|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
4-342 |
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: 601.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 4 IPVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 84 GQTGSGKTYTIGGGHIASVVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELET-SMKDLHIRED 161
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDtFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEDGSWYSPRHIVSKFH 241
Cdd:cd01372 161 SKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNSTFTSKFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01372 241 FVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 320
|
330 340
....*....|....*....|.
gi 429535822 322 SSNFDESLNSLKYANRARNIR 342
Cdd:cd01372 321 DSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
5-348 |
3.91e-146 |
|
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: 446.25 E-value: 3.91e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 78 ATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEH-PSIDFNVKVSYIEVYKEDLRDLLEleTSMKDL 156
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLN--PSSKKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEaaedgswySPRHI 236
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSS--------SGSGK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRrKSSHIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIA 303
|
330 340 350
....*....|....*....|....*....|..
gi 429535822 317 CVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:smart00129 304 NVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-341 |
3.28e-139 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 427.76 E-value: 3.28e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 11 RIRPLLCKEALHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 84 GQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELETSMKD-LHIRED 161
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKErSEFSVKVSYLEIYNEKIRDLLSPSNKNKRkLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEdgswyspRHIVSKFH 241
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEE-------SVKTGKLN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 242 FVDLAGSERVTKTGN-TGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSP 320
Cdd:pfam00225 228 LVDLAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALADK--KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISP 305
|
330 340
....*....|....*....|.
gi 429535822 321 SSSNFDESLNSLKYANRARNI 341
Cdd:pfam00225 306 SSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
5-339 |
4.48e-130 |
|
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: 403.56 E-value: 4.48e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 5 PVKVAVRIRPLLCKEAlhNHQVCVRVIPNSQQVIIG-------RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd00106 1 NVRVAVRVRPLNGREA--RSAKSVISVDGGKSVVLDppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 78 ATVFAYGQTGSGKTYTIGGGHiasvvEGQKGIIPRAIQEIFQSISEHPSIDFN--VKVSYIEVYKEDLRDLLELETSmKD 155
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKSSfsVSASYLEIYNEKIYDLLSPVPK-KP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 156 LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNMEAAEDgswyspRH 235
Cdd:cd00106 153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGE------SV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 236 IVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKssHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd00106 225 TSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMI 302
|
330 340
....*....|....*....|....
gi 429535822 316 TCVSPSSSNFDESLNSLKYANRAR 339
Cdd:cd00106 303 ACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
6-341 |
3.47e-112 |
|
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: 356.27 E-value: 3.47e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 6 VKVAVRIRPLLCKEALHNHQVCVRVI----------------------PNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNT 63
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdpkdeedgffhggsnNRDRRKRRNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 64 CIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISE-HPSIDFNVKVSYIEVYKED 142
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT------PQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 143 LRDLLEleTSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNM 222
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 223 EAAEDgswysprHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLL 302
Cdd:cd01370 234 SINQQ-------VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 429535822 303 KDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNI 341
Cdd:cd01370 307 KDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
6-341 |
4.92e-111 |
|
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: 352.02 E-value: 4.92e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSqqvIIGRDRV---FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQVAWEIDNDT---IYLVEPPstsFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 83 YGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLleLETSMKDLHIREDE 162
Cdd:cd01374 79 YGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDL--LSPTSQNLKIRDDV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 163 KGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcQVHKNMEAAEDGSwysprhIVSKFHF 242
Cdd:cd01374 151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI-ESSERGELEEGTV------RVSTLNL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01374 224 IDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAE 302
|
330
....*....|....*....
gi 429535822 323 SNFDESLNSLKYANRARNI 341
Cdd:cd01374 303 SHVEETLNTLKFASRAKKI 321
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
6-341 |
2.15e-109 |
|
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: 348.30 E-value: 2.15e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII--GRD------RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 78 ATVFAYGQTGSGKTYTIGGghiASVVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELETSmKDL 156
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEG---KREDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKDQT-KRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhKNMEAAEDGSwyspRHI 236
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI----ECSEKGEDGE----NHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 237 -VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01371 231 rVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
|
330 340
....*....|....*....|....*.
gi 429535822 316 TCVSPSSSNFDESLNSLKYANRARNI 341
Cdd:cd01371 309 ANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
11-343 |
8.32e-108 |
|
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: 343.42 E-value: 8.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 11 RIRPLLCKEALHNHQVCVRVIPNSQQVII----GRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQT 86
Cdd:cd01366 9 RVRPLLPSEENEDTSHITFPDEDGQTIELtsigAKQKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIFAYGQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 87 GSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISE--HPSIDFNVKVSYIEVYKEDLRDLL-ELETSMKDLHIRED-E 162
Cdd:cd01366 88 GSGKTYTMEG------PPESPGIIPRALQELFNTIKElkEKGWSYTIKASMLEIYNETIRDLLaPGNAPQKKLEIRHDsE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 163 KGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhkNMEAAEDGSwysprHIVSKFHF 242
Cdd:cd01366 162 KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-----SGRNLQTGE-----ISVGKLNL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALgdpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01366 232 VDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAE 308
|
330 340
....*....|....*....|.
gi 429535822 323 SNFDESLNSLKYANRARNIRN 343
Cdd:cd01366 309 SNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
6-341 |
5.08e-102 |
|
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: 327.75 E-value: 5.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 6 VKVAVRIRPLLCKEALHNHQVCVRvIPNSQQVIIGRD---RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVK-FDPEDTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 83 YGQTGSGKTYTIGGGHIAsvvEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLleLETSMKDLHIRED 161
Cdd:cd01369 83 YGQTSSGKTYTMEGKLGD---PESMGIIPRIVQDIFETIYSMDEnLEFHVKVSYFEIYMEKIRDL--LDVSKTNLSVHED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNMeaaEDGSWYSprhivSKFH 241
Cdd:cd01369 158 KNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ--ENV---ETEKKKS-----GKLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01369 228 LVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPS 305
|
330 340
....*....|....*....|
gi 429535822 322 SSNFDESLNSLKYANRARNI 341
Cdd:cd01369 306 SYNESETLSTLRFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
6-348 |
9.53e-102 |
|
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: 328.13 E-value: 9.53e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII--------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 78 ATVFAYGQTGSGKTYTIGGGHiaSVVEGQK-------GIIPRAIQEIFQSISEHpSIDFNVKVSYIEVYKEDLRDLLELE 150
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMEGDR--SPNEEYTweldplaGIIPRTLHQLFEKLEDN-GTEYSVKVSYLEIYNEELFDLLSPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 151 TS-MKDLHIRED--EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEd 227
Cdd:cd01364 161 SDvSERLRMFDDprNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 228 gswyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprrKSSHIPYRDAKITRLLKDSLG 307
Cdd:cd01364 240 ------LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLG 310
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 429535822 308 GSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01364 311 GRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
6-348 |
1.10e-101 |
|
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: 328.16 E-value: 1.10e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 6 VKVAVRIRPLLCKE---------ALHNHQVCVRVIPNSQQVIIGRDRV---FTFDFVF------GKN-STQDEVYNTCIK 66
Cdd:cd01365 3 VKVAVRVRPFNSREkernskcivQMSGKETTLKNPKQADKNNKATREVpksFSFDYSYwshdseDPNyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 67 PLVLSLIEGYNATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSI--SEHPSIDFNVKVSYIEVYKEDLR 144
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMG------TQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 145 DLLELETSMKD--LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNM 222
Cdd:cd01365 157 DLLNPKPKKNKgnLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQ--KRH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 223 EAAEDGSwyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR-----KSSHIPYRDAK 297
Cdd:cd01365 235 DAETNLT----TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 429535822 298 ITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01365 311 LTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
45-379 |
1.51e-84 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 287.79 E-value: 1.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 45 FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEH 124
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGT------EEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 125 PSI-DFNVKVSYIEVYKEDLRDLLELETsmKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEH 203
Cdd:COG5059 132 SMTkDFAVSISYLEIYNEKIYDLLSPNE--ESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 204 SSRSHAIFTISICQVHKNMeaaedgswysPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD 283
Cdd:COG5059 210 SSRSHSIFQIELASKNKVS----------GTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 284 PRrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDR-IDEMEFE 362
Cdd:COG5059 280 KK-KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReIEEIKFD 358
|
330
....*....|....*..
gi 429535822 363 IKLLREALQSQQAGVSQ 379
Cdd:COG5059 359 LSEDRSEIEILVFREQS 375
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
5-348 |
1.98e-84 |
|
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: 279.78 E-value: 1.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIG-RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 84 GQTGSGKTYTIGG--GHIASVVEGQKGIIPRAIQEIFQSISEH-----PSIDFNVKVSYIEVYKEDLRDLleLETSMKDL 156
Cdd:cd01373 82 GQTGSGKTYTMWGpsESDNESPHGLRGVIPRIFEYLFSLIQREkekagEGKSFLCKCSFLEIYNEQIYDL--LDPASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmEAAEDGSWYSpRHI 236
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI-------ESWEKKACFV-NIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD-PRRKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01373 232 TSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAII 311
|
330 340 350
....*....|....*....|....*....|...
