|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
10-371 |
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: 609.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 10 CSVKVAVHIRPLIGDERIQGCQDCVTVVTGKPQVQIG-SHSFTFDHVYGSSgSPSTEMYEECAAPLVDGLFQGYNATVLA 88
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGtDKSFTFDYVFDPS-TEQEEVYNTCVAPLVDGLFEGYNATVLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 89 YGQTGSGKTYTMGTGCG---DSSQTGIIPQVMNALFTKIETLKQQIEFQIHVSFIEIHKEEVQDLLDPCTvnksdtnntg 165
Cdd:cd01372 80 YGQTGSGKTYTMGTAYTaeeDEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPET---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 166 hvgkvahvPGKPPIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEQMRKIN 245
Cdd:cd01372 150 --------DKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 246 TDSPengaYNGSLKEEYLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKRkdGAHVPYRDS 325
Cdd:cd01372 222 PIAP----MSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKK--GAHVPYRDS 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 30695302 326 KLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNIR 371
Cdd:cd01372 296 KLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
11-377 |
3.40e-143 |
|
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: 431.61 E-value: 3.40e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 11 SVKVAVHIRPLIGDERIQGCQDCVTVVTGKPQV--------QIGSHSFTFDHVYGSSgSPSTEMYEECAAPLVDGLFQGY 82
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspknRQGEKKFTFDKVFDAT-ASQEDVFEETAAPLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 83 NATVLAYGQTGSGKTYTMGtgcGDSSQTGIIPQVMNALFTKIETLKQQIEFQIHVSFIEIHKEEVQDLLDPCtvnksdtn 162
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMI---GTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPS-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 163 ntghvgkvahvpgKPPIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEQMR 242
Cdd:smart00129 149 -------------SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 243 KintdspengaynGSLKEEYLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKRKdgaHVPY 322
Cdd:smart00129 216 K------------NSSSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR---HIPY 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 30695302 323 RDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNIRNKPVVN 377
Cdd:smart00129 281 RDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
18-370 |
1.21e-138 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 419.29 E-value: 1.21e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 18 IRPLIGDERIQGCQDCVTVVTGKPQVQIGS--------HSFTFDHVYGSSgSPSTEMYEECAAPLVDGLFQGYNATVLAY 89
Cdd:pfam00225 2 VRPLNEREKERGSSVIVSVESVDSETVESShltnknrtKTFTFDKVFDPE-ATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 90 GQTGSGKTYTMGtgcGDSSQTGIIPQVMNALFTKIETLKQQIEFQIHVSFIEIHKEEVQDLLDPctvnksDTNNtghvgk 169
Cdd:pfam00225 81 GQTGSGKTYTME---GSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSP------SNKN------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 170 vahvpgKPPIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEQmRKINTDSp 249
Cdd:pfam00225 146 ------KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQ-RNRSTGG- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 250 engayngslKEEYLCAKLHLVDLAGSERAKRTG-SDGLRFKEGVHINKGLLALGNVISALGDEKKrkdgAHVPYRDSKLT 328
Cdd:pfam00225 218 ---------EESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS----KHIPYRDSKLT 284
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 30695302 329 RLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNI 370
Cdd:pfam00225 285 RLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
11-368 |
2.34e-125 |
|
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: 384.68 E-value: 2.34e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 11 SVKVAVHIRPLIGDERiQGCQDCVTVVTGKpQVQI--------GSHSFTFDHVYGSSgSPSTEMYEECAAPLVDGLFQGY 82
Cdd:cd00106 1 NVRVAVRVRPLNGREA-RSAKSVISVDGGK-SVVLdppknrvaPPKTFAFDAVFDST-STQEEVYEGTAKPLVDSALEGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 83 NATVLAYGQTGSGKTYTMGTGcgDSSQTGIIPQVMNALFTKIETLKQQI-EFQIHVSFIEIHKEEVQDLLDPCTvnksdt 161
Cdd:cd00106 78 NGTIFAYGQTGSGKTYTMLGP--DPEQRGIIPRALEDIFERIDKRKETKsSFSVSASYLEIYNEKIYDLLSPVP------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 162 nntghvgkvahvpgKPPIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEQM 241
Cdd:cd00106 150 --------------KKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 242 RKintdSPENGAYNGSlkeeylcaKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKRkdgaHVP 321
Cdd:cd00106 216 NR----EKSGESVTSS--------KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK----HIP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 30695302 322 YRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRAR 368
Cdd:cd00106 280 YRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
11-370 |
6.55e-113 |
|
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: 352.80 E-value: 6.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 11 SVKVAVHIRPLIGDERIQGCQDCVTVVTG-------------------KPQVQIGSHS----FTFDHVYGSSGSpSTEMY 67
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNhmlvfdpkdeedgffhggsNNRDRRKRRNkelkYVFDRVFDETST-QEEVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 68 EECAAPLVDGLFQGYNATVLAYGQTGSGKTYTMgtgCGDSSQTGIIPQVMNALFTKIETLKQQIEFQIHVSFIEIHKEEV 147
Cdd:cd01370 80 EETTKPLVDGVLNGYNATVFAYGATGAGKTHTM---LGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 148 QDLLdpctvnksdTNNTGhvgkvahvpgkpPIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQS 227
Cdd:cd01370 157 RDLL---------NPSSG------------PLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 228 SRSHAIFTITVEQMRKintdspengayNGSLKEEYLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISA 307
Cdd:cd01370 216 SRSHAVLQITVRQQDK-----------TASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINA 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695302 308 LGDEKKRKdgAHVPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNI 370
Cdd:cd01370 285 LADPGKKN--KHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
11-377 |
1.49e-109 |
|
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: 344.34 E-value: 1.49e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 11 SVKVAVHIRPLIGDERIQGC-------QDCVTVVTGKPQVQIGS------HSFTFDHVYGSSGSP------STEMYEECA 71
Cdd:cd01365 2 NVKVAVRVRPFNSREKERNSkcivqmsGKETTLKNPKQADKNNKatrevpKSFSFDYSYWSHDSEdpnyasQEQVYEDLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 72 APLVDGLFQGYNATVLAYGQTGSGKTYTMgtgCGDSSQTGIIPQVMNALFTKIE-TLKQQIEFQIHVSFIEIHKEEVQDL 150
Cdd:cd01365 82 EELLQHAFEGYNVCLFAYGQTGSGKSYTM---MGTQEQPGIIPRLCEDLFSRIAdTTNQNMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 151 LDPCTVNKsdtnntghvgkvahvpgKPPIQIRE-TSNGVItLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSR 229
Cdd:cd01365 159 LNPKPKKN-----------------KGNLKVREhPVLGPY-VEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 230 SHAIFTITVEQMRkinTDSPENGAYNGSlkeeylcAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALG 309
Cdd:cd01365 221 SHAVFTIVLTQKR---HDAETNLTTEKV-------SKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695302 310 DEKKRKDGAH---VPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNIRNKPVVN 377
Cdd:cd01365 291 DMSSGKSKKKssfIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
9-370 |
1.34e-105 |
|
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: 332.76 E-value: 1.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 9 DCSVKVAVHIRPLIGDERIQGCQDCVTVvTGKPQVQIGS----HSFTFDHVYGSSGSPStEMYEECAAPLVDGLFQGYNA 84
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKF-DPEDTVVIATsetgKTFSFDRVFDPNTTQE-DVYNFAAKPIVDDVLNGYNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 85 TVLAYGQTGSGKTYTMGTGCGDSSQTGIIPQVMNALFTKIETLKQQIEFQIHVSFIEIHKEEVQDLLDPctvnkSDTNnt 164
Cdd:cd01369 79 TIFAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDV-----SKTN-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 165 ghvgkvahvpgkppIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEQmRKI 244
Cdd:cd01369 152 --------------LSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-ENV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 245 NTDSPENGayngslkeeylcaKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKrkdgAHVPYRD 324
Cdd:cd01369 217 ETEKKKSG-------------KLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK----THIPYRD 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 30695302 325 SKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNI 370
Cdd:cd01369 280 SKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
11-370 |
4.63e-104 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 329.04 E-value: 4.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 11 SVKVAVHIRPLIGDERIQGCQDCVTVVTGKPQVQIGS---------HSFTFDHVYGSsGSPSTEMYEECAAPLVDGLFQG 81
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNpkataneppKTFTFDAVFDP-NSKQLDVYDETARPLVDSVLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 82 YNATVLAYGQTGSGKTYTMGTGCGDSSQTGIIPQVMNALFTKIETLKQQIEFQIHVSFIEIHKEEVQDLLdpctvnksdT 161
Cdd:cd01371 81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLL---------G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 162 NNTGHVGKVAHVPGKppiqiretsnGVITLAGSTEVsVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEQM 241
Cdd:cd01371 152 KDQTKRLELKERPDT----------GVYVKDLSMFV-VKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 242 RKINTDspengayngslKEEYLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKrkdgAHVP 321
Cdd:cd01371 221 EKGEDG-----------ENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKS----THIP 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 30695302 322 YRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNI 370
Cdd:cd01371 286 YRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
11-370 |
4.23e-103 |
|
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: 325.83 E-value: 4.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 11 SVKVAVHIRPLIGDErIQGCQDCVTVVTGKP--QVQIGSHSFTFDHVYGSSgSPSTEMYEECAAPLVDGLFQGYNATVLA 88
Cdd:cd01374 1 KITVTVRVRPLNSRE-IGINEQVAWEIDNDTiyLVEPPSTSFTFDHVFGGD-STNREVYELIAKPVVKSALEGYNGTIFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 89 YGQTGSGKTYTMGtgcGDSSQTGIIPQVMNALFTKIETLKQQiEFQIHVSFIEIHKEEVQDLLDPCTVNksdtnntghvg 168
Cdd:cd01374 79 YGQTSSGKTFTMS---GDEDEPGIIPLAIRDIFSKIQDTPDR-EFLLRVSYLEIYNEKINDLLSPTSQN----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 169 kvahvpgkppIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEqmRKINTDS 248
Cdd:cd01374 144 ----------LKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIE--SSERGEL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 249 PENGAyngslkeeyLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKRKdgaHVPYRDSKLT 328
