|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
4-342 |
0e+00 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 601.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 4 IPVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 84 GQTGSGKTYTIGGGHIASVVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELET-SMKDLHIRED 161
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDtFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEDGSWYSPRHIVSKFH 241
Cdd:cd01372 161 SKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNSTFTSKFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01372 241 FVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 320
|
330 340
....*....|....*....|.
gi 1034670642 322 SSNFDESLNSLKYANRARNIR 342
Cdd:cd01372 321 DSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
5-348 |
2.66e-145 |
|
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: 445.86 E-value: 2.66e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 78 ATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEH-PSIDFNVKVSYIEVYKEDLRDLLEleTSMKDL 156
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLN--PSSKKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEaaedgswySPRHI 236
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSS--------SGSGK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRrKSSHIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIA 303
|
330 340 350
....*....|....*....|....*....|..
gi 1034670642 317 CVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:smart00129 304 NVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-341 |
1.62e-138 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 427.37 E-value: 1.62e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 11 RIRPLLCKEALHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 84 GQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELETSMKD-LHIRED 161
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKErSEFSVKVSYLEIYNEKIRDLLSPSNKNKRkLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEdgswyspRHIVSKFH 241
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEE-------SVKTGKLN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 242 FVDLAGSERVTKTGN-TGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSP 320
Cdd:pfam00225 228 LVDLAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALADK--KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISP 305
|
330 340
....*....|....*....|.
gi 1034670642 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 |
2.16e-129 |
|
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: 403.17 E-value: 2.16e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 5 PVKVAVRIRPLLCKEAlhNHQVCVRVIPNSQQVIIG-------RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd00106 1 NVRVAVRVRPLNGREA--RSAKSVISVDGGKSVVLDppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 78 ATVFAYGQTGSGKTYTIGGGHiasvvEGQKGIIPRAIQEIFQSISEHPSIDFN--VKVSYIEVYKEDLRDLLELETSmKD 155
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKSSfsVSASYLEIYNEKIYDLLSPVPK-KP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 156 LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNMEAAEDgswyspRH 235
Cdd:cd00106 153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGE------SV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 236 IVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKssHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd00106 225 TSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMI 302
|
330 340
....*....|....*....|....
gi 1034670642 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 |
1.82e-111 |
|
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: 355.50 E-value: 1.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 6 VKVAVRIRPLLCKEALHNHQVCVRVI----------------------PNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNT 63
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdpkdeedgffhggsnNRDRRKRRNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 64 CIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISE-HPSIDFNVKVSYIEVYKED 142
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT------PQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 143 LRDLLEleTSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNM 222
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 223 EAAEDgswysprHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLL 302
Cdd:cd01370 234 SINQQ-------VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034670642 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 |
1.42e-110 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 352.02 E-value: 1.42e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSqqvIIGRDRV---FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQVAWEIDNDT---IYLVEPPstsFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 83 YGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLleLETSMKDLHIREDE 162
Cdd:cd01374 79 YGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDL--LSPTSQNLKIRDDV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 163 KGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcQVHKNMEAAEDGSwysprhIVSKFHF 242
Cdd:cd01374 151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI-ESSERGELEEGTV------RVSTLNL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01374 224 IDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAE 302
|
330
....*....|....*....
gi 1034670642 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 |
8.63e-109 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 347.53 E-value: 8.63e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII--GRD------RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 78 ATVFAYGQTGSGKTYTIGGghiASVVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELETSmKDL 156
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEG---KREDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKDQT-KRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhKNMEAAEDGSwyspRHI 236
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI----ECSEKGEDGE----NHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 237 -VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01371 231 rVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
|
330 340
....*....|....*....|....*.
gi 1034670642 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 |
2.78e-107 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 343.42 E-value: 2.78e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 11 RIRPLLCKEALHNHQVCVRVIPNSQQVII----GRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQT 86
Cdd:cd01366 9 RVRPLLPSEENEDTSHITFPDEDGQTIELtsigAKQKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIFAYGQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 87 GSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISE--HPSIDFNVKVSYIEVYKEDLRDLL-ELETSMKDLHIRED-E 162
Cdd:cd01366 88 GSGKTYTMEG------PPESPGIIPRALQELFNTIKElkEKGWSYTIKASMLEIYNETIRDLLaPGNAPQKKLEIRHDsE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 163 KGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhkNMEAAEDGSwysprHIVSKFHF 242
Cdd:cd01366 162 KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-----SGRNLQTGE-----ISVGKLNL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALgdpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01366 232 VDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAE 308
|
330 340
....*....|....*....|.
gi 1034670642 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 |
1.25e-101 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 327.36 E-value: 1.25e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 6 VKVAVRIRPLLCKEALHNHQVCVRvIPNSQQVIIGRD---RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVK-FDPEDTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 83 YGQTGSGKTYTIGGGHIAsvvEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLleLETSMKDLHIRED 161
Cdd:cd01369 83 YGQTSSGKTYTMEGKLGD---PESMGIIPRIVQDIFETIYSMDEnLEFHVKVSYFEIYMEKIRDL--LDVSKTNLSVHED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNMeaaEDGSWYSprhivSKFH 241
Cdd:cd01369 158 KNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ--ENV---ETEKKKS-----GKLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01369 228 LVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPS 305
|
330 340
....*....|....*....|
gi 1034670642 322 SSNFDESLNSLKYANRARNI 341
Cdd:cd01369 306 SYNESETLSTLRFGQRAKTI 325
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
6-348 |
3.25e-101 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 327.77 E-value: 3.25e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 6 VKVAVRIRPLLCKE---------ALHNHQVCVRVIPNSQQVIIGRDRV---FTFDFVF------GKN-STQDEVYNTCIK 66
Cdd:cd01365 3 VKVAVRVRPFNSREkernskcivQMSGKETTLKNPKQADKNNKATREVpksFSFDYSYwshdseDPNyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 67 PLVLSLIEGYNATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSI--SEHPSIDFNVKVSYIEVYKEDLR 144
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMG------TQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 145 DLLELETSMKD--LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNM 222
Cdd:cd01365 157 DLLNPKPKKNKgnLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQ--KRH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 223 EAAEDGSwyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR-----KSSHIPYRDAK 297
Cdd:cd01365 235 DAETNLT----TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034670642 298 ITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01365 311 LTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
6-348 |
4.84e-101 |
|
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: 326.98 E-value: 4.84e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII--------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 78 ATVFAYGQTGSGKTYTIGGGHiaSVVEGQK-------GIIPRAIQEIFQSISEHpSIDFNVKVSYIEVYKEDLRDLLELE 150
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMEGDR--SPNEEYTweldplaGIIPRTLHQLFEKLEDN-GTEYSVKVSYLEIYNEELFDLLSPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 151 TS-MKDLHIRED--EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEd 227
Cdd:cd01364 161 SDvSERLRMFDDprNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 228 gswyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprrKSSHIPYRDAKITRLLKDSLG 307
Cdd:cd01364 240 ------LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLG 310
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034670642 308 GSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01364 311 GRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
5-348 |
3.17e-84 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 279.78 E-value: 3.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIG-RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 84 GQTGSGKTYTIGG--GHIASVVEGQKGIIPRAIQEIFQSISEH-----PSIDFNVKVSYIEVYKEDLRDLleLETSMKDL 156
Cdd:cd01373 82 GQTGSGKTYTMWGpsESDNESPHGLRGVIPRIFEYLFSLIQREkekagEGKSFLCKCSFLEIYNEQIYDL--LDPASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmEAAEDGSWYSpRHI 236
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI-------ESWEKKACFV-NIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD-PRRKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01373 232 TSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAII 311
|
330 340 350
....*....|....*....|....*....|...
gi 1034670642 316 TCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01373 312 ANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
45-379 |
9.74e-84 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 286.25 E-value: 9.74e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 45 FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEH 124
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGT------EEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 125 PSI-DFNVKVSYIEVYKEDLRDLLELETsmKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEH 203
Cdd:COG5059 132 SMTkDFAVSISYLEIYNEKIYDLLSPNE--ESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 204 SSRSHAIFTISICQVHKNMeaaedgswysPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD 283
Cdd:COG5059 210 SSRSHSIFQIELASKNKVS----------GTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 284 PRrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDR-IDEMEFE 362
Cdd:COG5059 280 KK-KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReIEEIKFD 358
|
330
....*....|....*..
gi 1034670642 363 IKLLREALQSQQAGVSQ 379
Cdd:COG5059 359 LSEDRSEIEILVFREQS 375
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
5-337 |
1.90e-83 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 276.87 E-value: 1.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVI-IGRDRV----------FTFDFVFGKNSTQDEVYNTCIKPLVLSLI 73
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVhEPKLKVdltkyienhtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 74 EGYNATVFAYGQTGSGKTYTIGGGHiaSVVEGQKGIIPRAIQEIFQSISEHPSID-FNVKVSYIEVYKEDLRDLLEletS 152
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKLPYKDnLGVTVSFFEIYGGKVFDLLN---R 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 153 MKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmEAAEDGSwys 232
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------RDRGTNK--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 233 prhIVSKFHFVDLAGSER-VTKTGNTGERFKESIQINSGLLALGNVISALGDPrrkSSHIPYRDAKITRLLKDSL-GGSA 310
Cdd:cd01367 226 ---LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQN---KAHIPFRGSKLTQVLKDSFiGENS 299
|
330 340
....*....|....*....|....*..