gi 429535822 316 TCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01373 312 ANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
5-337 |
1.19e-83 |
|
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: 276.87 E-value: 1.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVI-IGRDRV----------FTFDFVFGKNSTQDEVYNTCIKPLVLSLI 73
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVhEPKLKVdltkyienhtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 74 EGYNATVFAYGQTGSGKTYTIGGGHiaSVVEGQKGIIPRAIQEIFQSISEHPSID-FNVKVSYIEVYKEDLRDLLEletS 152
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKLPYKDnLGVTVSFFEIYGGKVFDLLN---R 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 153 MKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmEAAEDGSwys 232
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------RDRGTNK--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 233 prhIVSKFHFVDLAGSER-VTKTGNTGERFKESIQINSGLLALGNVISALGDPrrkSSHIPYRDAKITRLLKDSL-GGSA 310
Cdd:cd01367 226 ---LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQN---KAHIPFRGSKLTQVLKDSFiGENS 299
|
330 340
....*....|....*....|....*..
gi 429535822 311 KTVMITCVSPSSSNFDESLNSLKYANR 337
Cdd:cd01367 300 KTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
5-335 |
1.45e-83 |
|
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: 277.35 E-value: 1.45e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 5 PVKVAVRIRPLLCKEALHNHQVCVRVIpNSQQV----------------IIGRDRVFTFDFVFGKNSTQDEVYNTCIKPL 68
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVI-NSTTVvlhppkgsaanksernGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 69 VLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISehpsiDFNVKVSYIEVYKEDLRDLLE 148
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGS------PGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 149 LETS-----MKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNME 223
Cdd:cd01368 150 PSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 224 AAEDGSWYSPRhiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRRKSSHIPYRDAKITRL 301
Cdd:cd01368 230 GDVDQDKDQIT--VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLreNQLQGTNKMVPFRDSKLTHL 307
|
330 340 350
....*....|....*....|....*....|....
gi 429535822 302 LKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYA 335
Cdd:cd01368 308 FQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
5-339 |
4.16e-80 |
|
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: 266.68 E-value: 4.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 5 PVKVAVRIRPLLCKEALHNHQVCVRVIpNSQQVIIGRDRV------FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNA 78
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELADPRNhgetlkYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 79 TVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQsISEHPSIDFNVKVSYIEVYKEDLRDLLELETsmKDLHI 158
Cdd:cd01376 80 TVFAYGSTGAGKTFTMLG------SPEQPGLMPLTVMDLLQ-MTRKEAWALSFTMSYLEIYQEKILDLLEPAS--KELVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 159 REDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmeaAEDGSWYSPRHIVS 238
Cdd:cd01376 151 REDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV---------DQRERLAPFRQRTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 239 KFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRrksshIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALnkNLPR-----IPYRDSKLTRLLQDSLGGGSRCIMVA 296
|
330 340
....*....|....*....|...
gi 429535822 317 CVSPSSSNFDESLNSLKYANRAR 339
Cdd:cd01376 297 NIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
33-339 |
1.69e-73 |
|
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: 248.26 E-value: 1.69e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 33 NSQQviigRDRVFTFDFVFgKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHIASvveGQKGIIPR 112
Cdd:cd01375 42 NNQQ----EDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 113 AIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLL----ELETSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEM 188
Cdd:cd01375 114 ALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 189 GNAARHTGTTQMNEHSSRSHAIFTIsicqvHKNMEAAEDGswySPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQIN 268
Cdd:cd01375 194 GETNRIIASHTMNKNSSRSHCIFTI-----HLEAHSRTLS---SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYIN 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429535822 269 SGLLALGNVISALGDPRRksSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRAR 339
Cdd:cd01375 266 KSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
6-397 |
5.47e-62 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 232.90 E-value: 5.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 6 VKVAVRIRPLLCKEalhNHQVCVRVIPNSQQVIIGRdrVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQ 85
Cdd:PLN03188 100 VKVIVRMKPLNKGE---EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 86 TGSGKTYTIGGGHIASVVEG----QKGIIPRAIQEIFQSISEHP------SIDFNVKVSYIEVYKEDLRDLLEleTSMKD 155
Cdd:PLN03188 175 TGSGKTYTMWGPANGLLEEHlsgdQQGLTPRVFERLFARINEEQikhadrQLKYQCRCSFLEIYNEQITDLLD--PSQKN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 156 LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTisiCQVHKNMEAAEDG-SWYSpr 234
Cdd:PLN03188 253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT---CVVESRCKSVADGlSSFK-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 235 hiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR--KSSHIPYRDAKITRLLKDSLGGSAKT 312
Cdd:PLN03188 328 --TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 313 VMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDrIDEMEFEIKLLREALQSQQAGVSQTTQINREGSPDTN 392
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD-VNFLREVIRQLRDELQRVKANGNNPTNPNVAYSTAWN 484
|
....*
gi 429535822 393 RIHSL 397
Cdd:PLN03188 485 ARRSL 489
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
26-280 |
1.19e-23 |
|
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: 98.96 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 26 VCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCiKPLVLSLIEGYN-ATVFAYGQTGSGKTYTIggghiasvve 104
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 105 gqKGIIPRAIQEIFqsisehpsidfnvkvSYIEVYKEDLRDLLEletsmkdlhiredekgntvivgakECHVESAGEVMS 184
Cdd:cd01363 70 --KGVIPYLASVAF---------------NGINKGETEGWVYLT------------------------EITVTLEDQILQ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 185 LLEMGNAARhTGTTQMNEHSSRSHAIFTIsicqvhknmeaaedgswysprhivskfhFVDLAGSERvtktgntgerfkes 264
Cdd:cd01363 109 ANPILEAFG-NAKTTRNENSSRFGKFIEI----------------------------LLDIAGFEI-------------- 145
|
250
....*....|....*.
gi 429535822 265 iqINSGLLALGNVISA 280
Cdd:cd01363 146 --INESLNTLMNVLRA 159
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
6-147 |
3.25e-19 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 85.35 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 6 VKVAVRIRPLLCKEAlhnhQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQ 85
Cdd:pfam16796 22 IRVFARVRPELLSEA----QIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGYNVCIFAYGQ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429535822 86 TGSGKTytiggghiasvvegqKGIIPRAIQEIFQSISE-HPSIDFNVKVSYIEVYKEDLRDLL 147
Cdd:pfam16796 97 TGSGSN---------------DGMIPRAREQIFRFISSlKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
647-1220 |
4.43e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 647 DDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSD---LENEDLKIDCLQESQEL----NLQKLKNSERIL 719
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkKAEEKKKADEAKKAEEKkkadEAKKKAEEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 720 TEAKQKMRELtiniKMKEDLIKEliktgndaKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKL 799
Cdd:PTZ00121 1318 DEAKKKAEEA----KKKADAAKK--------KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 800 QKEFRKKMDAAKLRVQEIQLKTgqEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEEL 879
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKA--DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAK 1463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 880 EADLKKREAIVSKKEALLQEKSHlENKKLRSSQALNTDSLKISTRLNLLEQEL---SEKNVQLQTSTAEEKTKISEQVEV 956
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAkkaEEAKKADEAKKAEEAKKADEAKKA 1542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 957 LQKEK-DQLQK----RRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIE-----YRNESIQNRQKSLRASFHNLS- 1025
Cdd:PTZ00121 1543 EEKKKaDELKKaeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEevmklYEEEKKMKAEEAKKAEEAKIKa 1622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1026 ---RGEANVLEKLACLSPVEIRTIlfryfNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQCDRrltL 1102
Cdd:PTZ00121 1623 eelKKAEEEKKKVEQLKKKEAEEK-----KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA---L 1694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1103 QQKEHEQKMQLLLHHFKEQDGEGIMETFKTYEDKIQQLEKdlyfYKKTSRDHKKKLKEL-VGEAIRRQLA-PSEYQEAGD 1180
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE----AKKEAEEDKKKAEEAkKDEEEKKKIAhLKKEEEKKA 1770
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 429535822 1181 GVLKPEGGGMLSEELKWASRPESMKLSGREREMDSSASSL 1220
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
763-1072 |
1.52e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 763 KLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDLDACNLKRR 842
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 843 KGSFGSIDHLQKLDEQKKWLDEEVEKVlnqRQELEELEADLKK-REAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKi 921
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEEL---EAQIEQLKEELKAlREALDELRAELTLLNEEAANLRERLESLERRIAAT- 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 922 STRLNLLEQELSEKNVQLQTSTAE------EKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEG 995
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEieeleeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429535822 996 IEALEAAIeyrnESIQNRQKSLRAsfhnlsrGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMK 1072
Cdd:TIGR02168 917 LEELREKL----AQLELRLEGLEV-------RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
721-1035 |
4.75e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 721 EAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslKVTKLEHDAEQAKvELIETQKQLQELEnKDLSdvamkVKLQ 800
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELER--------------QLKSLERQAEKAE-RYKELKAELRELE-LALL-----VLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 801 KEFRKKMDAAK--LRVQEIQLKTGQEEgLKPKAEDLDACNLKRRKGSfGSIDHLQK------------------------ 854
Cdd:TIGR02168 235 EELREELEELQeeLKEAEEELEELTAE-LQELEEKLEELRLEVSELE-EEIEELQKelyalaneisrleqqkqilrerla 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 855 -LDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKL----RSSQALNTDSLKISTRLNLLE 929
Cdd:TIGR02168 313 nLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeeleSRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 930 QELSEKNVQLQtSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVlsPEEEHVLFQLEEGIEALEAA---IEYR 1006
Cdd:TIGR02168 393 LQIASLNNEIE-RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEELQEELERLEEAleeLREE 469
|
330 340
....*....|....*....|....*....
