|
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: 602.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 4 IPVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 84 GQTGSGKTYTIGGGHIASVVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELET-SMKDLHIRED 161
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDtFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEDGSWYSPRHIVSKFH 241
Cdd:cd01372 161 SKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNSTFTSKFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01372 241 FVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 320
|
330 340
....*....|....*....|.
gi 767957873 322 SSNFDESLNSLKYANRARNIR 342
Cdd:cd01372 321 DSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
5-348 |
7.99e-147 |
|
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: 447.40 E-value: 7.99e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 78 ATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEH-PSIDFNVKVSYIEVYKEDLRDLLEleTSMKDL 156
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLN--PSSKKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEaaedgswySPRHI 236
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSS--------SGSGK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRrKSSHIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIA 303
|
330 340 350
....*....|....*....|....*....|..
gi 767957873 317 CVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:smart00129 304 NVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-341 |
5.62e-140 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 428.92 E-value: 5.62e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 11 RIRPLLCKEALHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 84 GQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELETSMKD-LHIRED 161
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKErSEFSVKVSYLEIYNEKIRDLLSPSNKNKRkLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEdgswyspRHIVSKFH 241
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEE-------SVKTGKLN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 242 FVDLAGSERVTKTGN-TGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSP 320
Cdd:pfam00225 228 LVDLAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALADK--KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISP 305
|
330 340
....*....|....*....|.
gi 767957873 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 |
1.29e-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: 403.94 E-value: 1.29e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 5 PVKVAVRIRPLLCKEAlhNHQVCVRVIPNSQQVIIG-------RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd00106 1 NVRVAVRVRPLNGREA--RSAKSVISVDGGKSVVLDppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 78 ATVFAYGQTGSGKTYTIGGGHiasvvEGQKGIIPRAIQEIFQSISEHPSIDFN--VKVSYIEVYKEDLRDLLELETSmKD 155
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKSSfsVSASYLEIYNEKIYDLLSPVPK-KP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 156 LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNMEAAEDgswyspRH 235
Cdd:cd00106 153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGE------SV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 236 IVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKssHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd00106 225 TSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMI 302
|
330 340
....*....|....*....|....
gi 767957873 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 |
1.23e-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: 356.65 E-value: 1.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 6 VKVAVRIRPLLCKEALHNHQVCVRVI----------------------PNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNT 63
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdpkdeedgffhggsnNRDRRKRRNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 64 CIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISE-HPSIDFNVKVSYIEVYKED 142
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT------PQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 143 LRDLLEleTSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNM 222
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 223 EAAEDgswysprHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLL 302
Cdd:cd01370 234 SINQQ-------VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 767957873 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 |
1.75e-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: 352.79 E-value: 1.75e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSqqvIIGRDRV---FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQVAWEIDNDT---IYLVEPPstsFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 83 YGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLleLETSMKDLHIREDE 162
Cdd:cd01374 79 YGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDL--LSPTSQNLKIRDDV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 163 KGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcQVHKNMEAAEDGSwysprhIVSKFHF 242
Cdd:cd01374 151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI-ESSERGELEEGTV------RVSTLNL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01374 224 IDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAE 302
|
330
....*....|....*....
gi 767957873 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 |
5.63e-110 |
|
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: 349.07 E-value: 5.63e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII--GRD------RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 78 ATVFAYGQTGSGKTYTIGGghiASVVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELETSmKDL 156
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEG---KREDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKDQT-KRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhKNMEAAEDGSwyspRHI 236
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI----ECSEKGEDGE----NHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 237 -VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01371 231 rVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
|
330 340
....*....|....*....|....*.
gi 767957873 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 |
2.96e-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: 344.19 E-value: 2.96e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 11 RIRPLLCKEALHNHQVCVRVIPNSQQVII----GRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQT 86
Cdd:cd01366 9 RVRPLLPSEENEDTSHITFPDEDGQTIELtsigAKQKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIFAYGQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 87 GSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISE--HPSIDFNVKVSYIEVYKEDLRDLL-ELETSMKDLHIRED-E 162
Cdd:cd01366 88 GSGKTYTMEG------PPESPGIIPRALQELFNTIKElkEKGWSYTIKASMLEIYNETIRDLLaPGNAPQKKLEIRHDsE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 163 KGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhkNMEAAEDGSwysprHIVSKFHF 242
Cdd:cd01366 162 KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-----SGRNLQTGE-----ISVGKLNL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALgdpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01366 232 VDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAE 308
|
330 340
....*....|....*....|.
gi 767957873 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 |
1.52e-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: 328.52 E-value: 1.52e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 6 VKVAVRIRPLLCKEALHNHQVCVRvIPNSQQVIIGRD---RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVK-FDPEDTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 83 YGQTGSGKTYTIGGGHIAsvvEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLleLETSMKDLHIRED 161
Cdd:cd01369 83 YGQTSSGKTYTMEGKLGD---PESMGIIPRIVQDIFETIYSMDEnLEFHVKVSYFEIYMEKIRDL--LDVSKTNLSVHED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNMeaaEDGSWYSprhivSKFH 241
Cdd:cd01369 158 KNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ--ENV---ETEKKKS-----GKLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01369 228 LVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPS 305
|
330 340
....*....|....*....|
gi 767957873 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 |
2.46e-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: 329.29 E-value: 2.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII--------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 78 ATVFAYGQTGSGKTYTIGGGHiaSVVEGQK-------GIIPRAIQEIFQSISEHpSIDFNVKVSYIEVYKEDLRDLLELE 150
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMEGDR--SPNEEYTweldplaGIIPRTLHQLFEKLEDN-GTEYSVKVSYLEIYNEELFDLLSPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 151 TS-MKDLHIRED--EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEd 227
Cdd:cd01364 161 SDvSERLRMFDDprNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 228 gswyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprrKSSHIPYRDAKITRLLKDSLG 307
Cdd:cd01364 240 ------LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLG 310
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767957873 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 |
2.96e-102 |
|
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: 329.31 E-value: 2.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 6 VKVAVRIRPLLCKE---------ALHNHQVCVRVIPNSQQVIIGRDRV---FTFDFVF------GKN-STQDEVYNTCIK 66
Cdd:cd01365 3 VKVAVRVRPFNSREkernskcivQMSGKETTLKNPKQADKNNKATREVpksFSFDYSYwshdseDPNyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 67 PLVLSLIEGYNATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSI--SEHPSIDFNVKVSYIEVYKEDLR 144
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMG------TQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 145 DLLELETSMKD--LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNM 222
Cdd:cd01365 157 DLLNPKPKKNKgnLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQ--KRH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 223 EAAEDGSwyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR-----KSSHIPYRDAK 297
Cdd:cd01365 235 DAETNLT----TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767957873 298 ITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01365 311 LTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
45-379 |
4.77e-86 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 292.03 E-value: 4.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 45 FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEH 124
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGT------EEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 125 PSI-DFNVKVSYIEVYKEDLRDLLELETsmKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEH 203
Cdd:COG5059 132 SMTkDFAVSISYLEIYNEKIYDLLSPNE--ESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 204 SSRSHAIFTISICQVHKNMeaaedgswysPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD 283
Cdd:COG5059 210 SSRSHSIFQIELASKNKVS----------GTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 284 PRrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDR-IDEMEFE 362
Cdd:COG5059 280 KK-KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReIEEIKFD 358
|
330
....*....|....*..