gi 1034670642 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 |
3.39e-83 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 276.58 E-value: 3.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 5 PVKVAVRIRPLLCKEALHNHQVCVRVIpNSQQV----------------IIGRDRVFTFDFVFGKNSTQDEVYNTCIKPL 68
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVI-NSTTVvlhppkgsaanksernGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 69 VLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISehpsiDFNVKVSYIEVYKEDLRDLLE 148
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGS------PGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 149 LETS-----MKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNME 223
Cdd:cd01368 150 PSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 224 AAEDGSWYSPRhiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRRKSSHIPYRDAKITRL 301
Cdd:cd01368 230 GDVDQDKDQIT--VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLreNQLQGTNKMVPFRDSKLTHL 307
|
330 340 350
....*....|....*....|....*....|....
gi 1034670642 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 |
6.10e-80 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 266.29 E-value: 6.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 5 PVKVAVRIRPLLCKEALHNHQVCVRVIpNSQQVIIGRDRV------FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNA 78
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELADPRNhgetlkYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 79 TVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQsISEHPSIDFNVKVSYIEVYKEDLRDLLELETsmKDLHI 158
Cdd:cd01376 80 TVFAYGSTGAGKTFTMLG------SPEQPGLMPLTVMDLLQ-MTRKEAWALSFTMSYLEIYQEKILDLLEPAS--KELVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 159 REDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmeaAEDGSWYSPRHIVS 238
Cdd:cd01376 151 REDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV---------DQRERLAPFRQRTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 239 KFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRrksshIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALnkNLPR-----IPYRDSKLTRLLQDSLGGGSRCIMVA 296
|
330 340
....*....|....*....|...
gi 1034670642 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 |
2.53e-73 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 248.26 E-value: 2.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 33 NSQQviigRDRVFTFDFVFgKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHIASvveGQKGIIPR 112
Cdd:cd01375 42 NNQQ----EDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 113 AIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLL----ELETSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEM 188
Cdd:cd01375 114 ALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 189 GNAARHTGTTQMNEHSSRSHAIFTIsicqvHKNMEAAEDGswySPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQIN 268
Cdd:cd01375 194 GETNRIIASHTMNKNSSRSHCIFTI-----HLEAHSRTLS---SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYIN 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034670642 269 SGLLALGNVISALGDPRRksSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRAR 339
Cdd:cd01375 266 KSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
6-397 |
1.34e-61 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 232.13 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 6 VKVAVRIRPLLCKEalhNHQVCVRVIPNSQQVIIGRdrVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQ 85
Cdd:PLN03188 100 VKVIVRMKPLNKGE---EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 86 TGSGKTYTIGGGHIASVVEG----QKGIIPRAIQEIFQSISEHP------SIDFNVKVSYIEVYKEDLRDLLEleTSMKD 155
Cdd:PLN03188 175 TGSGKTYTMWGPANGLLEEHlsgdQQGLTPRVFERLFARINEEQikhadrQLKYQCRCSFLEIYNEQITDLLD--PSQKN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 156 LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTisiCQVHKNMEAAEDG-SWYSpr 234
Cdd:PLN03188 253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT---CVVESRCKSVADGlSSFK-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 235 hiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR--KSSHIPYRDAKITRLLKDSLGGSAKT 312
Cdd:PLN03188 328 --TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 313 VMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDrIDEMEFEIKLLREALQSQQAGVSQTTQINREGSPDTN 392
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD-VNFLREVIRQLRDELQRVKANGNNPTNPNVAYSTAWN 484
|
....*
gi 1034670642 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 |
1.48e-23 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 98.96 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 26 VCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCiKPLVLSLIEGYN-ATVFAYGQTGSGKTYTIggghiasvve 104
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 105 gqKGIIPRAIQEIFqsisehpsidfnvkvSYIEVYKEDLRDLLEletsmkdlhiredekgntvivgakECHVESAGEVMS 184
Cdd:cd01363 70 --KGVIPYLASVAF---------------NGINKGETEGWVYLT------------------------EITVTLEDQILQ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 185 LLEMGNAARhTGTTQMNEHSSRSHAIFTIsicqvhknmeaaedgswysprhivskfhFVDLAGSERvtktgntgerfkes 264
Cdd:cd01363 109 ANPILEAFG-NAKTTRNENSSRFGKFIEI----------------------------LLDIAGFEI-------------- 145
|
250
....*....|....*.
gi 1034670642 265 iqINSGLLALGNVISA 280
Cdd:cd01363 146 --INESLNTLMNVLRA 159
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
6-147 |
3.92e-19 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 85.35 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 6 VKVAVRIRPLLCKEAlhnhQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQ 85
Cdd:pfam16796 22 IRVFARVRPELLSEA----QIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGYNVCIFAYGQ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034670642 86 TGSGKTytiggghiasvvegqKGIIPRAIQEIFQSISE-HPSIDFNVKVSYIEVYKEDLRDLL 147
Cdd:pfam16796 97 TGSGSN---------------DGMIPRAREQIFRFISSlKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
658-1227 |
1.34e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 658 EEQDKVLHCQFSDNSDDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSDLENEDLKIDCLQESQELNLQK 737
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 738 LKNSERILTEAKQKMREltinIKMKEDLIKELIKTGNDAKSVSKqyslkvtklehdAEQAKVELIETQKQLQELENKD-L 816
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEE----KKKADEAKKKAEEDKKKADELKK------------AAAAKKKADEAKKKAEEKKKADeA 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 817 SDVAMKVKLQKEFRKKMDAAKlRVQVLQKKQQDSKKLASLSIQNE--KRANELEQSVDHMKyQKIQLQRKLREENEKRKQ 894
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAK-KKADEAKKAAEAKKKADE 1514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 895 LdaviKRDQQKIKEIQLKTGQEeglKPKAEDLDACNLKRRKgsfgsiDHLQKLDEQKKwlDEEVEKVLNQRQELEELEAD 974
Cdd:PTZ00121 1515 A----KKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKA------DELKKAEELKK--AEEKKKAEEAKKAEEDKNMA 1579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 975 LKKREAIVSKKEALLQE--KSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKiseqVEVLQKE 1052
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEvmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK----AEELKKA 1655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1053 KDQLQKRRHNVDEKLKngrvlspeeehvlfqlEEGIEALEAAIEYRNESIQNRQKSLRASfhnlsrgEANVLEKLACLSP 1132
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAE----------------EDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKKAEELKKKEA 1712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1133 VEIRtilfryfnKVVNLREAERKQQLYNEEMKMKVLERDNMVREL------ESALDHLKLQCDRRLTLQQKEHEQKMQll 1206
Cdd:PTZ00121 1713 EEKK--------KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE-- 1782
|
570 580
....*....|....*....|.
gi 1034670642 1207 lHHFKEQDGEGIMETFKTYED 1227
Cdd:PTZ00121 1783 -EELDEEDEKRRMEVDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
747-1312 |
1.80e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.95 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 747 EAK--QKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKdlsdvAMKVK 824
Cdd:PTZ00121 1241 EAKkaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK-----AEEAK 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 825 LQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLS-IQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQ 903
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 904 QKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVS 983
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 984 KKEALLQEKSHlENKKLRSSQALNTDSLKISTRLNLLEQEL---SEKNVQLQTSTAEEKTKISEQVEVLQKEK-DQLQK- 1058
Cdd:PTZ00121 1476 KKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAkkaEEAKKADEAKKAEEAKKADEAKKAEEKKKaDELKKa 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1059 ---RRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIE-----YRNESIQNRQKSLRASFHNLS----RGEANVLEK 1126
Cdd:PTZ00121 1555 eelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEevmklYEEEKKMKAEEAKKAEEAKIKaeelKKAEEEKKK 1634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1127 LACLSPVEIRTIlfryfNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQCDRrltLQQKEHEQKMQLL 1206
Cdd:PTZ00121 1635 VEQLKKKEAEEK-----KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA---LKKEAEEAKKAEE 1706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1207 LHHFKEQDGEGIMETFKTYEDKIQQLEKdlyfYKKTSRDHKKKLKEL-VGEAIRRQLA-PSEYQEAGDGVLKPEGGGMLS 1284
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEE----AKKEAEEDKKKAEEAkKDEEEKKKIAhLKKEEEKKAEEIRKEKEAVIE 1782
|
570 580
....*....|....*....|....*...
