd:PRK00409 508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEA-------EK 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823695 702 KAKKV----KCEYEKKLHAMNKELQRLQTAQKEHaRLLKNQSQYEKQLKKLQQDVMEMKKTK 759
Cdd:PRK00409 574 EAQQAikeaKKEADEIIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
643-826 |
3.13e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 643 IAIKQKLIDELENSQKRL-QTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvESYSEEKAKKVKCEYEKKL---HAMN 718
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLdEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQIEEREQKRQEEYEEKLqerEQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 719 KELQRLQTAQKEharllknqsQYEKQLKK---LQQDVMEMKKTKVRLMKQMKEEQEKarltESRRNREiAQLKKDQRKrd 795
Cdd:pfam13868 105 EIVERIQEEDQA---------EAEEKLEKqrqLREEIDEFNEEQAEWKELEKEEERE----EDERILE-YLKEKAERE-- 168
|
170 180 190
....*....|....*....|....*....|.
gi 157823695 796 hqlrllEAQKRNQEVVLRRKTEEVTALRRQV 826
Cdd:pfam13868 169 ------EEREAEREEIEEEKEREIARLRAQQ 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
650-889 |
3.21e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 650 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsveSYSEEKAKKVkceyEKKLHAMNKELQRLQTAQK 729
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----EALQAEIDKL----QAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 730 EHARLLKNQSQYEKQLKKL---------------QQDVMEMKKTKVRLMKQMKEEQEKArltESRRNREIAQLKKDQRKR 794
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 795 DHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIP 874
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250
....*....|....*
gi 157823695 875 VARVQALPTPTTNGT 889
Cdd:COG3883 247 AGAGAAGAAGAAAGS 261
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
645-784 |
3.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 645 IKQKLiDELENSQKRLQtlkkQYEEklmMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKCEYEKKLHAMNKELQRL 724
Cdd:PRK12704 77 LRERR-NELQKLEKRLL----QKEE---NLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIEEQLQELERI 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 725 QTAQKEHARllknqsqyEKQLKKLQqdvmemKKTKVRLMKQMKEEQEKARLTESRRNREI 784
Cdd:PRK12704 148 SGLTAEEAK--------EILLEKVE------EEARHEAAVLIKEIEEEAKEEADKKAKEI 193
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1381-1422 |
3.33e-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: 3.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 157823695 1381 FQSTGKLTGHLGPVMCLtvdQISNGQDLIITGSKDHYIKMFD 1422
Cdd:smart00320 2 GELLKTLKGHTGPVTSV---AFSPDGKYLASGSDDGTIKLWD 40
|
|
| mS26_PET12 |
cd23703 |
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ... |
690-800 |
3.48e-03 |
|
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.
Pssm-ID: 467916 [Multi-domain] Cd Length: 179 Bit Score: 40.23 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 690 QNLgsVESYSEEKAKKVKCEyekklhamNKELQRLQTAQKEHARLLKnqsQYEKQLKKLQ----QDVMEMKKTKVRLmkq 765
Cdd:cd23703 61 QNL--REGLRELEERKLKTE--------ELRAKRSERKQAERERALN---APEREDERLTlptiESALLGPLMRVRT--- 124
|
90 100 110
....*....|....*....|....*....|....*
gi 157823695 766 mkEEQEKARLTESRRNREIAQLKKDQRKRDHQLRL 800
Cdd:cd23703 125 --DPEREERAAKRRANREAKELAKKEARADALHEL 157
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
660-826 |
3.72e-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: 40.41 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 660 LQTLKKQYEEKLmmlQHKIRDTqleRDQVLQNLGSVESYSEEKAKKVKCE-----YEK-KLHAMNK-ELQRLQTAQKEha 732
Cdd:pfam15665 16 IQALKEAHEEEI---QQILAET---REKILQYKSKIGEELDLKRRIQTLEesleqHERmKRQALTEfEQYKRRVEERE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 733 rlLKNQSQYEKQLKKLQQDVMEMKKT---KVR----LMKQMKEEQEKArLTESRR--NREIAQLKKDQRKR-----DHQL 798
Cdd:pfam15665 88 --LKAEAEHRQRVVELSREVEEAKRAfeeKLEsfeqLQAQFEQEKRKA-LEELRAkhRQEIQELLTTQRAQsasslAEQE 164
|
170 180
....*....|....*....|....*....