gi 767957873 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 |
5.51e-85 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 280.93 E-value: 5.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIG-RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 84 GQTGSGKTYTIGG--GHIASVVEGQKGIIPRAIQEIFQSISEH-----PSIDFNVKVSYIEVYKEDLRDLleLETSMKDL 156
Cdd:cd01373 82 GQTGSGKTYTMWGpsESDNESPHGLRGVIPRIFEYLFSLIQREkekagEGKSFLCKCSFLEIYNEQIYDL--LDPASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmEAAEDGSWYSpRHI 236
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI-------ESWEKKACFV-NIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD-PRRKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01373 232 TSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAII 311
|
330 340 350
....*....|....*....|....*....|...
gi 767957873 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 |
6.45e-84 |
|
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: 277.25 E-value: 6.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVI-IGRDRV----------FTFDFVFGKNSTQDEVYNTCIKPLVLSLI 73
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVhEPKLKVdltkyienhtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 74 EGYNATVFAYGQTGSGKTYTIGGGHiaSVVEGQKGIIPRAIQEIFQSISEHPSID-FNVKVSYIEVYKEDLRDLLEletS 152
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKLPYKDnLGVTVSFFEIYGGKVFDLLN---R 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 153 MKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmEAAEDGSwys 232
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------RDRGTNK--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 233 prhIVSKFHFVDLAGSER-VTKTGNTGERFKESIQINSGLLALGNVISALGDPrrkSSHIPYRDAKITRLLKDSL-GGSA 310
Cdd:cd01367 226 ---LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQN---KAHIPFRGSKLTQVLKDSFiGENS 299
|
330 340
....*....|....*....|....*..
gi 767957873 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 |
7.98e-84 |
|
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: 277.74 E-value: 7.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 5 PVKVAVRIRPLLCKEALHNHQVCVRVIpNSQQV----------------IIGRDRVFTFDFVFGKNSTQDEVYNTCIKPL 68
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVI-NSTTVvlhppkgsaanksernGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 69 VLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISehpsiDFNVKVSYIEVYKEDLRDLLE 148
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGS------PGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 149 LETS-----MKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNME 223
Cdd:cd01368 150 PSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 224 AAEDGSWYSPRhiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRRKSSHIPYRDAKITRL 301
Cdd:cd01368 230 GDVDQDKDQIT--VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLreNQLQGTNKMVPFRDSKLTHL 307
|
330 340 350
....*....|....*....|....*....|....
gi 767957873 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 |
2.66e-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: 267.06 E-value: 2.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 5 PVKVAVRIRPLLCKEALHNHQVCVRVIpNSQQVIIGRDRV------FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNA 78
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELADPRNhgetlkYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 79 TVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQsISEHPSIDFNVKVSYIEVYKEDLRDLLELETsmKDLHI 158
Cdd:cd01376 80 TVFAYGSTGAGKTFTMLG------SPEQPGLMPLTVMDLLQ-MTRKEAWALSFTMSYLEIYQEKILDLLEPAS--KELVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 159 REDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmeaAEDGSWYSPRHIVS 238
Cdd:cd01376 151 REDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV---------DQRERLAPFRQRTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 239 KFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRrksshIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALnkNLPR-----IPYRDSKLTRLLQDSLGGGSRCIMVA 296
|
330 340
....*....|....*....|...
gi 767957873 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 |
1.07e-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: 248.65 E-value: 1.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 33 NSQQviigRDRVFTFDFVFgKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHIASvveGQKGIIPR 112
Cdd:cd01375 42 NNQQ----EDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 113 AIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLL----ELETSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEM 188
Cdd:cd01375 114 ALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 189 GNAARHTGTTQMNEHSSRSHAIFTIsicqvHKNMEAAEDGswySPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQIN 268
Cdd:cd01375 194 GETNRIIASHTMNKNSSRSHCIFTI-----HLEAHSRTLS---SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYIN 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767957873 269 SGLLALGNVISALGDPRRksSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRAR 339
Cdd:cd01375 266 KSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
6-397 |
8.56e-63 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 235.60 E-value: 8.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 6 VKVAVRIRPLLCKEalhNHQVCVRVIPNSQQVIIGRdrVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQ 85
Cdd:PLN03188 100 VKVIVRMKPLNKGE---EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 86 TGSGKTYTIGGGHIASVVEG----QKGIIPRAIQEIFQSISEHP------SIDFNVKVSYIEVYKEDLRDLLEleTSMKD 155
Cdd:PLN03188 175 TGSGKTYTMWGPANGLLEEHlsgdQQGLTPRVFERLFARINEEQikhadrQLKYQCRCSFLEIYNEQITDLLD--PSQKN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 156 LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTisiCQVHKNMEAAEDG-SWYSpr 234
Cdd:PLN03188 253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT---CVVESRCKSVADGlSSFK-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 235 hiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR--KSSHIPYRDAKITRLLKDSLGGSAKT 312
Cdd:PLN03188 328 --TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 313 VMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDrIDEMEFEIKLLREALQSQQAGVSQTTQINREGSPDTN 392
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD-VNFLREVIRQLRDELQRVKANGNNPTNPNVAYSTAWN 484
|
....*
gi 767957873 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 |
1.71e-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: 98.57 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 26 VCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCiKPLVLSLIEGYN-ATVFAYGQTGSGKTYTIggghiasvve 104
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 105 gqKGIIPRAIQEIFqsisehpsidfnvkvSYIEVYKEDLRDLLEletsmkdlhiredekgntvivgakECHVESAGEVMS 184
Cdd:cd01363 70 --KGVIPYLASVAF---------------NGINKGETEGWVYLT------------------------EITVTLEDQILQ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 185 LLEMGNAARhTGTTQMNEHSSRSHAIFTIsicqvhknmeaaedgswysprhivskfhFVDLAGSERvtktgntgerfkes 264
Cdd:cd01363 109 ANPILEAFG-NAKTTRNENSSRFGKFIEI----------------------------LLDIAGFEI-------------- 145
|
250
....*....|....*.