gi 1034670642 1285 EELKWASRPESMKLSGREREMDSSASSL 1312
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
789-1125 |
2.70e-13 |
|
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: 75.09 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 789 KLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELE 868
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 869 QSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIqlktgqEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLD 948
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL------REALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 949 EQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKN 1028
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1029 VQLQtSTAEEKTKISEQVEVLQKEKDQLQKR---RHNVD----EKLKNGRVLSPEE-EHVLFQLEEGIEAL----EAAI- 1095
Cdd:TIGR02168 915 RELE-ELREKLAQLELRLEGLEVRIDNLQERlseEYSLTleeaEALENKIEDDEEEaRRRLKRLENKIKELgpvnLAAIe 993
|
330 340 350
....*....|....*....|....*....|
gi 1034670642 1096 EYrnESIQNRQKSLRASFHNLSRGEANVLE 1125
Cdd:TIGR02168 994 EY--EELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
704-1119 |
1.53e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 704 ELSDTQDETQKSDLEN---EDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELtiniKMKEDLIK--ELIKTGNDAKS 778
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA----KKAEEAKKkaEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 779 VSKQySLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAK---LRVQVLQKKQQDSKKLAS 855
Cdd:PTZ00121 1478 KAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeAKKAEEKKKADELKKAEE 1556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 856 LSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEglKPKAEDLDACNLKRRK 935
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA--KIKAEELKKAEEEKKK 1634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 936 gsfgsIDHLQKLDEQKKWLDEEVEKvlnqRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKIST 1015
Cdd:PTZ00121 1635 -----VEQLKKKEAEEKKKAEELKK----AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1016 RLNLLEQELSEKNVQLQTSTAEEKTKISE----------QVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVlfqLE 1085
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEakkeaeedkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV---IE 1782
|
410 420 430
....*....|....*....|....*....|....
gi 1034670642 1086 EGIEALEaaiEYRNESIQNRQKSLRASFHNLSRG 1119
Cdd:PTZ00121 1783 EELDEED---EKRRMEVDKKIKDIFDNFANIIEG 1813
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
747-1118 |
7.51e-12 |
|
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: 70.47 E-value: 7.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 747 EAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslKVTKLEHDAEQAKvELIETQKQLQELEnKDLSdvamkVKLQ 826
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELER--------------QLKSLERQAEKAE-RYKELKAELRELE-LALL-----VLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 827 KEFRKKMDAAKlrvQVLQKKQQDSKKLASlsiqnekRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKI 906
Cdd:TIGR02168 235 EELREELEELQ---EELKEAEEELEELTA-------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 907 KEIQLKTGQ-EEGLKPKAEDLDacNLKRRKgsfgsIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKK 985
Cdd:TIGR02168 305 QILRERLANlERQLEELEAQLE--ELESKL-----DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 986 EALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQEL----SEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRH 1061
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1062 NVDEKLKNGRVLSPEEEHVLFQLEEGIEALEA---AIEYRNESIQNRQKSLRASFHNLSR 1118
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQArldSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
737-1260 |
8.76e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 8.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 737 KLKNSERILTEAKQKMRELTINIKMKE---DLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELEn 813
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELReelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 814 KDLSDVAMKVKLQKEFRKKMDA----AKLRVQVLQKKQQDSKKLASLsiqnEKRANELEQSVDHMKYQKIQLQRKLREEN 889
Cdd:PRK03918 273 KEIEELEEKVKELKELKEKAEEyiklSEFYEEYLDELREIEKRLSRL----EEEINGIEERIKELEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 890 EKRKQLdAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRkgsfgsidhLQKLDEQKKWLDEEVEKVLNQRQELE 969
Cdd:PRK03918 349 ELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE---------LEELEKAKEEIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 970 ELEADLKKreAIVSKKEAL-----------------LQEKSHLENKKLRSSQALNTDSL-KISTRLNLLEQELS-EKNVQ 1030
Cdd:PRK03918 419 KEIKELKK--AIEELKKAKgkcpvcgrelteehrkeLLEEYTAELKRIEKELKEIEEKErKLRKELRELEKVLKkESELI 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1031 LQTSTAEEKTKISEQVEVLQKEKDQLQKRRHnvdEKLKngrvlspeEEhvLFQLEEGIEALEAAIEyRNESIQNRQKSLR 1110
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKYNLEELEKKAEEY---EKLK--------EK--LIKLKGEIKSLKKELE-KLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1111 ASFHNLSRGEANVLEKL-----ACLSPVEIR-TILFRYFNKVVNLREAERKQQLYNEEMKM----------KVLERDNMV 1174
Cdd:PRK03918 563 KKLDELEEELAELLKELeelgfESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKleeeldkafeELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1175 RELESALDHLKLQCDrrltlqQKEHEQKMQLLLHhfKEQDGEGIMETFKTYEDKIQQLEKDLYFYK--KTSRDHKKKLKE 1252
Cdd:PRK03918 643 EELRKELEELEKKYS------EEEYEELREEYLE--LSRELAGLRAELEELEKRREEIKKTLEKLKeeLEEREKAKKELE 714
|
....*...
gi 1034670642 1253 LVGEAIRR 1260
Cdd:PRK03918 715 KLEKALER 722
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
731-1253 |
9.53e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 731 QELNLQKL----KNSERILTEAKQKMRELTINIKMKEDlIKELIKTgndaksvskqyslkvtklehdaeqAKVELIETQK 806
Cdd:PRK03918 153 QILGLDDYenayKNLGEVIKEIKRRIERLEKFIKRTEN-IEELIKE------------------------KEKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 807 QLQELEnkdlsdvamkvKLQKEFRKKMDAAKLRVQVLqkkqqdskklaslsiqnEKRANELEQSvdhmKYQKIQLQRKLR 886
Cdd:PRK03918 208 EINEIS-----------SELPELREELEKLEKEVKEL-----------------EELKEEIEEL----EKELESLEGSKR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 887 EENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKgsfgSIDHLQKLDEQKKWLDEEVEKVLNQRQ 966
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE----YLDELREIEKRLSRLEEEINGIEERIK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 967 ELEELEADLKKreaIVSKKEALLQEKSHLEN--KKLRSSQALNTDSLKISTRLNLLEQELSEKNVQlqtSTAEEKTKISE 1044
Cdd:PRK03918 332 ELEEKEERLEE---LKKKLKELEKRLEELEErhELYEEAKAKKEELERLKKRLTGLTPEKLEKELE---ELEKAKEEIEE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1045 QVEVLQKEKDQLQKRRHNVD---EKLKNGRVLSP------EEEHVLFQLEEGIEALEaAIEYRNESIQNRQKSLRASFHN 1115
Cdd:PRK03918 406 EISKITARIGELKKEIKELKkaiEELKKAKGKCPvcgrelTEEHRKELLEEYTAELK-RIEKELKEIEEKERKLRKELRE 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1116 LsRGEANVLEKLACLSPV--EIRTILFRYfnKVVNLREAERKQQLYnEEMKMKVLERDNMVRELESALDHLKLQCDRRLT 1193
Cdd:PRK03918 485 L-EKVLKKESELIKLKELaeQLKELEEKL--KKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034670642 1194 LQQKEHEQKMQLL-LHHFKEQDGegiMETFKTYEDKIQQLEKdlyFYKK--TSRDHKKKLKEL 1253
Cdd:PRK03918 561 LEKKLDELEEELAeLLKELEELG---FESVEELEERLKELEP---FYNEylELKDAEKELERE 617
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
789-1111 |
1.18e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 789 KLEHdAEQ--AKVELIETQ--KQLQELENKdlSDVAMKVK-LQKEFR-KKMDAAKLRVQVLQKKQQD-SKKLASLSIQNE 861
Cdd:COG1196 180 KLEA-TEEnlERLEDILGEleRQLEPLERQ--AEKAERYReLKEELKeLEAELLLLKLRELEAELEElEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 862 KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDacnlkrrkgsfgsi 941
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE-------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 942 dhlQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLE 1021
Cdd:COG1196 323 ---EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1022 QELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNES 1101
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
330
....*....|
gi 1034670642 1102 IQNRQKSLRA 1111
Cdd:COG1196 480 AELLEELAEA 489
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
709-1254 |
6.26e-10 |
|
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: 64.22 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 709 QDETQKSDLENEDLKIDCLQESQELNLQKLKNSERiltEAKQKMRELTINIKMKEDLiKELIKTGNDAKSVSKQyslKVT 788
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKL-ERRKVDDEEKLKESEK---EKK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 789 KLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELE 868
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 869 QSVDhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKpkaedldacnlkrrkgsfgsiDHLQKLD 948
Cdd:pfam02463 405 KEAQ----LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE---------------------LEKQELK 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 949 EQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRssqaLNTDSLKISTRLNLLEQELSEKN 1028
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL----LALIKDGVGGRIISAHGRLGDLG 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1029 VQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKS 1108
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1109 LRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAER----------KQQLYNEEMKMKVLERDNMVRELE 1178
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKsevkaslselTKELLEIQELQEKAESELAKEEIL 695
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034670642 1179 SALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDgEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKELV 1254
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ-DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
711-1253 |
1.82e-09 |
|
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: 62.35 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 711 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKEL----------IKTGNDAKSVS 780
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLnsdlskinseIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 781 KQYSLK------------------VTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEF---RKKMDAAKLR 839
Cdd:TIGR04523 123 EVELNKlekqkkenkknidkflteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIdkiKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 840 VQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQL----DAVIKRDQQKIKEI------ 909
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLkdeqNKIKKQLSEKQKELeqnnkk 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 910 ---------QLKTGQEEGLKPKAEDLDacnlKRRKGSFGSIDhlQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREA 980
Cdd:TIGR04523 283 ikelekqlnQLKSEISDLNNQKEQDWN----KELKSELKNQE--KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 981 IVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNvqlqtstaEEKTKISEQVEVLQKEKDQLQKRR 1060
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE--------KLNQQKDEQIKKLQQEKELLEKEI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1061 hnvdEKLKNGRVLSPEE----EHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIR 1136
Cdd:TIGR04523 429 ----ERLKETIIKNNSEikdlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1137 TILFRYFNKVVNLREAERKQQLynEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFK---EQ 1213
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKI--EKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQkslKK 582
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1034670642 1214 DGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKEL 1253
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
722-1236 |
2.03e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 722 LKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVEL 801
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 802 IETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQL 881
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 882 QRKLREENEKRKQLDAVIKRDQQKIkeIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKV 961
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 962 LNQRQELEELEADLKKREAIVSKKEALLQEKSHLE-------NKKLRSSQALNTDSLK------------ISTRLNLLEQ 1022
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkAALLLAGLRGLAGAVAvligveaayeaaLEAALAAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1023 ELSEKNVQ-LQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLK-----NGRVLSPEEEHVLFQLEEGIEALEAAIE 1096
Cdd:COG1196 550 NIVVEDDEvAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAigaavDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1097 YRNESIQNRQKSLRASFHNLSRG--EANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMV 1174
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEgeGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034670642 1175 RELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDGEGI-----METFKTYEDKIQQLEKDL 1236
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpePPDLEELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
875-1190 |
3.80e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 875 KYQKIQLQRKLREENEKRKQLDAVIK--RDQQKIKEIQLKTGQE-EGLKPKAEDLDACNLKRRKGSFgsIDHLQKLDEQK 951
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNelERQLKSLERQAEKAERyKELKAELRELELALLVLRLEEL--REELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 952 KWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLrssQALNTDSLKISTRLNLLEQELSEKNVQL 1031
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1032 QTStAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKngrvlspEEEHVLFQLEEGIEALEAAIEYRN----------ES 1101
Cdd:TIGR02168 326 EEL-ESKLDELAEELAELEEKLEELKEELESLEAELE-------ELEAELEELESRLEELEEQLETLRskvaqlelqiAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1102 IQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESAL 1181
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
....*....