gi 429535822 1007 NESIQNRQKSLRASFHNLsRGEANVLEKL 1035
Cdd:TIGR02168 470 LEEAEQALDAAERELAQL-QARLDSLERL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
756-1026 |
7.56e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 756 QYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEF--------RKKMDAAKLRVQEIQLKTGQEEgl 827
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisRLEQQKQILRERLANLERQLEE-- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 828 kpKAEDLDacNLKRRKgsfgsIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKK 907
Cdd:TIGR02168 321 --LEAQLE--ELESKL-----DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 908 LRSSQALNTDSLKISTRLNLLEQEL----SEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSP 983
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 429535822 984 EEEHVLFQLEEGIEALEA---AIEYRNESIQNRQKSLRASFHNLSR 1026
Cdd:TIGR02168 472 EAEQALDAAERELAQLQArldSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
677-914 |
1.91e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 677 VELSDTQDETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQ 756
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 757 YSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDLDA 836
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429535822 837 CNLKRRKgsfGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQAL 914
Cdd:COG1196 422 ELEELEE---ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
869-1144 |
2.00e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 869 VLNQRQELEELEADLKKREAIVSKKEALLQEKSHlenkklrSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKt 948
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRK-------ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 949 KISEQVEVLQKEKDQLQKRRHNVDEKLKngrvlspEEEHVLFQLEEGIEALEAAIEYRNESIQN---RQKSLRASFHNLS 1025
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLE-------EAEEELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1026 RGEANVLEKLACLSPvEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDhlklqcdrrltlQQK 1105
Cdd:TIGR02168 817 EEAANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN------------ERA 883
|
250 260 270
....*....|....*....|....*....|....*....
gi 429535822 1106 EHEQKMQLLLHHFKEQdgegiMETFKTYEDKIQQLEKDL 1144
Cdd:TIGR02168 884 SLEEALALLRSELEEL-----SEELRELESKRSELRREL 917
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-1168 |
2.34e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 685 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK------QYS 758
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKlsefyeEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 759 LKVTKLEHDAEQAKVELIETQKQLQELENKDlSDVAMKVKLQKEFRKKMDAAKLRV---QEIQLKTGQEEGLKPKAEDLD 835
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKE-ERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 836 ACNLKRRkgsfgsidhLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKreAIVSKKEAL-----------------LQ 898
Cdd:PRK03918 386 PEKLEKE---------LEELEKAKEEIEEEISKITARIGELKKEIKELKK--AIEELKKAKgkcpvcgrelteehrkeLL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 899 EKSHLENKKLRSSQALNTDSL-KISTRLNLLEQELS-EKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHnvdEKLK 976
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKErKLRKELRELEKVLKkESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY---EKLK 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 977 ngrvlspEEehvLFQLEEGIEALEAAIEyRNESIQNRQKSLRASFHNLSRGEANVLEKL-----ACLSPVEIR-TILFRY 1050
Cdd:PRK03918 532 -------EK---LIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERlKELEPF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1051 FNKVVNLREAERKQQLYNEEMKM----------KVLERDNMVRELESALDHLKLQCDrrltlqQKEHEQKMQLLLHhfKE 1120
Cdd:PRK03918 601 YNEYLELKDAEKELEREEKELKKleeeldkafeELAETEKRLEELRKELEELEKKYS------EEEYEELREEYLE--LS 672
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 429535822 1121 QDGEGIMETFKTYEDKIQQLEKDLYFYK--KTSRDHKKKLKELVGEAIRR 1168
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKeeLEEREKAKKELEKLEKALER 722
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
696-1002 |
4.54e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 696 LKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVEL 775
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 776 IETQKQLQELENKDLSDVAMKVKLQK---EFRKKMDAAKLRVQEIQLKTGQ--------EEGLKPKAEDLDACNLKRRKG 844
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEeleELEEELEEAEEELEEAEAELAEaeealleaEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 845 SFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTR 924
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429535822 925 LNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDqlQKRRHNVDEKLKNGRVLSpEEEHVLFQLEEGIEALEAA 1002
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG--VKAALLLAGLRGLAGAVA-VLIGVEAAYEAALEAALAA 546
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
864-1178 |
5.89e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 864 EEVEKVLNQRQELEELEADLkkreaivskkEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQelseknvqlqtsT 943
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKREL----------SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ------------L 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 944 AEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAaiEYRNESIQNRQKSLRASFHN 1023
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEE 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1024 LSRGEANVLEKLACLSPVEIRTILFRyfNKVVNL---------REAERKQQLYN-----EEMKMKVLERDNMVRELESAL 1089
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLE--KEIQELqeqridlkeQIKSIEKEIENlngkkEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1090 DHLKLQCDRRLT----LQQKEHEQKMQL--LLHHFKEQDG--EGIMETFKTYEDKIQQLEKdlYFYKKTSRDHKKKLKEL 1161
Cdd:TIGR02169 885 GDLKKERDELEAqlreLERKIEELEAQIekKRKRLSELKAklEALEEELSEIEDPKGEDEE--IPEEELSLEDVQAELQR 962
|
330 340
....*....|....*....|..
gi 429535822 1162 VGEAIRR-----QLAPSEYQEA 1178
Cdd:TIGR02169 963 VEEEIRAlepvnMLAIQEYEEV 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
852-1161 |
6.01e-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: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 852 LQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQE 931
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 932 LSEKNVQLQTSTA---EEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNE 1008
Cdd:TIGR02168 780 AEAEIEELEAQIEqlkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1009 SIQNRQKSLRAsfhnlSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMkmkvlerdnmvRELESA 1088
Cdd:TIGR02168 860 EIEELEELIEE-----LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL-----------EELREK 923
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429535822 1089 LDHLKLQCDRrltLQQKEHEQKMQLLLHHfkEQDGEGIMETFKTYEDKIQQLEKDLyfykktsRDHKKKLKEL 1161
Cdd:TIGR02168 924 LAQLELRLEG---LEVRIDNLQERLSEEY--SLTLEEAEALENKIEDDEEEARRRL-------KRLENKIKEL 984
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-984 |
6.58e-08 |
|
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: 57.34 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 685 ETQKSDLENE-----------DLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSV 753
Cdd:TIGR04523 390 ESQINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 754 SKQYSLKVTKLEHDAEQAKVELIETQKQLQEL--ENKDLSD-VAMKVKLQKEFRKKMDAAKLRVQEIQLKTGQEEglkpk 830
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLneEKKELEEkVKDLTKKISSLKEKIEKLESEKKEKESKISDLE----- 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 831 aedldacnlkrrkgsfgsiDHLQKLDEQKKWLDEEVEkVLNQRQELEELEADLKKREAIVSKKEALLQEKSHlENKKLRS 910
Cdd:TIGR04523 545 -------------------DELNKDDFELKKENLEKE-IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK-EKKDLIK 603
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429535822 911 SQALNTdsLKISTrlnlLEQELSEKNvqlqtstaEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPE 984
Cdd:TIGR04523 604 EIEEKE--KKISS----LEKELEKAK--------KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
755-1019 |
9.25e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 755 KQYSLKVTKLEHDAEQAKVELIETQKQLQELENKdlsdvamkvklQKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDL 834
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 835 DACNLKRRKGSFGSIDHLQK-LDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQA 913
Cdd:COG1196 304 IARLEERRRELEERLEELEEeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 914 LNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLE 993
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260
....*....|....*....|....*.
gi 429535822 994 EGIEALEAAIEYRNESIQNRQKSLRA 1019
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEA 489
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
705-1164 |
1.03e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 705 QELNLQKL----KNSERILTEAKQKMRELTINIKMKEDlIKELIKTgndaksvskqyslkvtklehdaeqAKVELIETQK 780
Cdd:PRK03918 153 QILGLDDYenayKNLGEVIKEIKRRIERLEKFIKRTEN-IEELIKE------------------------KEKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 781 QLQELENKdLSDVAMKVKLQKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDLdacnlkrrkgsfgsidhLQKLDEQKK 860
Cdd:PRK03918 208 EINEISSE-LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK-----------------IRELEERIE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 861 WLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQ--ELSEKNVQ 938
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERleELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 939 LQTSTA--EEKTKISEQVEVLQKEKDQLQKRRHNvdeklkngrvLSPEE-EHVLFQLEEGIEALEAAIEYRNE---SIQN 1012
Cdd:PRK03918 350 LEKRLEelEERHELYEEAKAKKEELERLKKRLTG----------LTPEKlEKELEELEKAKEEIEEEISKITArigELKK 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1013 RQKSLRASFHNL--SRGEANVLEKLacLSPVEIRTILFRYFNKVVNLRE-----AERKQQLYNEEMKM-KVLERDNMVRE 1084
Cdd:PRK03918 420 EIKELKKAIEELkkAKGKCPVCGRE--LTEEHRKELLEEYTAELKRIEKelkeiEEKERKLRKELRELeKVLKKESELIK 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1085 LESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDG-EGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKELVG 1163
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
|
.