Cdd:cd01374 212 EEGTV---------RVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG---HIPYRDSKLT 279
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 30695302 329 RLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNI 370
Cdd:cd01374 280 RILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
12-379 |
1.89e-99 |
|
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: 317.35 E-value: 1.89e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 12 VKVAVHIRPLIGDER-------IQGCQDC--VTVVTGKPQVQIGSHSFTFDHVYGSSgSPSTEMYEECAAPLVDGLFQGY 82
Cdd:cd01364 4 IQVVVRCRPFNLRERkasshsvVEVDPVRkeVSVRTGGLADKSSTKTYTFDMVFGPE-AKQIDVYRSVVCPILDEVLMGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 83 NATVLAYGQTGSGKTYTM--------GTGCGDSSQTGIIPQVMNALFTKIETlkQQIEFQIHVSFIEIHKEEVQDLLdpc 154
Cdd:cd01364 83 NCTIFAYGQTGTGKTYTMegdrspneEYTWELDPLAGIIPRTLHQLFEKLED--NGTEYSVKVSYLEIYNEELFDLL--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 155 tvnkSDTNNTGHvgkvahvpgkpPIQIRETSNGV--ITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHA 232
Cdd:cd01364 158 ----SPSSDVSE-----------RLRMFDDPRNKrgVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 233 IFTITVEQmrKINTDSPEngayngslkEEYLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEK 312
Cdd:cd01364 223 VFSITIHI--KETTIDGE---------ELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERA 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30695302 313 KrkdgaHVPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNIRNKPVVNRD 379
Cdd:cd01364 292 P-----HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
18-372 |
5.00e-96 |
|
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: 307.21 E-value: 5.00e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 18 IRPLIGDERIQGcQDCVTVVTGKPQV------QIGSHSFTFDHVYGSSGSPStEMYEEcAAPLVDGLFQGYNATVLAYGQ 91
Cdd:cd01366 10 VRPLLPSEENED-TSHITFPDEDGQTieltsiGAKQKEFSFDKVFDPEASQE-DVFEE-VSPLVQSALDGYNVCIFAYGQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 92 TGSGKTYTMGtgcGDSSQTGIIPQVMNALFTKIETLKQQ-IEFQIHVSFIEIHKEEVQDLLdpctvnksdtnNTGHVGKv 170
Cdd:cd01366 87 TGSGKTYTME---GPPESPGIIPRALQELFNTIKELKEKgWSYTIKASMLEIYNETIRDLL-----------APGNAPQ- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 171 ahvpgkPPIQIRETS-NGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEqmrkintdsp 249
Cdd:cd01366 152 ------KKLEIRHDSeKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIS---------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 250 engAYNgSLKEEYLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALgdekkRKDGAHVPYRDSKLTR 329
Cdd:cd01366 216 ---GRN-LQTGEISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL-----RQKQSHIPYRNSKLTY 286
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 30695302 330 LLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNIRN 372
Cdd:cd01366 287 LLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
50-522 |
7.17e-91 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 301.66 E-value: 7.17e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 50 FTFDHVYGSSgSPSTEMYEECAAPLVDGLFQGYNATVLAYGQTGSGKTYTMGtgcGDSSQTGIIPQVMNALFTKIETLKQ 129
Cdd:COG5059 58 YAFDKVFGPS-ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMS---GTEEEPGIIPLSLKELFSKLEDLSM 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 130 QIEFQIHVSFIEIHKEEVQDLLDPCTVNKSdtnntghvgkvahvpgkppiqIRETSNGVITLAGSTEVSVSTLKEMAACL 209
Cdd:COG5059 134 TKDFAVSISYLEIYNEKIYDLLSPNEESLN---------------------IREDSLLGVKVAGLTEKHVSSKEEILDLL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 210 DQGSVSRATGSTNMNNQSSRSHAIFTITVEQmrkintdspengayNGSLKEEYLCAKLHLVDLAGSERAKRTGSDGLRFK 289
Cdd:COG5059 193 RKGEKNRTTASTEINDESSRSHSIFQIELAS--------------KNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 290 EGVHINKGLLALGNVISALGDEKKRKdgaHVPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARN 369
Cdd:COG5059 259 EGASINKSLLTLGNVINALGDKKKSG---HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 370 IRNKPVVNRD---PVSSEMLKmRQQVEYLQAELSLRTGGSSCAEVQALKERIVWLETaneeLCRELHEYRSRCPG----- 441
Cdd:COG5059 336 IKNKIQVNSSsdsSREIEEIK-FDLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQS----LKKETETLKSRIDLimksi 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 442 VEHSEKDFKDIRADDIVgsvrpdgLKRSLHSIESsnypmvEATTGDSREIDEEAKEWEHKLLQNSMDKELYEL-NRRLEE 520
Cdd:COG5059 411 ISGTFERKKLLKEEGWK-------YKSTLQFLRI------EIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLlSSIPEE 477
|
..
gi 30695302 521 KE 522
Cdd:COG5059 478 TS 479
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
12-379 |
8.19e-86 |
|
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: 280.55 E-value: 8.19e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 12 VKVAVHIRPLIGDERIQGCQDCVTVVTGKPQVqigSHS-----FTFDHVYGSSgSPSTEMYEECAAPLVDGLFQGYNATV 86
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLV---LHSkppktFTFDHVADSN-TNQESVFQSVGKPIVESCLSGYNGTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 87 LAYGQTGSGKTYTMGTGCGDSSQT-----GIIPQVMNALFTKI----ETLKQQIEFQIHVSFIEIHKEEVQDLLDPCTVN 157
Cdd:cd01373 79 FAYGQTGSGKTYTMWGPSESDNESphglrGVIPRIFEYLFSLIqrekEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 158 ksdtnntghvgkvahvpgkppIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTIT 237
Cdd:cd01373 159 ---------------------LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 238 VEQMRKintdspENGAYNGSLkeeylcAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKRKDg 317
Cdd:cd01373 218 IESWEK------KACFVNIRT------SRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQ- 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695302 318 AHVPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNIRNKPVVNRD 379
Cdd:cd01373 285 RHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
12-366 |
7.65e-81 |
|
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: 266.47 E-value: 7.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 12 VKVAVHIRPLIGDERIQG--------CQDCVTVVTGKPQVQ----IGSHSFTFDHVYGSSgSPSTEMYEECAAPLVDGLF 79
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKeidvvsvpSKLTLIVHEPKLKVDltkyIENHTFRFDYVFDES-SSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 80 QGYNATVLAYGQTGSGKTYTM-GTGCGDSSQTGIIPQVMNALFTKIETLKQQIEFQIHVSFIEIHKEEVQDLLDPCTvnk 158
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMgGDFSGQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLNRKK--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 159 sdtnntghvgkvahvpgkpPIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTItv 238
Cdd:cd01367 158 -------------------RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 239 eQMRKINTDSpengayngslkeeyLCAKLHLVDLAGSER-AKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKkrkdg 317
Cdd:cd01367 217 -ILRDRGTNK--------------LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK----- 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 30695302 318 AHVPYRDSKLTRLLQDSL-GGNSRTVMIACISPADINAEETLNTLKYANR 366
Cdd:cd01367 277 AHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
12-364 |
2.78e-72 |
|
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: 243.46 E-value: 2.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 12 VKVAVHIRPLIGDERIQGCQDCVTVVTG-----KPQVQIGSHS-----------FTFDHVYGSSGSpSTEMYEECAAPLV 75
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEGCIEVINSttvvlHPPKGSAANKsernggqketkFSFSKVFGPNTT-QKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 76 DGLFQGYNATVLAYGQTGSGKTYTMGtgcGDSSQTGIIPQVMNALFTKIEtlkqqiEFQIHVSFIEIHKEEVQDLLDPCT 155
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTMQ---GSPGDGGILPRSLDVIFNSIG------GYSVFVSYIEIYNEYIYDLLEPSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 156 VNKSDTnntghvgkvahvpgKPPIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFT 235
Cdd:cd01368 153 SSPTKK--------------RQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 236 ITVEQmrkINTDSPENGAYNgslKEEYLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKRK 315
Cdd:cd01368 219 IKLVQ---APGDSDGDVDQD---KDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQG 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 30695302 316 DGAHVPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYA 364
Cdd:cd01368 293 TNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
12-368 |
1.19e-71 |
|
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: 240.87 E-value: 1.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 12 VKVAVHIRPLIGDERIQGCQDCVTVVTGK------PQVQIGSHSFTFDHVYGSSgSPSTEMYEECAAPLVDGLFQGYNAT 85
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCsveladPRNHGETLKYQFDAFYGEE-STQEDIYAREVQPIVPHLLEGQNAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 86 VLAYGQTGSGKTYTMgtgCGDSSQTGIIPQVMNALFTKIEtlKQQIEFQIHVSFIEIHKEEVQDLLDPCTVNksdtnntg 165
Cdd:cd01376 81 VFAYGSTGAGKTFTM---LGSPEQPGLMPLTVMDLLQMTR--KEAWALSFTMSYLEIYQEKILDLLEPASKE-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 166 hvgkvahvpgkppIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITV-EQMRKI 244
Cdd:cd01376 148 -------------LVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVdQRERLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 245 NTDSPEngayngslkeeylcAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKRkdgahVPYRD 324
Cdd:cd01376 215 PFRQRT--------------GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR-----IPYRD 275
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 30695302 325 SKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRAR 368
Cdd:cd01376 276 SKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
47-368 |
3.07e-68 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 232.09 E-value: 3.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 47 SHSFTFDHVYGSSgspSTEM-YEECAAPLVDGLFQGYNATVLAYGQTGSGKTYTMGTGCGDSSQTGIIPQVMNALFTKIE 125
Cdd:cd01375 47 DWSFKFDGVLHNA---SQELvYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 126 TLKQQIeFQIHVSFIEIHKEEVQDLLDPctvnksdtnnTGHVGkvahvPGKPPIQIRETSNGVITLAGSTEVSVSTLKEM 205
Cdd:cd01375 124 ERPTKA-YTVHVSYLEIYNEQLYDLLST----------LPYVG-----PSVTPMTILEDSPQNIFIKGLSLHLTSQEEEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 206 AACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEqMRKINTDSpengayngslkEEYLCAKLHLVDLAGSERAKRTGSDG 285
Cdd:cd01375 188 LSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLE-AHSRTLSS-----------EKYITSKLNLVDLAGSERLSKTGVEG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 286 LRFKEGVHINKGLLALGNVISALGDekkrKDGAHVPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYAN 365
Cdd:cd01375 256 QVLKEATYINKSLSFLEQAIIALSD----KDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFAS 331
|
...