gi 1034670642 1182 DHLKLQCDR 1190
Cdd:TIGR02168 478 DAAERELAQ 486
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
743-1328 |
7.47e-09 |
|
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: 60.76 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 743 RILTEAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslkvtKLEHDAEQAKVELIETQKQLQELENKDLSDVAMK 822
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKL-----------------QELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 823 VKLQKEFRKKMDA-AKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKR 901
Cdd:pfam02463 232 LKLNEERIDLLQElLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 902 DQQKIKEIQLKTGQEEGlkpkaedldacNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEAD-----LK 976
Cdd:pfam02463 312 DEEKLKESEKEKKKAEK-----------ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEellakKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 977 KREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQL 1056
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1057 QKRRHnVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIR 1136
Cdd:pfam02463 461 LKDEL-ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1137 TILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQcdrRLTLQQKEHEQKMQLLLHHFKEQDGE 1216
Cdd:pfam02463 540 NYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLP---LKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1217 GIMETFKTYEDKIQQLEKDLyfykktSRDHKKKLKELVGEAIRRQLAPSEYQEAGDGVLKPEGGGMLSEELKWASRPESM 1296
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTK------LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590
....*....|....*....|....*....|..
gi 1034670642 1297 KLSGREREMDSSASSLRTQPNPQKLWEDIPEL 1328
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
710-1072 |
1.25e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 710 DETQKSDlenEDLKIDCLQESQEL----NLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSL 785
Cdd:PTZ00121 1537 DEAKKAE---EKKKADELKKAEELkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 786 KVTKLEHDAEQAKVELiETQKQLQELENKDlsdvAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLAS-LSIQNEKRA 864
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAE-EEKKKVEQLKKKE----AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeAKKAEEDEK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 865 NELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGlKPKAEDLDACNLKRRKGSFGSIDHL 944
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-KKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 945 QKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREaiVSKKEALLQEKSHLENKKLRSSQALNTDSLK---ISTRLNLLE 1021
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD--IFDNFANIIEGGKEGNLVINDSKEMEDSAIKevaDSKNMQLEE 1845
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034670642 1022 QELSEKNVQLQTStaeEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRV 1072
Cdd:PTZ00121 1846 ADAFEKHKFNKNN---ENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKI 1893
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
838-1270 |
2.54e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 838 LRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVikrdQQKIKEIQlktgqee 917
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELEELR------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 918 glkpkaEDLDAcnLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEkshlen 997
Cdd:COG4717 116 ------EELEK--LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 998 kklrssqALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKtKISEQVEVLQKEKDQL--QKRRHNVDEKLKNGRVL-- 1073
Cdd:COG4717 182 -------LLEQLSLATEEELQDLAEELEELQQRLAELEEELE-EAQEELEELEEELEQLenELEAAALEERLKEARLLll 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1074 -----------------SPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLAC---LSPV 1133
Cdd:COG4717 254 iaaallallglggsllsLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1134 EIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVL--ERDNMVREL----ESALDHLKLQCDRRLTLQQKEHEQKMQLLL 1207
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELeqEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEE 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034670642 1208 hHFKEQDGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKELVGEaIRRQLAPSEYQEA 1270
Cdd:COG4717 414 -LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAE-LEQLEEDGELAEL 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
961-1236 |
2.97e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 961 VLNQRQELEELEADLKKREAIVSKKEALLQEKSHlenkklrSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKt 1040
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRK-------ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1041 KISEQVEVLQKEKDQLQKRRHNVDEKLKngrvlspEEEHVLFQLEEGIEALEAAIEYRNESIQN---RQKSLRASFHNLS 1117
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLE-------EAEEELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1118 RGEANVLEKLACLSPvEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDhlklqcdrrltlQQK 1197
Cdd:TIGR02168 817 EEAANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN------------ERA 883
|
250 260 270
....*....|....*....|....*....|....*....
gi 1034670642 1198 EHEQKMQLLLHHFKEQdgegiMETFKTYEDKIQQLEKDL 1236
Cdd:TIGR02168 884 SLEEALALLRSELEEL-----SEELRELESKRSELRREL 917
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
956-1270 |
9.66e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 956 EEVEKVLNQRQELEELEADLkkreaivskkEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQelseknvqlqtsT 1035
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKREL----------SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ------------L 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1036 AEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAaiEYRNESIQNRQKSLRASFHN 1115
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEE 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1116 LSRGEANVLEKLACLSPVEIRTILFRyfNKVVNL---------REAERKQQLYN-----EEMKMKVLERDNMVRELESAL 1181
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLE--KEIQELqeqridlkeQIKSIEKEIENlngkkEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1182 DHLKLQCDRRLT----LQQKEHEQKMQL--LLHHFKEQDG--EGIMETFKTYEDKIQQLEKdlYFYKKTSRDHKKKLKEL 1253
Cdd:TIGR02169 885 GDLKKERDELEAqlreLERKIEELEAQIekKRKRLSELKAklEALEEELSEIEDPKGEDEE--IPEEELSLEDVQAELQR 962
|
330 340
....*....|....*....|..
gi 1034670642 1254 VGEAIRR-----QLAPSEYQEA 1270
Cdd:TIGR02169 963 VEEEIRAlepvnMLAIQEYEEV 984
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
742-1201 |
4.94e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 742 ERILTEAKQKMRELTINIKMKEDliKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAK------VELI----ETQKQLQEL 811
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARetrdeaDEVLeeheERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 812 EnKDLSDVAMKVKlqkEFRKKMDAAKLRVQVLQKKQQD-----SKKLASLSIqNEKRANELEQSVDHMKYQKIQLQRKLR 886
Cdd:PRK02224 257 E-AEIEDLRETIA---ETEREREELAEEVRDLRERLEEleeerDDLLAEAGL-DDADAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 887 EENEKRKQLDAVIKRDQQKIKEIQlktGQEEGLKPKAEDLDA----CNLKRRKGSfGSIDHLQK---------------L 947
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLE---ERAEELREEAAELESeleeAREAVEDRR-EEIEELEEeieelrerfgdapvdL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 948 DEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLE-NKKLRSS---QALNTDSLKISTrlnlLEQE 1023
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEcGQPVEGSphvETIEEDRERVEE----LEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1024 LSEknVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQ 1103
Cdd:PRK02224 484 LED--LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1104 ---NRQKSLRASFHNLSRGEANVLEKLACLSpvEIRTILFR---YFNKVVNLREAERKQQLYNEEMKMKVLERDNMVREL 1177
Cdd:PRK02224 562 eaeEEAEEAREEVAELNSKLAELKERIESLE--RIRTLLAAiadAEDEIERLREKREALAELNDERRERLAEKRERKREL 639
|
490 500
....*....|....*....|....