gi 429535822 1164 E 1164
Cdd:PRK03918 578 E 578
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
760-1036 |
1.62e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 760 KVTKLEHDAEQAKVELIETQKQLQELENK-DLSDVAMKVKLQKEFRKKMDAAKLRvQEIQLKTGQEEGLKPKAEDLDACN 838
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLE-QDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 839 LKRRKgsfgsidHLQKLDEQkkwLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDS 918
Cdd:COG1196 326 AELEE-------ELEELEEE---LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 919 LKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKD------QLQKRRHNVDEKLKNGRVLSPEEEHVLFQL 992
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEeeealeEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 429535822 993 EEGIEALEAAIEyRNESIQNRQKSLRASFHNLSRGEANVLEKLA 1036
Cdd:COG1196 476 EAALAELLEELA-EAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
717-1063 |
1.90e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.75 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 717 RILTEAKQKMRELTINIKMKEDLIKELI----KTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSD 792
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 793 VA-----MKVKLQKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVE 867
Cdd:pfam02463 249 EQeeiesSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 868 KVLNQRQELEELEADLK----KREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQtsT 943
Cdd:pfam02463 329 ELKKEKEEIEELEKELKeleiKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--E 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 944 AEEKTKISEQVEVLQKEKDQ--------LQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQK 1015
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKeeleileeEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 429535822 1016 SLRASfhnLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERK 1063
Cdd:pfam02463 487 ELLLS---RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
681-1187 |
2.17e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 681 DTQDETQKSDLENedlKIDCLQESQELNLQKLKNSERI----LTEAKQKMRELTINIKMKEDLIKEliktgnDAKSVSKQ 756
Cdd:pfam15921 244 EDQLEALKSESQN---KIELLLQQHQDRIEQLISEHEVeitgLTEKASSARSQANSIQSQLEIIQE------QARNQNSM 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 757 YSLKVTKLEHDAEQAKVELIETQK----QLQELE------NKDLSDVAMKV--------KLQKEFRKKMDAAKLRVQEIQ 818
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRmyedKIEELEkqlvlaNSELTEARTERdqfsqesgNLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 819 LKTGQEEGLkpkaedldacnLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQEleELEADLKKREAIVSKKEALLQ 898
Cdd:pfam15921 395 LEKEQNKRL-----------WDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS--ECQGQMERQMAAIQGKNESLE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 899 EKSHLeNKKLRSSQALntdslkistrLNLLEQELSEKNVQLQTS---TAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKL 975
Cdd:pfam15921 462 KVSSL-TAQLESTKEM----------LRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEATNAEITKLRSRVDLKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 976 KNGRVLSPEEEHvLFQLEEGIEALEAAIEYRNESIQnrqkSLRASFHNLSR--GEANvleKLACLSPVEIRTIlfryfNK 1053
Cdd:pfam15921 531 QELQHLKNEGDH-LRNVQTECEALKLQMAEKDKVIE----ILRQQIENMTQlvGQHG---RTAGAMQVEKAQL-----EK 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1054 VVNLREAERKqqlyneEMKMKVLERDNMVRELESALDHLKLQcdrRLTLQQKEHEQkmqllLHHFKE--QDGEGIMETFK 1131
Cdd:pfam15921 598 EINDRRLELQ------EFKILKDKKDAKIRELEARVSDLELE---KVKLVNAGSER-----LRAVKDikQERDQLLNEVK 663
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 429535822 1132 TYEDKIQQLEKDLYFYKKTSRDHKKKLkELVGEAIRRQL--APSEYQEAGDGVLKPEG 1187
Cdd:pfam15921 664 TSRNELNSLSEDYEVLKRNFRNKSEEM-ETTTNKLKMQLksAQSELEQTRNTLKSMEG 720
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-1161 |
3.58e-07 |
|
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: 54.64 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 685 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILteakqkmrELTI-NIKMKEDLIKELIKTGNDAKSVSKQYSLKVTK 763
Cdd:TIGR04523 165 KKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL--------ELLLsNLKKKIQKNKSLESQISELKKQNNQLKDNIEK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 764 LEHDAEQAKVELIETQKQLQEL---ENKDLSDVAMKVKLQKEFRKKMDAAKLRVQeiQLKTGQEEGLKPKAEDLDacnlK 840
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLkdeQNKIKKQLSEKQKELEQNNKKIKELEKQLN--QLKSEISDLNNQKEQDWN----K 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 841 RRKGSFGSIDhlQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLK 920
Cdd:TIGR04523 311 ELKSELKNQE--KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 921 ISTRLNLLEQELSEKNvqlqtstaEEKTKISEQVEVLQKEKDQLQKRRhnvdEKLKNGRVLSPEE----EHVLFQLEEGI 996
Cdd:TIGR04523 389 LESQINDLESKIQNQE--------KLNQQKDEQIKKLQQEKELLEKEI----ERLKETIIKNNSEikdlTNQDSVKELII 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 997 EALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLynEEMKMKVL 1076
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI--EKLESEKK 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1077 ERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFK---EQDGEGIMETFKTYEDKIQQLEKDLYFYKKTSRD 1153
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQkslKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
....*...
gi 429535822 1154 HKKKLKEL 1161
Cdd:TIGR04523 615 LEKELEKA 622
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
852-1142 |
5.11e-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: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 852 LQKLDEQKkwldEEVEKVLNQRQELEELEADL--KKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTrLNLLE 929
Cdd:TIGR02168 202 LKSLERQA----EKAERYKELKAELRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 930 QELSEKNVQLQTSTAEEKTKISEqvevLQKEKDQLQKRRHNVDEKLKngrVLSPEEEHVLFQLEEGIEALeAAIEYRNES 1009
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISR----LEQQKQILRERLANLERQLE---ELEAQLEELESKLDELAEEL-AELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1010 IQNRQKSLRASFHNLSRGEANVLEKLAclspvEIRTILFRYFNKVVNLREAERKQQLyneemkmkvlerdnmvrELESAL 1089
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLE-----ELEEQLETLRSKVAQLELQIASLNN-----------------EIERLE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 429535822 1090 DHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDG------EGIMETFKTYEDKIQQLEK 1142
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAeleeleEELEELQEELERLEEALEE 465
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
678-1035 |
5.65e-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: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 678 ELSDTQDETQKSDLENEDLKIDCLQESQELNLQK--LKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 755
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 756 QYSLKVTKLEHDAEQAKVELIETQKQLQELeNKDLSDVAMKVkLQKEFRKKMDAAKLRVQEIQLKTGQEEgLKPKAEDLD 835
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLNEEA-ANLRERLESLERRIAATERRLEDLEEQ-IEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 836 ACNlkrrkgsfGSIDHLQKLDEQkkwLDEEVEKVLNQRQELEELEADLKKREAIVSKKealLQEKSHLENKKLRSSQALN 915
Cdd:TIGR02168 856 SLA--------AEIEELEELIEE---LESELEALLNERASLEEALALLRSELEELSEE---LRELESKRSELRRELEELR 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 916 TDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKN-GRV--LSPEE------- 985
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElGPVnlAAIEEyeelker 1001
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 429535822 986 -EHVLFQ---LEEGIEALEAAIEYRNESIQNRqksLRASFHNLSRGEANVLEKL 1035
Cdd:TIGR02168 1002 yDFLTAQkedLTEAKETLEEAIEEIDREARER---FKDTFDQVNENFQRVFPKL 1052
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
779-1178 |
9.15e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 779 QKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDL---------DACNLKRRKGSFGSI 849
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELeaeleelreELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 850 DHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEkshlenkklrssqALNTDSLKISTRLNLLE 929
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE-------------LLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 930 QELSEKNVQLQTSTAEEKtKISEQVEVLQKEKDQL--QKRRHNVDEKLKNGRVL-------------------SPEEEHV 988
Cdd:COG4717 199 EELEELQQRLAELEEELE-EAQEELEELEEELEQLenELEAAALEERLKEARLLlliaaallallglggsllsLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 989 LFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLAC---LSPVEIRTILFRYFNKVVNLREAERKQQ 1065
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgLPPDLSPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1066 LYNEEMKMKVL--ERDNMVREL----ESALDHLKLQCDRRLTLQQKEHEQKMQLLLhHFKEQDGEGIMETFKTYEDKIQQ 1139
Cdd:COG4717 358 ELEEELQLEELeqEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEE-LLGELEELLEALDEEELEEELEE 436
|
410 420 430
....*....|....*....|....*....|....*....
