|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
18-376 |
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: 608.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 18 LRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAG 97
Cdd:cd01372 7 VRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 98 KTYTMGTGFDVNIMEEEQGIISRAVKHLFKSIEEKKtsaikngvPPPEFKVNAQFLELYNEEVLDLFDTTRDidaknKKS 177
Cdd:cd01372 87 KTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKK--------DTFEFQLKVSFLEIYNEEIRDLLDPETD-----KKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 178 NIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaenvtdnkm 257
Cdd:cd01372 154 TISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIA--------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 258 vsESPQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSKLTRLLQ 337
Cdd:cd01372 225 --PMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQ 302
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958788848 338 DSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIK 376
Cdd:cd01372 303 DSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
19-375 |
2.28e-140 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 435.08 E-value: 2.28e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 19 RIRPQLAKEKIEGCHICTSVTPGEPQVFL-------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 91
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 92 GQTGAGKTYTMGTGfdvnimEEEQGIISRAVKHLFKSIEEKKTSaikngvppPEFKVNAQFLELYNEEVLDLFDTTrdid 171
Cdd:pfam00225 81 GQTGSGKTYTMEGS------DEQPGIIPRALEDLFDRIQKTKER--------SEFSVKVSYLEIYNEKIRDLLSPS---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 172 aKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTdaen 251
Cdd:pfam00225 143 -NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 252 vtdnkmvsespqmnEFETLTAKFHFVDLAGSERLKRTG-ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDS 330
Cdd:pfam00225 218 --------------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDS 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958788848 331 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 375
Cdd:pfam00225 282 KLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
19-382 |
1.43e-134 |
|
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: 419.67 E-value: 1.43e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 19 RIRPQLAKEKIEGCHICTSVTPGEPQV-------FLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 91
Cdd:smart00129 7 RVRPLNKREKSRKSPSVVPFPDKVGKTltvrspkNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNATIFAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 92 GQTGAGKTYTMGtGFdvnimEEEQGIISRAVKHLFKSIEEKKtsaikngvPPPEFKVNAQFLELYNEEVLDLFDTTrdid 171
Cdd:smart00129 87 GQTGSGKTYTMI-GT-----PDSPGIIPRALKDLFEKIDKRE--------EGWQFSVKVSYLEIYNEKIRDLLNPS---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 172 aknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDaen 251
Cdd:smart00129 149 ----SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSG--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 252 vtdnkmvsespqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRaTHVPYRDSK 331
Cdd:smart00129 222 ----------------SGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSK 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958788848 332 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 382
Cdd:smart00129 285 LTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
18-373 |
6.32e-119 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 376.60 E-value: 6.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 18 LRIRPQLAKEKiEGCHICTSVTPG------EPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 91
Cdd:cd00106 6 VRVRPLNGREA-RSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGTIFAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 92 GQTGAGKTYTMGTGFDvnimeEEQGIISRAVKHLFKSIEEKKTsaikngvPPPEFKVNAQFLELYNEEVLDLFDttrdid 171
Cdd:cd00106 85 GQTGSGKTYTMLGPDP-----EQRGIIPRALEDIFERIDKRKE-------TKSSFSVSASYLEIYNEKIYDLLS------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 172 aKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRvcPQTDAEN 251
Cdd:cd00106 147 -PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRN--REKSGES 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 252 VTdnkmvsespqmnefetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSK 331
Cdd:cd00106 224 VT-----------------SSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN--KHIPYRDSK 284
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958788848 332 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 373
Cdd:cd00106 285 LTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
19-375 |
1.51e-103 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 334.43 E-value: 1.51e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 19 RIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKA--------FTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFA 90
Cdd:cd01371 8 RCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPKAtaneppktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYNGTIFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 91 YGQTGAGKTYTMGtGFDVNimEEEQGIISRAVKHLFKSIEekKTSAIKNgvpppeFKVNAQFLELYNEEVldlfdttRDI 170
Cdd:cd01371 88 YGQTGTGKTYTME-GKRED--PELRGIIPNSFAHIFGHIA--RSQNNQQ------FLVRVSYLEIYNEEI-------RDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 171 DAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV-CqtrvcpqtdA 249
Cdd:cd01371 150 LGKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIeC---------S 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 250 ENVTDNKMVSEspqmnefetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKskRATHVPYRD 329
Cdd:cd01371 221 EKGEDGENHIR----------VGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRD 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958788848 330 SKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 375
Cdd:cd01371 289 SKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
19-377 |
2.85e-101 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 327.63 E-value: 2.85e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 19 RIRPQLAKEKIE-GCHICTSVTPGEPQVFLGKD---KAFTFDYVFDIDSQQEQIYTQcIEKLIEGCFEGYNATVFAYGQT 94
Cdd:cd01366 9 RVRPLLPSEENEdTSHITFPDEDGQTIELTSIGakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIFAYGQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 95 GAGKTYTM-GTgfdvnimEEEQGIISRAVKHLFKSIEEKKTSAIKngvpppeFKVNAQFLELYNEEVLDLFDTTRdidAK 173
Cdd:cd01366 88 GSGKTYTMeGP-------PESPGIIPRALQELFNTIKELKEKGWS-------YTIKASMLEIYNETIRDLLAPGN---AP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 174 NKKSNIRiHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRvcPQTDaenvt 253
Cdd:cd01366 151 QKKLEIR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRN--LQTG----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 254 dnkmvsespqmnefETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKratHVPYRDSKLT 333
Cdd:cd01366 223 --------------EISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS---HIPYRNSKLT 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958788848 334 RLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKN 377
Cdd:cd01366 286 YLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
18-375 |
2.61e-100 |
|
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: 325.84 E-value: 2.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 18 LRIRPQLAKEKIEGCHICTSVTPGEPQVF----------------------LGKDKAFTFDYVFDIDSQQEQIYTQCIEK 75
Cdd:cd01370 6 VRVRPFSEKEKNEGFRRIVKVMDNHMLVFdpkdeedgffhggsnnrdrrkrRNKELKYVFDRVFDETSTQEEVYEETTKP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 76 LIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVKHLFKSIEEKKTSAikngvpppEFKVNAQFLE 154
Cdd:cd01370 86 LVDGVLNGYNATVFAYGATGAGKTHTMlGT-------PQEPGLMVLTMKELFKRIESLKDEK--------EFEVSMSYLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 155 LYNEEVLDLFDTTrdidakNKKSNIRihEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIF 234
Cdd:cd01370 151 IYNETIRDLLNPS------SGPLELR--EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 235 TIHVCQTrvcpqtdaenvtdNKMVSESPQmnefeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISA 314
Cdd:cd01370 223 QITVRQQ-------------DKTASINQQ-----VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINA 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958788848 315 LGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 375
Cdd:cd01370 285 LADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
18-382 |
4.55e-97 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 317.37 E-value: 4.55e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 18 LRIRPQLAKEKIEGCHIC-------TSVTPGEPQVFLGKD-----KAFTFDYVFD-IDSQ------QEQIYTQCIEKLIE 78
Cdd:cd01365 7 VRVRPFNSREKERNSKCIvqmsgkeTTLKNPKQADKNNKAtrevpKSFSFDYSYWsHDSEdpnyasQEQVYEDLGEELLQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 79 GCFEGYNATVFAYGQTGAGKTYTMgTGFDvnimeEEQGIISRAVKHLFKSIEEKKTSAIKngvpppeFKVNAQFLELYNE 158
Cdd:cd01365 87 HAFEGYNVCLFAYGQTGSGKSYTM-MGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMS-------YSVEVSYMEIYNE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 159 EVLDLFDTtrdiDAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHV 238
Cdd:cd01365 154 KVRDLLNP----KPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 239 CQTRvcpqTDAENVTDNKMVSespqmnefetltaKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGD- 317
Cdd:cd01365 230 TQKR----HDAETNLTTEKVS-------------KISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADm 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958788848 318 ----KSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 382
Cdd:cd01365 293 ssgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
17-375 |
2.23e-96 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 313.88 E-value: 2.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 17 LLRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKD--KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQT 94
Cdd:cd01369 7 VCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSEtgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFAYGQT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 95 GAGKTYTMgtgFDVNIMEEEQGIISRAVKHLFKSIEeKKTSAIkngvpppEFKVNAQFLELYNEEVLDLFDTTRDidakn 174
Cdd:cd01369 87 SSGKTYTM---EGKLGDPESMGIIPRIVQDIFETIY-SMDENL-------EFHVKVSYFEIYMEKIRDLLDVSKT----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 175 kksNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQtrvcpqtdaENVTD 254
Cdd:cd01369 151 ---NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ---------ENVET 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 255 NKmvsespqmnefeTLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTR 334
Cdd:cd01369 219 EK------------KKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTR 284
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958788848 335 LLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNI 375
Cdd:cd01369 285 ILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
17-384 |
1.65e-92 |
|
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: 303.86 E-value: 1.65e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 17 LLRIRPQLAKEKIEGCHICTSVTPGEPQVFL--------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATV 88
Cdd:cd01364 7 VVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYNCTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 89 FAYGQTGAGKTYTMgTGFDVNIME------EEQGIISRAVKHLFKSIEEKKTsaikngvpppEFKVNAQFLELYNEEVLD 162
Cdd:cd01364 87 FAYGQTGTGKTYTM-EGDRSPNEEytweldPLAGIIPRTLHQLFEKLEDNGT----------EYSVKVSYLEIYNEELFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 163 LFDttrdiDAKNKKSNIRIHEDS--TGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcq 240
Cdd:cd01364 156 LLS-----PSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITI-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 241 trvcpqtdaenvtdnkMVSESPQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK 320
Cdd:cd01364 229 ----------------HIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAP 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958788848 321 ratHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 384
Cdd:cd01364 293 ---HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
48-515 |
2.11e-91 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 308.59 E-value: 2.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 48 GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVKHLF 126
Cdd:COG5059 53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMsGT-------EEEPGIIPLSLKELF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 127 KSIEEKKTSAikngvpppEFKVNAQFLELYNEEVLDLFDttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 206
Cdd:COG5059 126 SKLEDLSMTK--------DFAVSISYLEIYNEKIYDLLS--------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 207 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtdAENVTDNKmvsespqmnefETLTAKFHFVDLAGSERLK 286
Cdd:COG5059 190 DLLRKGEKNRTTASTEINDESSRSHSIFQIEL----------ASKNKVSG-----------TSETSKLSLVDLAGSERAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 287 RTGATGERAKEGISINCGLLALGNVISALGDKSKRAtHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTL 366