gi 767957873 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 |
2.72e-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: 85.73 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 6 VKVAVRIRPLLCKEAlhnhQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQ 85
Cdd:pfam16796 22 IRVFARVRPELLSEA----QIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGYNVCIFAYGQ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767957873 86 TGSGKTytiggghiasvvegqKGIIPRAIQEIFQSISE-HPSIDFNVKVSYIEVYKEDLRDLL 147
Cdd:pfam16796 97 TGSGSN---------------DGMIPRAREQIFRFISSlKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
673-1173 |
9.74e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 673 DDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSD---LENEDLKIDCLQESQEL----NLQKLKNSERIL 745
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkKAEEKKKADEAKKAEEKkkadEAKKKAEEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 746 TEAKQKMRELtiniKMKEDLIKEliktgndaKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKL 825
Cdd:PTZ00121 1318 DEAKKKAEEA----KKKADAAKK--------KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 826 QKEFRKKMDAAKLRVQVLQKKQQDSKKLAslsiQNEKRANELEQsvdhmKYQKIQLQRKLREENEKRKQLDAVIKRDQQK 905
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKKAA----AAKKKADEAKK-----KAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 906 IKEIQLKTGQEEglKPKAEDLDACNLKRRKGSFGSIDHLQEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNL 985
Cdd:PTZ00121 1457 KKAEEAKKKAEE--AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 986 SRGEANVLEKLACLSPVEirtilfryfnKVVNLREAERKQQLyneEMKMKVLERDNM-VRELESALDHLKLQCDRRLTLQ 1064
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELK----------KAEELKKAEEKKKA---EEAKKAEEDKNMaLRKAEEAKKAEEARIEEVMKLY 1601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1065 QKEHEQKMQLLLhhfKEQDGEGIMETFKtyedKIQQLEKDLYFYKKTSRDHKKKLKELVGEAIRRQLAPSEYQEagdgvl 1144
Cdd:PTZ00121 1602 EEEKKMKAEEAK---KAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK------ 1668
|
490 500
....*....|....*....|....*....
gi 767957873 1145 KPEGGGMLSEELKWASRPESMKLSGRERE 1173
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
789-1122 |
1.59e-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: 59.30 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 789 KLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELE 868
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 869 QSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIqlktgqEEGLKPKAEDLDACNLKRRKGSFGSIDHLQEEH 948
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL------REALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 949 vlfQLEEGIEALEAAIEYRNESIQN---RQKSLRASFHNLSRgEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQ 1025
Cdd:TIGR02168 835 ---ATERRLEDLEEQIEELSEDIESlaaEIEELEELIEELES-ELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1026 QLYNEEMkmkvlerdnmvRELESALDHLKLQCDRrltLQQKEHEQKMQLLLHHfkEQDGEGIMETFKTYEDKIQQLEKDL 1105
Cdd:TIGR02168 911 SELRREL-----------EELREKLAQLELRLEG---LEVRIDNLQERLSEEY--SLTLEEAEALENKIEDDEEEARRRL 974
|
330
....*....|....*..
gi 767957873 1106 yfykktsRDHKKKLKEL 1122
Cdd:TIGR02168 975 -------KRLENKIKEL 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
711-1184 |
2.20e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 711 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDlIKELIKTGNDAKSVSKQYSLKVTKL 790
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 791 EHDAEQAKVELIETQKQLQELENKDlSDVAMKVKLQKEFRKKMDAAKLRVQVLQK-------KQQDSKKLASLSIQnekr 863
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKE-ERLEELKKKLKELEKRLEELEERHELYEEakakkeeLERLKKRLTGLTPE---- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 864 anELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKrdqqkikeiQLKTGQEEGLKPKAEdldaCNLKRRKgsfgsidh 943
Cdd:PRK03918 388 --KLEKELEELEKAKEEIEEEISKITARIGELKKEIK---------ELKKAIEELKKAKGK----CPVCGRE-------- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 944 LQEEHVLFQLEEGIEALEaAIEYRNESIQNRQKSLRASFHNLsRGEANVLEKLACLSPV--EIRTILFRYfnKVVNLREA 1021
Cdd:PRK03918 445 LTEEHRKELLEEYTAELK-RIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELaeQLKELEEKL--KKYNLEEL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1022 ERKQQLYnEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLL-LHHFKEQDGegiMETFKTYEDKIQQ 1100
Cdd:PRK03918 521 EKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAeLLKELEELG---FESVEELEERLKE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1101 LEKdlyFYKK--TSRDHKKKLKELVGEAIRRQLAPSEYQEAGDGVLK--PEGGGMLSEELKWASRPESMKLSGREREMDS 1176
Cdd:PRK03918 597 LEP---FYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKrlEELRKELEELEKKYSEEEYEELREEYLELSR 673
|
....*...
gi 767957873 1177 SASSLRTQ 1184
Cdd:PRK03918 674 ELAGLRAE 681
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
704-1096 |
2.38e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 704 ELSDTQDETQKSDLEN---EDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELtiniKMKEDLIK--ELIKTGNDAKS 778
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA----KKAEEAKKkaEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 779 VSKQySLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAK---LRVQVLQKKQQDSKKLAS 855
Cdd:PTZ00121 1478 KAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeAKKAEEKKKADELKKAEE 1556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 856 LSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEglKPKAEDLDACNLKRRK 935
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA--KIKAEELKKAEEEKKK 1634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 936 GSFGSIDHLQEEHVLFQL--EEGIEALEAAIEYRNESIQNR--QKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRY 1011
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1012 FNKVVNLREAERKQQLYNEEMKMKVLERDNMVREL------ESALDHLKLQCDRRLTLQQKEHEQKMQlllHHFKEQDGE 1085
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE---EELDEEDEK 1791
|
410
....*....|.
gi 767957873 1086 GIMETFKTYED 1096
Cdd:PTZ00121 1792 RRMEVDKKIKD 1802
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
704-1197 |
7.53e-08 |
|
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: 57.29 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 704 ELSDTQDETQKS--DLENEDLKIDCLQESQELNLQKLKNSERiltEAKQKMRELTINIKMKEDLiKELIKTGNDAKSVSK 781
Cdd:pfam02463 245 LLRDEQEEIESSkqEIEKEEEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKL-ERRKVDDEEKLKESE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 782 QyslKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNE 861
Cdd:pfam02463 321 K---EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 862 KRANELEQSVDhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKpkaEDLDACNLKRRKGSFGSI 941
Cdd:pfam02463 398 ELKSEEEKEAQ----LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE---LEKQELKLLKDELELKKS 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 942 DHLQEEHVLFQLEEGIEALEAAIE-----YRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVV 1016
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKleersQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1017 NLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQcdrRLTLQQKEHEQKMQLLLHHFKEQDGEGIMETFKTYED 1096
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLP---LKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEG 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1097 KIQQLEKDLyfykktSRDHKKKLKELVGEAIRRQLAPSEYQEAGDGVLKPEGGGMLSEELKWASRPESMKLSGREREMDS 1176
Cdd:pfam02463 628 ILKDTELTK------LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
490 500
....*....|....*....|.