gi 429535822 1140 LEKDLYFYKKTSRDHKKKLKELVGEaIRRQLAPSEYQEA 1178
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAE-LEQLEEDGELAEL 474
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
684-1154 |
1.15e-06 |
|
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: 53.19 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 684 DETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKS------VSKQY 757
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKeledikMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 758 SLKVTK-LEHDAEQAKVELI----ETQKQLQELENKDLSDVAMKVKL--------------QKEFRKKMDAAKLRVQEIQ 818
Cdd:pfam05483 308 SMSTQKaLEEDLQIATKTICqlteEKEAQMEELNKAKAAHSFVVTEFeattcsleellrteQQRLEKNEDQLKIITMELQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 819 LKTGQEEGLKpKAEDLDACNLKRRKGSFGSIDHL-------QKLDEQKKWLDEEVEKVLNQRQ-ELEELEADLKkreAIV 890
Cdd:pfam05483 388 KKSSELEEMT-KFKNNKEVELEELKKILAEDEKLldekkqfEKIAEELKGKEQELIFLLQAREkEIHDLEIQLT---AIK 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 891 SKKEALLQE----KSHLENKKLRSSQaLNTDSLKISTRLNLLEQELSEKNVQLQ------TSTAEEKTKISEQVEVLQKE 960
Cdd:pfam05483 464 TSEEHYLKEvedlKTELEKEKLKNIE-LTAHCDKLLLENKELTQEASDMTLELKkhqediINCKKQEERMLKQIENLEEK 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 961 KDQLQKRRHNVDEKLKNGRvlsPEEEHVLFQLEEGIEALEAAI---EYRNESIQNRQKSLRASFHNLSRG------EANV 1031
Cdd:pfam05483 543 EMNLRDELESVREEFIQKG---DEVKCKLDKSEENARSIEYEVlkkEKQMKILENKCNNLKKQIENKNKNieelhqENKA 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1032 LEKLACLSPVEIRTILFRYFNKVVNLREAERK----QQLYNEEMKMKVLERDNMVRELESAldhlKLQCDRRLTLqQKEH 1107
Cdd:pfam05483 620 LKKKGSAENKQLNAYEIKVNKLELELASAKQKfeeiIDNYQKEIEDKKISEEKLLEEVEKA----KAIADEAVKL-QKEI 694
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 429535822 1108 EQKMQlllHHFKEQdgEGIMETFKTYEDKI-QQLEKDLYFYKKTSRDH 1154
Cdd:pfam05483 695 DKRCQ---HKIAEM--VALMEKHKHQYDKIiEERDSELGLYKNKEQEQ 737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
703-1004 |
1.57e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 703 ESQELNlQKLKNSERILTEAKQKMRELtinikmkEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQL 782
Cdd:TIGR02169 675 ELQRLR-ERLEGLKRELSSLQSELRRI-------ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 783 QELENKDLSDVAMKVKLQKEF-RKKMDAAKLRVQEIQLKTG-QEEGLKPKAEDLDACN--LKRRKGSFGSIDH-LQKLDE 857
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIeELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEeeVSRIEARLREIEQkLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 858 QKKWLDEEvekvlnqRQELEELEADLKKREAIVSKKEALLqekshleNKKLRSsqaLNTDSLKISTRLNLLEQELSE--- 934
Cdd:TIGR02169 827 EKEYLEKE-------IQELQEQRIDLKEQIKSIEKEIENL-------NGKKEE---LEEELEELEAALRDLESRLGDlkk 889
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429535822 935 --KNVQLQTSTAEEK-TKISEQVEVLQKEKDQLQKRRHNVDEKLK------NGRVLSPEEEHVLFQLEEGIEALEAAIE 1004
Cdd:TIGR02169 890 erDELEAQLRELERKiEELEAQIEKKRKRLSELKAKLEALEEELSeiedpkGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
679-958 |
1.93e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.61 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 679 LSDTQ---DETQKSDLENEDLKIDCLQESQEL-----NLQKLKNSEriLTEAKQKMRELTInikmkEDLIKELIKTGNDA 750
Cdd:PRK11281 65 LEQTLallDKIDRQKEETEQLKQQLAQAPAKLrqaqaELEALKDDN--DEETRETLSTLSL-----RQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 751 KSVSK---QYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAaklrvqEIQLktgqeegl 827
Cdd:PRK11281 138 QNAQNdlaEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQA------EQAL-------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 828 kpkaedLDACNLKRRKgSFGSIDHLQKLDEQKkwLDEEVEKVLNQRQELEELEADLKKREAIVSKK---EALLQEK--SH 902
Cdd:PRK11281 204 ------LNAQNDLQRK-SLEGNTQLQDLLQKQ--RDYLTARIQRLEHQLQLLQEAINSKRLTLSEKtvqEAQSQDEaaRI 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429535822 903 LENKKLRSSQALNT----DSLKISTRLN-LLEQELSEKNvQLQTSTAEEKTkISEQVEVLQ 958
Cdd:PRK11281 275 QANPLVAQELEINLqlsqRLLKATEKLNtLTQQNLRVKN-WLDRLTQSERN-IKEQISVLK 333
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
707-1276 |
4.03e-06 |
|
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: 51.51 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 707 LNLQKLKNSERILTEAKQKMRELTINIKmKEDLIKELIKtgNDAKSVSKQYSLKVTKLEHDAEQakveLIETQKQLQELE 786
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAE-LLTLRSQLLT--LCTPCMPDTYHERKQVLEKELKH----LREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 787 NKdlsdVAMKVKLQKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDLdacNLKRRKGSFgsIDHLQKLDEqkkwLDEEV 866
Cdd:TIGR00618 243 AY----LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI---NRARKAAPL--AAHIKAVTQ----IEQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 867 EKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTstAEE 946
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL--QQQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 947 KTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLS-----PEEEHVLFQLEEGIEALEAAIEYRNESIQNR-QKSLRAS 1020
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQgqlahAKKQQELQQRYAELCAAAITCTAQCEKLEKIhLQESAQS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1021 FHNLSRGEANVleKLACLSPVEIRTILFRYFNKVVNLR----------EAERKQQLYNEEMKMKVLERDNMVRELESALD 1090
Cdd:TIGR00618 468 LKEREQQLQTK--EQIHLQETRKKAVVLARLLELQEEPcplcgscihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1091 HLKLQCDrRLTLQQKEHEQKMQLLLHHFkeQDGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKelvgEAIRRQL 1170
Cdd:TIGR00618 546 DVYHQLT-SERKQRASLKEQMQEIQQSF--SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA----CEQHALL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1171 APSEYQEAGDGVLKPEGGGMLSEELKWASRPESMKLSGREREMDSSASS--------LRTQPNPQKLWEDIPELPPIHSS 1242
Cdd:TIGR00618 619 RKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIrvlpkellASRQLALQKMQSEKEQLTYWKEM 698
|
570 580 590
....*....|....*....|....*....|....
gi 429535822 1243 LAPPSGHMLGNENKTETDDNQFTKSHSRLSSQIQ 1276
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
761-1145 |
7.98e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 761 VTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQEiqlktgQEEGLKPKAEDLDACNLK 840
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL------ELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 841 RRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEadlKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLK 920
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE---EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 921 ISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQK--RRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEA 998
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEleKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 999 LEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLAcLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKV--- 1075
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL-EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSedl 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1076 LERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDGEGIMETFKTYEDKIQQLEKDLY 1145
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
710-983 |
1.35e-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: 48.99 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 710 QKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKd 789
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 790 lsdvamKVKLQKEFRKKMDAAklrvqeiqLKTGQEEGLKPkaedldacnLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKV 869
Cdd:COG4942 99 ------LEAQKEELAELLRAL--------YRLGRQPPLAL---------LLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 870 LNQRQELEELEADL-KKREAIVSKKEALLQEKSHLENKKLRSSQALNtdslKISTRLNLLEQELSEKnvqlqtstAEEKT 948
Cdd:COG4942 156 RADLAELAALRAELeAERAELEALLAELEEERAALEALKAERQKLLA----RLEKELAELAAELAEL--------QQEAE 223
|
250 260 270
....*....|....*....|....*....|....*
gi 429535822 949 KISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSP 983
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPAAGFAALKGKLPWP 258
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
683-1171 |
1.45e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 683 QDETQKSDLENEDLKIDCLQESQELNLQKLKNSERiltEAKQKMRELTINIKMKEDLiKELIKTGNDAKSVSKQyslKVT 762
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKL-ERRKVDDEEKLKESEK---EKK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 763 KLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDLDACNLKRR 842
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 843 KGSFGSIDHLQ-KLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKI 921
Cdd:pfam02463 405 KEAQLLLELARqLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 922 STRLNLLEQELSEKNVQLQTSTAEEKTKISEQ---VEVLQKEKDQLQKRRHNVDEKLKNGRVLS-PEEEHVLFQLEEGIE 997
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIkdgVGGRIISAHGRLGDLGVAVENYKVAISTAvIVEVSATADEVEERQ 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 998 ALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLyneemKMKVLE 1077
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTE-----LTKLKE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1078 RDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDGEGIMETFKTYEdkiQQLEKDLYFYKKTSRDHKKK 1157
Cdd:pfam02463 640 SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR---RQLEIKKKEQREKEELKKLK 716
|
490
....*....|....
gi 429535822 1158 LKELVGEAIRRQLA 1171
Cdd:pfam02463 717 LEAEELLADRVQEA 730
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
710-1029 |
1.49e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.69 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 710 QKLKNSERIlteaKQKMRELTINIKM--KEDLIKELIKTGNDaksvSKQYSLKVTKLEHDAEQAKVELIETQKQLQELEN 787
Cdd:COG5022 820 IKLQKTIKR----EKKLRETEEVEFSlkAEVLIQKFGRSLKA----KKRFSLLKKETIYLQSAQRVELAERQLQELKIDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 788 KDLSDVAMK-VKLQKE-FRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDLDACNLKRRKgsFGSIDHLQKLDEQKKWLDEE 865
Cdd:COG5022 892 KSISSLKLVnLELESEiIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIE--YVKLPELNKLHEVESKLKET 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 866 VEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHlENKKLRSSQALNTDSLKISTRLNLLEQELSEknvqlQTSTAE 945
Cdd:COG5022 970 SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSK-QYGALQESTKQLKELPVEVAELQSASKIISS-----ESTELS 1043
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 946 EKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEhvlfqLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLS 1025
Cdd:COG5022 1044 ILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLY-----QLESTENLLKTINVKDLEVTNRNLVKPANVLQFI 1118
|
....