gi 1034670642 1178 ESALDhlklqcDRRLTLQQKEHEQ 1201
Cdd:PRK02224 640 EAEFD------EARIEEAREDKER 657
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
707-1092 |
5.85e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.35 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 707 DTQDETQKSDLENedlKIDCLQESQELNLQKLKNSERI----LTEAKQKMRELTINIKMKEDLIKEliktgnDAKSVSKQ 782
Cdd:pfam15921 244 EDQLEALKSESQN---KIELLLQQHQDRIEQLISEHEVeitgLTEKASSARSQANSIQSQLEIIQE------QARNQNSM 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 783 YSLKVTKLEHDAEQAKVELIETQK----QLQELE------NKDLSDVAMKvklQKEFRKKMDAAKLRVQVLQKKQQDSKK 852
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRmyedKIEELEkqlvlaNSELTEARTE---RDQFSQESGNLDDQLQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 853 LASLSIQNEKRANELEQ----SVDHmkyqkiqLQRKLREENEKRKQLDAVIKRDQQKIKeiqlktGQEEGlkpkaedlda 928
Cdd:pfam15921 392 ELSLEKEQNKRLWDRDTgnsiTIDH-------LRRELDDRNMEVQRLEALLKAMKSECQ------GQMER---------- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 929 cNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLnqrQELEELEADLKKREAIVSKKEALLQEKShlenkklRSSQALNT 1008
Cdd:pfam15921 449 -QMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV---EELTAKKMTLESSERTVSDLTASLQEKE-------RAIEATNA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1009 DSLKISTRLNLLEQELSE--------KNVQLQTSTAE----EKTKISE----QVE--------------VLQKEKDQLQK 1058
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHlknegdhlRNVQTECEALKlqmaEKDKVIEilrqQIEnmtqlvgqhgrtagAMQVEKAQLEK 597
|
410 420 430
....*....|....*....|....*....|....
gi 1034670642 1059 RRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALE 1092
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
944-1234 |
7.43e-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: 53.91 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 944 LQKLDEQKkwldEEVEKVLNQRQELEELEADL--KKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTrLNLLE 1021
Cdd:TIGR02168 202 LKSLERQA----EKAERYKELKAELRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1022 QELSEKNVQLQTSTAEEKTKISEqvevLQKEKDQLQKRRHNVDEKLKngrVLSPEEEHVLFQLEEGIEALeAAIEYRNES 1101
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISR----LEQQKQILRERLANLERQLE---ELEAQLEELESKLDELAEEL-AELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1102 IQNRQKSLRASFHNLSRGEANVLEKLAclspvEIRTILFRYFNKVVNLREAERKQQLyneemkmkvlerdnmvrELESAL 1181
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLE-----ELEEQLETLRSKVAQLELQIASLNN-----------------EIERLE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670642 1182 DHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDG------EGIMETFKTYEDKIQQLEK 1234
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAeleeleEELEELQEELERLEEALEE 465
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
710-1246 |
1.85e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 710 DETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKtgndaksvsKQYSLkvTK 789
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE---------KKDHL--TK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 790 LEHDAEQAKVELIETQKQLQE---LENKDLSDVAMKVKLQKEFRKKMDAAklRVQVLQKKQQDSKKLASLSIQNEKRane 866
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEdlqIATKTICQLTEEKEAQMEELNKAKAA--HSFVVTEFEATTCSLEELLRTEQQR--- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 867 LEQSVDHMKYQKIQLQRKLREENEKRKQLDAvikrdqqkiKEIQLktgqEEGLKPKAEDLDACNLKRRkgsfgsidhLQK 946
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNN---------KEVEL----EELKKILAEDEKLLDEKKQ---------FEK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 947 LDEQKKWLDEEVEKVLNQRQ-ELEELEADLKkreAIVSKKEALLQE----KSHLENKKLRSSQaLNTDSLKISTRLNLLE 1021
Cdd:pfam05483 430 IAEELKGKEQELIFLLQAREkEIHDLEIQLT---AIKTSEEHYLKEvedlKTELEKEKLKNIE-LTAHCDKLLLENKELT 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1022 QELSEKNVQLQ------TSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRvlsPEEEHVLFQLEEGIEALEAAI 1095
Cdd:pfam05483 506 QEASDMTLELKkhqediINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG---DEVKCKLDKSEENARSIEYEV 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1096 ---EYRNESIQNRQKSLRASFHNLSRG------EANVLEKLACLSPVEIRTILFRYFNKVVNLREAERK----QQLYNEE 1162
Cdd:pfam05483 583 lkkEKQMKILENKCNNLKKQIENKNKNieelhqENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKfeeiIDNYQKE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1163 MKMKVLERDNMVRELESAldhlKLQCDRRLTLqQKEHEQKMQlllHHFKEQdgEGIMETFKTYEDKI-QQLEKDLYFYKK 1241
Cdd:pfam05483 663 IEDKKISEEKLLEEVEKA----KAIADEAVKL-QKEIDKRCQ---HKIAEM--VALMEKHKHQYDKIiEERDSELGLYKN 732
|
....*
gi 1034670642 1242 TSRDH 1246
Cdd:pfam05483 733 KEQEQ 737
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
711-1058 |
2.16e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 711 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAksvskqySLKVTKL 790
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM-------TLELKKH 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 791 EHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRvqvLQKKQQDSKKLASLSIQNEKRANELEQS 870
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK---LDKSEENARSIEYEVLKKEKQMKILENK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 871 VDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEglkpkaedldaCNLKRRKGSFGSI-DHLQKLDE 949
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE-----------LELASAKQKFEEIiDNYQKEIE 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 950 QKKWLDE----EVEKVLNQRQELEELEADLKKR-EAIVSKKEALLQEKSHLENKKLRSSqalntdslkiSTRLNLL---E 1021
Cdd:pfam05483 665 DKKISEEklleEVEKAKAIADEAVKLQKEIDKRcQHKIAEMVALMEKHKHQYDKIIEER----------DSELGLYknkE 734
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1034670642 1022 QELSEKNVQLQTSTAE---EKTKISEQVEVLQKEKDQLQK 1058
Cdd:pfam05483 735 QEQSSAKAALEIELSNikaELLSLKKQLEIEKEEKEKLKM 774
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
711-1110 |
2.18e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 711 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDlIKELIKTGNDAKSVSKQYSLKVTKL 790
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 791 EHDAEQAKVELIETQKQLQELENKDlSDVAMKVKLQKEFRKKMDAAKLRVQVLQK-------KQQDSKKLASLSIQN--- 860
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKE-ERLEELKKKLKELEKRLEELEERHELYEEakakkeeLERLKKRLTGLTPEKlek 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 861 -----EKRANELEQSVDHMKYQKIQLQRKLREEN----------------------EKRKQLDAVIKRDQQKI-KEIQLK 912
Cdd:PRK03918 392 eleelEKAKEEIEEEISKITARIGELKKEIKELKkaieelkkakgkcpvcgrelteEHRKELLEEYTAELKRIeKELKEI 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 913 TGQEEGLKPKAEDLD---------------ACNLKRRKGSFGSIDhLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKK 977
Cdd:PRK03918 472 EEKERKLRKELRELEkvlkkeseliklkelAEQLKELEEKLKKYN-LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 978 REAIVSKKEALLQEKSHLENKK---LRSSQALNTDSLK-ISTRLNLLEqELSEKNVQLQTSTAE----------EKTKIS 1043
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELaelLKELEELGFESVEeLEERLKELE-PFYNEYLELKDAEKElereekelkkLEEELD 629
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034670642 1044 EQVEVLQKEKDQLQKRRHNVDEKLKNgrvLSPEE----EHVLFQLEEGIEALEAAIEYRNESIQNRQKSLR 1110
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKK---YSEEEyeelREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
711-1076 |
2.41e-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: 52.33 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 711 ETQKSDLENEDLKIDCLQES-QELNlQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTK 789
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIiSQLN-EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 790 LEHDAEQAK---------VELIETQKQLQELENKDLSDVAMKVKLQ-KEFRKKMDAAKLRVQVL-QKKQQDSKKLASLSI 858
Cdd:TIGR04523 396 LESKIQNQEklnqqkdeqIKKLQQEKELLEKEIERLKETIIKNNSEiKDLTNQDSVKELIIKNLdNTRESLETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 859 QNEKRANELEQSVDHMKYQKiqlqRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDldacNLKRRKgsf 938
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKE----KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES----KISDLE--- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 939 gsiDHLQKLDEQKKWLDEEVEkVLNQRQELEELEADLKKREAIVSKKEALLQEKSHlENKKLRSSQALNTdsLKISTrln 1018
Cdd:TIGR04523 545 ---DELNKDDFELKKENLEKE-IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK-EKKDLIKEIEEKE--KKISS--- 614
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034670642 1019 lLEQELSEKNvqlqtstaEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPE 1076
Cdd:TIGR04523 615 -LEKELEKAK--------KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
770-1257 |
2.45e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 770 IKTGNDAKSVSKQYSLKVTKLEHDAEQAKveLIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAK----LRVQVLQK 845
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAAR--KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaeeERNNEEIR 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 846 KQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKqLDAVIKRDQQKIKEIQLKTGQEEG------L 919
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAkkkadaA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 920 KPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLD-----------------EEVEKVLNQRQELEELEA---DLKKRE 979
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkeeakkkadaakkkaEEKKKADEAKKKAEEDKKkadELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 980 AIVSKKEAL---LQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTS-----TAEEKTKISEQVEVLQK 1051
Cdd:PTZ00121 1415 AAKKKADEAkkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeakkKAEEAKKADEAKKKAEE 1494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1052 EKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKlacLS 1131
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA---KK 1571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1132 PVEIRTILFRyfnKVVNLREAERKQ-----QLYNEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLL 1206
Cdd:PTZ00121 1572 AEEDKNMALR---KAEEAKKAEEARieevmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1034670642 1207 LHHFKEQDGEGIM----ETFKTYEDKIQQLEkdlyfYKKTSRDHKKKLKELVGEA 1257
Cdd:PTZ00121 1649 AEELKKAEEENKIkaaeEAKKAEEDKKKAEE-----AKKAEEDEKKAAEALKKEA 1698
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
843-1075 |
3.45e-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: 50.92 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 843 LQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ------------ 910
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaeleaqkeelae 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 911 -LKTGQEEGLKPKAEdldacNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADL-KKREAIVSKKEAL 988
Cdd:COG4942 109 lLRALYRLGRQPPLA-----LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELeAERAELEALLAEL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 989 LQEKSHLENKKLRSSQALNtdslKISTRLNLLEQELSEKnvqlqtstAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLK 1068
Cdd:COG4942 184 EEERAALEALKAERQKLLA----RLEKELAELAAELAEL--------QQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
....*..