gi 767957873 1177 SASSLRTQPNPQKLWEDIPEL 1197
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEEL 722
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
710-988 |
2.57e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 710 DETQKSDlenEDLKIDCLQESQEL----NLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSL 785
Cdd:PTZ00121 1537 DEAKKAE---EKKKADELKKAEELkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 786 KVTKLEHDAEQAKVELiETQKQLQELENKDlsdvAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLAS-LSIQNEKRA 864
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAE-EEKKKVEQLKKKE----AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeAKKAEEDEK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 865 NELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGlKPKAEDldacnLKRRKGSFGSIDHL 944
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-KKKAEE-----AKKDEEEKKKIAHL 1762
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767957873 945 QEEHVLfQLEEGIEALEAAIE--------YRNESIQNRQKSLRASFHNLSRG 988
Cdd:PTZ00121 1763 KKEEEK-KAEEIRKEKEAVIEeeldeedeKRRMEVDKKIKDIFDNFANIIEG 1813
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
747-1059 |
3.17e-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: 55.06 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 747 EAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslKVTKLEHDAEQAKvELIETQKQLQELEnKDLSDVAMKVKLQ 826
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELER--------------QLKSLERQAEKAE-RYKELKAELRELE-LALLVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 827 KEFRKKMDAAKLRVQVLQKKQQDSKKLASLSiQNEKRANELEQSVDH--------------MKYQKIQLQRKLREENEKR 892
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEEIEElqkelyalaneisrLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 893 KQLDAVIKRDQQKIKEIQLKTGQ-EEGLKPKAEDLDACNLKrrkgsfgsidhLQEEH-VLFQLEEGIEALEAAIEYRN-- 968
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAElEEKLEELKEELESLEAE-----------LEELEaELEELESRLEELEEQLETLRsk 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 969 --------ESIQNRQKSLRA----SFHNLSRGEANVLEKLACLSPVEIRTILFRyfnkVVNLREAERKQQLYNEEMKMKV 1036
Cdd:TIGR02168 388 vaqlelqiASLNNEIERLEArlerLEDRRERLQQEIEELLKKLEEAELKELQAE----LEELEEELEELQEELERLEEAL 463
|
330 340
....*....|....*....|...
gi 767957873 1037 LERDNMVRELESALDHLKLQCDR 1059
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQ 486
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
658-1181 |
4.55e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 658 EEQDKVLHCQFSDNSDDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSDlenEDLKIDCLQESQElnlqK 737
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE---AEAAADEAEAAEE----K 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 738 LKNSERILTEAKQKMRELtiniKMKedliKELIKTGNDAKSVSKQYSLKVTKLEhDAEQAKVELIETQKQLQELENKD-L 816
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAA----KKK----AEEKKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKADeA 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 817 SDVAMKVKLQKEFRKKMDAAKlRVQVLQKKQQDSKKLASLSIQNE--KRANELEQSVDHMKYQKIQLQRK---------L 885
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAKKKADEAKKAaeakkkadeA 1515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 886 REENEKRKQLDAviKRDQQKIKEIQLKTGQE----EGLKpKAEDLDACNLKR-----RKGSFGSIDHLQEEHVLFQLEEg 956
Cdd:PTZ00121 1516 KKAEEAKKADEA--KKAEEAKKADEAKKAEEkkkaDELK-KAEELKKAEEKKkaeeaKKAEEDKNMALRKAEEAKKAEE- 1591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 957 iEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKV 1036
Cdd:PTZ00121 1592 -ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1037 LERDNMVRELESALDHLKLQCDRrltLQQKEHEQKMQLLLHHFKEQDGEGIMETFKTYEDKIQQLEKdlyfYKKTSRDHK 1116
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEA---LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE----AKKEAEEDK 1743
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767957873 1117 KKLKEL-VGEAIRRQLA-PSEYQEAGDGVLKPEGGGMLSEELKWASRPESMKLSGREREMDSSASSL 1181
Cdd:PTZ00121 1744 KKAEEAkKDEEEKKKIAhLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
722-980 |
2.12e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 722 LKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVEL 801
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 802 IETQKQLQELENKDLSDVAMKVKLQKEfrkkMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRAN-ELEQSVDHMKYQKIQ 880
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEALLEAEaELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 881 LQRKLREENEKRKQLDAVIKRDQQKIKEI-QLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQEEHVLFQLEEGIEA 959
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLeRLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260
....*....|....*....|.
gi 767957873 960 LEAAIEYRNESIQNRQKSLRA 980
Cdd:COG1196 468 LLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-985 |
2.91e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 704 ELSDTQDETQKSDLENEDLKIDCLQESQELNLQK--LKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 781
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 782 QYSLKVTKLEHDAEQAKVELIETQKQLQELEN--KDLSDVAMKV--KLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLS 857
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAelTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 858 IQNEK---RANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIqlktgqEEGLKPKAEDLDACNLkRR 934
Cdd:TIGR02168 859 AEIEEleeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL------RRELEELREKLAQLEL-RL 931
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767957873 935 KGSFGSIDHLQEE-HVLFQLE-EGIEALEAAIEYRNESIQNRQKSLRASFHNL 985
Cdd:TIGR02168 932 EGLEVRIDNLQERlSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
711-932 |
6.18e-06 |
|
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: 50.79 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 711 ETQKSDLENE-----------DLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSV 779
Cdd:TIGR04523 390 ESQINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 780 SKQYSLKVTKLEHDAEQAKVELIETQKQLQEL--ENKDLSdvamkvKLQKEFRKKMDAAKLRVQVLQK-KQQDSKKLASL 856
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLneEKKELE------EKVKDLTKKISSLKEKIEKLESeKKEKESKISDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 857 -----SIQNEKRANELEQSVDHM--KYQKIQLQRKLREENEKRKQLDAVIKRDQQK--IKEIQLKTGQEEGLKPKAEDLD 927
Cdd:TIGR04523 544 edelnKDDFELKKENLEKEIDEKnkEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdlIKEIEEKEKKISSLEKELEKAK 623
|
....*
gi 767957873 928 ACNLK 932
Cdd:TIGR04523 624 KENEK 628
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
743-1106 |
6.78e-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: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 743 RILTEAKQKMRELTINIKMKEDLIKELI----KTGNDAKSVSKQYSLKVTKLEHDAEQAKV-ELIETQKQLQELENKDLS 817
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLdYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 818 DVAMKVKLQKEFRKKMD--AAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQsvDHMKYQKIQLQRKLREENEKRKQL 895
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL--LKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 896 DAVIKRDQQKI----KEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQEEHVLFQLEEGIEALEAAIEYRNESI 971
Cdd:pfam02463 327 EKELKKEKEEIeeleKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 972 QNRQKSLRASFHNLSRGEANVLEKLAcLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKV---LERDNMVRELES 1048
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEIL-EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSedlLKETQLVKLQEQ 485
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 767957873 1049 ALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDGEGIMETFKTYEDKIQQLEKDLY 1106
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
723-938 |
8.28e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 723 KIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELI 802
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 803 ETQKQLQE-----------------LENKDLSDVAMKVKLQKEFrkkmdaAKLRVQVLQKKQQDSKKLASLSIQNEKRAN 865
Cdd:COG4942 101 AQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYL------APARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 866 ELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGL--------KPKAEDLDACNLKRRKGS 937
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiarleaeaAAAAERTPAAGFAALKGK 254
|
.