gi 429535822 1026 RGEA 1029
Cdd:COG5022 1119 VAQM 1122
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
852-1020 |
2.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 852 LQKLDEQKKWLDEEVEKVLNQ----RQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQA-----------LNT 916
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEynelQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsggsvsyldvlLGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 917 DSL-KISTRLNLLEQeLSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEG 995
Cdd:COG3883 112 ESFsDFLDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180
....*....|....*....|....*
gi 429535822 996 IEALEAAIEYRNESIQNRQKSLRAS 1020
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
737-1004 |
2.58e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 737 EDLIKELI----KTGNDAKSVSKQYslkvTKLEhDAEQAKVELIETQKQLQELEnkDLSDVAMKVKLQKEFRKKMDAAkL 812
Cdd:COG4913 210 DDFVREYMleepDTFEAADALVEHF----DDLE-RAHEALEDAREQIELLEPIR--ELAERYAAARERLAELEYLRAA-L 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 813 RVQEIQLKTGQeegLKPKAEDLDAcNLKRRKgsfgsiDHLQKLDEQKKWLDEEVEKVLNQR-----QELEELEADLKKRE 887
Cdd:COG4913 282 RLWFAQRRLEL---LEAELEELRA-ELARLE------AELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 888 AIVSKKEALLQE-KSHLENKKLR---SSQALNTDSLKISTRLNLLEQELsEKNVQLQTSTAEEKTKISEQVEVLQKEKDQ 963
Cdd:COG4913 352 RELEERERRRARlEALLAALGLPlpaSAEEFAALRAEAAALLEALEEEL-EALEEALAEAEAALRDLRRELRELEAEIAS 430
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 429535822 964 LQKRRHNVDEKLKNGR-----VLSPEEEHVLF-----QLEEGIEALEAAIE 1004
Cdd:COG4913 431 LERRKSNIPARLLALRdalaeALGLDEAELPFvgeliEVRPEEERWRGAIE 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
733-949 |
3.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 733 IKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELEnKDLSdvamkvKLQKEFRKKMDAAKL 812
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ-AEIA------EAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 813 RVQEIQlKTGQeeGLKPKAEDLDAcnlkrrkGSFGS-IDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADL-KKREAIV 890
Cdd:COG3883 91 RARALY-RSGG--SVSYLDVLLGS-------ESFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELeAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 429535822 891 SKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTK 949
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
760-1019 |
3.99e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 760 KVTKLEHDAEQAKVELIETQKQLQELEnkDLSDVAMKVKLQKEFRKkmDAAKLRVQ---EIQLKTGQEEGLKPKAEDLDA 836
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE--DLVEAEDRIERLEERRE--DLEELIAErreTIEEKRERAEELRERAAELEA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 837 CNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNT 916
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAE 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 917 DSLKISTrlnlLEQELSEKNV---QLQTSTAEE-KTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHvlfqL 992
Cdd:PRK02224 632 KRERKRE----LEAEFDEARIeeaREDKERAEEyLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREA----L 703
|
250 260
....*....|....*....|....*..
gi 429535822 993 EEGIEALEAAIEyRNESIQNRQKSLRA 1019
Cdd:PRK02224 704 ENRVEALEALYD-EAEELESMYGDLRA 729
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
685-1109 |
1.59e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 685 ETQKSDLENEdlkIDCLQESQELNLQKLKNSERILTEAKQKMRELTI---NIKMKEDLIKELIKTGNDAKSVSKQYSLKV 761
Cdd:PRK02224 212 ESELAELDEE---IERYEEQREQARETRDEADEVLEEHEERREELETleaEIEDLRETIAETEREREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 762 TKLEHDAEQAKVEL------IET-QKQLQELENKD--LSDVAMKVKLQ-KEFRKKMDAAKLRVQEIQlktGQEEGLKPKA 831
Cdd:PRK02224 289 EELEEERDDLLAEAglddadAEAvEARREELEDRDeeLRDRLEECRVAaQAHNEEAESLREDADDLE---ERAEELREEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 832 EDLDA----CNLKRRKGSfGSIDHLQK---------------LDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSK 892
Cdd:PRK02224 366 AELESeleeAREAVEDRR-EEIEELEEeieelrerfgdapvdLGNAEDFLEELREERDELREREAELEATLRTARERVEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 893 KEALLQEKSHLE-NKKLRSS---QALNTDSLKISTrlnlLEQELSEknVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRR 968
Cdd:PRK02224 445 AEALLEAGKCPEcGQPVEGSphvETIEEDRERVEE----LEAELED--LEEEVEEVEERLERAEDLVEAEDRIERLEERR 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 969 HNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQ---NRQKSLRASFHNLSRGEANVLEKLACLSpvEIRT 1045
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAeaeEEAEEAREEVAELNSKLAELKERIESLE--RIRT 596
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429535822 1046 ILFR---YFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDhlklqcDRRLTLQQKEHEQ 1109
Cdd:PRK02224 597 LLAAiadAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD------EARIEEAREDKER 657
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
706-1171 |
2.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 706 ELNLQKLKNSERILTEAKQKMRELTINIKMKEDL---IKELIKTGNDAKSVSKQYSLKVTKLEHDAE--QAKVELIETQK 780
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 781 QLQELENkdlsdvamKVKLQKEFRKKMDAAKLRVQEIQlktgqeeglkpkaedlDACNLKRRKGSFGSIDHLQKLDEQKK 860
Cdd:COG4717 147 RLEELEE--------RLEELRELEEELEELEAELAELQ----------------EELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 861 WLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKK-----------LRSSQALNTDSLKISTRLNLLE 929
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 930 QELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNES 1009
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1010 IQnrQKSLRASFHNLsrgeanvLEKLACLSPVEIRTILFRYfNKVVNLRE--AERKQQLYNEEMKMKVLERDNMVRELES 1087
Cdd:COG4717 363 LQ--LEELEQEIAAL-------LAEAGVEDEEELRAALEQA-EEYQELKEelEELEEQLEELLGELEELLEALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1088 ALDHLKlQCDRRLTLQQKEHEQKMQLLLHHFKEqdgegiMETFKTYEDKIQQLEkdlyfykktsrDHKKKLKELVGEAIR 1167
Cdd:COG4717 433 ELEELE-EELEELEEELEELREELAELEAELEQ------LEEDGELAELLQELE-----------ELKAELRELAEEWAA 494
|
....