gi 1034670642 1069 NGRVLSP 1075
Cdd:COG4942 252 KGKLPWP 258
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
723-1121 |
3.46e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 52.00 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 723 KIDCLQESQELNLQ-KLKNSERILTEAKQKMRELTINIKMKE--DLIKELIKTGNDAKSVSKQYSLKVTKLEHDAE---Q 796
Cdd:COG5022 770 RIKKIQVIQHGFRLrRLVDYELKWRLFIKLQPLLSLLGSRKEyrSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvliQ 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 797 AKVELIETQKQLQELENKDLSDvamkvklqkEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQsvdhmky 876
Cdd:COG5022 850 KFGRSLKAKKRFSLLKKETIYL---------QSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKK------- 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 877 qkiQLQRKLREENEKRKQLDAVIKRdqqKIKEIQLKTGQEEglkpkaedldacnlkrrkgSFGSIDHLQKLDEQKKWLDE 956
Cdd:COG5022 914 ---SLSSDLIENLEFKTELIARLKK---LLNNIDLEEGPSI-------------------EYVKLPELNKLHEVESKLKE 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 957 EVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHlENKKLRSSQALNTDSLKISTRLNLLEQELSEknvqlQTSTA 1036
Cdd:COG5022 969 TSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSK-QYGALQESTKQLKELPVEVAELQSASKIISS-----ESTEL 1042
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1037 EEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEhvlfqLEEGIEALEAAIEYRNESIQNRQKSLRASFHNL 1116
Cdd:COG5022 1043 SILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLY-----QLESTENLLKTINVKDLEVTNRNLVKPANVLQF 1117
|
....*
gi 1034670642 1117 SRGEA 1121
Cdd:COG5022 1118 IVAQM 1122
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
736-987 |
4.81e-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: 50.53 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 736 QKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQElenkd 815
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 816 lsdvamkvkLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQN----EKRANELEQSVDHMKYQKIQLQRKLREENEK 891
Cdd:COG4942 95 ---------LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfldaVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 892 RKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLdacnlkrrkgsfgsidhLQKLDEQKKWLDEEVEKVLNQRQELEEL 971
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKL-----------------LARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....*.
gi 1034670642 972 EADLKKREAIVSKKEA 987
Cdd:COG4942 229 IARLEAEAAAAAERTP 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
732-1121 |
7.09e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 732 ELNLQKLKNSERILTEAKQKMRELTINIKMKEDL---IKELIKTGNDAKSVSKQYSLKVTKLEHDAE--QAKVELIETQK 806
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 807 QLQELENkdlsdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLR 886
Cdd:COG4717 147 RLEELEE----------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 887 EENEKRKQLDAVIKR---------DQQKIKEIQLKTGQE------EGLKPKAEDLDACNLKRRKGSFGSI-DHLQKLDEQ 950
Cdd:COG4717 217 EAQEELEELEEELEQleneleaaaLEERLKEARLLLLIAaallalLGLGGSLLSLILTIAGVLFLVLGLLaLLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 951 KKWLDEEVEKV--LNQRQELE--ELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKIstRLNLLEQELSE 1026
Cdd:COG4717 297 KASLGKEAEELqaLPALEELEeeELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1027 KNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSpeEEHVLFQLEEGIEALEAAIEYRNE---SIQ 1103
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEeleELR 452
|
410
....*....|....*...
gi 1034670642 1104 NRQKSLRASFHNLSRGEA 1121
Cdd:COG4717 453 EELAELEAELEQLEEDGE 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
890-1128 |
1.04e-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: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 890 EKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDAcNLKRRKGSfgsidhLQKLDEQKKWLDEEVEKVlnqRQELE 969
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARR------IRALEQELAALEAELAEL---EKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 970 ELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQtstaEEKTKISEQVEVL 1049
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR----ADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670642 1050 QKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIeyrnESIQNRQKSLRASFHNLSRGEANVLEKLA 1128
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL----AELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
827-1096 |
1.05e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 827 KEFRKKMDAAKLRVQVLQKKQQDSKKLAslsiQNEKRANELEQSVDHMKYQKIQ-----LQRKLREENEKRKQLDAVIKR 901
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYA----AARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 902 DQQKIKEIQlktgqeeglkpkaEDLDACNLKRRKGSFGSIDHLQKldeQKKWLDEEVEKVLNQRQELEELEADLKkreai 981
Cdd:COG4913 314 LEARLDALR-------------EELDELEAQIRGNGGDRLEQLER---EIERLERELEERERRRARLEALLAALG----- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 982 vskkEALLQEKSHLENKKLRSSQALNTdslkISTRLNLLEQELSEKNVQLQTSTAEEKTkiseqvevLQKEKDQLQKRRH 1061
Cdd:COG4913 373 ----LPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDLRRELRE--------LEAEIASLERRKS 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034670642 1062 NVDEKLKNGR-----VLSPEEEHVLF-----QLEEGIEALEAAIE 1096
Cdd:COG4913 437 NIPARLLALRdalaeALGLDEAELPFvgeliEVRPEEERWRGAIE 481
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
704-1184 |
1.39e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.05 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 704 ELSDTQDETQKSDLENEDLKIDCLQESQEL----NLQKLKNSERILTEAKQ---KMRELTINIKMKEDLIKELIKTGNDa 776
Cdd:TIGR01612 1319 DINDIKKELQKNLLDAQKHNSDINLYLNEIaniyNILKLNKIKKIIDEVKEytkEIEENNKNIKDELDKSEKLIKKIKD- 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 777 ksvskQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSD---VAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKL 853
Cdd:TIGR01612 1398 -----DINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEesnIDTYFKNADENNENVLLLFKNIEMADNKSQHILKI 1472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 854 ASLSIQNEK--RANELEQSVDHMKYQKIQLQrKLREENEKRKQLDAVIKRD----QQKIKEIQLKTGQEEGLKPKAEDLD 927
Cdd:TIGR01612 1473 KKDNATNDHdfNINELKEHIDKSKGCKDEAD-KNAKAIEKNKELFEQYKKDvtelLNKYSALAIKNKFAKTKKDSEIIIK 1551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 928 ACNLKRRKGSFGSIDHLQKLDEQKK---WLDEEVEK-------VLNQRQELEELEADLKKREAIVSKKEALLQEKSHLEN 997
Cdd:TIGR01612 1552 EIKDAHKKFILEAEKSEQKIKEIKKekfRIEDDAAKndksnkaAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEK 1631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 998 KKlrSSQALNTDSLKISTRLNLLE--QELSEknvqlqtSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNgrvlsp 1075
Cdd:TIGR01612 1632 KI--SSFSIDSQDTELKENGDNLNslQEFLE-------SLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKN------ 1696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1076 EEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLA----------------------CLSPV 1133
Cdd:TIGR01612 1697 YEIGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEeynteigdiyeefielyniiagCLETV 1776
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670642 1134 --------EIRTILFRYFNKVVNLREAERKQQLYNEEMKMKvlERDNMVRELESALDHL 1184
Cdd:TIGR01612 1777 skepitydEIKNTRINAQNEFLKIIEIEKKSKSYLDDIEAK--EFDRIINHFKKKLDHV 1833
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
827-1103 |
1.64e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 827 KEFRKKMDAAKlrvQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKI 906
Cdd:pfam02463 166 RLKRKKKEALK---KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 907 KEIQLKTGQEEGLKPKAEDLDACNLKRRKgsfgsidHLQKLDEQKKWLDEEVEKVLNQRQELEELEA-DLKKREAIVSKK 985
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVL-------KENKEEEKEKKLQEEELKLLAKEEEELKSELlKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 986 EALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQK--RRHNV 1063
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaaKLKEE 395
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034670642 1064 DEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQ 1103
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
748-1067 |
1.99e-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: 49.30 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 748 AKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslKVTKLEHDAEQAkVELIETQKQLQELENKDLsdvamkVKLQK 827
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQ--------------QLERLRREREKA-ERYQALLKEKREYEGYEL------LKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 828 EFRKKMDAAKLRVQVLQKKQQDSKKLASlsiQNEKRANELEQSVDHMKYQ--------KIQLQRKLREENEKRKQLDAVI 899
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKikdlgeeeQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 900 --KRDQQKIKEIQLKTGQEE--GLKPKAEDLDacnlkrrkgsfGSIDHLQKLDEQKKWLDEEVEKVLNQ-RQELEELEAD 974
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEidKLLAEIEELE-----------REIEEERKRRDKLTEEYAELKEELEDlRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 975 L-----------KKREAIVSKKEALLQEKSHLENKKLRSSQA---LNTDSLKISTRLNLLEQELSEKNVQLQT------S 1034
Cdd:TIGR02169 380 FaetrdelkdyrEKLEKLKREINELKRELDRLQEELQRLSEEladLNAAIAGIEAKINELEEEKEDKALEIKKqewkleQ 459
|
330 340 350
....*....|....*....|....*....|...