gi 30695302 366 RAR 368
Cdd:cd01375 332 RVK 334
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
9-377 |
1.94e-64 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 238.68 E-value: 1.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 9 DCSVKVAVHIRPLIGDERiqgcQDCVTVVTGKPQVQIGSHSFTFDHVyGSSGSPSTEMYEECAAPLVDGLFQGYNATVLA 88
Cdd:PLN03188 97 DSGVKVIVRMKPLNKGEE----GEMIVQKMSNDSLTINGQTFTFDSI-ADPESTQEDIFQLVGAPLVENCLAGFNSSVFA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 89 YGQTGSGKTYTM-GTGCG------DSSQTGIIPQVMNALFTKI--ETLK---QQIEFQIHVSFIEIHKEEVQDLLDPCTV 156
Cdd:PLN03188 172 YGQTGSGKTYTMwGPANGlleehlSGDQQGLTPRVFERLFARIneEQIKhadRQLKYQCRCSFLEIYNEQITDLLDPSQK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 157 NksdtnntghvgkvahvpgkppIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTI 236
Cdd:PLN03188 252 N---------------------LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 237 TVEQMRKINTDSPEngayngSLKEeylcAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKRKD 316
Cdd:PLN03188 311 VVESRCKSVADGLS------SFKT----SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGK 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695302 317 GAHVPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNIRNKPVVN 377
Cdd:PLN03188 381 QRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN 441
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
46-349 |
8.18e-17 |
|
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: 78.93 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 46 GSHSFTFDHVYGSSGSPStEMYEECAaPLVDGLFQGYN-ATVLAYGQTGSGKTYTMgtgcgdssqTGIIPQVMNALFTKI 124
Cdd:cd01363 16 DSKIIVFYRGFRRSESQP-HVFAIAD-PAYQSMLDGYNnQSIFAYGESGAGKTETM---------KGVIPYLASVAFNGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 125 ETLKQQIEFQIHVSFIEIhKEEVQDLLdpctvnksdtnntgHVGKvahvpgkppiqiretSNGvitlagstevsvstlke 204
Cdd:cd01363 85 NKGETEGWVYLTEITVTL-EDQILQAN--------------PILE---------------AFG----------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 205 maacldqgsvsraTGSTNMNNQSSRSHAIFTItveqmrkintdspengayngslkeeylcaklhLVDLAGSERakrtgsd 284
Cdd:cd01363 118 -------------NAKTTRNENSSRFGKFIEI--------------------------------LLDIAGFEI------- 145
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695302 285 glrfkegvhINKGLLALGNVISAlgdekkrkdgahvpyrdskltrllqdslggnSRTVMIACISP 349
Cdd:cd01363 146 ---------INESLNTLMNVLRA-------------------------------TRPHFVRCISP 170
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
10-151 |
2.86e-16 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 76.88 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 10 CSVKVAVHIRPLIGDE-RIQGCQDCVTvvtgKPQVQIGSHSFTFDHVYGSSgSPSTEMYEECAApLVDGLFQGYNATVLA 88
Cdd:pfam16796 20 GNIRVFARVRPELLSEaQIDYPDETSS----DGKIGSKNKSFSFDRVFPPE-SEQEDVFQEISQ-LVQSCLDGYNVCIFA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695302 89 YGQTGSGKTYTMgtgcgdssqtgiIPQVMNALFTKIETLKQQIEFQIHVSFIEIHKEEVQDLL 151
Cdd:pfam16796 94 YGQTGSGSNDGM------------IPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
480-705 |
8.88e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.65 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 480 MVEATTGDSREIDEEAKEWehkllqnsMDKELYELNRRLEEKESEMKLF----DGYDPAALKQHFGKKIAEVEDEKRSVQ 555
Cdd:COG3206 161 YLEQNLELRREEARKALEF--------LEEQLPELRKELEEAEAALEEFrqknGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 556 EERNRLLAEIENLAS--DGQAQKLQDVHA-QNLKALEAQILDLKKKQEsqvQLLKQKQKSDDAARRLQDEIQSIKAQKVQ 632
Cdd:COG3206 233 AELAEAEARLAALRAqlGSGPDALPELLQsPVIQQLRAQLAELEAELA---ELSARYTPNHPDVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695302 633 LQHRMKQEAEQFRQWKASREKELlqlrkEGRKSEYERhKLQALNQRQK--MVLQRkteEAAMATKRLKELLEARK 705
Cdd:COG3206 310 EAQRILASLEAELEALQAREASL-----QAQLAQLEA-RLAELPELEAelRRLER---EVEVARELYESLLQRLE 375
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
489-769 |
9.71e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 489 REIDEEAKEWEHKLLQNsmdkELYELNRRLEEKESEmklfdgydpaalkqhfgkkIAEVEDEKRSVQEERNRLLAEIENL 568
Cdd:COG1196 216 RELKEELKELEAELLLL----KLRELEAELEELEAE-------------------LEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 569 ASDGQAQKLQDVHAQN-LKALEAQILDLKKKQESQVQLLKQKQksdDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQW 647
Cdd:COG1196 273 RLELEELELELEEAQAeEYELLAELARLEQDIARLEERRRELE---ERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 648 KA---SREKELLQLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLKELLEARKSSPREHSAgtngfgtngqt 724
Cdd:COG1196 350 EEeleEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER----------- 418
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 30695302 725 NEKSLQRWLDHELEVMVNVHEVRHEYEKQSHVRAALAEELAVLRQ 769
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
542-769 |
4.60e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 542 KKIAEVEDEKRSVQEERNRLLAEIENLASDG-QAQKLQDVHAQNLKALEAQILDLKKKQEsqvQLLKQKQKSDDAARRLQ 620
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELeQLRKELEELSRQISALRKDLARLEAEVE---QLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 621 DEIQSIKAQKVQLQ---HRMKQEAEQFRQWKASREKELLQLRKEGR--KSEYERHKLQALNQRQKmvLQRKTEEAAMATK 695
Cdd:TIGR02168 761 AEIEELEERLEEAEeelAEAEAEIEELEAQIEQLKEELKALREALDelRAELTLLNEEAANLRER--LESLERRIAATER 838
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695302 696 RLKELlEARKSSPREHSAGTNGFGTNGQTNEKSLQRWLDHELEVM----VNVHEVRHEYEKQSHVRAALAEELAVLRQ 769
Cdd:TIGR02168 839 RLEDL-EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERasleEALALLRSELEELSEELRELESKRSELRR 915
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
493-905 |
1.41e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 493 EEAKEWEHKllqnsmdKELYELNRRLEEKESEMKLFDGYDPAALKQHFGKKIAEVEDEKRSVQEERNRLLA-EIENLASD 571
Cdd:PTZ00121 1293 DEAKKAEEK-------KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdEAEAAEEK 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 572 GQAQKLQDVHAQN-LKALEAQILDLKKKQESQVQLLKQKQKSDD-----AARRLQDEIQSiKAQKVQLQHRMKQEAEQFR 645
Cdd:PTZ00121 1366 AEAAEKKKEEAKKkADAAKKKAEEKKKADEAKKKAEEDKKKADElkkaaAAKKKADEAKK-KAEEKKKADEAKKKAEEAK 1444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 646 QWKASREK--------ELLQLRKEGRKSEYERHKlqALNQRQKMVLQRKTEEAAMATKRLKELLEARKSSPREHSAgtng 717
Cdd:PTZ00121 1445 KADEAKKKaeeakkaeEAKKKAEEAKKADEAKKK--AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA---- 1518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 718 fgtngqtnEKSLQRWLDHELEVMVNVHEVRHEYEKQSHVRAALAEELAVLRQVDEFAVKGLSPPRgKNGFARASSLSPNA 797
Cdd:PTZ00121 1519 --------EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED-KNMALRKAEEAKKA 1589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 798 RMARIsslENMLVISSNSLVAMASQLSEAEEReraftnRGRWNQLRSMGEAKNLLQYMFNSLAETRcqlwEKDVEIKEMK 877
Cdd:PTZ00121 1590 EEARI---EEVMKLYEEEKKMKAEEAKKAEEA------KIKAEELKKAEEEKKKVEQLKKKEAEEK----KKAEELKKAE 1656
|
410 420
....*....|....*....|....*...