gi 429535822 1168 RQLA 1171
Cdd:COG4717 495 LKLA 498
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
767-1036 |
2.83e-04 |
|
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: 44.75 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 767 DAEQAKVELIETQKQLQELEnkdlsdvamkvKLQKEFRKKMDAAKLRVQEIQLKTGQeeglkpkaedldacnLKRRkgsf 846
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELE-----------KELAALKKEEKALLKQLAALERRIAA---------------LARR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 847 gsidhLQKLDEQKKWLDEEVEKVlnqRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLN 926
Cdd:COG4942 71 -----IRALEQELAALEAELAEL---EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 927 LLEQELSEKNVQLQtstaEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIeyr 1006
Cdd:COG4942 143 YLAPARREQAEELR----ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL--- 215
|
250 260 270
....*....|....*....|....*....|
gi 429535822 1007 nESIQNRQKSLRASFHNLSRGEANVLEKLA 1036
Cdd:COG4942 216 -AELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
710-975 |
3.70e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 710 QKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELEnKD 789
Cdd:TIGR02169 195 EKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE-QL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 790 LSDVAMKVK-----LQKEFRKKMdaAKLRVQEIQLKTGQEEgLKPKAEDLDAcnlkRRKGSFGSIDHLQ--------KLD 856
Cdd:TIGR02169 274 LEELNKKIKdlgeeEQLRVKEKI--GELEAEIASLERSIAE-KERELEDAEE----RLAKLEAEIDKLLaeieelerEIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 857 EQKKWLD------EEVEKVLNQ-RQELEELEADL-----------KKREAIVSKKEALLQEKSHLENKKLRSSQA---LN 915
Cdd:TIGR02169 347 EERKRRDklteeyAELKEELEDlRAELEEVDKEFaetrdelkdyrEKLEKLKREINELKRELDRLQEELQRLSEEladLN 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429535822 916 TDSLKISTRLNLLEQELSEKNVQLQT------STAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKL 975
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKqewkleQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
710-933 |
4.58e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 710 QKLKNSERILTEAKQKMRELTINIkmkEDLIKELIKTGNDAKsvskQYSLKVTKLEHDAEQAKVELIETQKQLQELENKD 789
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKL---NELIASLEELERELE----QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 790 LSdvamkvKLQKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAedldacnLKRRKgsfgSIDHLQKLDEQKKWLDEEVEKV 869
Cdd:PRK00409 568 LE------EAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAS-------VKAHE----LIEARKRLNKANEKKEKKKKKQ 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429535822 870 LNQRQELEE-----LEADLKKRE--AIVSKKEALLQE---KSHLENKKLRSSQALNTDSLKISTRLNLLEQELS 933
Cdd:PRK00409 631 KEKQEELKVgdevkYLSLGQKGEvlSIPDDKEAIVQAgimKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTVS 704
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
618-994 |
5.02e-04 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 44.73 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 618 AGFRTRSQMLLGHIEEQDKV--LHCQFSDNSDDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSD-----TQDETQKSD 690
Cdd:COG5192 359 AGEGEKMKMQLQEIEQDPGVdgVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEETSRedelsFDDSDVSTS 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 691 LENEDlkIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELiktgndAKSVSKQYSLKVTKLEHDAEQ 770
Cdd:COG5192 439 DENED--VDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASKL------AYSQSGKRGRNIQKIFYDESL 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 771 AKVELIETQKQlQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDLDACNLKRRKGS-FGSI 849
Cdd:COG5192 511 SPEECIEEYKG-ESAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFEELKKKWSSLAQLKSRFQKDAtLDSI 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 850 DHLQKL--DEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKlrssqalntdslKISTRLNL 927
Cdd:COG5192 590 EGEEELiqDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARK------------KEELRGNF 657
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429535822 928 LEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEE 994
Cdd:COG5192 658 ELEERGDPEKKDVDWYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYRAGRYVRIVLSHVPLEFVD 724
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
800-1154 |
5.84e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 800 QKEFRKKMDAAKLRVQEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDH----LQKLDEQKKWLDEEVEKVLNQRQ- 874
Cdd:PLN02939 46 QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHnrasMQRDEAIAAIDNEQQTNSKDGEQl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 875 ---ELEELEADLKKREA-IVSKKEALLQEKSHLEnKKLRSSQALNTdslkistRLNLLEQELSEKNVQLQTStAEEKTki 950
Cdd:PLN02939 126 sdfQLEDLVGMIQNAEKnILLLNQARLQALEDLE-KILTEKEALQG-------KINILEMRLSETDARIKLA-AQEKI-- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 951 seQVEVLQkekDQLQKRRHNVDEK--LKNGRVLSPEEEHVLFQLE-----EGIEALEAAI------EYRNESIQNRQKSL 1017
Cdd:PLN02939 195 --HVEILE---EQLEKLRNELLIRgaTEGLCVHSLSKELDVLKEEnmllkDDIQFLKAELievaetEERVFKLEKERSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1018 RASFHNLSRGEANVLEKLACLSPVEIRTilfrYFNKVVNLREAERKQQLYNEEMKMkVLERD----NMVRELESALDHLK 1093
Cdd:PLN02939 270 DASLRELESKFIVAQEDVSKLSPLQYDC----WWEKVENLQDLLDRATNQVEKAAL-VLDQNqdlrDKVDKLEASLKEAN 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429535822 1094 LQ--CDRRLTLQQkeheQKMQLLLHHFKEQDGEgIMETFKTYEDKIQQ----LEKDLYFYKKTSRDH 1154
Cdd:PLN02939 345 VSkfSSYKVELLQ----QKLKLLEERLQASDHE-IHSYIQLYQESIKEfqdtLSKLKEESKKRSLEH 406
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
803-959 |
7.26e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 803 FRKKMDAAKLRVQEIQLKTGQEEGLKpkaedlDACNLKRRKgsfgsidhlqKLDEQKKWLD--EEVEKVLNQR-QELEEL 879
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKK------EAEAIKKEA----------LLEAKEEIHKlrNEFEKELRERrNELQKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 880 EADLKKREAIVSKKEALLQEKSHlenkklrssqalntdslkistRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQK 959
Cdd:PRK12704 88 EKRLLQKEENLDRKLELLEKREE---------------------ELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
860-1069 |
7.65e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 860 KWLDEEVEKVlnqRQELEELEADL---KKREAIVS---KKEALLQEKSHLENKKlrssQALNTDSLKISTRLNLLEQELS 933
Cdd:COG3206 178 EFLEEQLPEL---RKELEEAEAALeefRQKNGLVDlseEAKLLLQQLSELESQL----AEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 934 EKNVQL-QTSTAEEKTKISEQVEVLQKEKDQLQKR---RH----NVDEKLKNGRVlspeeehvlfQLEEGIEALEAAIEY 1005
Cdd:COG3206 251 SGPDALpELLQSPVIQQLRAQLAELEAELAELSARytpNHpdviALRAQIAALRA----------QLQQEAQRILASLEA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429535822 1006 RNESIQNRQKSLRASFHNLsRGEANVLEKLAclspVEIRTIlfryfnkvvnLREAERKQQLYNE 1069
Cdd:COG3206 321 ELEALQAREASLQAQLAQL-EARLAELPELE----AELRRL----------EREVEVARELYES 369
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
748-1070 |
9.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 748 NDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQEIQLKTGQEEGL 827
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 828 KPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKK 907
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 908 LRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEH 987
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 988 VLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLY 1067
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
...
gi 429535822 1068 NEE 1070
Cdd:COG4372 368 ADG 370
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
800-917 |
9.97e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 800 QKEFRKKMDAAKLRVQEIQ---LKTGQEEGLKPKAEDLDACNLKRRKgsfgsIDHLQKLDEQKK-WLDEEVEKVLNQRQE 875
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKkeaLLEAKEEIHKLRNEFEKELRERRNE-----LQKLEKRLLQKEeNLDRKLELLEKREEE 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 429535822 876 LEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTD 917
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
765-1163 |
1.31e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 765 EHDAEQAKVELIETQKQLQE--LENKDLSDVAMKVKLQKEFRKKMDAAKLRV--QEIQLKTGQEEGLKPKAEDL-DACNL 839
Cdd:pfam10174 179 EDWERTRRIAEAEMQLGHLEvlLDQKEKENIHLREELHRRNQLQPDPAKTKAlqTVIEMKDTKISSLERNIRDLeDEVQM 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 840 KRRKGSFGSIDHLQKLdeqkkwldEEVEKVLNQ----RQELEELEADLKKRE----AIVSKKEALLQE----KSHLE--- 904
Cdd:pfam10174 259 LKTNGLLHTEDREEEI--------KQMEVYKSHskfmKNKIDQLKQELSKKEsellALQTKLETLTNQnsdcKQHIEvlk 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 905 ---NKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISE-------------QVEVLQKEKDQLQKRR 968
Cdd:pfam10174 331 eslTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEirdlkdmldvkerKINVLQKKIENLQEQL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 969 HNVDEKLKN--GRVLSPEEEH-----VLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLspv 1041
Cdd:pfam10174 411 RDKDKQLAGlkERVKSLQTDSsntdtALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSAL--- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1042 eiRTILFRYFNKVVNLREAERKQqlyneemKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQlllhhfkEQ 1121
Cdd:pfam10174 488 --QPELTEKESSLIDLKEHASSL-------ASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEA-------VR 551
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 429535822 1122 DGEGIMetfktyeDKIQQLEKDLYFYKKTSRDHKKKLKELVG 1163
Cdd:pfam10174 552 TNPEIN-------DRIRLLEQEVARYKEESGKAQAEVERLLG 586
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
707-893 |
1.39e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 707 LNLQKLKNSeriLTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELE 786
Cdd:COG1579 10 LDLQELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 787 N-KDLSDvamkvkLQKEfrkkMDAAKLRVQ----EIQLKTGQEEGLKPKAEDLDAcNLKRRKGSFGSIdhLQKLDEQKKW 861
Cdd:COG1579 87 NnKEYEA------LQKE----IESLKRRISdledEILELMERIEELEEELAELEA-ELAELEAELEEK--KAELDEELAE 153
|
170 180 190
....*....|....*....|....*....|....
gi 429535822 862 LDEEVEKVLNQRQELEE-LEADLKKR-EAIVSKK 893
Cdd:COG1579 154 LEAELEELEAEREELAAkIPPELLALyERIRKRK 187
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
701-1111 |
1.40e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 701 LQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKvELIETQK 780
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE-TLLGTIM 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 781 QLQELENKDLSDVAMKVKLQ---KEFRKKMDAAKLRVQEIQLKTGQEEgLKPKAEDLDacnlKRRKGSFGSIDHLQKLDE 857
Cdd:TIGR00606 779 PEEESAKVCLTDVTIMERFQmelKDVERKIAQQAAKLQGSDLDRTVQQ-VNQEKQEKQ----HELDTVVSKIELNRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 858 QKKWLDEEVEKVLNQ-RQELEELEADLKKREAIVSKKEALLQEKSHLENKklrSSQALNTDSlkistRLNLLEQELSEKN 936
Cdd:TIGR00606 854 DQQEQIQHLKSKTNElKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIRE---IKDAKEQDS-----PLETFLEKDQQEK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 937 VQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRvlspeeEHVLFQLEEGIEALEAAI---EYRNESIQNR 1013
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK------DDYLKQKETELNTVNAQLeecEKHQEKINED 999
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1014 QKSLRASFHNLSRGEANVLEKLACLSPVEirtilfryfnkvvNLREAERKQQLYNEEM-KMKVLERDNMVRELESALDHL 1092
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQERWLQDNLTLRKREN-------------ELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLI 1066
|
410
....*....|....*....