gi 1034670642 1035 TAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKL 1067
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
706-1056 |
2.14e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 706 SDTQDETQKSDLENEDLKIDCLQESQELN----LQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 781
Cdd:pfam10174 434 TDTALTTLEEALSEKERIIERLKEQREREdrerLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGL 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 782 QYSLKVTKLEHDAEQAKVELIETQKQLQELENkdlsdVAMKVKLQKEFrkkmdaaKLRVQVLQKKQQDSKKLASlsiqne 861
Cdd:pfam10174 514 KKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-----AEEAVRTNPEI-------NDRIRLLEQEVARYKEESG------ 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 862 KRANELEQSVDHMKYQKiqlqrklREENEKRKQLDAVIKRDQQKIKE-----IQLKTGQEEGLKPKAEDLDacNLKRRKG 936
Cdd:pfam10174 576 KAQAEVERLLGILREVE-------NEKNDKDKKIAELESLTLRQMKEqnkkvANIKHGQQEMKKKGAQLLE--EARRRED 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 937 SFGSIDHLQKLDEqkkwLDEEVEKVlnqRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKIStr 1016
Cdd:pfam10174 647 NLADNSQQLQLEE----LMGALEKT---RQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAA-- 717
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034670642 1017 lnlleqeLSEK--NVQLQTSTAEEKTKISEQVEVLQKEKDQL 1056
Cdd:pfam10174 718 -------ISEKdaNIALLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
723-938 |
2.39e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 723 KIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELI 802
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 803 ETQKQLQE-----------------LENKDLSDVAMKVKLQKEFrkkmdaAKLRVQVLQKKQQDSKKLASLSIQNEKRAN 865
Cdd:COG4942 101 AQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYL------APARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 866 ELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ--------LKTGQEEGLKPKAEDLDACNLKRRKGS 937
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQqeaeeleaLIARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 1034670642 938 F 938
Cdd:COG4942 255 L 255
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
878-1009 |
2.53e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 878 KIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKgsfgsIDHLQKLDEQKK-WLDE 956
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE-----LQKLEKRLLQKEeNLDR 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034670642 957 EVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTD 1009
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
658-1217 |
2.79e-05 |
|
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: 48.96 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 658 EEQDKV--LHCQFSDNSDDEESEGQ-EKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSdlenedlkidclqesqeLN 734
Cdd:pfam15921 253 ESQNKIelLLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQNS-----------------MY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 735 LQKLKNSERILTEAKQKMRELTiniKMKEDLIKELIKTG-------NDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQ 807
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAK---RMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 808 L--QELENKDLSDVAMKVKLQ-KEFRKKMDAAKLRVQVL----------------------QKKQQDSKKLASLSIQNEK 862
Cdd:pfam15921 393 LslEKEQNKRLWDRDTGNSITiDHLRRELDDRNMEVQRLeallkamksecqgqmerqmaaiQGKNESLEKVSSLTAQLES 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 863 RANELEQSVDHMKYQKIQLQRKLREEN-------EKRKQLDA-------VIKRDQQKIKEIQLKTGQEEGLKPKAEDLDA 928
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESSERTVSdltaslqEKERAIEAtnaeitkLRSRVDLKLQELQHLKNEGDHLRNVQTECEA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 929 CNLKRrKGSFGSIDHLQKLDEQKKWL--------------DEEVEKVLNQRQ-ELEELEADLKKREAIVSKKEA------ 987
Cdd:pfam15921 553 LKLQM-AEKDKVIEILRQQIENMTQLvgqhgrtagamqveKAQLEKEINDRRlELQEFKILKDKKDAKIRELEArvsdle 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 988 -------------------LLQEKSHLENKKLRSSQALNTdslkISTRLNLLEQELSEKNVQLQTSTaeekTKISEQVEV 1048
Cdd:pfam15921 632 lekvklvnagserlravkdIKQERDQLLNEVKTSRNELNS----LSEDYEVLKRNFRNKSEEMETTT----NKLKMQLKS 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1049 LQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLrasfHNLSRGEANVLEKLA 1128
Cdd:pfam15921 704 AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELS 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1129 CLSPVEirtilfryfNKVVNLREAERKQQlynEEMKMKVlerdnmvRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLH 1208
Cdd:pfam15921 780 TVATEK---------NKMAGELEVLRSQE---RRLKEKV-------ANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
650
....*....|..
gi 1034670642 1209 H---FKEQDGEG 1217
Cdd:pfam15921 841 HtldVKELQGPG 852
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
789-1051 |
3.38e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 48.31 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 789 KLEHDAEQAKVELIETQKQLQELENKDLS----DVAMKVKLQkEFRKKMDAAKLRVQ-VLQKKQQDSKKLASLsiqnEKR 863
Cdd:pfam09726 399 RLEQDIKKLKAELQASRQTEQELRSQISSltslERSLKSELG-QLRQENDLLQTKLHnAVSAKQKDKQTVQQL----EKR 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 864 ANELEQSvdhmkyqKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGqeEGLKPKAEDLDAcnlkrrkgsfgsidH 943
Cdd:pfam09726 474 LKAEQEA-------RASAEKQLAEEKKRKKEEEATAARAVALAAASRGECT--ESLKQRKRELES--------------E 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 944 LQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENkklrssqalntdSLKISTRLNL-LEQ 1022
Cdd:pfam09726 531 IKKLTHDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAMQDKNQHLEN------------SLSAETRIKLdLFS 598
|
250 260
....*....|....*....|....*....
gi 1034670642 1023 ELSEKNVQLQTSTAEEKTKISEQVEVLQK 1051
Cdd:pfam09726 599 ALGDAKRQLEIAQGQIYQKDQEIKDLKQK 627
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
708-1103 |
3.49e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 708 TQDETQKSDLENEDLKIDClqesqelNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGND------------ 775
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITC-------TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvlarllelqeep 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 776 ---AKSVSKQYSLKVTKLEHDAEQAKVE-LIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSK 851
Cdd:TIGR00618 504 cplCGSCIHPNPARQDIDNPGPLTRRMQrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 852 KLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLK----TGQEEGLKPKAEDLD 927
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltalHALQLTLTQERVREH 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 928 ACNLKRRKGSFGSIDHLQKLDEQKKW----------------LDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQE 991
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKeqltywkemlaqcqtlLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 992 K------------SHLENKKLRSSQALNTDsLKISTRLNLLEQELSEKNVQLQTST-------AEEKTKISEQVEVLQKE 1052
Cdd:TIGR00618 744 SlkelmhqartvlKARTEAHFNNNEEVTAA-LQTGAELSHLAAEIQFFNRLREEDThllktleAEIGQEIPSDEDILNLQ 822
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1034670642 1053 KDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQ 1103
Cdd:TIGR00618 823 CETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
728-991 |
3.86e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 728 QESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELiktgndaksvsKQYSLKVTKLEHDAEQAKVELIETQKQ 807
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-----------EELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 808 LQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLRE 887
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 888 ENEKRKQLDAVIKRDQQKIKEIQLKtGQEEGLKPKAEDLDacNLKRRKGsfgsidhlqKLDEQKKwldeEVEKVLNQRQE 967
Cdd:PRK03918 659 EEYEELREEYLELSRELAGLRAELE-ELEKRREEIKKTLE--KLKEELE---------EREKAKK----ELEKLEKALER 722
|
250 260
....*....|....*....|....