gi 30695302 878 DQFKeivglLRQSELRRKEAEKELKLRE 905
Cdd:PTZ00121 1657 EENK-----IKAAEEAKKAEEDKKKAEE 1679
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
489-716 |
3.86e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 489 REIDEEAKEWEHKLLQNSMD---KELYELNRRLEEKESEMKlfdgyDPAALKQHFGKKIAEVEDEKRSVQEERNrllaei 565
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEelrEELEELQEELKEAEEELE-----ELTAELQELEEKLEELRLEVSELEEEIE------ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 566 enlasdgQAQKLQDVHAQNLKALEAQILDLKKKQES--------QVQLLKQKQKSDDAAR---RLQDEIQSIKAQKVQLQ 634
Cdd:TIGR02168 285 -------ELQKELYALANEISRLEQQKQILRERLANlerqleelEAQLEELESKLDELAEelaELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 635 HRMKQEAEQFRQWK---ASREKELLQLRKE----GRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLKELLEARKSS 707
Cdd:TIGR02168 358 AELEELEAELEELEsrlEELEEQLETLRSKvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
....*....
gi 30695302 708 PREHSAGTN 716
Cdd:TIGR02168 438 LQAELEELE 446
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
482-714 |
9.55e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 482 EATTGDSREIDEEAKEWEHKLLQNSmdKELYELNRRLEEKESEMKLFDGYDPAALKQHFGK----------KIAEVEDEK 551
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELE--KRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGEleaeiaslerSIAEKEREL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 552 RSVQEERNRLLAEIENLASD--GQAQKLQDVHAQnLKALEAQILDLKKKQESQVQLLKQKQKSDDAARR----------- 618
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEieELEREIEEERKR-RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDelkdyreklek 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 619 LQDEIQSIKAQKVQLQHR----------MKQEAEQFRQWKASREKELLQLRKEGRKSEYERHKLQALNQRQKMVLQRKTE 688
Cdd:TIGR02169 397 LKREINELKRELDRLQEElqrlseeladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
250 260 270
....*....|....*....|....*....|..
gi 30695302 689 EAAMATKRLKEL------LEARKSSPREHSAG 714
Cdd:TIGR02169 477 EYDRVEKELSKLqrelaeAEAQARASEERVRG 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
509-721 |
1.37e-06 |
|
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: 51.69 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 509 KELYELNRRLEEKESEMKLFDGYDPAALKQ--HFGKKIAEVEDEKRSVQEERNRLLAEIENLASdgQAQKLQDVHAQNLK 586
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQlaALERRIAALARRIRALEQELAALEAELAELEK--EIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 587 ALEAQILDL-KKKQESQVQLLKQKQKSDDAARRL----------QDEIQSIKAQKVQLQH------RMKQEAEQFRQWKA 649
Cdd:COG4942 105 ELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLqylkylaparREQAEELRADLAELAAlraeleAERAELEALLAELE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695302 650 SREKELLQLRKegrkseyERHKLQALNQRQKMVLQRKTEEAAMATKRLKELLEA--RKSSPREHSAGTNGFGTN 721
Cdd:COG4942 185 EERAALEALKA-------ERQKLLARLEKELAELAAELAELQQEAEELEALIARleAEAAAAAERTPAAGFAAL 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-909 |
5.53e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 384 EMLKMRQQVEYLQAELSLRTGgsscaEVQALKERIVWLETANEEL---CRELHEYRSRCPGVEHSEKDFKDIRA--DDIV 458
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEG-----SKRKLEEKIRELEERIEELkkeIEELEEKVKELKELKEKAEEYIKLSEfyEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 459 -----GSVRPDGLKRSLHSIESSnypMVEATTGDSR--EIDEEAKEWEHKLLQNSMDKELYELNRRL-EEKESEMKLFDG 530
Cdd:PRK03918 307 delreIEKRLSRLEEEINGIEER---IKELEEKEERleELKKKLKELEKRLEELEERHELYEEAKAKkEELERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 531 YDPAALKqhfgKKIAEVEDEKRSVQEERNRLLAEIENLasdgqaqklqdvhaqnlkalEAQILDLKKKQEsqvQLLKQKQ 610
Cdd:PRK03918 384 LTPEKLE----KELEELEKAKEEIEEEISKITARIGEL--------------------KKEIKELKKAIE---ELKKAKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 611 KSDDAARRLQDEiqsikaQKVQLQHRMKQEAEQFRQWKASREKELLQLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEA 690
Cdd:PRK03918 437 KCPVCGRELTEE------HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 691 AMATKRLKELlEARKSSPREHSAGTNGFGTNGQTNEKSLQRWLDHELEVMVNVHEVRHEYEKQSHVRAALAEELAVLRQV 770
Cdd:PRK03918 511 KLKKYNLEEL-EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 771 DEFAVKGLSPPrgkngFARASSLSPNARmaRISSLENMLVISSNSLVAMASQLSEAEERERAFtnRGRWNQLR---SMGE 847
Cdd:PRK03918 590 LEERLKELEPF-----YNEYLELKDAEK--ELEREEKELKKLEEELDKAFEELAETEKRLEEL--RKELEELEkkySEEE 660
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695302 848 AKNLlqymFNSLAETRCQLWEKDVEIKEMKDQFKEIVGLLRQSELR---RKEAEKELKLREQAIA 909
Cdd:PRK03918 661 YEEL----REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEleeREKAKKELEKLEKALE 721
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
573-832 |
6.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 573 QAQKLQDvHAQNLKALEAQILDLKKkqesQVQLLKQkqksddaARRLQDEIQSIKAQKVQLQhrmkQEAEQFRQWKASRE 652
Cdd:COG4913 226 AADALVE-HFDDLERAHEALEDARE----QIELLEP-------IRELAERYAAARERLAELE----YLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 653 KELLQLRKEGRKSEYERHKLQalnqrqkmvLQRKTEEAAMATKRLKELLEARKSsprehsagtngfgtNGQTNEKSLQRw 732
Cdd:COG4913 290 LELLEAELEELRAELARLEAE---------LERLEARLDALREELDELEAQIRG--------------NGGDRLEQLER- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 733 ldhELEvmvnvhEVRHEYEKQSHVRAALAEELAVLrqvdefavkGLSPPRGKNGFARASSLSPnarmARISSLENMLVIS 812
Cdd:COG4913 346 ---EIE------RLERELEERERRRARLEALLAAL---------GLPLPASAEEFAALRAEAA----ALLEALEEELEAL 403
|
250 260
....*....|....*....|
gi 30695302 813 SNSLVAMASQLSEAEERERA 832
Cdd:COG4913 404 EEALAEAEAALRDLRRELRE 423
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
489-669 |
6.34e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 489 REIDEEAKEWEHKLLQ-NSMDKELYELNRRLEEKESEMKLFDGYDpaalkQHFGKKIAEVEDEKRsVQEERNRLLAEIEN 567
Cdd:COG3096 498 RELLRRYRSQQALAQRlQQLRAQLAELEQRLRQQQNAERLLEEFC-----QRIGQQLDAAEELEE-LLAELEAQLEELEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 568 LASDGQAQKLQdvHAQNLKALEAQILDLKKKQESQVqllkqkqKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQw 647
Cdd:COG3096 572 QAAEAVEQRSE--LRQQLEQLRARIKELAARAPAWL-------AAQDALERLREQSGEALADSQEVTAAMQQLLERERE- 641
|
170 180
....*....|....*....|..