gi 429535822 1093 KLQCDRRLTLQQKEHEQKM 1111
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIK 1085
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
786-1112 |
1.84e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 786 ENKDLSDVAMKVKLQKEFRKKMDAAKL-RVQEIQLKTGQEEglkpKAEDLDacnlKRRKGSFGSIDHLQKLDEQKKWLDE 864
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKFeKMEQERLRQEKEE----KAREVE----RRRKLEEAEKARQAEMDRQAAIYAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 865 EVEKVLNQRQELEELEADLKKREaivskKEALLQEKSHLENKKLRSSQALNTDSLKISTRlnlLEQELsEKNVQLQTSTA 944
Cdd:pfam17380 339 QERMAMERERELERIRQEERKRE-----LERIRQEEIAMEISRMRELERLQMERQQKNER---VRQEL-EAARKVKILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 945 EEKTKISEQ-VEVLQKEKDQLQKRRHNVdeklkngRVLSPEEEHVLFQL-EEGIEALEAAIEYRNESIQNRQKSLRASFH 1022
Cdd:pfam17380 410 ERQRKIQQQkVEMEQIRAEQEEARQREV-------RRLEEERAREMERVrLEEQERQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1023 NLSRGEANVLEKlaclspveirtilfryfnKVVNLREAERKQQLYNEEMKMKVLErdnmvRELESALDHLKLQCDRRLTL 1102
Cdd:pfam17380 483 KRDRKRAEEQRR------------------KILEKELEERKQAMIEEERKRKLLE-----KEMEERQKAIYEEERRREAE 539
|
330
....*....|
gi 429535822 1103 QQKEHEQKMQ 1112
Cdd:pfam17380 540 EERRKQQEME 549
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
474-1125 |
1.96e-03 |
|
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: 42.80 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 474 TVLQLKRELKKCQCVLAADEVVFNQKELEVKELKNQVQMMVQEnkghavslkeaqkvnrLQNEKIIEQQLLVDQLS--EE 551
Cdd:pfam15921 111 SVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHE----------------LEAAKCLKEDMLEDSNTqiEQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 552 LTKLNLSvtssakencgdgPDARIPERRPYTVPFDTHLGHYIYipsRQDS-RKVHTSPPMYSLDRIFAGFRTRSQMLLGH 630
Cdd:pfam15921 175 LRKMMLS------------HEGVLQEIRSILVDFEEASGKKIY---EHDSmSTMHFRSLGSAISKILRELDTEISYLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 631 I------------EEQDKV--LHCQFSDNSDDEESEGQ-EKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSdlened 695
Cdd:pfam15921 240 IfpvedqlealksESQNKIelLLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQNS------ 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 696 lkidclqesqeLNLQKLKNSERILTEAKQKMRELTiniKMKEDLIKELIKTG-------NDAKSVSKQYSLKVTKLEHDA 768
Cdd:pfam15921 314 -----------MYMRQLSDLESTVSQLRSELREAK---RMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 769 EQAKVELIETQKQL--QELENKDLSDVAMKVKLQ-KEFRKKMDAAKLRVQEIQ--LKTGQEEGLKPKAEDLDACnlkrrK 843
Cdd:pfam15921 380 QKLLADLHKREKELslEKEQNKRLWDRDTGNSITiDHLRRELDDRNMEVQRLEalLKAMKSECQGQMERQMAAI-----Q 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 844 GSFGSIDHLQKLDEQKKWLDEEVEKVLnqrQELEELEADLKKREAIVSKKEALLQEKShlenkklRSSQALNTDSLKIST 923
Cdd:pfam15921 455 GKNESLEKVSSLTAQLESTKEMLRKVV---EELTAKKMTLESSERTVSDLTASLQEKE-------RAIEATNAEITKLRS 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 924 RLNLLEQELSE--------KNVQLQTSTAE----EKTKISE----QVE--------------VLQKEKDQLQKRRHNVDE 973
Cdd:pfam15921 525 RVDLKLQELQHlknegdhlRNVQTECEALKlqmaEKDKVIEilrqQIEnmtqlvgqhgrtagAMQVEKAQLEKEINDRRL 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 974 KLKNGRVLSPEEEHVLFQLEE---------------GIEALEAAIEYRNESIQ--NRQKSLRASFHNLS----------R 1026
Cdd:pfam15921 605 ELQEFKILKDKKDAKIRELEArvsdlelekvklvnaGSERLRAVKDIKQERDQllNEVKTSRNELNSLSedyevlkrnfR 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1027 GEANVLE-----------------------------------KLACLSPVEI---RTILFRYFNKVVNLREA-------- 1060
Cdd:pfam15921 685 NKSEEMEtttnklkmqlksaqseleqtrntlksmegsdghamKVAMGMQKQItakRGQIDALQSKIQFLEEAmtnankek 764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 1061 ----ERKQQLyNEEMKMKVLERDNMVRELES-----------------ALDHLKLQCDRRLTLQQKEHEQKMQLLLHH-- 1117
Cdd:pfam15921 765 hflkEEKNKL-SQELSTVATEKNKMAGELEVlrsqerrlkekvanmevALDKASLQFAECQDIIQRQEQESVRLKLQHtl 843
|
....*....
gi 429535822 1118 -FKEQDGEG 1125
Cdd:pfam15921 844 dVKELQGPG 852
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
867-1010 |
2.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 867 EKVLNQRQELEELEADL----KKREAIVSKKEALLQEKShlENKKLRSSqalntdslkistrlnlLEQELSEKNVQLQTs 942
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKE--EIHKLRNE----------------FEKELRERRNELQK- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429535822 943 tAEEKTK-----ISEQVEVLQKEKDQLQKRRHNVDEKLKNgrvlspeeehvLFQLEEGIEALEAAIEYRNESI 1010
Cdd:PRK12704 87 -LEKRLLqkeenLDRKLELLEKREEELEKKEKELEQKQQE-----------LEKKEEELEELIEEQLQELERI 147
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
705-972 |
2.19e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 705 QELNLQKLKNSERILT---EAKQKMRELTINIKMKEDLIK---ELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIET 778
Cdd:TIGR01612 1069 ELLNKEILEEAEINITnfnEIKEKLKHYNFDDFGKEENIKyadEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEI 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 779 QKQLQELEnkDLSDVAMKVKLQKEFRKKMDAAklrVQEIQLKTGQEEGLKPKAEDL-----DACNLKRRKG---SFGSid 850
Cdd:TIGR01612 1149 KAQINDLE--DVADKAISNDDPEEIEKKIENI---VTKIDKKKNIYDEIKKLLNEIaeiekDKTSLEEVKGinlSYGK-- 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 851 HLQKLDEQKkwLDEEVEKVLNQRQELEELEADLK--KREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLL 928
Cdd:TIGR01612 1222 NLGKLFLEK--IDEEKKKSEHMIKAMEAYIEDLDeiKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDEN 1299
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 429535822 929 EQELSEKNVQLqTSTAEEKTKISEQVEVLQKEKDQLQKrrHNVD 972
Cdd:TIGR01612 1300 ISDIREKSLKI-IEDFSEESDINDIKKELQKNLLDAQK--HNSD 1340
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
750-899 |
5.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 750 AKSVSKQyslKVTKLEHDA----EQAKVElIETQKQLQELENKDLSDvAMKVKLQKEFRKKMDaaKLRVQEIQLKTgQEE 825
Cdd:PRK12704 25 RKKIAEA---KIKEAEEEAkrilEEAKKE-AEAIKKEALLEAKEEIH-KLRNEFEKELRERRN--ELQKLEKRLLQ-KEE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429535822 826 GLKPKAEDLDacnlKRRK---GSFGSIDHLQK-LDEQKKWLDEEVEKvlnQRQELEELeADLKKREAivskKEALLQE 899
Cdd:PRK12704 97 NLDRKLELLE----KREEeleKKEKELEQKQQeLEKKEEELEELIEE---QLQELERI-SGLTAEEA----KEILLEK 162
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
710-1031 |
5.56e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 710 QKLKNSERILTEAKQKMRELTINIKMKEDLIKELiktgndaksvsKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKD 789
Cdd:TIGR01612 1541 KTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEI-----------KKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKF 1609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 790 L--SDVAMKV----KLQKEFRKKMDAAKLRVQEIQLKTgQEEGLKPKAEDLDAcnLKRRKgsfgsidhlQKLDEQKKWLD 863
Cdd:TIGR01612 1610 LkiSDIKKKIndclKETESIEKKISSFSIDSQDTELKE-NGDNLNSLQEFLES--LKDQK---------KNIEDKKKELD 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 864 E---EVEKV---LNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSL----------KISTRLNL 927
Cdd:TIGR01612 1678 EldsEIEKIeidVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLegidpnekleEYNTEIGD 1757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535822 928 LEQELSE---------KNVQLQTSTAEE--KTKISEQVEVLQkekdqlqkrrhNVDEKLKNGRVLSPEEEHvlfQLEEGI 996
Cdd:TIGR01612 1758 IYEEFIElyniiagclETVSKEPITYDEikNTRINAQNEFLK-----------IIEIEKKSKSYLDDIEAK---EFDRII 1823
|
330 340 350
....*....|....*....|....*....|....*
gi 429535822 997 EALEAAIEYRNESIQNRQKSLRASFHNLSRGEANV 1031
Cdd:TIGR01612 1824 NHFKKKLDHVNDKFTKEYSKINEGFDDISKSIENV 1858
|
|
| |