gi 157823695 799 RLLEAQKrnQEVV-LRRKTEEVTALRRQV 826
Cdd:pfam15665 165 KLEELHK--AELEsLRKEVEDLRKEKKKL 191
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
648-815 |
3.94e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 648 KLIDELENSQKRLQTLKKQYEEKLMML--------QHKirDTQL----ERDQVLQNLGSVESYSEEKAKKVKCEYEKKLH 715
Cdd:PRK11637 103 KQIDELNASIAKLEQQQAAQERLLAAQldaafrqgEHT--GLQLilsgEESQRGERILAYFGYLNQARQETIAELKQTRE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 716 AMNKELQRLQTAQKEHARLLKNQSQyekQLKKLQQDVMEMKKTKVRLMKQMKEEQekARLTESRRNR-----EIAQLKKD 790
Cdd:PRK11637 181 ELAAQKAELEEKQSQQKTLLYEQQA---QQQKLEQARNERKKTLTGLESSLQKDQ--QQLSELRANEsrlrdSIARAERE 255
|
170 180
....*....|....*....|....*..
gi 157823695 791 QRKR-DHQLRllEAQK-RNQEVVLRRK 815
Cdd:PRK11637 256 AKARaEREAR--EAARvRDKQKQAKRK 280
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
647-778 |
3.97e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 647 QKLIDELENSQKRLQTLKKQYEEklmmlQH-KIRDTQLERDQVLQNLgsvesysEEKAKKVKCEYEKKLHAMNKELQRLQ 725
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 157823695 726 TAQKEHARLLKNQSQYEKQLKKLQQDVmemkKTKVRLMKQMKEEQEKARLTES 778
Cdd:COG3206 334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
362-593 |
5.17e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 362 LKYANRARNIKNKVMVNQDR-ASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIK 440
Cdd:COG1196 216 RELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEE-----------LRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 441 AMQETVDALRARITQLVSE---------QANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRAT 511
Cdd:COG1196 285 EAQAEEYELLAELARLEQDiarleerrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 512 ARspYFSASSAFSPTILSSDKETIEIIDLAKKDLEKLKRKEKKKKKSVAGKDDNADTDQEKKEEKGVSEKENNELDVEEN 591
Cdd:COG1196 365 EA--LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
..
gi 157823695 592 QE 593
Cdd:COG1196 443 AL 444
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
701-827 |
5.58e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 40.35 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 701 EKAKKVKCEYEKKLHAMNK-ELQRLQ--TAQKEHARLLKNQSQYEKQLKKLQQDVMEmkktkvrlmkqmkEEQEKARLTE 777
Cdd:pfam12037 29 ERAAKAARELESSPHAKKAlELMKKQeqTRQAELQAKIKEYEAAQEQLKIERQRVEY-------------EERRKTLQEE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 157823695 778 SRRNREIAQlKKDQ--RKRdHQLRLLEAQKRNQEVVlrRKTEEVTALRRQVR 827
Cdd:pfam12037 96 TKQKQQRAQ-YQDElaRKR-YQDQLEAQRRRNEELL--RKQEESVAKQEAMR 143
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
440-1060 |
7.31e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 440 KAMQETVDALRARITQLVSEQANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARspYFSA 519
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE--EYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 520 SSAfsptiLSSDKETIEIIDLAKKDLEKLKRKEKKKKKSVAGKDDNADTD-QEKKEEKGVSEKENNELDVEENQEVSDHE 598
Cdd:COG1196 294 LAE-----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEElEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 599 DEEEEEEdeeeeddiegeessdesDSESDEKANYQADLANITcEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKI 678
Cdd:COG1196 369 EAEAELA-----------------EAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 679 RDTQLERDQVLQNLgsvesyseekakkvkceyEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEmKKT 758
Cdd:COG1196 431 AELEEEEEEEEEAL------------------EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAA 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 759 KVRLMKQMKEEQE-----KARLTESRRNREIAQLKKDQRKRDHQLRLLEAQkRNQEVVLRRKTEEVTALRRQVRPMSDKV 833
Cdd:COG1196 492 RLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 834 AGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVARvqalptpttngtrkkYQRKGFTGRVFTSKTARMKWQ 913
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR---------------YYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 914 LLERRVTD----IIMQKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYIN 989
Cdd:COG1196 636 LRRAVTLAgrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823695 990 DSIADCQANIMQMEEAKEEGETLDvtavinacTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1060
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLE--------ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
669-892 |