gi 30695302 648 kASREKELLQLRKEGRKSEYER 669
Cdd:COG3096 642 -ATVERDELAARKQALESQIER 662
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
513-710 |
7.32e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 513 ELNRRLEEKESEMKLfdgydpaalKQHFGKKIAEVEDEKRSVQEERNRLLAEIENLASDgqaqklqdvhaqnLKALEAQI 592
Cdd:PRK03918 173 EIKRRIERLEKFIKR---------TENIEELIKEKEKELEEVLREINEISSELPELREE-------------LEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 593 LDLKKKQESQVQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFR-----QWKASREKELLQLRKEGRKSEY 667
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 30695302 668 ERHKLQALNQRQKMVLQRKTEEAAMATKRLKELLEARKSSPRE 710
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
409-710 |
1.80e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 409 AEVQALKERIVWLETANEELCRELHEYRSRcpgVEHSEKDFKDIRADDIVGSVRPDGLKRSLHSIESSnypmVEATTGDS 488
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKE---LEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 489 REIDEEAKEWEHKLlqNSMDKELYELNRRLEEKESEMKLFDGYDPAALKQH--FGKKIAEVEDEKRSVQEERNRLLAEIE 566
Cdd:TIGR02168 750 AQLSKELTELEAEI--EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkaLREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 567 NLASD-GQAQKLQDVHAQNLKALEAQILDLKKKQESQVQLLKQKQksdDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFR 645
Cdd:TIGR02168 828 SLERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE---SELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30695302 646 QWkasrEKELLQLRKEGRKSEYERHK----LQALNQRQKMVLQRKTEEAAMATKRLKELLEARKSSPRE 710
Cdd:TIGR02168 905 EL----ESKRSELRRELEELREKLAQlelrLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
489-696 |
2.31e-05 |
|
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: 47.84 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 489 REIDEEAKEWEHKLLQ-NSMDKELYELNRRLEEKESEMKLFDgydpaalkqhfgKKIAEVEDEKRSVQEERNRLLAEIEN 567
Cdd:COG4942 41 KELAALKKEEKALLKQlAALERRIAALARRIRALEQELAALE------------AELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 568 LASDGQAQKLQD-----VHAQNLKALEAQILDLKKKQESQVQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAE 642
Cdd:COG4942 109 LLRALYRLGRQPplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 30695302 643 QFRQWKASREKELLQLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKR 696
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
336-909 |
2.83e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 336 GGNSRTVMIACISPADINAEETLNTLKyanrarNIRNKPVVNRDPVSSEMLKMRQQVEYLQAELSLRTGGSSCA-EVQAL 414
Cdd:pfam12128 173 DSESPLRHIDKIAKAMHSKEGKFRDVK------SMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRpEFTKL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 415 KERIVWLETANEELCRELHEYRSRCPGVEHSEKDFKDIRADdivgsvrpdgLKRSLHSIESSNYPMVEATTGDSREIDEE 494
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE----------LNQLLRTLDDQWKEKRDELNGELSAADAA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 495 AKEWEHKL----------LQNSMDKELYELNR------RLEEKESEMKLFDG--------YDP--AALKQHFGKKIAEVE 548
Cdd:pfam12128 317 VAKDRSELealedqhgafLDADIETAAADQEQlpswqsELENLEERLKALTGkhqdvtakYNRrrSKIKEQNNRDIAGIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 549 DEKRSVQEERNRLLAEIENlASDGQAQKLQDVH-AQNLKALEAQILDLKKKQESQVQLlkqkqksdDAARRLQDEIQSIk 627
Cdd:pfam12128 397 DKLAKIREARDRQLAVAED-DLQALESELREQLeAGKLEFNEEEYRLKSRLGELKLRL--------NQATATPELLLQL- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 628 AQKVQLQHRMKQEAEQFRQWKASREKELLQLRKegrKSEYERHKLQALNQRqkmVLQRKTEEAAM------ATKRLKELL 701
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEVERLQSELRQARK---RRDQASEALRQASRR---LEERQSALDELelqlfpQAGTLLHFL 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 702 EARKSSPREH------------------------SAGTNGFGTNGQTNEKSLQRWLDHELEVMVNVHEVRHEYEKQSHVR 757
Cdd:pfam12128 541 RKEAPDWEQSigkvispellhrtdldpevwdgsvGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 758 AALAEELAVLRQVDEFAVKGLSpprgkngFARASSLSPNARMARIsslenmlvisSNSLVAMASQLSEAEERERAFTNRg 837
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREET-------FARTALKNARLDLRRL----------FDEKQSEKDKKNKALAERKDSANE- 682
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695302 838 rwnQLRSM-GEAKNLLQYMFNSLAETRCQLWEKDVeikEMKDQFKEIVGLLRQSELRRKEAekELKLREQAIA 909
Cdd:pfam12128 683 ---RLNSLeAQLKQLDKKHQAWLEEQKEQKREART---EKQAYWQVVEGALDAQLALLKAA--IAARRSGAKA 747
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
543-690 |
3.20e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 543 KIAEVEDEKRSVQEERNRLLAEIENLASD-GQAQKLQDVHAQNLKALEAQildLKKKQESQVQLLKQKQKSDDAARRLQD 621
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEElEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695302 622 EIQSIKAQKVQLQHR---MKQEAEQFRQWKASREKELLQLRKEgrkSEYERHKLQALNQRQKMVLQRKTEEA 690
Cdd:COG4372 116 ELEELQKERQDLEQQrkqLEAQIAELQSEIAEREEELKELEEQ---LESLQEELAALEQELQALSEAEAEQA 184
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
513-674 |
6.72e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 513 ELNRRLEEKESEMKLFDGYDPAALKQHFGKKIAEVEDEKRSVQEERNRLLAEIENLAS--DGQAQKLQDVHAQ------- 583
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEArlDALREELDELEAQirgnggd 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 584 NLKALEAQILDLKKKQESQVQLLKQKQksdDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQWKASREKELLQLRKEGR 663
Cdd:COG4913 339 RLEQLEREIERLERELEERERRRARLE---ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
170
....*....|.
gi 30695302 664 KSEYERHKLQA 674
Cdd:COG4913 416 DLRRELRELEA 426
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
545-916 |
6.84e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 545 AEVEDEKRSVQEERNRLL--AEIENLASDGQAQKLQDVhAQNLKALEAQILD-LKKKQESQVQlLKQKQKSDDAARRLQD 621
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTlrSQLLTLCTPCMPDTYHER-KQVLEKELKHLREaLQQTQQSHAY-LTQKREAQEEQLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 622 EIQSIKAQKVQLQHRMKQEAEQfrqwkasrEKELLQLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLKELL 701
Cdd:TIGR00618 261 LLKQLRARIEELRAQEAVLEET--------QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 702 EARKSSprehsagtngfgtNGQTNEKSLQRWLDHELEVMVNvHEVRHEYEKQSHVRAALAEELAVLRQVDEFAVKGLSPP 781
Cdd:TIGR00618 333 HVKQQS-------------SIEEQRRLLQTLHSQEIHIRDA-HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 782 RGKNGFARASSLSPNARMARISSLENMLVISSNSLVAmasQLSEAEERERAFTnrgrwNQLRSMGEAKNLLQYMFNSLAE 861
Cdd:TIGR00618 399 CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAIT-----CTAQCEKLEKIHLQESAQSLKE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 30695302 862 TRCQLWEKDVEIKemkdQFKEIVGLLRQSELRRKEAEKELKLRE---QAIATSLGTPP 916
Cdd:TIGR00618 471 REQQLQTKEQIHL----QETRKKAVVLARLLELQEEPCPLCGSCihpNPARQDIDNPG 524
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
511-690 |
8.27e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 511 LYELNRRLEEKESEMKLFDGYDPAALKQHFGKKIAEVEDEKRSVQEERNRLLAEIENLASDGQA--QKLQDvhAQNLK-A 587
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDfrQKYED--ELNLRtS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 588 LEAQILDLKK----------KQESQVQLLK-----------------QKQKSD-------DAARR--LQDEIQSIKAQKV 631
Cdd:pfam00038 101 AENDLVGLRKdldeatlarvDLEAKIESLKeelaflkknheeevrelQAQVSDtqvnvemDAARKldLTSALAEIRAQYE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695302 632 QLQHRMKQEAEQFRQWK-------ASREKELLQLRKEgRKSEYeRHKLQALN------QRQKMVLQRKTEEA 690
Cdd:pfam00038 181 EIAAKNREEAEEWYQSKleelqqaAARNGDALRSAKE-EITEL-RRTIQSLEielqslKKQKASLERQLAET 250
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-738 |
9.43e-05 |
|
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: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 542 KKIAEVEDEKRSVQEERNRLLAEIENLASDGQAQKLQDVHAQNLKALEAQILDLKKKQEsqvqllkqkqksddAARRLQD 621
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAER--------------EIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 622 EIQSIKAQKVQLQhRMKQEAEQFRQWKASREKELLQLRKEGRKSEyerHKLQALNQRQKMVLQRKTEEAAMATKRLKELL 701
Cdd:COG4913 676 ELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLE---KELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
170 180 190
....*....|....*....|....*....|....*..