gi 767957873 938 F 938
Cdd:COG4942 255 L 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
736-969 |
1.05e-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: 49.38 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 736 QKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQElenkd 815
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 816 lsdvamkvkLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQN----EKRANELEQSVDHMKYQKIQLQRKLREENEK 891
Cdd:COG4942 95 ---------LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfldaVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767957873 892 RKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQEEHVlfQLEEGIEALEAAIEYRNE 969
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE--ELEALIARLEAEAAAAAE 241
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
776-909 |
1.83e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 776 AKSVSKQyslKVTKLEHDA----EQAKVElIETQKQLQELENKDLSDvAMKVKLQKEFR-KKMDAAKLRVQVLQKKQQDS 850
Cdd:PRK12704 25 RKKIAEA---KIKEAEEEAkrilEEAKKE-AEAIKKEALLEAKEEIH-KLRNEFEKELReRRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767957873 851 KKLASLsiqnEKRANELEQsvdhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEI 909
Cdd:PRK12704 100 RKLELL----EKREEELEK-------KEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
704-909 |
2.23e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 704 ELSDTQDETQKSDLE---NEDL--KIDCLQESQELNLQKLKNSERILTE----AKQKMRELTINIKMKEDLIKELIKTGN 774
Cdd:pfam17380 349 ELERIRQEERKRELErirQEEIamEISRMRELERLQMERQQKNERVRQEleaaRKVKILEEERQRKIQQQKVEMEQIRAE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 775 DAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSK--- 851
Cdd:pfam17380 429 QEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqam 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767957873 852 ----------------KLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAvIKRDQQKIKEI 909
Cdd:pfam17380 509 ieeerkrkllekemeeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEA-MEREREMMRQI 581
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
704-997 |
8.93e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 704 ELSDTQDETqkSDLENEdlkIDCLQESQELNLQKLKNSERILTEAKQkmrELTINIKMKEDLIKELiktgNDAKSVSKQY 783
Cdd:TIGR02169 710 ELSDASRKI--GEIEKE---IEQLEQEEEKLKERLEELEEDLSSLEQ---EIENVKSELKELEARI----EELEEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 784 SLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDV--AMKVKLQKEFRKK-------------MDAAKLRVQVLQKKQQ 848
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARlrEIEQKLNRLTLEKeylekeiqelqeqRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 849 DSK-KLASLSIQNEKRANELEQ----------SVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEE 917
Cdd:TIGR02169 858 NLNgKKEELEEELEELEAALRDlesrlgdlkkERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 918 GLKPKAEDLDACNLkrrkgsfgSIDHLQEEhvLFQLEEGIEALE----AAI-EYrnESIQNRQKSLRASFHNLSRGEANV 992
Cdd:TIGR02169 938 DPKGEDEEIPEEEL--------SLEDVQAE--LQRVEEEIRALEpvnmLAIqEY--EEVLKRLDELKEKRAKLEEERKAI 1005
|
....*
gi 767957873 993 LEKLA 997
Cdd:TIGR02169 1006 LERIE 1010
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
732-1139 |
1.22e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 732 ELNLQKLKNSERILTEAKQKMRELTINIKMKEDL---IKELIKTGNDAKSVSKQYSLKVTKLEHDAE--QAKVELIETQK 806
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 807 QLQELENKdlsdvamkVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNE-----KRANELEQSVDHMKYQKIQL 881
Cdd:COG4717 147 RLEELEER--------LEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 882 QRKLREENEKRKQL--DAVIKRDQQKIKEIQLKTGQEEGLkpkaedldaCNLKRRKGSFGSidHLQEEHVLFQLEEGIEA 959
Cdd:COG4717 219 QEELEELEEELEQLenELEAAALEERLKEARLLLLIAAAL---------LALLGLGGSLLS--LILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 960 LEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLAC---LSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKV 1036
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1037 L--ERDNMVREL----ESALDHLKLQCDRRLTLQQKEHEQKMQLLLhHFKEQDGEGIMETFKTYEDKIQQLEKDLYFYKK 1110
Cdd:COG4717 368 LeqEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEE-LLGELEELLEALDEEELEEELEELEEELEELEE 446
|
410 420
....*....|....*....|....*....
gi 767957873 1111 TSRDHKKKLKELVGEaIRRQLAPSEYQEA 1139
Cdd:COG4717 447 ELEELREELAELEAE-LEQLEEDGELAEL 474
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
736-916 |
1.58e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 736 QKLKNSERILTEAKQKMRELTINIkmkEDLIKELIKTGNDAKsvskQYSLKVTKLEHDAEQAKVELIETQKQLQELENKD 815
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKL---NELIASLEELERELE----QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 816 LSdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIqnekRANELEQSvdhmkyqkiqlQRKLREENEKRKQl 895
Cdd:PRK00409 568 LE------EAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV----KAHELIEA-----------RKRLNKANEKKEK- 625
|
170 180
....*....|....*....|.
gi 767957873 896 daviKRDQQKIKEIQLKTGQE 916
Cdd:PRK00409 626 ----KKKKQKEKQEELKVGDE 642
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
729-976 |
1.60e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 729 ESQELNLQKLKNSERILTEAKQkmRELtinikmkedlikELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVElietqkql 808
Cdd:pfam17380 338 EQERMAMERERELERIRQEERK--REL------------ERIRQEEIAMEISRMRELERLQMERQQKNERVR-------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 809 QELEnkdlsdVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQR-KLRE 887
Cdd:pfam17380 396 QELE------AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERlRQQE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 888 ENEKRKQLDAVI-KRDQQKIKEIQLKTGQEEglkpkaedldacnLKRRKGSFgsidhLQEEHVLFQLEEGIEALEAAI-- 964
Cdd:pfam17380 470 EERKRKKLELEKeKRDRKRAEEQRRKILEKE-------------LEERKQAM-----IEEERKRKLLEKEMEERQKAIye 531
|
250
....*....|...