Cdd:COG5059 249 RTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 367 KYANRARNIKNKVMVNQDRASQ-QINALRSEITRLQMELMEYKTGKRIIDEEgvesiNDMFHENAMLQT---ENNNLRVR 442
Cdd:COG5059 328 KFASRAKSIKNKIQVNSSSDSSrEIEEIKFDLSEDRSEIEILVFREQSQLSQ-----SSLSGIFAYMQSlkkETETLKSR 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958788848 443 IK-AMQETVDALRARITQLVSEqanqvlaraGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKSLTRAT 515
Cdd:COG5059 403 IDlIMKSIISGTFERKKLLKEE---------GWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDL 467
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
17-384 |
1.02e-89 |
|
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: 295.96 E-value: 1.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 17 LLRIRPQLAKEKIEGCHICTSVTPGEPQVFLGK-DKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTG 95
Cdd:cd01373 6 FVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKpPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYGQTG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 96 AGKTYTM--GTGFDVNIMEEEQGIISRAVKHLFKSIEEKKTSAIKNgvppPEFKVNAQFLELYNEEVLDLFDTTrdidak 173
Cdd:cd01373 86 SGKTYTMwgPSESDNESPHGLRGVIPRIFEYLFSLIQREKEKAGEG----KSFLCKCSFLEIYNEQIYDLLDPA------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 174 nkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtdaenvt 253
Cdd:cd01373 156 --SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI--------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 254 dnkmvsES-PQMNEFETL-TAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSK-RATHVPYRDS 330
Cdd:cd01373 219 ------ESwEKKACFVNIrTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYRDS 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958788848 331 KLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQD 384
Cdd:cd01373 293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
51-375 |
1.40e-89 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 294.24 E-value: 1.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 51 KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGfdvnimEEEQGIISRAVKHLFKSIE 130
Cdd:cd01374 39 TSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 131 EKKTSaikngvpppEFKVNAQFLELYNEEVLDLFDTTrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLK 210
Cdd:cd01374 113 DTPDR---------EFLLRVSYLEIYNEKINDLLSPT--------SQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 211 LGALSRTTASTQMNVQSSRSHAIFTIHVcQTRVCPQTDAENVTdnkmvsespqmneFETLTakfhFVDLAGSERLKRTGA 290
Cdd:cd01374 176 RGEKNRHVGETDMNERSSRSHTIFRITI-ESSERGELEEGTVR-------------VSTLN----LIDLAGSERAAQTGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 291 TGERAKEGISINCGLLALGNVISALGDkSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYAN 370
Cdd:cd01374 238 AGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFAS 316
|
....*
gi 1958788848 371 RARNI 375
Cdd:cd01374 317 RAKKI 321
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
18-373 |
2.52e-69 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 236.25 E-value: 2.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 18 LRIRPQLAKEKIEGCHICTSVTpGEPQVFL------GKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAY 91
Cdd:cd01376 6 VRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATVFAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 92 GQTGAGKTYTMGTGFdvnimeEEQGIISRAVKHLFkSIEEKKTSAikngvpppeFKVNAQFLELYNEEVLDLFDTtrdid 171
Cdd:cd01376 85 GSTGAGKTFTMLGSP------EQPGLMPLTVMDLL-QMTRKEAWA---------LSFTMSYLEIYQEKILDLLEP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 172 aknKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpqtdaen 251
Cdd:cd01376 144 ---ASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 252 vtdnkmvSESPQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALgdkSKRATHVPYRDSK 331
Cdd:cd01376 208 -------DQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL---NKNLPRIPYRDSK 277
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958788848 332 LTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRAR 373
Cdd:cd01376 278 LTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
52-371 |
3.83e-69 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 236.04 E-value: 3.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 52 AFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGFDVNimEEEQGIISRAVKHLFksiEE 131
Cdd:cd01367 51 TFRFDYVFDESSSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQ--EESKGIYALAARDVF---RL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 132 KKTSAIKNGvpppeFKVNAQFLELYNEEVLDLFdttrdidakNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKL 211
Cdd:cd01367 126 LNKLPYKDN-----LGVTVSFFEIYGGKVFDLL---------NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIES 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 212 GALSRTTASTQMNVQSSRSHAIFTIhVCQTRvcpqtdaenvtdnkmvsespqmnEFETLTAKFHFVDLAGSER-LKRTGA 290
Cdd:cd01367 192 GSSLRTTGQTSANSQSSRSHAILQI-ILRDR-----------------------GTNKLHGKLSFVDLAGSERgADTSSA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 291 TGERAKEGISINCGLLALGNVISALGDKSkraTHVPYRDSKLTRLLQDSL-GGNSQTIMIACVSPSDRDFMETLNTLKYA 369
Cdd:cd01367 248 DRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYA 324
|
..
gi 1958788848 370 NR 371
Cdd:cd01367 325 DR 326
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
50-373 |
9.96e-69 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 235.17 E-value: 9.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 50 DKAFTFDYVFDiDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMgTGFDVNImeEEQGIISRAVKHLFKSI 129
Cdd:cd01375 47 DWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTM-TGGTENY--KHRGIIPRALQQVFRMI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 130 EEKKTSAIKngvpppefkVNAQFLELYNEEVLDLFDTTRDIDAKNKKsnIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCL 209
Cdd:cd01375 123 EERPTKAYT---------VHVSYLEIYNEQLYDLLSTLPYVGPSVTP--MTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 210 KLGALSRTTASTQMNVQSSRSHAIFTIHvcqtrvcpqtdaenvtdnkMVSESPQMNEFETLTAKFHFVDLAGSERLKRTG 289
Cdd:cd01375 192 FLGETNRIIASHTMNKNSSRSHCIFTIH-------------------LEAHSRTLSSEKYITSKLNLVDLAGSERLSKTG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 290 ATGERAKEGISINCGLLALGNVISALGDKSKraTHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 369
Cdd:cd01375 253 VEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330
|
....
gi 1958788848 370 NRAR 373
Cdd:cd01375 331 SRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
18-369 |
6.73e-65 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 224.58 E-value: 6.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 18 LRIRPQLAKEKI---EGC-HI--CTSVTPGEPQVFLG---------KDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFE 82
Cdd:cd01368 7 LRVRPLSKDELEsedEGCiEVinSTTVVLHPPKGSAAnksernggqKETKFSFSKVFGPNTTQKEFFQGTALPLVQDLLH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 83 GYNATVFAYGQTGAGKTYTM-GTgfdvnimEEEQGIISRAVKHLFKSIeekktsaikngvppPEFKVNAQFLELYNEEVL 161
Cdd:cd01368 87 GKNGLLFTYGVTNSGKTYTMqGS-------PGDGGILPRSLDVIFNSI--------------GGYSVFVSYIEIYNEYIY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 162 DLFDTTRDIDAKNKKSnIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQt 241
Cdd:cd01368 146 DLLEPSPSSPTKKRQS-LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQ- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 242 rvcpqtdAENVTDNKMVSESPQMNefetlTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKR 321
Cdd:cd01368 224 -------APGDSDGDVDQDKDQIT-----VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQ 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958788848 322 AT--HVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYA 369
Cdd:cd01368 292 GTnkMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
51-408 |
2.74e-63 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 237.91 E-value: 2.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 51 KAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTM----GTGFDVNIMEEEQGIISRAVKHLF 126
Cdd:PLN03188 132 QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMwgpaNGLLEEHLSGDQQGLTPRVFERLF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 127 KSIEEKKtsaIKNGVPPPEFKVNAQFLELYNEEVLDLFDTTrdidaknkKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMM 206
Cdd:PLN03188 212 ARINEEQ---IKHADRQLKYQCRCSFLEIYNEQITDLLDPS--------QKNLQIREDVKSGVYVENLTEEYVKTMKDVT 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 207 QCLKLGALSRTTASTQMNVQSSRSHAIFTIHVcqtrvcpQTDAENVTDNkmvsespqMNEFETltAKFHFVDLAGSERLK 286
Cdd:PLN03188 281 QLLIKGLSNRRTGATSINAESSRSHSVFTCVV-------ESRCKSVADG--------LSSFKT--SRINLVDLAGSERQK 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 287 RTGATGERAKEGISINCGLLALGNVISALGDKSK--RATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLN 364
Cdd:PLN03188 344 LTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFS 423
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958788848 365 TLKYANRARNIKNKVMVNQDrASQQINALRSEITRLQMELMEYK 408
Cdd:PLN03188 424 TLRFAQRAKAIKNKAVVNEV-MQDDVNFLREVIRQLRDELQRVK 466
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1249-1562 |
3.12e-59 |
|
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: 206.03 E-value: 3.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1249 CVHVAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWDI 1325
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDgkLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSdKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1326 rESAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLGP 1404
Cdd:cd00200 81 -ETGECVRTLTGH----------------------TSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKCLTTLRGHTDW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1405 VMCLTVDQisnGQDLIITGSKDHYIKMFDVTEGalgtvSPTHNFEpPHYDGIEALAIQGDN--LFSGSRDNGIKKWDLAQ 1482
Cdd:cd00200 138 VNSVAFSP---DGTFVASSSQDGTIKLWDLRTG-----KCVATLT-GHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1483 KGLLQQVPnAHKDWVCALGLVPGHPILLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAISV--NSTHVFTAADDRTVRI 1560
Cdd:cd00200 209 GKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRI 287
|
..
gi 1958788848 1561 WK 1562
Cdd:cd00200 288 WD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1248-1565 |
8.81e-48 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 176.64 E-value: 8.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1248 QCVHVAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVvsvkycnyTSLVFT------VSTSY 1319
Cdd:COG2319 111 LLLRTLTGHTGAVRSVAFSPDgkTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--------TSVAFSpdgkllASGSD 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1320 ---IKVWDIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQST 1395
Cdd:COG2319 183 dgtVRLWDLA-TGKLLRTLTGH----------------------TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1396 GKLTGHLGPVMCLTVDqiSNGQdLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAI--QGDNLFSGSRDN 1473
Cdd:COG2319 240 RTLTGHSGSVRSVAFS--PDGR-LLASGSADGTVRLWDLATGELLRTLTGHS------GGVNSVAFspDGKLLASGSDDG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1474 GIKKWDLAQkGLLQQVPNAHKDWVCALGLVPGHPILLSGCRGGILKLWNVDTFVPVGEMRGHDSPIN--AISVNSTHVFT 1551
Cdd:COG2319 311 TVRLWDLAT-GKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTsvAFSPDGRTLAS 389
|
330
....*....|....
gi 1958788848 1552 AADDRTVRIWKAHN 1565
Cdd:COG2319 390 GSADGTVRLWDLAT 403
|
|
| Rcc_KIF21A |
cd22263 |
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ... |
929-1010 |
1.05e-43 |
|
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: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 929 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIAKESGEGDKNLVNISEEMESLTANIDYINDSIADCQANIMQMEE 1008
Cdd:cd22263 1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSISDCQANIMQMEE 80
|
..
gi 1958788848 1009 AK 1010
Cdd:cd22263 81 AK 82
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1248-1479 |
1.49e-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: 137.47 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1248 QCVHVAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVWD 1324
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFSPDgrILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1325 IReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWDLKRFQSTGKLTGHLG 1403
Cdd:cd00200 164 LR-TGKCVATLTGH----------------------TGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGHEN 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958788848 1404 PVMCLTVdqiSNGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNfepphyDGIEALAIQGDN--LFSGSRDNGIKKWD 1479
Cdd:cd00200 221 GVNSVAF---SPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT------NSVTSLAWSPDGkrLASGSADGTIRIWD 289
|
|
| Rcc_KIF21 |
cd22248 |
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ... |
929-1010 |
3.28e-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: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 929 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKiAKESGEGDKNLVNISEEMESLTANIDYINDSIADCQANIMQMEE 1008
Cdd:cd22248 1 NKQTISNLERDMERWLKEREKLSKELEKLEKKRER-ALDEGKDESVLRDLEEEIDSLKANIDYVQENITECQSNIMQMEE 79
|
..