gi 30695302 702 EARKSsprehsagtngfGTNGQTNEKSLQRWLDHELE 738
Cdd:COG4913 752 EERFA------------AALGDAVERELRENLEERID 776
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
542-910 |
1.27e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 542 KKIAEVEDEKRSVQEERNRLLAEIENLASDGQAQKLQDVHAQNLKALEAQILDLKKKQESQVQLLKQKQKSDDAARRLQD 621
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 622 EIQSIKAQKVQLQHRMKQEAEQFRQWKASREKELLQLRKE-----GRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKR 696
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEleelqQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 697 LKELLEARKSSPREHSAGTnGFGTNGQTNEKSLQRWLDHELEVMVNVHEVRHEYEKQSHVRAALAEELAVLRQVDEFAVK 776
Cdd:COG4717 241 LEERLKEARLLLLIAAALL-ALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 777 GLSPPRGKNGFARASSLSP-----------NARMARISSLENMLVISS-----NSLVAMASQLSEAEERERAftnrGRWN 840
Cdd:COG4717 320 ELEELLAALGLPPDLSPEEllelldrieelQELLREAEELEEELQLEEleqeiAALLAEAGVEDEEELRAAL----EQAE 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 841 QLRSMGEAKNLLQYMFNSLAETRCQLWEKDVEiKEMKDQFKEIVGLLRQSELRRKEAEKELKLREQAIAT 910
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
387-767 |
1.46e-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: 45.88 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 387 KMRQQVEYLQAElslrtgGSSCAEVQALKERivwLETANEELCRELHEYRSRCPGVEHSEKDFKDIRADdivgsvrpdgL 466
Cdd:pfam15921 445 QMERQMAAIQGK------NESLEKVSSLTAQ---LESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS----------L 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 467 KRSLHSIESSNypmVEATTGDSReIDEEAKEWEHklLQNSMDkelyelnrRLEEKESEMKlfdgydpaALKQHFGKKIAE 546
Cdd:pfam15921 506 QEKERAIEATN---AEITKLRSR-VDLKLQELQH--LKNEGD--------HLRNVQTECE--------ALKLQMAEKDKV 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 547 VEDEKRSVqEERNRLLAEIENLASDGQAQKLQdvhaqnlkaLEAQILDlKKKQESQVQLLKQKQksDDAARRLQDEIQSI 626
Cdd:pfam15921 564 IEILRQQI-ENMTQLVGQHGRTAGAMQVEKAQ---------LEKEIND-RRLELQEFKILKDKK--DAKIRELEARVSDL 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 627 KAQKVQLQHRMKQEAEQFRQWKASREkellQLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLKELLEARKS 706
Cdd:pfam15921 631 ELEKVKLVNAGSERLRAVKDIKQERD----QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695302 707 SPRE------HSAGTNG------FGTNGQTNEK-----SLQRWLDHELEVMVNVHEVRHEYEKQshvRAALAEELAVL 767
Cdd:pfam15921 707 ELEQtrntlkSMEGSDGhamkvaMGMQKQITAKrgqidALQSKIQFLEEAMTNANKEKHFLKEE---KNKLSQELSTV 781
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
489-913 |
1.70e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 489 REIDEEAKEWEHKLLQNSMDKELYELNRRLEEKESEMKLFdgydpAALKQHFGKKIAEVEDEKRSVQEERNRLLAEIENL 568
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL-----EEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 569 ASD-GQAQKLQDVHAQNLKALEAQILDLKKKQESQVQLLKQKQ-KSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQF-- 644
Cdd:COG1196 462 LELlAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAle 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 645 -------------RQWKASREKELLQLRKEGRkseyerhklqalnqrqkmvlqrkteeaamATKRLKELLEARKSSPREH 711
Cdd:COG1196 542 aalaaalqnivveDDEVAAAAIEYLKAAKAGR-----------------------------ATFLPLDKIRARAALAAAL 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 712 SAGTNGFGTNGqtnEKSLQRWLDHELEVMVNVHEVRHEYEKQSHVRAALAEELAVLRQVDEFAVKGLSPPRGKNGFARAs 791
Cdd:COG1196 593 ARGAIGAAVDL---VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR- 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 792 slspnARMARISSLENMLVISSNSLVAMASQLSEAEERERAFTNRGRWNQLRSMGEAKNLLQYMFNSLAETRCQLWEKDV 871
Cdd:COG1196 669 -----ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 30695302 872 EIKEMKDQFKEIVgllrQSELRRKEAEKELKLREQAIAtSLG 913
Cdd:COG1196 744 EEELLEEEALEEL----PEPPDLEELERELERLEREIE-ALG 780
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
545-700 |
1.75e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.51 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 545 AEVEDEKRSVQEERNRLLAEIENLA-----SDGQAQKLQDVHAQNLKALEAQI-LDLKKKQESQVQLLKQ-------KQK 611
Cdd:pfam07111 477 ADLSLELEQLREERNRLDAELQLSAhliqqEVGRAREQGEAERQQLSEVAQQLeQELQRAQESLASVGQQlevarqgQQE 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 612 SDDAARRLQDEI---QSIKAQKVQ-----LQHRMKQEAE--QFRQWKASRE--KELLQLRKEGRKSEYERHKLQALNQRQ 679
Cdd:pfam07111 557 STEEAASLRQELtqqQEIYGQALQekvaeVETRLREQLSdtKRRLNEARREqaKAVVSLRQIQHRATQEKERNQELRRLQ 636
|
170 180
....*....|....*....|.
gi 30695302 680 KmvlQRKTEEAAMATKRLKEL 700
Cdd:pfam07111 637 D---EARKEEGQRLARRVQEL 654
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
487-710 |
2.08e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 487 DSREIDEEAKEWEHKllqnSMDKELYELNRRLEEKESEMKLFDGYDPAALKQHFGKKIAEVE---DEKRSVQEERNRLLA 563
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDK----NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQ 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 564 EIENLASD-GQAQKLQDVHAQN-LKALEaqildLKKKQEsqvqllKQKQKSDDAARRLQDEIQsiKAQKVQLQHRMKQEA 641
Cdd:PTZ00121 1638 LKKKEAEEkKKAEELKKAEEENkIKAAE-----EAKKAE------EDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKA 1704
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695302 642 EQFRQWKASREKELLQLRK--EGRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLKELLEARKSSPRE 710
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
516-691 |
2.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 516 RRLEEKESEMklfdgydpAALKQHF---GKKIAEVEDEKRSVQEERnRLLAEIENLASD-----GQAQKLQDVHAQ---- 583
Cdd:COG4913 610 AKLAALEAEL--------AELEEELaeaEERLEALEAELDALQERR-EALQRLAEYSWDeidvaSAEREIAELEAElerl 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 584 -----NLKALEAQILDLKKKQEsqvQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQWKASRekeLLQL 658
Cdd:COG4913 681 dassdDLAALEEQLEELEAELE---ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEER 754
|
170 180 190
....*....|....*....|....*....|...
gi 30695302 659 RKEGRKSEYERHKLQALNQRQKmVLQRKTEEAA 691
Cdd:COG4913 755 FAAALGDAVERELRENLEERID-ALRARLNRAE 786
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
532-704 |
3.03e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 532 DPAALKQHFGKKIAEVEDEKRSvQEERNRLLAEIENlasdgQAQKLQDVHAQNLKALEAQIL---DLKKKQESQVQL--L 606
Cdd:PRK09510 56 DPGAVVEQYNRQQQQQKSAKRA-EEQRKKKEQQQAE-----ELQQKQAAEQERLKQLEKERLaaqEQKKQAEEAAKQaaL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 607 KQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQ-EAEQFRQWKASREKellqlrkegrKSEYERHKLQALNQRQKMVLQR 685
Cdd:PRK09510 130 KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKaAAEAKKKAEAEAAK----------KAAAEAKKKAEAEAAAKAAAEA 199
|
170
....*....|....*....
gi 30695302 686 KTEEAAMATKRLKELLEAR 704
Cdd:PRK09510 200 KKKAEAEAKKKAAAEAKKK 218
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
487-707 |
3.28e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 487 DSREIDEEAKEWEHKLLQNSMDKElyELNRRLEEKESEMKLFDGYDpaALKQHFGKKIAEVE-DEKRSVQEERNRllAEI 565
Cdd:PTZ00121 1216 EARKAEDAKKAEAVKKAEEAKKDA--EEAKKAEEERNNEEIRKFEE--ARMAHFARRQAAIKaEEARKADELKKA--EEK 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 566 ENLASDGQAQKLQDVHAQNLKALEAQILD-LKKKQEsqvqllKQKQKSDDAARRLQDEIQSIKAQKVQlQHRMKQEAEqf 644
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADeAKKKAE------EAKKKADAAKKKAEEAKKAAEAAKAE-AEAAADEAE-- 1360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695302 645 rqwKASREKELLQLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLKELLEARKSS 707
Cdd:PTZ00121 1361 ---AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA 1420
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
493-764 |
4.75e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 493 EEAKEWEHKLLQNSMDKELYELNRRLEEKESEMKLFDGYDPAALKQHFGKKIAEVE---DEKRSVQEERN-RLLAEIENL 568
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKKaDEAKKAEEA 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 569 ASDGQAQKLQDVH-AQNLKALEaqilDLKKKQE-SQVQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQ 646
Cdd:PTZ00121 1534 KKADEAKKAEEKKkADELKKAE----ELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 647 WKASREKELLQLRKEGRKSEYERHKLQALNQRQKMVlQRKTEEAAMA--TKRLKELLEARKSSPREHSAGTngfGTNGQT 724
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE-KKKAEELKKAeeENKIKAAEEAKKAEEDKKKAEE---AKKAEE 1685
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 30695302 725 NEKSLQRWLDHELEVMVNVHEVR----------HEYEKQSHVRAALAEEL 764
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKkkeaeekkkaEELKKAEEENKIKAEEA 1735
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
532-620 |
6.95e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 532 DPAALKQHFGKKIAEVEDEKRSVQEERNRLLAEIENLASDGQAQ-KLQDVHAQNLKALEAQILDLKKKQESQVQLLKQKQ 610
Cdd:PRK11448 139 DPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALeGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKR 218
|
90
....*....|..
gi 30695302 611 K--SDDAARRLQ 620
Cdd:PRK11448 219 KeiTDQAAKRLE 230
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
542-705 |
6.97e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 542 KKIAEVEDEKRSVQEERNRLLAEIENLAsdgQAQKLQDVHAQNLKALEAQILDL-KKKQESQVQLLKQKQKSDDAARRLQ 620
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEE---KEEERKEERKRYRQELEEQIEEReQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 621 DEIQSIKAQKVQLQHRMKQEAEQF-RQWKASREKELLQLRKEGRK-SEYERHKLQALNQRQKMVLQRKtEEAAMATKRLK 698
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFnEEQAEWKELEKEEEREEDERiLEYLKEKAEREEEREAEREEIE-EEKEREIARLR 190
|
....*..