7.39e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.19 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 669 EKLMMLQHKIRDTQLERDQvLQNLGSVESYSEEKAK---KVKCEYEKKLHAMNKElQRLQTAQKEHARLLKNQSQYEKQL 745
Cdd:PTZ00108 1102 EKVEKLNAELEKKEKELEK-LKNTTPKDMWLEDLDKfeeALEEQEEVEEKEIAKE-QRLKSKTKGKASKLRKPKLKKKEK 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 746 KKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 825
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDE 1259
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823695 826 VRPMSDKVAGKVTRKLSSSE---------SPAPDTGSSAASGEADTSRPGTQQKMR-IPVARVQALPTPTTNGTRKK 892
Cdd:PTZ00108 1260 FSSDDLSKEGKPKNAPKRVSavqysppppSKRPDGESNGGSKPSSPTKKKVKKRLEgSLAALKKKKKSEKKTARKKK 1336
|
|
| Cep57_CLD |
pfam14073 |
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ... |
674-802 |
7.98e-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: 39.15 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 674 LQHKIRDTQLERDQ-----------------VLQNLGSVESYSEEKAKKVKCEYEKKLHA-------MNKELQR----LQ 725
Cdd:pfam14073 9 LQEKIRRLELERKQaednlkqlsretshykeVLQKENDARDPSRGEVSKQNQELISQLAAaesrcslLEKQLEYmrkmVE 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823695 726 TAQKEHARLLKNQSQYEKQlkkLQQDVMEMKKtkvRLMKQMKEEQEKARLTESRRNRE--IAQLKKDQRKRDHQLRLLE 802
Cdd:pfam14073 89 NAEKERTAVLEKQASLERE---RSQDSSELQA---QLEKLEKLEQEYLRLTRTQSLAEtkIKELEEKLQEEEHQRKLVQ 161
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
727-855 |
8.25e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 38.90 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 727 AQKEHARLLKNQSQYEKQLKKLQQdvmemKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK---------KDQRKRDHQ 797
Cdd:pfam11600 11 EEKEKQRLEKDKERLRRQLKLEAE-----KEEKERLKEEAKAEKERAKEEARRKKEEEKELKekerrekkeKDEKEKAEK 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157823695 798 LRLLEAQKRNQEVVL------RRKTEEVTALRRQVRPMSDKVAGkVTRKLSSSESP-APDTGSSA 855
Cdd:pfam11600 86 LRLKEEKRKEKQEALeakleeKRKKEEEKRLKEEEKRIKAEKAE-ITRFLQKPKTQqAPKTLAGS 149
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
647-963 |
8.62e-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: 40.93 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 647 QKLIDEL---ENSQKRL----QTLKKQYEEKLmmlqhKIRDTQLE--RDQVLQNLGSVESYSEE--KAKKVKCEYEKKLH 715
Cdd:pfam01576 702 EELEDELqatEDAKLRLevnmQALKAQFERDL-----QARDEQGEekRRQLVKQVRELEAELEDerKQRAQAVAAKKKLE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 716 AMNKELQ-RLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrrnrEIAQLKKD---- 790
Cdd:pfam01576 777 LDLKELEaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA----ELLQLQEDlaas 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 791 --QRKRDHQLR---------------LLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVagkvtRKLSSSEspapDTGS 853
Cdd:pfam01576 853 erARRQAQQERdeladeiasgasgksALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL-----RKSTLQV----EQLT 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 854 SAASGEADTSrpgtqQKmripvarvqalptptTNGTRKKYQRKgftgrvftSKTARMKWQLLERRVTDiiMQKMTISNME 933
Cdd:pfam01576 924 TELAAERSTS-----QK---------------SESARQQLERQ--------NKELKAKLQEMEGTVKS--KFKSSIAALE 973
|
330 340 350
....*....|....*....|....*....|...
gi 157823695 934 ADMNRLLRQREELTKRRE---KLSKRREKIVKE 963
Cdd:pfam01576 974 AKIAQLEEQLEQESRERQaanKLVRRTEKKLKE 1006
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
659-788 |
9.10e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 38.45 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 659 RLQTLKKQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYE-KKLHAMNKELQRLQTAQKEHARLL- 735
Cdd:TIGR02473 6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 157823695 736 KNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 788
Cdd:TIGR02473 86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
704-806 |
9.71e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 39.37 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823695 704 KKVKCEYEKKLHAMNKelQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESrRNRE 783
Cdd:pfam14988 10 AKKTEEKQKKIEKLWN--QYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKES-QERE 86
|
90 100
....*....|....*....|....*
gi 157823695 784 IAQLKKDQRK--RDHQLRLLEAQKR 806
Cdd:pfam14988 87 IQDLEEEKEKvrAETAEKDREAHLQ 111
|
|
| |