gi 1958788848 1009 AK 1010
Cdd:cd22248 80 SK 81
|
|
| Rcc_KIF21B |
cd22262 |
regulatory coiled-coil domain found in kinesin-like protein KIF21B; KIF21B is a plus-end ... |
929-1010 |
6.00e-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: 108.35 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 929 QKMTISNMEADMNRLLRQREELTKRREKLSKRREKIAKESGEGDKNLVNISEEMESLTANIDYINDSIADCQANIMQMEE 1008
Cdd:cd22262 1 QRMTIINLEADMERLLKKREELSLLQEALVRKRQKLLSESPEEEKGVQELNEEIEVLNANIDYINDSISDCQATIVQIEE 80
|
..
gi 1958788848 1009 AK 1010
Cdd:cd22262 81 TK 82
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
19-163 |
5.73e-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: 87.66 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 19 RIRPQLAKEkiegCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYtQCIEKLIEGCFEGYNATVFAYGQTGAGK 98
Cdd:pfam16796 27 RVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVF-QEISQLVQSCLDGYNVCIFAYGQTGSGS 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958788848 99 TYTMgtgfdvnimeeeqgiISRAVKHLFKSIEEKKTSaikngvppPEFKVNAQFLELYNEEVLDL 163
Cdd:pfam16796 102 NDGM---------------IPRAREQIFRFISSLKKG--------WKYTIELQFVEIYNESSQDL 143
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1247-1388 |
1.04e-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: 85.46 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1247 LQCVHVAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVST-SYIKVW 1323
Cdd:cd00200 167 GKCVATLTGHTGEVNSVAFSPDgeKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVW 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788848 1324 DIReSAKCIRTLTSSgqvtlgeacsastsrtvaipsgESQINQIALNPTGTFLYAASG-NAVRMWD 1388
Cdd:cd00200 247 DLR-TGECVQTLSGH----------------------TNSVTSLAWSPDGKRLASGSAdGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1378-1570 |
1.11e-15 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 81.11 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1378 AASGNAVRMWDLKRFQSTGKLTGHLGPVMCLTVDQISNGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNFEPPHYdgie 1457
Cdd:COG2319 9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSV---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1458 ALAIQGDNLFSGSRDNGIKKWDLAQkGLLQQVPNAHKDWVCALGLVPGHPILLSGCRGGILKLWNVDTFVPVGEMRGHDS 1537
Cdd:COG2319 85 AFSPDGRLLASASADGTVRLWDLAT-GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1958788848 1538 PIN--AISVNSTHVFTAADDRTVRIWkahNLQDGQ 1570
Cdd:COG2319 164 AVTsvAFSPDGKLLASGSDDGTVRLW---DLATGK 195
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
17-314 |
5.96e-13 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 68.53 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 17 LLRIRPQLAKEKIEGCHIctsvtpgepqvflgkdkaFTFDYVFDIDSQQEQIYTQCiEKLIEGCFEGYN-ATVFAYGQTG 95
Cdd:cd01363 2 LVRVNPFKELPIYRDSKI------------------IVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 96 AGKTYTMgtgfdvnimeeeQGIISRAVKHLFKSIEEKKTSAikngvpppefkvnaqflelyneevldlfdttrdidaknk 175
Cdd:cd01363 63 AGKTETM------------KGVIPYLASVAFNGINKGETEG--------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 176 ksnirihedstggiyTVGVTTRTVNTEPEMMQCLKLGALSRtTASTQMNVQSSRSHAIFTIhvcqtrvcpqtdaenvtdn 255
Cdd:cd01363 92 ---------------WVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------------- 136
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958788848 256 kmvsespqmnefetltakfhFVDLAGSERlkrtgatgerakegisINCGLLALGNVISA 314
Cdd:cd01363 137 --------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
633-844 |
1.93e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 633 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV---LQNLGSVESYSEEKAKK 709
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 710 VKCEYEKKLHAM---------------------NKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMK 768
Cdd:COG4942 102 QKEELAELLRALyrlgrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 769 QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK---------VAG 839
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAalkgklpwpVSG 261
|
....*
gi 1958788848 840 KVTRK 844
Cdd:COG4942 262 RVVRR 266
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
633-1031 |
1.72e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.82 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 633 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEkAKKVKC 712
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE-VEDLKT 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 713 EYEKKlHAMNKEL-QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMK--EEQEKARLTESRRNREIA 789
Cdd:pfam05483 479 ELEKE-KLKNIELtAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEF 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 790 QLKKDQ-----RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKV-----AGKVTRKLSSSESPTPDAgSSV 859
Cdd:pfam05483 558 IQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIeelhqENKALKKKGSAENKQLNA-YEI 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 860 TSGEADASRPGTQQKMRipvarvQALPTPTTNGTRKRYQRKGFTGRVFTSKTARMKWQLLERRVTEIIMQKmtISNMEAD 939
Cdd:pfam05483 637 KVNKLELELASAKQKFE------EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHK--IAEMVAL 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 940 MNRLLRQREELTKRREK---LSKRREK---IAKESGEGDknLVNISEEMESLTAnidyindsiadcqanimQMEEAKEEG 1013
Cdd:pfam05483 709 MEKHKHQYDKIIEERDSelgLYKNKEQeqsSAKAALEIE--LSNIKAELLSLKK-----------------QLEIEKEEK 769
|
410
....*....|....*...
gi 1958788848 1014 ETLDVTAVINACTLTEAR 1031
Cdd:pfam05483 770 EKLKMEAKENTAILKDKK 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
633-1016 |
3.04e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 633 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE---KLMMLQHKIRdtqlERDQVLQNLGSVESYSEEKAKK 709
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHE----LYEEAKAKKEELERLKKRLTGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 710 VKCEYEKKLHAMNKelqRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVR--LMKQMKEEQEKARLTESRRnRE 787
Cdd:PRK03918 385 TPEKLEKELEELEK---AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYT-AE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 788 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRrKTEEVTALRR---QVRPMSDKVAG-------KVTRKLSSSESPTPDAGS 857
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeQLKELEEKLKKynleeleKKAEEYEKLKEKLIKLKG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 858 SVTSGEADASR-PGTQQKMRIPVARVQALPTPTTNgTRKRYQRKGFT------GRVFTSKTARMKW-------QLLERRV 923
Cdd:PRK03918 540 EIKSLKKELEKlEELKKKLAELEKKLDELEEELAE-LLKELEELGFEsveeleERLKELEPFYNEYlelkdaeKELEREE 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 924 TEIIMQKMTISNMEADMNRLLRQREELTKRREKLSKR-----REKIAKESGEGDKNLVNISEEMESLTANIDYINDSIAD 998
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
410
....*....|....*...
gi 1958788848 999 CQANIMQMEEAKEEGETL 1016
Cdd:PRK03918 699 LKEELEEREKAKKELEKL 716
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
636-839 |
4.57e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 636 YQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYE 715
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 716 KKLHAMNkelQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRL---MKQMKEEQEKA--RLTESRRN---RE 787
Cdd:TIGR02168 365 AELEELE---SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELlkKLEEAELKelqAE 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958788848 788 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAG 839
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
656-959 |
5.57e-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: 61.22 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 656 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQTAQKEH 735
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 736 ARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMK-QMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRlleaqKRNQEV 814
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD-----TVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 815 VLRRKTEEvtALRRQVRPMSDKVAGKVTRKLSSSESPtpdAGSSVTSGEADASRPGTQQKMR-IPVARVQALPTPTTNGT 893
Cdd:TIGR00606 846 ELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNL---QRRQQFEEQLVELSTEVQSLIReIKDAKEQDSPLETFLEK 920
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958788848 894 RKRYQRKGFTGRVFTSKTARMKWQLLERRVTEIIMQKMTISNM------------EADMNRLLRQREELTKRREKLSK 959
Cdd:TIGR00606 921 DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkddylkqkETELNTVNAQLEECEKHQEKINE 998
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
661-1016 |
1.62e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 661 QKRLQTLKKQYEEK--LMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKvkceyekklHAMNKELQRLQtaqkEHARl 738
Cdd:pfam15921 244 EDQLEALKSESQNKieLLLQQHQDRIEQLISEHEVEITGLTEKASSARSQA---------NSIQSQLEIIQ----EQAR- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 739 lkNQ-SQYEKQLKKLQQDVTEMKkTKVRLMKQMKE----EQEK------ARLTESRRNREiaQLKKDQRKRDHQLRLLEA 807
Cdd:pfam15921 310 --NQnSMYMRQLSDLESTVSQLR-SELREAKRMYEdkieELEKqlvlanSELTEARTERD--QFSQESGNLDDQLQKLLA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 808 QkrnqevvLRRKTEEVTALRRQVRPMSDKvagkvtrklsssesptpDAGSSVTsgeADASRPGTQQKmRIPVARVQALPT 887
Cdd:pfam15921 385 D-------LHKREKELSLEKEQNKRLWDR-----------------DTGNSIT---IDHLRRELDDR-NMEVQRLEALLK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 888 PTTNGTRKRYQR-------KGFTGRVFTSKTARMKW--QLLERRVTEIIMQKMTISNME---ADMNRLLRQREE-LTKRR 954
Cdd:pfam15921 437 AMKSECQGQMERqmaaiqgKNESLEKVSSLTAQLEStkEMLRKVVEELTAKKMTLESSErtvSDLTASLQEKERaIEATN 516
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788848 955 EKLSKRREKIakesgegDKNLvnisEEMESLTANIDYINDSIADCQANIMQMEEAKEEGETL 1016
Cdd:pfam15921 517 AEITKLRSRV-------DLKL----QELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL 567
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
638-1024 |
5.07e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 638 ADLANITCEIAIKQKLIDELENSQKRLQTlkkqyeeklmmlqhkirdtqlERDQvlqnlgsVESYSEEKAKKVKCEYEKK 717
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRR---------------------EREK-------AERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 718 LHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKE--EQEKARLTESRRN--REIAQLKK 793
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGEleAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 794 DQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgKVTRKLSSSEsptpdagssvtsgeadasrpgtqQ 873
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KLTEEYAELK-----------------------E 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 874 KMRIPVARVQALPTP--TTNGTRKRYQRK--GFTGRVFTSKTARMKWQLLERRVTeiimqkMTISNMEADMNRLLRQREE 949
Cdd:TIGR02169 365 ELEDLRAELEEVDKEfaETRDELKDYREKleKLKREINELKRELDRLQEELQRLS------EELADLNAAIAGIEAKINE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 950 LTKRREKLSKRREKIAKESGEGDKNLVNISEEMESLTANIDYINDSIADCQANIMQMEEAK-----EEGETLDVTAVINA 1024
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseeRVRGGRAVEEVLKA 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
688-1010 |
5.25e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 688 ERDQVLQNLGSVESY--SEEKAKKVKCEYEKKLHAMNKELQRlqTAQKEhaRLLKNQsqyEKQLKKLQQDVTEMKKTKVR 765
Cdd:PRK03918 146 SREKVVRQILGLDDYenAYKNLGEVIKEIKRRIERLEKFIKR--TENIE--ELIKEK---EKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 766 LMKQMKE-EQEKARLTESRRnrEIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMsDKVAGKVT-- 842
Cdd:PRK03918 219 LREELEKlEKEVKELEELKE--EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEey 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 843 RKLSSSESPTPDAGSSVTSGEADASRpgtqqkmRIpvarvqalptpttNGTRKRYQRkgftgrvFTSKTARMKWqlLERR 922
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEE-------EI-------------NGIEERIKE-------LEEKEERLEE--LKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 923 VTEIIMQKMTISNMEADMNRLLRQREELTKRREKLSKRR-EKIAKESGEGDKNLVNISEEMESLTANIDYINDSIADCQA 1001
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
....*....