gi 767957873 965 -EYRNESIQNRQK 976
Cdd:pfam17380 532 eERRREAEEERRK 544
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
708-1123 |
1.62e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 708 TQDETQK--SDLENEDLKIDCLQESQELNLQKL-KNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYS 784
Cdd:TIGR00606 689 TEAELQEfiSDLQSKLRLAPDKLKSTESELKKKeKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 785 LKVTKLEH-DAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNE-- 861
Cdd:TIGR00606 769 EQETLLGTiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEln 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 862 --------KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDldacnLKR 933
Cdd:TIGR00606 849 rkliqdqqEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK-----DQQ 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 934 RKGSFGSIDHLQEEHVLFQLEEGIEALEAAIEYRnESIQNRQKSLRASFhnLSRGEANVLEKLACLSPVEIRTILFRYFN 1013
Cdd:TIGR00606 924 EKEELISSKETSNKKAQDKVNDIKEKVKNIHGYM-KDIENKIQDGKDDY--LKQKETELNTVNAQLEECEKHQEKINEDM 1000
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1014 KVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDGEgIMETFKT 1093
Cdd:TIGR00606 1001 RLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVL-ALGRQKG 1079
|
410 420 430
....*....|....*....|....*....|
gi 767957873 1094 YEDKIQQLEKDLyfYKKTSRDHKKKLKELV 1123
Cdd:TIGR00606 1080 YEKEIKHFKKEL--REPQFRDAEEKYREMM 1107
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
728-936 |
2.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 728 QESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELiktgndaksvsKQYSLKVTKLEHDAEQAKVELIETQKQ 807
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-----------EELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 808 LQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLRE 887
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767957873 888 ENEKRKQLDAVIKRDQQKIKEIQLKtGQEEGLKPKAEDLDacNLKRRKG 936
Cdd:PRK03918 659 EEYEELREEYLELSRELAGLRAELE-ELEKRREEIKKTLE--KLKEELE 704
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
763-981 |
3.21e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 763 EDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKdlSDVAMK--VKLQKEFRKKMDAAKLRV 840
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE--IDKLQAeiAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 841 QVLQKKQQDSKKLASL----SIQNE-KRANELEQSVDHMKyQKIQLQRKLREENE-KRKQLDAVIKRDQQKIKEIQLKTG 914
Cdd:COG3883 93 RALYRSGGSVSYLDVLlgseSFSDFlDRLSALSKIADADA-DLLEELKADKAELEaKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767957873 915 QEEGLKPKAEDLdacnlkrrkgsfgsIDHLQEEHVlfQLEEGIEALEAAIEYRNESIQNRQKSLRAS 981
Cdd:COG3883 172 ELEAQQAEQEAL--------------LAQLSAEEA--AAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
711-917 |
3.33e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 711 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKEL----------IKTGNDAKSVS 780
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLnsdlskinseIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 781 KQYSLK------------------VTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEF---RKKMDAAKLR 839
Cdd:TIGR04523 123 EVELNKlekqkkenkknidkflteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIdkiKNKLLKLELL 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767957873 840 VQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLdaviKRDQQKIKEiQLKTGQEE 917
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL----KDEQNKIKK-QLSEKQKE 275
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
752-889 |
4.55e-04 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 44.26 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 752 MRELTINIKMKEDLIKELIKTGNDA-----------KSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVA 820
Cdd:smart00435 233 LQEQLKELTAKDGNVAEKILAYNRAnrevailcnhqRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRK 312
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767957873 821 MKVKLQKEFRkkmdaaKLRVQVLQKKQQDSKKLASlsiqnEKRANELEQSVdhmkyQKIQLQRKLREEN 889
Cdd:smart00435 313 LKSKFERDNE------KLDAEVKEKKKEKKKEEKK-----KKQIERLEERI-----EKLEVQATDKEEN 365
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
850-1139 |
4.57e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 850 SKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQ--------EEGLKP 921
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQleqeeeklKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 922 KAEDLDACNLKRRKGSfGSIDHLQEEhvLFQLEEGIEALEAAIE-----YRNESIQNRQKSLRASFHNLSRGEANVLEKL 996
Cdd:TIGR02169 742 LEEDLSSLEQEIENVK-SELKELEAR--IEELEEDLHKLEEALNdlearLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 997 ACLSPVEIRTILFRyfNKVVNL---------REAERKQQLYN-----EEMKMKVLERDNMVRELESALDHLKLQCDRRLT 1062
Cdd:TIGR02169 819 QKLNRLTLEKEYLE--KEIQELqeqridlkeQIKSIEKEIENlngkkEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1063 ----LQQKEHEQKMQL--LLHHFKEQDG--EGIMETFKTYEDKIQQLEKdlYFYKKTSRDHKKKLKELVGEAIRR----- 1129
Cdd:TIGR02169 897 qlreLERKIEELEAQIekKRKRLSELKAklEALEEELSEIEDPKGEDEE--IPEEELSLEDVQAELQRVEEEIRAlepvn 974
|
330
....*....|
gi 767957873 1130 QLAPSEYQEA 1139
Cdd:TIGR02169 975 MLAIQEYEEV 984
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
733-910 |
6.12e-04 |
|
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: 42.99 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 733 LNLQKLKNSeriLTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELE 812
Cdd:COG1579 10 LDLQELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 813 N-KDLSDvamkvkLQKEfrkkMDAAKLRVQVLQKKQqdskklaslsIQNEKRANELEQSVDHMKYQKIQLQRKLreeNEK 891
Cdd:COG1579 87 NnKEYEA------LQKE----IESLKRRISDLEDEI----------LELMERIEELEEELAELEAELAELEAEL---EEK 143
|
170
....*....|....*....
gi 767957873 892 RKQLDAVIKRDQQKIKEIQ 910
Cdd:COG1579 144 KAELDEELAELEAELEELE 162
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
715-910 |
6.36e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 715 SDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslKVTKLEHDA 794
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------------EIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 795 EQAKVELIETQKQLQE-----------LENKDLSDVAMKVKLQKEFrkkMDAAKlrvQVLQKKQQDSKKLASLSIQNEKR 863
Cdd:COG3883 82 EERREELGERARALYRsggsvsyldvlLGSESFSDFLDRLSALSKI---ADADA---DLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767957873 864 ANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ 910
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
731-1051 |
9.03e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 731 QELNLQKLKNSERILT---EAKQKMRELTINIKMKEDLIK---ELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIET 804
Cdd:TIGR01612 1069 ELLNKEILEEAEINITnfnEIKEKLKHYNFDDFGKEENIKyadEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEI 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 805 QKQLQELEnkDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVD-HMKYQKIQLQR 883
Cdd:TIGR01612 1149 KAQINDLE--DVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGiNLSYGKNLGKL 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 884 KLREENEKRKQLDAVIK------RDQQKIKE----IQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHlqEEHVLFQL 953
Cdd:TIGR01612 1227 FLEKIDEEKKKSEHMIKameayiEDLDEIKEkspeIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKH--DENISDIR 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 954 EEGIEALEAaiEYRNESIQNRQKSLRASFHNLSRGEANV---LEKLACLSPV----EIRTIL--FRYFNKVVNLREAERK 1024
Cdd:TIGR01612 1305 EKSLKIIED--FSEESDINDIKKELQKNLLDAQKHNSDInlyLNEIANIYNIlklnKIKKIIdeVKEYTKEIEENNKNIK 1382
|
330 340 350
....*....|....*....|....*....|.
gi 767957873 1025 QQLYNEEMKMKVLERDNMVRE----LESALD 1051
Cdd:TIGR01612 1383 DELDKSEKLIKKIKDDINLEEckskIESTLD 1413
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
736-1129 |
1.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 736 QKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKd 815
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 816 lsdvamkvklQKEFRKKMDAAKLRVQVLQKKQQDSKK-------------LASLSIQNEKRANELEQSVDHMK---YQKI 879
Cdd:PRK03918 400 ----------KEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpVCGRELTEEHRKELLEEYTAELKrieKELK 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 880 QLQRKLREENEKRKQLDAVIKRDQQKIKEIQLkTGQEEGLKPKAEDLDACNLKRRKGSFgsiDHLQEEhvLFQLEEGIEA 959
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKEL-AEQLKELEEKLKKYNLEELEKKAEEY---EKLKEK--LIKLKGEIKS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 960 LEAAIEyRNESIQNRQKSLRASFHNLSRGEANVLEKL-----ACLSPVEIR-TILFRYFNKVVNLREAERKQQLYNEEMK 1033
Cdd:PRK03918 544 LKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERlKELEPFYNEYLELKDAEKELEREEKELK 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1034 M----------KVLERDNMVRELESALDHLKLQCDrrltlqQKEHEQKMQLLLHhfKEQDGEGIMETFKTYEDKIQQLEK 1103
Cdd:PRK03918 623 KleeeldkafeELAETEKRLEELRKELEELEKKYS------EEEYEELREEYLE--LSRELAGLRAELEELEKRREEIKK 694
|
410 420
....*....|....*....|....*...