gi 30695302 699 ELLEARK 705
Cdd:pfam13868 191 AQQEKAQ 197
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
543-906 |
7.31e-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: 43.63 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 543 KIAEVEDEKRSVQEERNRLLAEIENLASD-GQAQKlqdvhaqNLKALEAQILDLKKKQESQVQllkQKQKSDDAARRLQD 621
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQkNNALK-------KIRELEAQISELQEDLESERA---ARNKAEKQRRDLGE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 622 EIQsikAQKVQLQHRMKQEAEQfRQWKASREKELLQLRKEGrKSEYERH--KLQALNQRQKMVLQRKTEEAAMAtKRLKE 699
Cdd:pfam01576 300 ELE---ALKTELEDTLDTTAAQ-QELRSKREQEVTELKKAL-EEETRSHeaQLQEMRQKHTQALEELTEQLEQA-KRNKA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 700 LLEARKSSPREHSAgtngfgtNGQTNEKSL-QRWLDHE-----LEVMVNVHEVRH-EYEKQshvRAALAEELAVLrQVDE 772
Cdd:pfam01576 374 NLEKAKQALESENA-------ELQAELRTLqQAKQDSEhkrkkLEGQLQELQARLsESERQ---RAELAEKLSKL-QSEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 773 FAVKGLspprgkngfarasslspnarmarISSLENMLVISSNSLVAMASQLSEAEERERAFTnRGRWN---QLRSMGEAK 849
Cdd:pfam01576 443 ESVSSL-----------------------LNEAEGKNIKLSKDVSSLESQLQDTQELLQEET-RQKLNlstRLRQLEDER 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695302 850 NLLQYMFNSLAETRC----QLWEKDVEIKEMKDQFKEIVGLLRQSELRRKEAEKELKLREQ 906
Cdd:pfam01576 499 NSLQEQLEEEEEAKRnverQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
547-699 |
9.38e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 547 VEDEKRSVQEERNRLLAEIENLASDGQAQKLQDVHAQNLKAlEAQILDlKKKQESQVQ-----------LLKQKQKsddA 615
Cdd:PRK10929 74 IDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQV-SSQLLE-KSRQAQQEQdrareisdslsQLPQQQT---E 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 616 ARRLQDEIQS------------IKAQKVQLQ-----HRMKQEAEQFRQWKASREKELLQLRKEGRKSEYER--HKLQALN 676
Cdd:PRK10929 149 ARRQLNEIERrlqtlgtpntplAQAQLTALQaesaaLKALVDELELAQLSANNRQELARLRSELAKKRSQQldAYLQALR 228
|
170 180
....*....|....*....|...
gi 30695302 677 QRQKMVLQRKTEEAAMATKRLKE 699
Cdd:PRK10929 229 NQLNSQRQREAERALESTELLAE 251
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
583-705 |
9.85e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 583 QNLKALEAQILDLKKKQEsqvQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQWKASREKELLQLRKEG 662
Cdd:TIGR02794 33 GGAEIIQAVLVDPGAVAQ---QANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQ 109
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 30695302 663 RKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLKEllEARK 705
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKE--EAAK 150
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
490-625 |
9.96e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 490 EIDEEAKEWEHKLLqnsmdkelyELNRRLEEKESEMK-LFDGYDPAALK---QHFGKKIAEVEDEKRSVQEERNRLLAEI 565
Cdd:COG4717 392 EQAEEYQELKEELE---------ELEEQLEELLGELEeLLEALDEEELEeelEELEEELEELEEELEELREELAELEAEL 462
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 566 ENLASDGQAQKLQDVHAQnlkaLEAQILDLKKKQESQVQLLkqkQKSDDAARRLQDEIQS 625
Cdd:COG4717 463 EQLEEDGELAELLQELEE----LKAELRELAEEWAALKLAL---ELLEEAREEYREERLP 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
487-700 |
1.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 487 DSREIDEEAKEWEHKL--LQNSMDkELYELNRRLEEKESEmklfdgydpaalkqhfgkkIAEVEDEKRSVQEERNRLLAE 564
Cdd:COG4913 662 DVASAEREIAELEAELerLDASSD-DLAALEEQLEELEAE-------------------LEELEEELDELKGEIGRLEKE 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 565 IENlASDGQAQKLQDVHAQNLKALEAQILDLkkkqESQVQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQF 644
Cdd:COG4913 722 LEQ-AEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF 796
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695302 645 -RQWKASR-------------EKELLQLRKEG---RKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLKEL 700
Cdd:COG4913 797 nREWPAETadldadleslpeyLALLDRLEEDGlpeYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
540-686 |
1.13e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 40.67 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 540 FGKKIAEVEDEKRSVQEERNRLLAEIENLASDGQAQKL-QDVHAQNLKALEAQiLDLKKKQESQVQLlKQKQKSDDAARR 618
Cdd:cd12923 6 LAKKLKEINKEYLDKSREYDELYEKYNKLSQEIQLKRQaLEAFEEAVKMFEEQ-LRTQEKFQKEAQP-HEKQRLMENNEL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695302 619 LQDEIQSIKAQKVQLQHRMKQEAEQFRQwkasREKELLQLRKEGrkseyerHKLQALNQRQKMVLQRK 686
Cdd:cd12923 84 LKSRLKELEESKEQLEEDLRKQVAYNRE----LEREMNSLKPEL-------MQLRKQKDQYLRWLKRK 140
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
389-706 |
1.43e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 389 RQQVEYLQAELS-LRTGGSSC-AEVQALKERIVWLETANEELCRELHEYRSRCpGVEHSEKDFKDIRADDIvgSVRPDGL 466
Cdd:PRK02224 250 REELETLEAEIEdLRETIAETeREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARREEL--EDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 467 KRSLH----SIESSNyPMVEATTGDSREIDEEAKEWEHKllQNSMDKELYELNRRLEEKESEMKLFDGyDPAALKQHFGK 542
Cdd:PRK02224 327 RDRLEecrvAAQAHN-EEAESLREDADDLEERAEELREE--AAELESELEEAREAVEDRREEIEELEE-EIEELRERFGD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 543 ---KIAEVEDEKRSVQEERNRLLAEIENLASDGQ--------AQKL----------QDV----HA-------QNLKALEA 590
Cdd:PRK02224 403 apvDLGNAEDFLEELREERDELREREAELEATLRtarerveeAEALleagkcpecgQPVegspHVetieedrERVEELEA 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 591 QILDLKKKQESqvqlLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFrqwkASREKELLQLRKEGRKSEYERH 670
Cdd:PRK02224 483 ELEDLEEEVEE----VEERLERAEDLVEAEDRIERLEERREDLEELIAERRETI----EEKRERAEELRERAAELEAEAE 554
|
330 340 350
....*....|....*....|....*....|....*.
gi 30695302 671 KLQALNQRQKMVLQRKTEEAAMATKRLKELLEARKS 706
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
493-705 |
1.48e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 493 EEAKEWEHKLLQNsmDKELYELNRRLEEKESEMKLFDgydpaalkqhfgKKIAEVEDEKRSVQEERNRLLAEIENLASdg 572
Cdd:TIGR04523 124 VELNKLEKQKKEN--KKNIDKFLTEIKKKEKELEKLN------------NKYNDLKKQKEELENELNLLEKEKLNIQK-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 573 qaqKLQDVHAQNLKaLEAQILDLKKKQESQVQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQWKASRE 652
Cdd:TIGR04523 188 ---NIDKIKNKLLK-LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30695302 653 KELLQLRKEGRKSEYERHKLQALN---QRQKMVLQR-KTEEAAMATKRLKELLEARK 705
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEkqlNQLKSEISDlNNQKEQDWNKELKSELKNQE 320
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
547-774 |
1.53e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.44 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 547 VEDEKRSVQEERNRLLAEIE-------------NLASDGQAQKLQDvHAQ-NLKALEAQILDLKKKQESQVQ--LLKQKQ 610
Cdd:pfam09731 245 VDQYKELVASERIVFQQELVsifpdiipvlkedNLLSNDDLNSLIA-HAHrEIDQLSKKLAELKKREEKHIEraLEKQKE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 611 KSDDAARRLQDEIQSIKAQKVQlQHRMKQEAEQFRQWKASREKELLQLRkegRKSEYERHKLQALNQRQKMVLQRKTE-- 688
Cdd:pfam09731 324 ELDKLAEELSARLEEVRAADEA-QLRLEFEREREEIRESYEEKLRTELE---RQAEAHEEHLKDVLVEQEIELQREFLqd 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 689 -EAAMATKR--LKELLEARKSSPREHSAGTNGFGTNGQTNEKSLQRWldhelevmVNVHEVRHEYEKQSHV--RAALAEE 763
Cdd:pfam09731 400 iKEKVEEERagRLLKLNELLANLKGLEKATSSHSEVEDENRKAQQLW--------LAVEALRSTLEDGSADsrPRPLVRE 471
|
250
....*....|....
gi 30695302 764 LAVLRQV---DEFA 774
Cdd:pfam09731 472 LKALKELasdDEVV 485
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
553-695 |
1.54e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 42.36 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 553 SVQEERNRLLAEIENLAsdgQAQKLQDVHAQNLKALEAQIldlkKKQESQVQLLKQKQKSDDAARRLQDEIQSIKAQKvq 632
Cdd:pfam04747 46 SINDQRKEAFASLELTE---QPQQVEKVKKSEKKKAQKQI----AKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQE-- 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695302 633 lqhrmkqeaEQFRQWKASREKellqLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEAAMATK 695
Cdd:pfam04747 117 ---------EEHKQWKAEQER----IQKEQEKKEADLKKLQAEKKKEKAVKAEKAEKAEKTKK 166
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
568-705 |
1.68e-03 |
|
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: 42.06 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 568 LASDGQAQKLQDVHAQnLKALEAQILDLKKKQEsqvQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQw 647
Cdd:COG4942 13 LAAAAQADAAAEAEAE-LEQLQQEIAELEKELA---ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695302 648 kASREKELLQLRKEGRKSEYERH--KLQALNQRQKMVL---QRKTEEAAMATKRLKELLEARK 705
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARR 149
|
|
| RRP36 |
pfam06102 |
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA. |
595-698 |
2.00e-03 |
|
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
Pssm-ID: 461829 [Multi-domain] Cd Length: 158 Bit Score: 39.85 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 595 LKKKQESQVQLLKQ---KQKSDDAARRLQDEIQSIKAQKVQLQHRMKQeaeqfRQWKASREKELLQLRKEGRKSEY---- 667
Cdd:pfam06102 54 LDEYRKKEIEELKKqlkKTKDPEEKEELKRTLQSMESRLKAKKRKDRE-----REVLKEHKKEEKEKVKQGKKPFYlkks 128
|
90 100 110
....*....|....*....|....*....|.