gi 1958788848 1002 NIMQMEEAK 1010
Cdd:PRK03918 427 AIEELKKAK 435
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
633-873 |
3.85e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 633 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNL---GSVESYSEE--KA 707
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVllGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 708 KKvkceyekkLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNRE 787
Cdd:COG3883 112 ES--------FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 788 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPTPDAGSSVTSGEADAS 867
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
|
....*.
gi 1958788848 868 RPGTQQ 873
Cdd:COG3883 264 AAGAAA 269
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
635-838 |
4.97e-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: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 635 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAKKVK 711
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 712 CEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEK-ARLTESRRN----- 785
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEEleeli 868
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788848 786 ----REIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVA 838
Cdd:TIGR02168 869 eeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
719-1017 |
5.17e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.84 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 719 HAMNKELQR--------LQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKK-------TKVRLMKQMkeEQEKARLTESR 783
Cdd:pfam12128 596 AASEEELRErldkaeeaLQSAREKQAAAEEQLVQANGELEKASREETFARTalknarlDLRRLFDEK--QSEKDKKNKAL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 784 RnREIAQLKKDQRKRDHQLRLLEAQKRN-----QEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESptpdagss 858
Cdd:pfam12128 674 A-ERKDSANERLNSLEAQLKQLDKKHQAwleeqKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSG-------- 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 859 vtsgeADASRPGTQQKMRIPVARVQalPTPTTNGTRKRyQRKGFTGR-----VFTSKTARMKWQLLERRVTEIIMQKMTI 933
Cdd:pfam12128 745 -----AKAELKALETWYKRDLASLG--VDPDVIAKLKR-EIRTLERKieriaVRRQEVLRYFDWYQETWLQRRPRLATQL 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 934 SNMEADMNRLlrqREELTKRREKLSKRREKIAKESGEGDKNLVNISEEMESLTANIDYINDSIADCQANimqmEEAKEEG 1013
Cdd:pfam12128 817 SNIERAISEL---QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSE----QAQGSIG 889
|
....
gi 1958788848 1014 ETLD 1017
Cdd:pfam12128 890 ERLA 893
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1248-1283 |
7.49e-07 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 46.95 E-value: 7.49e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1958788848 1248 QCVHVAEGHTKAVLCVDSTDD--LLFTGSKDRTCKVWN 1283
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
650-830 |
1.70e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.82 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 650 KQKLIDELENSQK-------RLQTLKKQ---YEEKLMMLQHkiRDTQLERDQVLQNLGSVESYSEEKakkVKCEYEKKlh 719
Cdd:pfam17380 305 KEEKAREVERRRKleeaekaRQAEMDRQaaiYAEQERMAME--RERELERIRQEERKRELERIRQEE---IAMEISRM-- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 720 amnKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESR-----RNREIAQLKKD 794
Cdd:pfam17380 378 ---RELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeeRAREMERVRLE 454
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958788848 795 QRKRDHQLRLL---EAQKRNQEVVL---RRKTEEVTALRRQV 830
Cdd:pfam17380 455 EQERQQQVERLrqqEEERKRKKLELekeKRDRKRAEEQRRKI 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
648-822 |
1.94e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 648 AIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQR 727
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 728 LQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLtesrRNREIAQLKKDQRKRDHQLRLLEA 807
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI----KAAEEAKKAEEDKKKAEEAKKAEE 1685
|
170
....*....|....*
gi 1958788848 808 QKRNQEVVLRRKTEE 822
Cdd:PTZ00121 1686 DEKKAAEALKKEAEE 1700
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
637-831 |
1.96e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 637 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEK 716
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE-ELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 717 KLHAMNKELQRLQTAQKE-HARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQ 795
Cdd:COG1196 338 ELEELEEELEEAEEELEEaEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958788848 796 RKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVR 831
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
656-986 |
2.30e-06 |
|
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: 52.20 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 656 ELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNK-------ELQRL 728
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIR-ELEEDIKTLTQrvleretELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 729 QTAQKEHARLLKNQSQYEKQLK-KLQQDVTEMKKtkvrlmkqMKEEQEKARLTESRRNREIAQLKKDQRKRdhQLRLLEA 807
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQaKLQQTEEELRS--------LSKEFQELRNSLAQRDTQVLQLQDTITTL--TQKLTTA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 808 QkrnqevvlrRKTEEVTALRRQVRPMSDkvagkvtrKLSSSESPTPDAGSSVTSgeADASRPGTQQKMRipVARVQALPT 887
Cdd:pfam07888 226 H---------RKEAENEALLEELRSLQE--------RLNASERKVEGLGEELSS--MAAQRDRTQAELH--QARLQAAQL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 888 pttngtrkryqrkgftgrvfTSKTARMKWQLLERRVTEIIMQKMTISNMEADMNRLLRQREELTKRREKLSK---RREKI 964
Cdd:pfam07888 285 --------------------TLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermEREKL 344
|
330 340
....*....|....*....|...
gi 1958788848 965 AKESG-EGDKNLVNISEEMESLT 986
Cdd:pfam07888 345 EVELGrEKDCNRVQLSESRRELQ 367
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
635-1012 |
2.67e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 635 NYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKV---K 711
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIaqlS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 712 CEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL 791
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 792 KKDQRkrdhQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSEsptpdAGSSVTSGEADASRpgT 871
Cdd:TIGR02168 834 AATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE-----ALALLRSELEELSE--E 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 872 QQKMRipvARVQALptpttngtrkRYQRKGFTGRVftsKTARMKWQLLERRVTEIIMQ-----KMTISNMEADMNRLLRQ 946
Cdd:TIGR02168 903 LRELE---SKRSEL----------RRELEELREKL---AQLELRLEGLEVRIDNLQERlseeySLTLEEAEALENKIEDD 966
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788848 947 REELtkrREKLSKRREKIAKesgEGDKNLVNIsEEMESLTANIDYINDSIADCQANIMQMEEAKEE 1012
Cdd:TIGR02168 967 EEEA---RRRLKRLENKIKE---LGPVNLAAI-EEYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1248-1283 |
3.12e-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: 45.38 E-value: 3.12e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1958788848 1248 QCVHVAEGHTKAVLCVD--STDDLLFTGSKDRTCKVWN 1283
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
654-808 |
4.23e-06 |
|
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: 49.92 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 654 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAM--NKELQRLQta 731
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVrnNKEYEALQ-- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788848 732 qKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQ 808
Cdd:COG1579 96 -KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
651-826 |
4.35e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 651 QKLIDELENSQKRLQTLKKQY---EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQR 727
Cdd:COG4372 55 EQAREELEQLEEELEQARSELeqlEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE-ELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 728 LQTAQKEHARLLKNQ----SQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLR 803
Cdd:COG4372 134 LEAQIAELQSEIAEReeelKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180
....*....|....*....|...
gi 1958788848 804 LLEAQKRNQEVVLRRKTEEVTAL 826
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALS 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
637-831 |
5.70e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 637 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDT-QLERDQVLQNLGSvesySEEKAKKVKCEYE 715
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQA----ELSKLEEEVSRIE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 716 KKLHAMNKELQRL----QTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRnreiAQL 791
Cdd:TIGR02169 812 ARLREIEQKLNRLtlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDL 887
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958788848 792 KKDQRKRDHQLRllEAQKRNQEVVLRRKTEEVTALRRQVR 831
Cdd:TIGR02169 888 KKERDELEAQLR--ELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
646-1084 |
8.92e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 8.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 646 EIAIKQKL-IDELENSQKRLQTLKKQYEEKLMMLQHKIrdtqlerdqvlqnlgSVESYSEEKAKKVKCEYEKKLHAMNKE 724
Cdd:PRK03918 148 EKVVRQILgLDDYENAYKNLGEVIKEIKRRIERLEKFI---------------KRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 725 LQRLQTAQKEHARLLKNQsqyeKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK--KDQRKRDHQL 802
Cdd:PRK03918 213 SSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 803 -------RLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAgkvtrKLSSSESPTpdagssvtsGEADASRPGTQQKM 875
Cdd:PRK03918 289 kekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-----ELEEKEERL---------EELKKKLKELEKRL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 876 RIPVARVQALPTPTTNGTRKRYQRKGFTGRvfTSKTARMKWQLLERRVTEIimqkmtisnmEADMNRLLRQREELTKRRE 955
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEI----------EEEISKITARIGELKKEIK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 956 KLSKRREKIAKESGEGDKNLVNISEE-----MESLTANIDYINDSIADCQANIMQMEEAKEEGETLdvtaVINACTLTEA 1030
Cdd:PRK03918 423 ELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV----LKKESELIKL 498
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958788848 1031 RYLLDhflsmginkglqaaqkeaQIKVLEGRLKQTEITSATQNQLLFHMLKEKA 1084
Cdd:PRK03918 499 KELAE------------------QLKELEEKLKKYNLEELEKKAEEYEKLKEKL 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
706-1101 |
9.97e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 706 KAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKN---QSQYEKQLKKLQQDVTEMKKT-KVRLMKQMKEEQEKARLTE 781
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSlerQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 782 SRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRqvrpmsdKVAGKVTRKLSSSESptpDAGSSVTS 861
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN-------EISRLEQQKQILRER---LANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 862 GEADASRPGTQQKMRIPVARVQALptpTTNGTRKRYQRKGFTGRVftsKTARMKWQLLERRVTEIIMQkmtISNMEADMN 941
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQ---LETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 942 RLLRQREELTKRREKLSKRREKIAKESgegDKNLVNISEEMESLTANidYINDSIADCQANIMQMEEAKEEGETLDVTAV 1021
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1022 INACTLTEARYLLDHFLSmginkglQAAQKEAQIKVLEGRLKQTE-----ITSATQNQLLFH----MLKEKAELNPE--- 1089
Cdd:TIGR02168 465 ELREELEEAEQALDAAER-------ELAQLQARLDSLERLQENLEgfsegVKALLKNQSGLSgilgVLSELISVDEGyea 537
|
410
....*....|...