gi 767957873 1104 DLYFYK--KTSRDHKKKLKELVGEAIRR 1129
Cdd:PRK03918 695 TLEKLKeeLEEREKAKKELEKLEKALER 722
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
736-1053 |
1.56e-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: 43.12 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 736 QKLKNSERILTEAKQKMRELTINIKMKEDLIKELiktgndaksvsKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKD 815
Cdd:TIGR01612 1541 KTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEI-----------KKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKF 1609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 816 LSDVAMKVKLQkefrkkmdaaklrvQVLQKKQQDSKKLASLSI--------QNEKRANELEQSVDHMKYQKIQLQRKLRE 887
Cdd:TIGR01612 1610 LKISDIKKKIN--------------DCLKETESIEKKISSFSIdsqdtelkENGDNLNSLQEFLESLKDQKKNIEDKKKE 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 888 ENEKRKQLDAV-IKRDQ----------QKIKEIQLKTGQE-EGLKPKAEDldacNLKRRKGSFGSIDHlqeehvlfqleE 955
Cdd:TIGR01612 1676 LDELDSEIEKIeIDVDQhkknyeigiiEKIKEIAIANKEEiESIKELIEP----TIENLISSFNTNDL-----------E 1740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 956 GIEALEAAIEYRNEsiqnrQKSLRASFHNLSRGEANVLEKLA--CLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMK 1033
Cdd:TIGR01612 1741 GIDPNEKLEEYNTE-----IGDIYEEFIELYNIIAGCLETVSkePITYDEIKNTRINAQNEFLKIIEIEKKSKSYLDDIE 1815
|
330 340
....*....|....*....|
gi 767957873 1034 MKvlERDNMVRELESALDHL 1053
Cdd:TIGR01612 1816 AK--EFDRIINHFKKKLDHV 1833
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
706-976 |
1.67e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 706 SDTQDETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNdaksvskqysl 785
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE----------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 786 kvtKLEHDAEQAKVELIETQKQLQELENKDlsdvAMKVKLQKEFRKKMDAAKLRVQVLQKKqqdSKKLASLSIQNEKRAN 865
Cdd:TIGR04523 423 ---LLEKEIERLKETIIKNNSEIKDLTNQD----SVKELIIKNLDNTRESLETQLKVLSRS---INKIKQNLEQKQKELK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 866 ELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQ-EEGLKPKAEDLDACNLKrrkgsfGSIDHL 944
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDlEDELNKDDFELKKENLE------KEIDEK 566
|
250 260 270
....*....|....*....|....*....|..
gi 767957873 945 QEEhvLFQLEEGIEALEAAIEYRNESIQNRQK 976
Cdd:TIGR04523 567 NKE--IEELKQTQKSLKKKQEEKQELIDQKEK 596
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
787-1144 |
1.83e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 787 VTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQ-QDSKKLASLSIQNEKRAN 865
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 866 ELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLdacnLKRRKgsfgSIDHLQ 945
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK----LERRK----VDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 946 EEHVLFQLEEGIEALEAAIEYRNEsIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQ 1025
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEE-LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1026 QlYNEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDGEGI-METFKTYEDKIQQLEKD 1104
Cdd:pfam02463 395 E-ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKqELKLLKDELELKKSEDL 473
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767957873 1105 LYFYKKTSRDHKKKLKELVGEAIRRQLAPSEYQEAGDGVL 1144
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLL 513
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
752-907 |
2.10e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 752 MRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRK 831
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767957873 832 KMDAAKLRVQVLQKKQQDSKKLAslsiqneKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIK 907
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLT-------QRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
820-919 |
2.12e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 820 AMKVKLQKEFRKKMDAAKLRVQVLQKKQQD-SKKLASLSI-QNEKRANELEQSVdhMKYQkiQLQRKLREENEKRKQldA 897
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKlQKDAATLSEaAREKKEKELQKKV--QEFQ--RKQQKLQQDLQKRQQ--E 91
|
90 100
....*....|....*....|..
gi 767957873 898 VIKRDQQKIKEIQLKTGQEEGL 919
Cdd:smart00935 92 ELQKILDKINKAIKEVAKKKGY 113
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
805-980 |
2.78e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 805 QKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQK------ 878
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllply 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 879 ---IQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQ----EEGLKPKAEDLDACNLKRRKGSFGSIDHLQEEhvLF 951
Cdd:COG4717 132 qelEALEAELAELPERLEELEERLEELRELEEELEELEAElaelQEELEELLEQLSLATEEELQDLAEELEELQQR--LA 209
|
170 180
....*....|....*....|....*....