gi 30695302 668 ERHKLQALNQRQKMVLQRKTeEAAMATKRLK 698
Cdd:pfam06102 129 EKKKLLLKEKFEELKKSGKL-DKAIEKKRKK 158
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
479-724 |
2.18e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 479 PMVEATTGDSREIDEEAKEWEHKLlqNSMDKELYELNRRLEEKESEMKlfdgydpaALKQhfgkKIAEVEDEKRSVQEER 558
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAEL--DALQAELEELNEEYNELQAELE--------ALQA----EIDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 559 NRLLAEIENLASD------------------------GQAQKLQDVHAQNLKALEAQildlkkkQESQVQLLKQKQKSDD 614
Cdd:COG3883 82 EERREELGERARAlyrsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEEL-------KADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 615 AARRLQDEIQSIKAQKVQLQhrmKQEAEQfrqwkasrEKELLQLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEAAMAT 694
Cdd:COG3883 155 KLAELEALKAELEAAKAELE---AQQAEQ--------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250 260 270
....*....|....*....|....*....|
gi 30695302 695 KRLKELLEARKSSPREHSAGTNGFGTNGQT 724
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAAAASAAGAGAAG 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
488-699 |
2.25e-03 |
|
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: 42.02 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 488 SREIDEEAKewehklLQNSMDKELYELNRRLEEKES---EMKLFDGY---------DPAALKQHFGKKIAEVEDEKRSVQ 555
Cdd:pfam05483 390 SSELEEMTK------FKNNKEVELEELKKILAEDEKlldEKKQFEKIaeelkgkeqELIFLLQAREKEIHDLEIQLTAIK 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 556 EERNRLLAEIENLASDGQAQKLQDVHAQ---NLKALEAQ---------ILDLKKKQE-------SQVQLLKQKQKSDDAA 616
Cdd:pfam05483 464 TSEEHYLKEVEDLKTELEKEKLKNIELTahcDKLLLENKeltqeasdmTLELKKHQEdiinckkQEERMLKQIENLEEKE 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 617 RRLQDEIQSIKAQKVQLQHRMKQEAEQFRQWKASREKELLQLRKEGRKSEYERHKL-QALNQRQKMVLQRKTEEAAMATK 695
Cdd:pfam05483 544 MNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLkKQIENKNKNIEELHQENKALKKK 623
|
....
gi 30695302 696 RLKE 699
Cdd:pfam05483 624 GSAE 627
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
486-666 |
3.10e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 486 GDSREIDEEAK----EWEHKLlqNSMDKELYELNRRLEEKESEMklfdgydpAALKQHFGKKIAEVEDEKRSVQEERNRL 561
Cdd:PRK00409 498 GLPENIIEEAKkligEDKEKL--NELIASLEELERELEQKAEEA--------EALLKEAEKLKEELEEKKEKLQEEEDKL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 562 LAEienlasdgQAQKLQdvhaqnlKALEAqildLKKKQESQVQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEA 641
Cdd:PRK00409 568 LEE--------AEKEAQ-------QAIKE----AKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKK 628
|
170 180
....*....|....*....|....*
gi 30695302 642 EQFRQWKASREKELLQLRKEGRKSE 666
Cdd:PRK00409 629 KQKEKQEELKVGDEVKYLSLGQKGE 653
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
531-693 |
3.55e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 531 YDPAALKQHFGKKIAEVEDEKRSVQEERNRLLAEIENLAsdgqaqklqdvhaQNLKALEAQILDLKKKQESQvqllKQKQ 610
Cdd:TIGR02794 43 VDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAE-------------KQRAAEQARQKELEQRAAAE----KAAK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 611 KSDDAARrlqdeiQSIKAQKVQLQHRMKQEAEQFRQWKASREKELLQLRKegRKSEYERH-KLQALNQRQKMVLQRKTEE 689
Cdd:TIGR02794 106 QAEQAAK------QAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAA--KQAEEEAKaKAAAEAKKKAEEAKKKAEA 177
|
....
gi 30695302 690 AAMA 693
Cdd:TIGR02794 178 EAKA 181
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
585-689 |
3.92e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 585 LKALEAQILDLKKKQESQVQllKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQWKASREKEllqLRKEGRK 664
Cdd:COG0542 413 LDELERRLEQLEIEKEALKK--EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL---EQRYGKI 487
|
90 100
....*....|....*....|....*
gi 30695302 665 SEYERhKLQALNQRQKMVLQRKTEE 689
Cdd:COG0542 488 PELEK-ELAELEEELAELAPLLREE 511
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
550-699 |
4.36e-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: 40.88 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 550 EKRSVQEERNRLLAEIENLASDGQAQKLQDVHAQNLKALEAQILDLKKKQESQVQLLKQKQKSDDAARRLQDEI------ 623
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIameisr 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 624 ----QSIKAQKVQLQHRMKQEAEQFRQWKASREKELLQLRKEGRKSEYERHKLQALNQRQkmvLQRKTEEAAMATKRLKE 699
Cdd:pfam17380 377 mrelERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE---VRRLEEERAREMERVRL 453
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
509-701 |
5.37e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 39.27 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 509 KELYELNRRLEEKESEM----KLFDGYDPAALKQhfgkkIAEVEDEKRSVQEERNRLLAEIENLASDgqaqklqdvhaqn 584
Cdd:pfam05010 22 LEINELKAKYEELRRENlemrKIVAEFEKTIAQM-----IEEKQKQKELEHAEIQKVLEEKDQALAD------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 585 LKALEAQILDLKKKQESQVQLLKQKQKSDdaarrlqdeiQSIKAQKVQLQHRMKQEAEQFRQWKASREKELLQLRKE--- 661
Cdd:pfam05010 84 LNSVEKSFSDLFKRYEKQKEVISGYKKNE----------ESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEiaq 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 30695302 662 -GRKSEYERHKLQALNQRQKM-------VLQRKTEEAAMATKRLKELL 701
Cdd:pfam05010 154 vRSKAKAETAALQASLRKEQMkvqslerQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
542-913 |
6.32e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 542 KKIAEVEDEKRSVQE--ER-NRLLAEIENlasdgQAQKLQdvhAQNLKALEAQILDLKKKQESQVQLLKQKQKSDDAARR 618
Cdd:COG1196 172 ERKEEAERKLEATEEnlERlEDILGELER-----QLEPLE---RQAEKAERYRELKEELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 619 LQDEIQSIKAqkvqlqhrmkqEAEQFRQWKASREKELLQLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLK 698
Cdd:COG1196 244 LEAELEELEA-----------ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 699 ELLEARkssprehsagtngfgtngQTNEKSLQRWLDHELEVMVNVHEVRHEYEKQSHVRAALAEELAVLRQvdefavkgl 778
Cdd:COG1196 313 ELEERL------------------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE--------- 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 779 spprgkngfARASSLSpnARMARISSLENMLVISSNSLVAMASQLSEAEERERAFTNRGRwNQLRSMGEAKNLLQymfnS 858
Cdd:COG1196 366 ---------ALLEAEA--ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEE----A 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 30695302 859 LAETRCQLWEKDVEIKEMKDQFKEIVGLLRQSELRRKEAEKELKLREQAIATSLG 913
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
489-637 |
6.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 489 REIDEEAKEWEHKLLQNsmDKELYELNRRLEEKESEMKLFDGYDPAALKQhfgkKIAEVEDEKRSVQEERNRLLAEIENL 568
Cdd:COG4913 298 EELRAELARLEAELERL--EARLDALREELDELEAQIRGNGGDRLEQLER----EIERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695302 569 -----ASDGQAQKLQDVHAQNLKALEAQildLKKKQESQVQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRM 637
Cdd:COG4913 372 glplpASAEEFAALRAEAAALLEALEEE---LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
536-680 |
7.45e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 38.98 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 536 LKQHFGKKIAEVEDEKRSVQEERNRLLAEIENLASdgQAQKLQDVHAQNLKALEaQILDLKKKQESQVQLLKQKQKSddA 615
Cdd:pfam14988 23 LWNQYVQECEEIERRRQELASRYTQQTAELQTQLL--QKEKEQASLKKELQALR-PFAKLKESQEREIQDLEEEKEK--V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 616 ARRLQDEIQSIKAQKVQLQHRMKQEAEQFR-----------------QWKAS-------------RE-----KELLQLRK 660
Cdd:pfam14988 98 RAETAEKDREAHLQFLKEKALLEKQLQELRilelgeratrelkrkaqALKLAakqalsefcrsikREnrqlqKELLQLIQ 177
|
170 180
....*....|....*....|
gi 30695302 661 EGRKSEYERHKLQALNQRQK 680
Cdd:pfam14988 178 ETQALEAIKSKLENRKQRLK 197
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
496-684 |
9.50e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 496 KEWEHKLLQNSMDKELYELNRRLEEKESEMKLFDGYDPAALKQhfgkkIAEVEDEKRSVQEERNRLLAEIENlASDGQAQ 575
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ-----CQTLLRELETHIEEYDREFNEIEN-ASSSLGS 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695302 576 KLQ---DVHAQNLK--------ALEAQILDLKKKQESQVQLLKQKQKSDDAARRLQDEIQSIKAQKVQL----------- 633
Cdd:TIGR00618 733 DLAareDALNQSLKelmhqartVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLktleaeigqei 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695302 634 ----------QHRMKQEAEQFRQWKASREKELLQLRKEGRKSEYERHKLQALNQRQKMVLQ 684
Cdd:TIGR00618 813 psdedilnlqCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| |