gi 1958788848 1090 -LDALLGNALQDL 1101
Cdd:TIGR02168 538 aIEAALGGRLQAV 550
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
652-847 |
2.05e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 652 KLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKEL----QR 727
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE-QLEEELEQARSELeqleEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 728 LQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEA 807
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEE----LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958788848 808 QkrnqevvLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSS 847
Cdd:COG4372 158 Q-------LESLQEELAALEQELQALSEAEAEQALDELLK 190
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
647-859 |
2.20e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 647 IAIKQKLIDELEnsqKRLQTLKKQYEEklmmLQhKIRDTQLERDQVLQNLGSVESYSEEKAkkvkcEYEKKLHAMNKELQ 726
Cdd:COG4913 612 LAALEAELAELE---EELAEAEERLEA----LE-AELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 727 RLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRL---MKQMKEEQEKARltesRRNREIAQLKKDQRKRDHQLR 803
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLekeLEQAEEELDELQ----DRLEAAEDLARLELRALLEER 754
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788848 804 LLEAQKRNQEVVLRRK-TEEVTALRRQVRPMSDKVAGKVTRKLSSSESPTPDAGSSV 859
Cdd:COG4913 755 FAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL 811
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1525-1562 |
2.36e-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: 42.68 E-value: 2.36e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1958788848 1525 TFVPVGEMRGHDSPINAISV--NSTHVFTAADDRTVRIWK 1562
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
669-849 |
2.64e-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: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 669 KQYEEKLMMLQHKI-RDTQLE--RDQVLQNLgSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQY 745
Cdd:COG2433 346 DAYKNKFERVEKKVpPDVDRDevKARVIRGL-SIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVER 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 746 -EKQLKKLQQDVTEMKKT------KVRLMKQmkEEQEKARLTE--SRRNREIAQLKKdqrkrdhqlRLLEAQKRNQEvvL 816
Cdd:COG2433 425 lEAEVEELEAELEEKDERierlerELSEARS--EERREIRKDReiSRLDREIERLER---------ELEEERERIEE--L 491
|
170 180 190
....*....|....*....|....*....|...
gi 1958788848 817 RRKTEEVTALRRQVRpMSDKVAGKVTRKLSSSE 849
Cdd:COG2433 492 KRKLERLKELWKLEH-SGELVPVKVVEKFTKEA 523
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
705-831 |
3.31e-05 |
|
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: 44.91 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 705 EKAKKVKCEYEKKLHamnkelqrlqtaqkeharllknqsQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRR 784
Cdd:pfam20492 2 EEAEREKQELEERLK------------------------QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKR 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788848 785 N------REIAQLKKDQRKRDHQL--RLLEAQKRNQ--EVVLRRKTEEVTALRRQVR 831
Cdd:pfam20492 58 QeaeeekERLEESAEMEAEEKEQLeaELAEAQEEIArlEEEVERKEEEARRLQEELE 114
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
646-819 |
3.94e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 646 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQV-LQNLGSVEsyseekakkvkceyekklhamnke 724
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLE------------------------ 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 725 lQRLQTAQKEHARLLKNQSQYEKQLKKL-------QQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRK 797
Cdd:COG4913 345 -REIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
170 180
....*....|....*....|....
gi 1958788848 798 RDHQLRLLEAQKRN--QEVVLRRK 819
Cdd:COG4913 424 LEAEIASLERRKSNipARLLALRD 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
594-846 |
5.14e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 594 ENQEASDHEDEEDEEEEDEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE 673
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 674 KLMMLQHKIRDTQLERDQV---LQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLK 750
Cdd:COG1196 324 ELAELEEELEELEEELEELeeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 751 KLQQDVTEMKKTKVRLmkqmKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQV 830
Cdd:COG1196 404 ELEEAEEALLERLERL----EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250
....*....|....*.
gi 1958788848 831 RPMSDKVAGKVTRKLS 846
Cdd:COG1196 480 AELLEELAEAAARLLL 495
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
662-814 |
5.55e-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: 46.90 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 662 KRLQTLKKQYEEK-------LMMLQHKIR------DTQLERDQVLqnlgsvesysEEKAKKVKCEYEKKlHAMNKELQRL 728
Cdd:pfam02841 155 EERDKLEAKYNQVprkgvkaEEVLQEFLQskeaveEAILQTDQAL----------TAKEKAIEAERAKA-EAAEAEQELL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 729 QTAQKEHARLLKNQ-SQYEKQLKKLQQdvtEMKKTKvrlmKQMKEEQEkaRLTESRRNREIAQLKKDQRKrdhqlrllEA 807
Cdd:pfam02841 224 REKQKEEEQMMEAQeRSYQEHVKQLIE---KMEAER----EQLLAEQE--RMLEHKLQEQEELLKEGFKT--------EA 286
|
....*..
gi 1958788848 808 QKRNQEV 814
Cdd:pfam02841 287 ESLQKEI 293
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
650-819 |
7.26e-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: 46.84 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 650 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGsVESYSEEKAKKVKCEYEKKLhAMNKELQRLQ 729
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY-QEEQERKERQKEREEAEKKA-RQRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 730 TAQKEHARLLKnqsqyEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL---KKDQRKRDHQLRLLE 806
Cdd:pfam13868 242 EEQIELKERRL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQieeREEQRAAEREEELEE 316
|
170
....*....|...
gi 1958788848 807 AQKRNQEVVLRRK 819
Cdd:pfam13868 317 GERLREEEAERRE 329
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1526-1561 |
7.85e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 41.18 E-value: 7.85e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1958788848 1526 FVPVGEMRGHDSPINAI--SVNSTHVFTAADDRTVRIW 1561
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLafSPDGKLLASGSDDGTVKVW 38
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
646-836 |
1.09e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 646 EIAIKQKLIDELEnsqkRLQTLKKQYEEKLMM-----LQHKIRDTQLERDQVLQNLGSVESYSE-EKAKKVKCEYEKKLH 719
Cdd:pfam17380 369 EIAMEISRMRELE----RLQMERQQKNERVRQeleaaRKVKILEEERQRKIQQQKVEMEQIRAEqEEARQREVRRLEEER 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 720 AMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQE----KARLTESRRNREIaqLKKDQ 795
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEleerKQAMIEEERKRKL--LEKEM 522
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958788848 796 RKRdhQLRLLEAQKRNQEVVLRRKTEEVTALRR---QVRPMSDK 836
Cdd:pfam17380 523 EER--QKAIYEEERRREAEEERRKQQEMEERRRiqeQMRKATEE 564
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
679-822 |
1.10e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 679 QHKIRDTQLERDQVLQN-LGSVESYSEEK-------AKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQY----E 746
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEaKKEAEAIKKEAlleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELlekrE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788848 747 KQLKKLQQDVTEMKKTkvrlMKQMKEEQEKARLTESRRNREIAQLKKDQrKRDHQLRLLEAQKRNQEVVLRRKTEE 822
Cdd:PRK12704 110 EELEKKEKELEQKQQE----LEKKEEELEELIEEQLQELERISGLTAEE-AKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
716-836 |
1.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 716 KKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKK--TKVRLMKQMKEEQEKARLTESRRNREIAQLKK 793
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958788848 794 dQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDK 836
Cdd:COG4717 151 -LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
637-822 |
1.33e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 637 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEE--KLMMLQHKIRDT------QLER-DQVLQNLGSVESYSEEKA 707
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDElreiekRLSRlEEEINGIEERIKELEEKE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 708 KKVKcEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKArltESRRNRE 787
Cdd:PRK03918 338 ERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE---ISKITAR 413
|
170 180 190
....*....|....*....|....*....|....*
gi 1958788848 788 IAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEE 822
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
663-831 |
1.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 663 RLQTLKKQYEEkLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQ 742
Cdd:COG4913 226 AADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 743 SQYEKQLKKLQQDVTEMKKTKVRLMKQMKEE--QEKARLTesrrnREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKT 820
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLE-----REIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170
....*....|.
gi 1958788848 821 EEVTALRRQVR 831
Cdd:COG4913 380 EEFAALRAEAA 390
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
646-963 |
2.11e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 646 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESysEEKAKKVKCEYEKKlhamnKEL 725
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEKK-----KAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 726 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKA------------RLTESRRNREIAQLKK 793
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAeaakaeaeaaadEAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 794 DQRKRDHQlrllEAQKRNQEVvlrRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPTpdagSSVTSGEADASRPGTQQ 873
Cdd:PTZ00121 1374 EEAKKKAD----AAKKKAEEK---KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK----KAEEKKKADEAKKKAEE 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 874 KMRIPVARVQALPTPTTNGTRKRYQRKgftgrvftSKTARMKWQLLERRVTEIIMQKMTISNMEADMnrlLRQREELTKR 953
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEA--------KKADEAKKKAEEAKKADEAKKKAEEAKKKADE---AKKAAEAKKK 1511
|
330
....*....|
gi 1958788848 954 REKLSKRREK 963
Cdd:PTZ00121 1512 ADEAKKAEEA 1521
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
676-819 |
2.54e-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: 44.31 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 676 MMLQHKIRDTQLERdqvlqnlGSVESYSEEKAKKvKCEYEKKLhaMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQD 755
Cdd:pfam13904 38 LTYARKLEGLKLER-------QPLEAYENWLAAK-QRQRQKEL--QAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQ 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958788848 756 vtemkKTKVRLMKQMKEEQEKARLTESRRNREIAQ-----------LKKDQRKRDHQLRLLEAQKRNQEVVLRRK 819
Cdd:pfam13904 108 -----QTKKREESHKQKAAESASKSLAKPERKVSQeeakevlqeweRKKLEQQQRKREEEQREQLKKEEEEQERK 177
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
649-788 |
2.57e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 649 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESySEEKAKKVKCEYEKKLHAMNKELQRL 728
Cdd:PRK12704 69 LRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIEEQLQELERI 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 729 QTAQKEHARllknqsqyEKQLKKLQqdvtemKKTKVRLMKQMKEEQEKARLTESRRNREI 788
Cdd:PRK12704 148 SGLTAEEAK--------EILLEKVE------EEARHEAAVLIKEIEEEAKEEADKKAKEI 193
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
649-821 |
2.63e-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: 43.99 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 649 IKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSeekakKVKCEYEKKLHAMNKELQRL 728
Cdd:pfam14988 23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFA-----KLKESQEREIQDLEEEKEKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 729 Q-----TAQKEHARLLKNQSQYEKQLKklQQDVTEM---KKTKVRLMKQMKEEQEKARLTESRRN--REIAQLKKDQRKR 798
Cdd:pfam14988 98 RaetaeKDREAHLQFLKEKALLEKQLQ--ELRILELgerATRELKRKAQALKLAAKQALSEFCRSikRENRQLQKELLQL 175
|
170 180
....*....|....*....|...