gi 767957873 952 QLEEGIEALEAAIEYRNESIQNRQKSLRA 980
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
711-917 |
2.86e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 711 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAksvskqySLKVTKL 790
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM-------TLELKKH 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 791 EHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRvqvLQKKQQDSKKLASLSIQNEKRANELEQS 870
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK---LDKSEENARSIEYEVLKKEKQMKILENK 595
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767957873 871 VDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEE 917
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE 642
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
826-910 |
3.43e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 38.70 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 826 QKEFRKKMDAAKLRVQVLQKKQQdskklaslsiQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQK 905
Cdd:pfam13863 19 REEIERLEELLKQREEELEKKEQ----------ELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQ 88
|
....*
gi 767957873 906 IKEIQ 910
Cdd:pfam13863 89 IEELK 93
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
721-1086 |
3.76e-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: 41.64 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 721 DLKidcLQEsqelnLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVE 800
Cdd:pfam15921 527 DLK---LQE-----LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 801 LIETQKQLQELEN-KDLSDVAMK------VKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDH 873
Cdd:pfam15921 599 INDRRLELQEFKIlKDKKDAKIRelearvSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 874 MKyqkiqlqRKLREENEKrkqldavIKRDQQKIKeIQLKTGQEEGLKPKAedldacNLKRRKGSFGsidHLQEEHVLFQL 953
Cdd:pfam15921 679 LK-------RNFRNKSEE-------METTTNKLK-MQLKSAQSELEQTRN------TLKSMEGSDG---HAMKVAMGMQK 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 954 E-----EGIEALEAAIEYRNESIQNRQKSLrasfHNLSRGEANVLEKLACLSPVEirtilfryfNKVVNLREAERKQQly 1028
Cdd:pfam15921 735 QitakrGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELSTVATEK---------NKMAGELEVLRSQE-- 799
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767957873 1029 nEEMKMKVLerdNMvrelESALDHLKLQCDRRLTLQQKEHEQKMQLLLHH---FKEQDGEG 1086
Cdd:pfam15921 800 -RRLKEKVA---NM----EVALDKASLQFAECQDIIQRQEQESVRLKLQHtldVKELQGPG 852
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
735-1123 |
3.91e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.74 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 735 LQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAK--------SVSKQYSLKVTKLEHDAEQAKVeLIETQK 806
Cdd:PTZ00440 392 IETLLDSEYFISKYTNIISLSEHTLKAAEDVLKENSQKIADYAlysnleiiEIKKKYDEKINELKKSINQLKT-LISIMK 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 807 ---QLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQ----QDSKKLASLSIQNEKRANELEQSVDHMKYQKI 879
Cdd:PTZ00440 471 sfyDLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNnivnNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQ 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 880 QLQRKLREENEKRKQLDAV------IKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNL-------KRRKGSFGSIDHLQE 946
Cdd:PTZ00440 551 SIETLIKDEKLKRSMKNDIknkikyIEENVDHIKDIISLNDEIDNIIQQIEELINEALfnkekfiNEKNDLQEKVKYILN 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 947 EHVLFQLEEGIEALEAAIE------YRNESIQNRQkslraSFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLRE 1020
Cdd:PTZ00440 631 KFYKGDLQELLDELSHFLDdhkylyHEAKSKEDLQ-----TLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKE 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 1021 AERKQQLYNEEMKM-KVLER-DNMVRELESALDHLKLQcDRRLTLQQKEHEQKMQLLLHHFKEQD-----GEGIMETFKT 1093
Cdd:PTZ00440 706 NIIKKQLNNIEQDIsNSLNQyTIKYNDLKSSIEEYKEE-EEKLEVYKHQIINRKNEFILHLYENDkdlpdGKNTYEEFLQ 784
|
410 420 430
....*....|....*....|....*....|
gi 767957873 1094 YEDKIQQLEKDLYFYKKTSRDHKKKLKELV 1123
Cdd:PTZ00440 785 YKDTILNKENKISNDINILKENKKNNQDLL 814
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-994 |
4.15e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 703 VELSDTQDETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQ 782
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 783 YSLKVTKLEHDAEQAKVELIETQKQLQELENkdlsdvamkvkLQKEFRKKMDAAKLRVQVLQKKQQDSkklaslsiqnEK 862
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLN-----------ERASLEEALALLRSELEELSEELREL----------ES 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 863 RANELEQsvdhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRkgsfgsid 942
Cdd:TIGR02168 909 KRSELRR-------ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR-------- 973
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767957873 943 hlqeehvLFQLEEGIEAL----EAAI-EYrnESIQNRQKSLRASFHNLSRGEANVLE 994
Cdd:TIGR02168 974 -------LKRLENKIKELgpvnLAAIeEY--EELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
820-919 |
4.20e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 820 AMKVKLQKEFRKKMDAAKLRVQVLQKKQQD-SKKLASLSIQNEKRANELEQsvdhmKYQKIQ-LQRKLREENEKRKQldA 897
Cdd:pfam03938 19 AAQAQLEKKFKKRQAELEAKQKELQKLYEElQKDGALLEEEREEKEQELQK-----KEQELQqLQQKAQQELQKKQQ--E 91
|
90 100
....*....|....*....|..
gi 767957873 898 VIKRDQQKIKEIQLKTGQEEGL 919
Cdd:pfam03938 92 LLQPIQDKINKAIKEVAKEKGY 113
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
709-979 |
6.73e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 709 QDETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKtgndaKSVSKQYSLKVT 788
Cdd:pfam02463 213 YQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK-----EEEKEKKLQEEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 789 KLEHDAEQAKVElietqKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKlrvQVLQKKQQDSKKLASLSIQNEKRANELE 868
Cdd:pfam02463 288 LKLLAKEEEELK-----SELLKLERRKVDDEEKLKESEKEKKKAEKELK---KEKEEIEELEKELKELEIKREAEEEEEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 869 qsvdhmkyqkiQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFgsiDHLQEEH 948
Cdd:pfam02463 360 -----------ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE---DLLKEEK 425
|
250 260 270
....*....|....*....|....*....|.
gi 767957873 949 VlfQLEEGIEALEAAIEYRNESIQNRQKSLR 979
Cdd:pfam02463 426 K--EELEILEEEEESIELKQGKLTEEKEELE 454
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
705-895 |
6.77e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 705 LSDTQ---DETQKSDLENEDLKIDCLQESQEL-----NLQKLKNSEriLTEAKQKMRELTInikmkEDLIKELIKTGNDA 776
Cdd:PRK11281 65 LEQTLallDKIDRQKEETEQLKQQLAQAPAKLrqaqaELEALKDDN--DEETRETLSTLSL-----RQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 777 KSVSK---QYSLKVTKLEHDAEQAKVELIETQKQLQELEN---------KDLSDvAMKVKLQKE---------FRKKMDA 835
Cdd:PRK11281 138 QNAQNdlaEYNSQLVSLQTQPERAQAALYANSQRLQQIRNllkggkvggKALRP-SQRVLLQAEqallnaqndLQRKSLE 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767957873 836 AKLRVQVLQKKQQDskkLASLSIQ-------------NEKRANELEQSVDHM----KYQKIQLQRKLREENEKRKQL 895
Cdd:PRK11281 217 GNTQLQDLLQKQRD---YLTARIQrlehqlqllqeaiNSKRLTLSEKTVQEAqsqdEAARIQANPLVAQELEINLQL 290
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
690-925 |
8.14e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 690 RSWIQKPDSVCSLVELSDTQDEtqksdLENEDLKIDCLQESQELNLQKLKNsERILTEAKqkmreLTINIKMKEDLIKEL 769
Cdd:COG5022 882 RQLQELKIDVKSISSLKLVNLE-----LESEIIELKKSLSSDLIENLEFKT-ELIARLKK-----LLNNIDLEEGPSIEY 950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 770 IKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQ--KQLQELENKDlSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQ 847
Cdd:COG5022 951 VKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREgnKANSELKNFK-KELAELSKQYGALQESTKQLKELPVEVAELQ 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 848 QDSKKLAS--------LSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGL 919
Cdd:COG5022 1030 SASKIISSestelsilKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLV 1109
|
....*.
gi 767957873 920 KPKAED 925
Cdd:COG5022 1110 KPANVL 1115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
704-869 |
9.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 704 ELSDTQDETQK--SDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELI----KTGN--- 774
Cdd:COG3883 24 ELSELQAELEAaqAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyRSGGsvs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957873 775 ------DAKSVSkQYSLKVTKLEHDAEQAKvELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQ 848
Cdd:COG3883 104 yldvllGSESFS-DFLDRLSALSKIADADA-DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180
....*....|....*....|.
gi 767957873 849 dsKKLASLSIQNEKRANELEQ 869
Cdd:COG3883 182 --ALLAQLSAEEAAAEAQLAE 200
|
|
| |