gi 1958788848 799 DHQLRLLEAQKRNQEvvlRRKTE 821
Cdd:pfam14988 176 IQETQALEAIKSKLE---NRKQR 195
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
654-827 |
3.56e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 654 IDELENSQKRLQTLK-------KQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESY---SEEKAK---KVKCEYEkklhA 720
Cdd:pfam01576 112 LDEEEAARQKLQLEKvtteakiKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNlaeEEEKAKslsKLKNKHE----A 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 721 MNKELQ-RLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRK-R 798
Cdd:pfam01576 188 MISDLEeRLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKiR 267
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958788848 799 DHQLRLLEAQK--------RNQEVVLRRK-TEEVTALR 827
Cdd:pfam01576 268 ELEAQISELQEdleseraaRNKAEKQRRDlGEELEALK 305
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
636-823 |
4.64e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 636 YQADLANITCEIAIKQK----LIDELENSQKRLQTLK---KQYEEKLMMLQHKIRDTQLERDQVLQNLgsvESYSEEKAk 708
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEeledLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKRELDRLQEEL---QRLSEELA- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 709 kvkcEYEKKLHAMNKELQRLQTAQKEHARLLKNQsqyEKQLKKLQQDVTemkktkvrlmkqmKEEQEKARLTEsrrnrEI 788
Cdd:TIGR02169 424 ----DLNAAIAGIEAKINELEEEKEDKALEIKKQ---EWKLEQLAADLS-------------KYEQELYDLKE-----EY 478
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958788848 789 AQLKKDQRKRDHQLRLLEAQKR--NQEVVLRRKTEEV 823
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARasEERVRGGRAVEEV 515
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
655-788 |
5.33e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 655 DELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVlqnlgsvesysEEKAKKVKCEYEKKLHAMNKELQ-RLQTAQK 733
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLEEAEKEAQqAIKEAKK 584
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788848 734 EHARLLKNQSQYEKQLKKLQ--QDVTEMKKtkvrLMKQMKEEQEKARLTESRRNREI 788
Cdd:PRK00409 585 EADEIIKELRQLQKGGYASVkaHELIEARK----RLNKANEKKEKKKKKQKEKQEEL 637
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
308-517 |
5.34e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 308 LGNVISALG-DKSKRATHVPYRDskLTRLLQDSLG----GNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVN 382
Cdd:COG3206 96 LERVVDKLNlDEDPLGEEASREA--AIERLRKNLTvepvKGSNVIEISYTSPDPELAAAVANALAEAYLEQNLELRREEA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 383 QDRAS---QQINALRSEITRLQMELMEYKTGKRIIDEEG-----VESINDMFHENAMLQTENNNLRVRIKAMQE------ 448
Cdd:COG3206 174 RKALEfleEQLPELRKELEEAEAALEEFRQKNGLVDLSEeakllLQQLSELESQLAEARAELAEAEARLAALRAqlgsgp 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 449 ----------TVDALRARITQLVSEQAnQVLARAGEGNEEISNMihsyIKEIEDLRAKLL-ESEAVNENLRKSLTRATAR 517
Cdd:COG3206 254 dalpellqspVIQQLRAQLAELEAELA-ELSARYTPNHPDVIAL----RAQIAALRAQLQqEAQRILASLEAELEALQAR 328
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
636-1012 |
5.36e-04 |
|
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: 45.04 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 636 YQADLANITCEIA--IKQKLIDELENSQKrLQTLKKQYEEKLMMLQHkirdtqLERDQVLQNLGSVESySEEKAKKVKCE 713
Cdd:TIGR01612 669 YEDDIDALYNELSsiVKENAIDNTEDKAK-LDDLKSKIDKEYDKIQN------METATVELHLSNIEN-KKNELLDIIVE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 714 YEKKLHA-----MNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKK--TKVRLMKQMKEEQEKARLTESRRNR 786
Cdd:TIGR01612 741 IKKHIHGeinkdLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNhyNDQINIDNIKDEDAKQNYDKSKEYI 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 787 EIAQLKKDQ-RKRDHQLRLLEAQ---KRNQEVVLRRK-TEEVTALRRQVRPMSDKVAGKVT-RKLSSSESPTPDAGSSVT 860
Cdd:TIGR01612 821 KTISIKEDEiFKIINEMKFMKDDflnKVDKFINFENNcKEKIDSEHEQFAELTNKIKAEISdDKLNDYEKKFNDSKSLIN 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 861 ----SGEADASRPGTQQKmripVARVQALPTPTTNGTRKRYQRKGFTGRVFTSKTARMK-WQLLER------------RV 923
Cdd:TIGR01612 901 einkSIEEEYQNINTLKK----VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKeSNLIEKsykdkfdntlidKI 976
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 924 TEI--IMQKMTISNMEADMNRLLRQ----REELTKRREKL--------SKRREKIAKESGEGDKN-----------LVNI 978
Cdd:TIGR01612 977 NELdkAFKDASLNDYEAKNNELIKYfndlKANLGKNKENMlyhqfdekEKATNDIEQKIEDANKNipnieiaihtsIYNI 1056
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958788848 979 SEEMESLTA-NIDYINDSI-ADCQANIMQMEEAKEE 1012
Cdd:TIGR01612 1057 IDEIEKEIGkNIELLNKEIlEEAEINITNFNEIKEK 1092
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
649-970 |
5.95e-04 |
|
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: 44.72 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 649 IKQ---KLIDELENSQKRLQTLKKQYE----------EKLMM----LQHKIRDTQLERDQVLQNLGSVESySEEKAKKVK 711
Cdd:pfam15921 651 IKQerdQLLNEVKTSRNELNSLSEDYEvlkrnfrnksEEMETttnkLKMQLKSAQSELEQTRNTLKSMEG-SDGHAMKVA 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 712 CEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQL 791
Cdd:pfam15921 730 MGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANM 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 792 KKDQRKRdhQLRLLEAQ---KRNQEVVLRRKTEEVTALRRQVRP-------MSDKVAGKVTRKLSSSESPTPDAGSSVTS 861
Cdd:pfam15921 810 EVALDKA--SLQFAECQdiiQRQEQESVRLKLQHTLDVKELQGPgytsnssMKPRLLQPASFTRTHSNVPSSQSTASFLS 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 862 GEADASRPGTQQKMRIPVARVQALPTPTTNGTRKRYQRKGFTGRVFTSKTarmkwqlLERRVTEIIMQKMTISNMEADMN 941
Cdd:pfam15921 888 HHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGA-------LDDRVRDCIIESSLRSDICHSSS 960
|
330 340
....*....|....*....|....*....
gi 1958788848 942 RLLRQREelTKRREKLSkrREKIAKESGE 970
Cdd:pfam15921 961 NSLQTEG--SKSSETCS--REPVLLHAGE 985
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
637-781 |
6.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 637 QADLANITCEIAIKQKLIDELENSQKRLQTLKKQY---------EEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKA 707
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958788848 708 KKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTE 781
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
645-813 |
6.42e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 43.90 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 645 CEIAIKQKLidELENSQKRLQTLKKQYEE---KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAK---KVKCEYEKKL 718
Cdd:pfam15742 54 QEENIKIKA--ELKQAQQKLLDSTKMCSSltaEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQeksRVADAEEKIL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 719 hamnkELQRlqtaQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRN------------- 785
Cdd:pfam15742 132 -----ELQQ----KLEHAHKVCLTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNelqqqvrslqdke 202
|
170 180 190
....*....|....*....|....*....|..
gi 1958788848 786 ----REIAQLKKDQRKRDHQLRLLEAQKRNQE 813
Cdd:pfam15742 203 aqleMTNSQQQLRIQQQEAQLKQLENEKRKSD 234
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
705-1086 |
7.77e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 44.28 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 705 EKAKKVKCEYEKKLHAMNKELQRL-QTAQKEHARLLKNQsqYEKQLKKLQQDVTEM-------KKTKVRLMKQMKEEQEK 776
Cdd:pfam13166 99 AKLKKEIKDHEEKLDAAEANLQKLdKEKEKLEADFLDEC--WKKIKRKKNSALSEAlngfkyeANFKSRLLREIEKDNFN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 777 A--RLTESRRNREIAQLKKDQRKRdhqLRLLEAQKRNQEvvlrrkteevtALRRQVRPMSDKVA-GKVTRKLSSSesptP 853
Cdd:pfam13166 177 AgvLLSDEDRKAALATVFSDNKPE---IAPLTFNVIDFD-----------ALEKAEILIQKVIGkSSAIEELIKN----P 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 854 DAGSSVTSG----EADASR-PGTQQKmrIPVARVQALptpttngtrKRYQRKGFTGRVFT-----SKTARMKWQLLERrV 923
Cdd:pfam13166 239 DLADWVEQGlelhKAHLDTcPFCGQP--LPAERKAAL---------EAHFDDEFTEFQNRlqkliEKVESAISSLLAQ-L 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 924 TEIIMQKMTISNMEADMNRLLRQREELTKR----REKLSKRREKIAKESgegdkNLVNISEEMESLTANIDYINDSIADC 999
Cdd:pfam13166 307 PAVSDLASLLSAFELDVEDIESEAEVLNSQldglRRALEAKRKDPFKSI-----ELDSVDAKIESINDLVASINELIAKH 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1000 QANIMQMEEAKEEGETLDVTAVINACTLTEARYLLDHFLSMGINKGLQAAQK---------EAQIKVLEGRLKQTEITSA 1070
Cdd:pfam13166 382 NEITDNFEEEKNKAKKKLRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKnleaeikklREEIKELEAQLRDHKPGAD 461
|
410
....*....|....*.
gi 1958788848 1071 TQNQLLFHMLKEKAEL 1086
Cdd:pfam13166 462 EINKLLKAFGFGELEL 477
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
651-825 |
7.87e-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: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 651 QKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLErdqvLQNLGSVESYSEEKAKKVKcEYEKKLHAMNKELQRLQT 730
Cdd:pfam05622 310 QQLLEDANRRKNELETQNRLANQRILELQQQVEELQKA----LQEQGSKAEDSSLLKQKLE-EHLEKLHEAQSELQKKKE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 731 AQKEHARllKNQSQYEKQLKKLQQDVT----EMKKTKVRLMKQMKEEQEKARLTESRRNR----EIAQLKKDQRKRDHQL 802
Cdd:pfam05622 385 QIEELEP--KQDSNLAQKIDELQEALRkkdeDMKAMEERYKKYVEKAKSVIKTLDPKQNPasppEIQALKNQLLEKDKKI 462
|
170 180
....*....|....*....|....*.
gi 1958788848 803 RLLEAQKrnQEVVLRRKTEE---VTA 825
Cdd:pfam05622 463 EHLERDF--EKSKLQREQEEkliVTA 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
646-831 |
8.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 646 EIAIKQKLIDELENSQKRLQTLKKQYEE----------KLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYE 715
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEEleaeleeleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 716 KKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVtemkktkVRLMKQMKEE--QEKARLTES-RRNREIAQLK 792
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-------ERAMRAFNREwpAETADLDADlESLPEYLALL 821
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958788848 793 KDQRKRDhqlrLLEAQKRNQEVVLRRKTEEVTALRRQVR 831
Cdd:COG4913 822 DRLEEDG----LPEYEERFKELLNENSIEFVADLLSKLR 856
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
633-763 |
1.11e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 633 KANYQADLANItceiaikQKLIDELENSQKRLQT-------LKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEE 705
Cdd:PRK00409 508 KKLIGEDKEKL-------NELIASLEELERELEQkaeeaeaLLKEAEKLKEELEEKKEKLQEEEDKLLEEA-------EK 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788848 706 KAKKV----KCEYEKKLHAMNKELQRLQTAQKEHaRLLKNQSQYEKQLKKLQQDVTEMKKTK 763
Cdd:PRK00409 574 EAQQAikeaKKEADEIIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-1064 |
1.12e-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: 43.89 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 382 NQDRASQQINALRSEITRLQMELMEYKTgkriIDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRARitqlv 461
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQK----ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK----- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 462 SEQANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKSLTRATARSPFFSASSAFSSTILSSDKETIEI 541
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 542 IDLAKKDLEKLKRKEKRKKKSVAGKENNADPDQEKKE--------EKGVSEKESSEVDVDENQEASDHEDEEDEEEEDEE 613
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqeelERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 614 EDDIEGEESSDESDSESDEKANYQADLANITC------------EIAIK-------QKLIDELENSQKR-LQTLKKQYEE 673
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLSGILGvlselisvdegyEAAIEaalggrlQAVVVENLNAAKKaIAFLKQNELG 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 674 KLMMLQHK-IRDTQLE--RDQVLQNLGSVESYSEEKAKKVKcEYEKKLH----------------AMNKELQRLQT---- 730
Cdd:TIGR02168 572 RVTFLPLDsIKGTEIQgnDREILKNIEGFLGVAKDLVKFDP-KLRKALSyllggvlvvddldnalELAKKLRPGYRivtl 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 731 ---------------AQKEHARLLKNQS--QYEKQLKKLQQDVTEMKKTKVRLMKQ---MKEEQEKARLTESRRNREIAQ 790
Cdd:TIGR02168 651 dgdlvrpggvitggsAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISA 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 791 LKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVrpmsdkvagkvtrklssSESPTPDAGSSVTSGEADASRPG 870
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL-----------------EEAEEELAEAEAEIEELEAQIEQ 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 871 TQQKMRIPVARVQALPTPTTNgTRKRYQRKGFTGRVFTSKTARMKwQLLERRVTEIIMQKMTISNMEADMNRLLRQREEL 950
Cdd:TIGR02168 794 LKEELKALREALDELRAELTL-LNEEAANLRERLESLERRIAATE-RRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 951 TKRREKLSKRREKIAKESGEGDKNLVNISEEMESLTANIDYINDSIADCQANIMQMEEAKEEgetLDVTAVINACTLTE- 1029
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG---LEVRIDNLQERLSEe 948
|
730 740 750
....*....|....*....|....*....|....*
gi 1958788848 1030 ARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1064
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
642-844 |
1.28e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 642 NITCEIAIKQKLIDELENSQK-RLQTLKKQYEEKL-MMLQHKIRDTQLErDQVLQNLGSVESYSEEKAK--------KVK 711
Cdd:PHA02562 192 HIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVeEAKTIKAEIEELT-DELLNLVMDIEDPSAALNKlntaaakiKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 712 CEYEKKLHAMNKE-------LQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEkarltesrR 784
Cdd:PHA02562 271 IEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE--------L 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 785 NREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRK 844
Cdd:PHA02562 343 KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
651-793 |
1.56e-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: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 651 QKLIDELENSQKRLQTLK----KQYEEKLMMLQHKIRdtQLER-----DQVLQN-LGSVESYSE----------EKAKKV 710
Cdd:cd16269 123 QELSAPLEEKISQGSYSVpggyQLYLEDREKLVEKYR--QVPRkgvkaEEVLQEfLQSKEAEAEailqadqaltEKEKEI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 711 KCEYEKKlHAMNKELQRLQTAQKEHARLLKNQSQ-YEKQLKKLQQDVTEMKKTKVRLMKQMKEE--QEKARLTESRRNRE 787
Cdd:cd16269 201 EAERAKA-EAAEQERKLLEEQQRELEQKLEDQERsYEEHLRQLKEKMEEERENLLKEQERALESklKEQEALLEEGFKEQ 279
|
....*.
gi 1958788848 788 IAQLKK 793
Cdd:cd16269 280 AELLQE 285
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1392-1433 |
1.58e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 1.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958788848 1392 FQSTGKLTGHLGPVMCLTvdqISNGQDLIITGSKDHYIKMFD 1433
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLA---FSPDGKLLASGSDDGTVKVWD 39
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
644-808 |
1.63e-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: 41.43 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 644 TCEIAIKQKLIDELENSQKRLQTLKKQYEEKLmmlqHKIRDTQLERDQVLQnlgsveSYSEE------KAKKVKCEY--- 714
Cdd:pfam15619 17 QNELAELQSKLEELRKENRLLKRLQKRQEKAL----GKYEGTESELPQLIA------RHNEEvrvlreRLRRLQEKErdl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 715 EKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQlkKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKD 794
Cdd:pfam15619 87 ERKLKEKEAELLRLRDQLKRLEKLSEDKNLAERE--ELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKK 164
|
170
....*....|....
gi 1958788848 795 QRKRDHQLRLLEAQ 808
Cdd:pfam15619 165 HKEAQEEVKILQEE 178
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
692-829 |
1.64e-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: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 692 VLQNLGSVESYSEEKAKKVKCEyekKLHAMNKELQRLQTAQKEHARL---LKNQSQYEKqlKKLQQDVTE-MKKTKVRLM 767
Cdd:pfam15709 305 VTGNMESEEERSEEDPSKALLE---KREQEKASRDRLRAERAEMRRLeveRKRREQEEQ--RRLQQEQLErAEKMREELE 379
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788848 768 KQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQ 829
Cdd:pfam15709 380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
652-819 |
1.82e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 652 KLIDELENSQKRLQTLKKQYEEKL------MMLQHKIRDTQL----ERDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAM 721
Cdd:PRK11637 103 KQIDELNASIAKLEQQQAAQERLLaaqldaAFRQGEHTGLQLilsgEESQRGERILAYFGYLNQARQETIAELKQTREEL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 722 NKELQRLQTAQKEHARLLKNQSQyekQLKKLQQDVTEMKKTKVRLMKQMKEEQekARLTESRRNR-----EIAQLKKDQR 796
Cdd:PRK11637 183 AAQKAELEEKQSQQKTLLYEQQA---QQQKLEQARNERKKTLTGLESSLQKDQ--QQLSELRANEsrlrdSIARAEREAK 257
|
170 180
....*....|....*....|....*
gi 1958788848 797 KR-DHQLRllEAQK-RNQEVVLRRK 819
Cdd:PRK11637 258 ARaEREAR--EAARvRDKQKQAKRK 280
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
646-849 |
1.86e-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: 43.09 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 646 EIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLErdqvLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKEL 725
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI----IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 726 QRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRL-----------------MKQMKEEQEKARLTESRR--NR 786
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLesekkekeskisdledeLNKDDFELKKENLEKEIDekNK 568
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958788848 787 EIAQLKKDQRKrdhqlrLLEAQKRNQEvVLRRKTEEVTALRRQVRpMSDKVAGKVTRKLSSSE 849
Cdd:TIGR04523 569 EIEELKQTQKS------LKKKQEEKQE-LIDQKEKEKKDLIKEIE-EKEKKISSLEKELEKAK 623
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
650-831 |
1.88e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 650 KQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsvesysEEKAKKVKCEYEKKLHAMNKELQRLQ 729
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-------EAEREEIEEEKEREIARLRAQQEKAQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 730 TAQKEH--ARLLKNQSQYE-----KQLKKLQQDVTEMKKTKVRLMKQMKEEqEKARLTESRRNREIAQLKKDQRKRDHQL 802
Cdd:pfam13868 198 DEKAERdeLRAKLYQEEQErkerqKEREEAEKKARQRQELQQAREEQIELK-ERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
170 180
....*....|....*....|....*....
gi 1958788848 803 RLLEAQKRNQevvlrRKTEEVTALRRQVR 831
Cdd:pfam13868 277 EQEEAEKRRM-----KRLEHRRELEKQIE 300
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-734 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 370 NRARNIKNkvmvnqdrASQQINALRSEITRLQMELMEYKTGKRIIDEEGVEsindmfhenamLQTENNNLRVRIKAMQET 449
Cdd:TIGR02168 674 ERRREIEE--------LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-----------LRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 450 VDALRARItqlvsEQANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKSLTRATARSpffsassafss 529
Cdd:TIGR02168 735 LARLEAEV-----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL----------- 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 530 tilssdKETIEIIDLAKKDLEKLKRKEKRKKKSVAGKENNADpDQEKKEEKGVSEKESSEVDVDENQEASDHEDEEDEEE 609
Cdd:TIGR02168 799 ------KALREALDELRAELTLLNEEAANLRERLESLERRIA-ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 610 EDEEEDDIEGeessdesdsesdeKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLER 689
Cdd:TIGR02168 872 ESELEALLNE-------------RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958788848 690 DQVLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKE 734
Cdd:TIGR02168 939 DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
728-855 |
2.05e-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: 42.57 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 728 LQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKqmkeEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEA 807
Cdd:pfam07888 310 QQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR----EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958788848 808 QKrnQEV-----VLRRKTEEVTALRRQVRPMSDKvaGKVTRKLSSSESPTPDA 855
Cdd:pfam07888 386 EK--QELleyirQLEQRLETVADAKWSEAALTST--ERPDSPLSDSEDENPEA 434
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
655-829 |
2.17e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 655 DELENSQKRLQTLKKQyeeklmmlqHKIRDTQLERDQVLQNLGSVES-YSEEKAKKVkcEYEKKLHAMNKELQRLQTAQK 733
Cdd:COG3206 189 KELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESqLAEARAELA--EAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 734 EH------ARLLKNQSQYEKQLKKLQQ-------DVTEMKKTKVRLMKQMKEEQEKArLTESRRNREIAQLKKD---QRK 797
Cdd:COG3206 258 ELlqspviQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRI-LASLEAELEALQAREAslqAQL 336
|
170 180 190
....*....|....*....|....*....|..
gi 1958788848 798 RDHQLRLLEAQKRNQEvvLRRKTEEVTALRRQ 829
Cdd:COG3206 337 AQLEARLAELPELEAE--LRRLEREVEVAREL 366
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
661-825 |
2.27e-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: 42.63 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 661 QKRLQTLKKQYEEKLmmlqhkirDTQLERDQvlqnlgsvESYSEE-KAKKVKCEYEKKLHAMNKELQRLQ-TAQKEHARL 738
Cdd:pfam15709 360 QRRLQQEQLERAEKM--------REELELEQ--------QRRFEEiRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 739 lkNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQlrlLEAQKRNQEVVLRR 818
Cdd:pfam15709 424 --QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQ---EAEEKARLEAEERR 498
|
....*..
gi 1958788848 819 KTEEVTA 825
Cdd:pfam15709 499 QKEEEAA 505
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
650-809 |
2.69e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.01 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 650 KQKLidELENSQKRLQtLKKQY---EEKLMMLQHKIRDTQLERDQV----------LQNLGSVESYSE----EKAKKVKC 712
Cdd:pfam03528 24 KQQL--EAEFNQKRAK-FKELYlakEEDLKRQNAVLQEAQVELDALqnqlalaraeMENIKAVATVSEntkqEAIDEVKS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 713 EYEKK---LHAMNKELQRLQTAQKeHARLLKNQSQYEKQLKKLQQDVTEMKKtkvRL------------MKQMKEEQEKA 777
Cdd:pfam03528 101 QWQEEvasLQAIMKETVREYEVQF-HRRLEQERAQWNQYRESAEREIADLRR---RLsegqeeenledeMKKAQEDAEKL 176
|
170 180 190
....*....|....*....|....*....|..
gi 1958788848 778 RLTESRRNREIAQLKKDQRKRDHQLRLLEAQK 809
Cdd:pfam03528 177 RSVVMPMEKEIAALKAKLTEAEDKIKELEASK 208
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1392-1433 |
3.35e-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: 3.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958788848 1392 FQSTGKLTGHLGPVMCLtvdQISNGQDLIITGSKDHYIKMFD 1433
Cdd:smart00320 2 GELLKTLKGHTGPVTSV---AFSPDGKYLASGSDDGTIKLWD 40
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
633-828 |
3.48e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 633 KANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDqvlqnlgSVESYSEEKAKKVKC 712
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-------AEELKKAEEENKIKA 1663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 713 EYEKKLHAMNK----ELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMK----------QMKEEQ---- 774
Cdd:PTZ00121 1664 AEEAKKAEEDKkkaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKaeeenkikaeEAKKEAeedk 1743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958788848 775 ---EKARLTESRRNReIAQLKKDQRKRDHQLRlleaqkRNQEVVLRRKTEEVTALRR 828
Cdd:PTZ00121 1744 kkaEEAKKDEEEKKK-IAHLKKEEEKKAEEIR------KEKEAVIEEELDEEDEKRR 1793
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
703-810 |
3.57e-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: 40.06 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 703 SEEKAK------KVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKlqqdvteMKKTKVRLMKQMKEEQEK 776
Cdd:pfam11600 10 QEEKEKqrlekdKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEK-------ELKEKERREKKEKDEKEK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958788848 777 A---RLTESRRNREIAQLK---KDQRKRDHQLRLLEAQKR 810
Cdd:pfam11600 83 AeklRLKEEKRKEKQEALEaklEEKRKKEEEKRLKEEEKR 122
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
651-782 |
3.58e-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: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 651 QKLIDELENSQKRLQTLKKQYEEklmmlQH-KIRDTQLERDQVLQNLgsvesysEEKAKKVKCEYEKKLHAMNKELQRLQ 729
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYTP-----NHpDVIALRAQIAALRAQL-------QQEAQRILASLEAELEALQAREASLQ 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958788848 730 TAQKEHARLLKNQSQYEKQLKKLQQDVtemkKTKVRLMKQMKEEQEKARLTES 782
Cdd:COG3206 334 AQLAQLEARLAELPELEAELRRLEREV----EVARELYESLLQRLEEARLAEA 382
|
|
| mS26_PET12 |
cd23703 |
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ... |
732-804 |
4.07e-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: 39.84 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 732 QKEHARLLKNQSQYEKQLKKLQQD----VTEMKKTKVRL-------------MKQMKEEQEKARLTESRRNREIAQLKKD 794
Cdd:cd23703 68 RELEERKLKTEELRAKRSERKQAEreraLNAPEREDERLtlptiesallgplMRVRTDPEREERAAKRRANREAKELAKK 147
|
90
....*....|
gi 1958788848 795 QRKRDHQLRL 804
Cdd:cd23703 148 EARADALHEL 157
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
654-906 |
4.08e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 654 IDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLgsveSYSEEKAKKVkceyEKKLHAMNKELQRLQTAQK 733
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----EALQAEIDKL----QAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 734 EHARLLKNQSQYEKQLKKL---------------QQDVTEMKKTKVRLMKQMKEEQEKArltESRRNREIAQLKKDQRKR 798
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAK---KAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 799 DHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMS--DKVAGKVTRKLSSSESPTPDAGSSVTSGEADASRPGTQQKMR 876
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEaeLAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260 270
....*....|....*....|....*....|
gi 1958788848 877 IPVARVQALPTPTTNGTRKRYQRKGFTGRV 906
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAGAAGAGA 276
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
396-1090 |
4.11e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 396 EITRLQMelmeyKTGKR--IIDEEGVESINDM--------FHENAMLQTENNNLRVRIKAmQETVDALRARITQlvSEQA 465
Cdd:pfam02463 143 KIEIIAM-----MKPERrlEIEEEAAGSRLKRkkkealkkLIEETENLAELIIDLEELKL-QELKLKEQAKKAL--EYYQ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 466 NQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKSLTRATARSPFFSASSAFSSTILSSDKETIEIIDLA 545
Cdd:pfam02463 215 LKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 546 KKDLEKLKRKEKRKKKSVAGKENNADPDQEKKEEKGVSEKESSEVDVDENQEASDHEDEEDEEEEDEEEDdiegeessde 625
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL---------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 626 sdsesdekanyQADLANITCEIAIKQKLIDELENSQKRLQtlkkqyeEKLMMLQHKIRDTQLERDQVLQNLGS-VESYSE 704
Cdd:pfam02463 365 -----------QEKLEQLEEELLAKKKLESERLSSAAKLK-------EEELELKSEEEKEAQLLLELARQLEDlLKEEKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 705 EKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRLMKQ-MKEEQEKARLTESR 783
Cdd:pfam02463 427 EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSrQKLEERSQKESKAR 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 784 RNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPTPDAGSSVTSGE 863
Cdd:pfam02463 507 SGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPK 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 864 AdasrpGTQQKMRIPVARVQALPTPTTNGTRKRYQRKGFTGRVFTSKTARMKWQLLERRVTEIIMQ-KMTISNMEADMNR 942
Cdd:pfam02463 587 L-----KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGlRKGVSLEEGLAEK 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 943 LLRQREELTKRREKLSKrREKIAKESGEGDKNLVNISEEMESLTANIDYINDSIADCQANIMQMEEAKEEGETLDVTAVI 1022
Cdd:pfam02463 662 SEVKASLSELTKELLEI-QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL 740
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958788848 1023 NACTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTEITSatQNQLLFHMLKEKAELNPEL 1090
Cdd:pfam02463 741 LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK--VEEEKEEKLKAQEEELRAL 806
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
655-798 |
4.78e-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: 41.65 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 655 DELENsQKRLQTLKKQYEEKLmmlQHKIRDTQLERDQVL---QNLGSVESYSEEKAKKVkCEYEKKLHAMNKELQRLQTA 731
Cdd:pfam17380 454 EEQER-QQQVERLRQQEEERK---RKKLELEKEKRDRKRaeeQRRKILEKELEERKQAM-IEEERKRKLLEKEMEERQKA 528
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958788848 732 QKEHARLLKNQSQYEKQLkklqqdvtEMKKTKvRLMKQM-KEEQEKARLTESRRNREIA-QLKKDQRKR 798
Cdd:pfam17380 529 IYEEERRREAEEERRKQQ--------EMEERR-RIQEQMrKATEERSRLEAMEREREMMrQIVESEKAR 588
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
932-1016 |
4.99e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 932 TISNMEADMNRLLRQREEL----TKRREKLSKRREKIAKESGEGDKN---------------LVNISEEMESLTANIDYI 992
Cdd:PRK02224 600 AIADAEDEIERLREKREALaelnDERRERLAEKRERKRELEAEFDEArieearedkeraeeyLEQVEEKLDELREERDDL 679
|
90 100
....*....|....*....|....
gi 1958788848 993 NDSIADCQANIMQMEEAKEEGETL 1016
Cdd:PRK02224 680 QAEIGAVENELEELEELRERREAL 703
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
690-825 |
6.77e-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: 39.50 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 690 DQVLQNLGSVESYSEEKA--KKVKCEYEKKLHAMNKELQR----LQTAQKEHARLLKNQSQYEKqlkklqqDVTEMKKTK 763
Cdd:pfam13851 19 DITRNNLELIKSLKEEIAelKKKEERNEKLMSEIQQENKRltepLQKAQEEVEELRKQLENYEK-------DKQSLKNLK 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958788848 764 VRL------MKQMKEEQE--KARLTESRRNREiaQLKKDQRKrdhqlRLLEAQKR--NQEVVLRRKTEEVTA 825
Cdd:pfam13851 92 ARLkvlekeLKDLKWEHEvlEQRFEKVERERD--ELYDKFEA-----AIQDVQQKtgLKNLLLEKKLQALGE 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
444-1064 |
7.25e-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: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 444 KAMQETVDALRARITQLVSEQANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKSLTRATARSPffsa 523
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY---- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 524 ssafsstILSSDKETIEiidlakkdleklkrkekrkkksvagkeNNADPDQEKKEEkgvSEKESSEVDVDENQEASDHED 603
Cdd:COG1196 292 -------ELLAELARLE---------------------------QDIARLEERRRE---LEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 604 EEDEEEEDEEEDDIEGEESSDESDSESDEKANYQADLAnitcEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIR 683
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA----ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 684 DTQLERDQVLQNLGSVESYSEEKAKKV---KCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVTEmK 760
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEeeeEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-A 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 761 KTKVRLMKQMKEEQE-----KARLTESRRNREIAQLKKDQRKRDHQLRLLEAQkRNQEVVLRRKTEEVTALRRQVRPMSD 835
Cdd:COG1196 490 AARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 836 KVAGKVTRKLSSSESPTPDAGSSVTSGEADASRPGTQQKMRIPVARVQALptpttngtrkryqRKGFTGRVFTSKTARMK 915
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL-------------GDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 916 WQLLERRVTE--IIMQKMTISNMEADMNRLLRQREELTKRREKLSKRREKIAKESGEGDKNLVNISEEMESLTANIDYIN 993
Cdd:COG1196 636 LRRAVTLAGRlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958788848 994 DSIADCQANIMQMEEAKEEGETLDvtavinacTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQ 1064
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLE--------ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
690-1090 |
8.29e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 690 DQVLQnLGSVESYsEEKAKKVKCEYEKKLHAMNKELQRL--QTAQKEHARLLKNQSQYEKQLKKLQQDVTEMKKTKVRlM 767
Cdd:PRK02224 156 DDLLQ-LGKLEEY-RERASDARLGVERVLSDQRGSLDQLkaQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQ-A 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 768 KQMKEEQEkARLTESRRNR-EIAQLKKDQRKrdhqlrlLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKvtrkLS 846
Cdd:PRK02224 233 RETRDEAD-EVLEEHEERReELETLEAEIED-------LRETIAETEREREELAEEVRDLRERLEELEEERDDL----LA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 847 SSESPTPDAgSSVTSGEADASRPGTQQKMRIPVARVQAlptpttngTRKRYQRKGFTGRVFTsktarmkwqlLERRVTEI 926
Cdd:PRK02224 301 EAGLDDADA-EAVEARREELEDRDEELRDRLEECRVAA--------QAHNEEAESLREDADD----------LEERAEEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 927 IMQKMTI-SNMEADmnrllrqREELTKRREKLSKRREKI---AKESGEGDKNLVNISEEMESLTANIDYINDSIADCQAN 1002
Cdd:PRK02224 362 REEAAELeSELEEA-------REAVEDRREEIEELEEEIeelRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 1003 IMQMEEAKEEGETL-----------DVTAVINACTLTEARYLLDHflsmginkgLQA--AQKEAQIKVLEGRLKQTEITS 1069
Cdd:PRK02224 435 LRTARERVEEAEALleagkcpecgqPVEGSPHVETIEEDRERVEE---------LEAelEDLEEEVEEVEERLERAEDLV 505
|
410 420
....*....|....*....|.
gi 1958788848 1070 ATQNQLlfHMLKEKAELNPEL 1090
Cdd:PRK02224 506 EAEDRI--ERLEERREDLEEL 524
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
663-792 |
8.91e-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: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788848 663 RLQTLKKQYEEKLMM-LQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYE-KKLHAMNKELQRLQTAQKEHARLL- 739
Cdd:TIGR02473 6 KLLDLREKEEEQAKLeLAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSaLELSNYQRFIRQLDQRIQQQQQELa 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958788848 740 KNQSQYEKQLKKLQQDVTEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLK 792
Cdd:TIGR02473 86 LLQQEVEAKRERLLEARRELKALEKLKEKKQKEYRAEEAKREQKEMDELATQR 138
|
|
| |