gi 1034670642 968 LEELEADLKKREAIVskKEALLQE 991
Cdd:PRK03918 723 VEELREKVKKYKALL--KERALSK 744
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
776-909 |
4.01e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 776 AKSVSKQyslKVTKLEHDA----EQAKVElIETQKQLQELENKDLSDvAMKVKLQKEFR-KKMDAAKLRVQVLQKKQQDS 850
Cdd:PRK12704 25 RKKIAEA---KIKEAEEEAkrilEEAKKE-AEAIKKEALLEAKEEIH-KLRNEFEKELReRRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670642 851 KKLASLsiqnEKRANELEQsvdhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEI 909
Cdd:PRK12704 100 RKLELL----EKREEELEK-------KEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
944-1112 |
4.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 944 LQKLDEQKKWLDEEVEKVLNQ----RQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQA-----------LNT 1008
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEynelQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsggsvsyldvlLGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1009 DSL-KISTRLNLLEQeLSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEG 1087
Cdd:COG3883 112 ESFsDFLDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180
....*....|....*....|....*
gi 1034670642 1088 IEALEAAIEYRNESIQNRQKSLRAS 1112
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
705-1050 |
4.31e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 705 LSDTQ---DETQKSDLENEDLKIDCLQESQEL-----NLQKLKNSEriLTEAKQKMRELTInikmkEDLIKELIKTGNDA 776
Cdd:PRK11281 65 LEQTLallDKIDRQKEETEQLKQQLAQAPAKLrqaqaELEALKDDN--DEETRETLSTLSL-----RQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 777 KSVSK---QYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAaklrvqvlqkkqqdskKL 853
Cdd:PRK11281 138 QNAQNdlaEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQA----------------EQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 854 ASLSIQNEKRANELEQSVdhmkyqkiQLQRKLreeNEKRKQLDAVIKRDQQKIKEIQlktgqeeglkpkaedlDACNLKR 933
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNT--------QLQDLL---QKQRDYLTARIQRLEHQLQLLQ----------------EAINSKR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 934 RKGSfgsidhlqkldEQKkwldeeVEKVLNQRQELEELEADLKKREAIVskkeallqekshleNKKLrsSQALntdsLKI 1013
Cdd:PRK11281 255 LTLS-----------EKT------VQEAQSQDEAARIQANPLVAQELEI--------------NLQL--SQRL----LKA 297
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034670642 1014 STRLN-LLEQELSEKNvQLQTSTAEEKTkISEQVEVLQ 1050
Cdd:PRK11281 298 TEKLNtLTQQNLRVKN-WLDRLTQSERN-IKEQISVLK 333
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
839-1111 |
4.81e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 839 RVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKyqkiQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEG 918
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 919 LKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENK 998
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 999 KLRSSQALNTDSLKISTrlnlLEQELSEKNV---QLQTSTAEE-KTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLS 1074
Cdd:PRK02224 622 NDERRERLAEKRERKRE----LEAEFDEARIeeaREDKERAEEyLEQVEEKLDELREERDDLQAEIGAVENELEELEELR 697
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034670642 1075 PEEEHvlfqLEEGIEALEAAIEyRNESIQNRQKSLRA 1111
Cdd:PRK02224 698 ERREA----LENRVEALEALYD-EAEELESMYGDLRA 729
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
715-1266 |
5.43e-05 |
|
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: 47.79 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 715 SDLENEDLKIDCLQESQELNLQ----KLKNSERILTEAKQKMRELT-----INIKMKEDLI--KELIKTGNDA------- 776
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKqkenKLQENRKIIEAQRKAIQELQfenekVSLKLEEEIQenKDLIKENNATrhlcnll 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 777 KSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQEL--------ENKDLSDVAMKVKLQ----------KEFRKKMDAAKL 838
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMilafeelrVQAENARLEMHFKLKedhekiqhleEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 839 RVQVL----QKKQQDSKKLASLSIQNEKRANELEQSV--------------DHMKYQ----KIQLQRKLREENEKRKQLD 896
Cdd:pfam05483 241 QVSLLliqiTEKENKMKDLTFLLEESRDKANQLEEKTklqdenlkeliekkDHLTKElediKMSLQRSMSTQKALEEDLQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 897 AVIKRDQQKIKEiqlKTGQEEGLKpKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLN-----QRQELEEL 971
Cdd:pfam05483 321 IATKTICQLTEE---KEAQMEELN-KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITmelqkKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 972 -------EADLKKREAIVSKKEALLQEKSHLEnkklRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKtKISE 1044
Cdd:pfam05483 397 tkfknnkEVELEELKKILAEDEKLLDEKKQFE----KIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEE-HYLK 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1045 QVEVLQKEKDQlqkrrhnvdEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRN--ESIQNRQKS---LRASFHNLSRG 1119
Cdd:pfam05483 472 EVEDLKTELEK---------EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKhqEDIINCKKQeerMLKQIENLEEK 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1120 EANVLEKLACLSPVEIRT---ILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQ 1196
Cdd:pfam05483 543 EMNLRDELESVREEFIQKgdeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1197 KEHEQKMQLLLHHFKEQDGEGIMETFKtyedkiQQLEKDLYFYKKTSRDHKKKLKELVGEAIRRQLAPSE 1266
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNKLELELASAK------QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
704-909 |
6.74e-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: 47.43 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 704 ELSDTQDETQKSDLE---NEDL--KIDCLQESQELNLQKLKNSERILTE----AKQKMRELTINIKMKEDLIKELIKTGN 774
Cdd:pfam17380 349 ELERIRQEERKRELErirQEEIamEISRMRELERLQMERQQKNERVRQEleaaRKVKILEEERQRKIQQQKVEMEQIRAE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 775 DAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSK--- 851
Cdd:pfam17380 429 QEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqam 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034670642 852 ----------------KLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAvIKRDQQKIKEI 909
Cdd:pfam17380 509 ieeerkrkllekemeeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEA-MEREREMMRQI 581
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
729-1002 |
8.62e-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: 47.04 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 729 ESQELNLQKLKNSERILTEAKQkmRELtinikmkedlikELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVElietqkql 808
Cdd:pfam17380 338 EQERMAMERERELERIRQEERK--REL------------ERIRQEEIAMEISRMRELERLQMERQQKNERVR-------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 809 QELEnkdlsdVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQR-KLRE 887
Cdd:pfam17380 396 QELE------AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERlRQQE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 888 ENEKRKQLDAVI-KRDQQKIKEIQLKTGQEEGLKPKAEDLDACNlkRRKGSFGSIDHLQK--LDEQKKWLDEEVEKVLNQ 964
Cdd:pfam17380 470 EERKRKKLELEKeKRDRKRAEEQRRKILEKELEERKQAMIEEER--KRKLLEKEMEERQKaiYEEERRREAEEERRKQQE 547
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034670642 965 RQELEELEADLKKREAIVSKKEALLQEKSHL----ENKKLRS 1002
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMrqivESEKARA 589
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
704-999 |
9.65e-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: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 704 ELSDTQDETqkSDLENEdlkIDCLQESQELNLQKLKNSERILTEAKQkmrELTINIKMKEDLIKELiktgNDAKSVSKQY 783
Cdd:TIGR02169 710 ELSDASRKI--GEIEKE---IEQLEQEEEKLKERLEELEEDLSSLEQ---EIENVKSELKELEARI----EELEEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 784 SLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDV--AMKVKLQKEFRKK-------------MDAAKLRVQVLQKKQQ 848
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARlrEIEQKLNRLTLEKeylekeiqelqeqRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 849 DSK-KLASLSIQNEKRANELEQ----------SVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEE 917
Cdd:TIGR02169 858 NLNgKKEELEEELEELEAALRDlesrlgdlkkERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 918 GLKPKAEDLDACNLKrrkgsfgsidhLQKLDEQKKWLDEEVEKV--LNQR--QELEELEADL----KKREAIVSKKEALL 989
Cdd:TIGR02169 938 DPKGEDEEIPEEELS-----------LEDVQAELQRVEEEIRALepVNMLaiQEYEEVLKRLdelkEKRAKLEEERKAIL 1006
|
330
....*....|
gi 1034670642 990 QEKSHLENKK 999
Cdd:TIGR02169 1007 ERIEEYEKKK 1016
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
752-1060 |
9.80e-05 |
|
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: 46.81 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 752 MRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRK 831
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 832 KMDAAKLRVQVLQKKQQDSKKLAslsiqneKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIkrdQQKIKEIQL 911
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLT-------QRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL---QQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 912 KTGQEEGLKPKAEDLDACNLKRRKgsfgSIDHLQKLDEQKKWLDEEVEKVLNQRQELEE-LEADLKKREAIVSKKEALLQ 990
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQD----TITTLTQKLTTAHRKEAENEALLEELRSLQErLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034670642 991 EKSH----LENKKLRSSQAlntdSLKIS-TRLNLLEQE--LSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRR 1060
Cdd:pfam07888 266 QRDRtqaeLHQARLQAAQL----TLQLAdASLALREGRarWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER 338
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
711-977 |
1.32e-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: 46.55 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 711 ETQKSDLENE-----------DLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSV 779
Cdd:TIGR04523 390 ESQINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 780 SKQYSLKVTKLEHDAEQAKVELIETQKQLQEL--ENKDLSdvamkvKLQKEFRKKMDAAKLRVQVLQK-KQQDSKKLASL 856
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLneEKKELE------EKVKDLTKKISSLKEKIEKLESeKKEKESKISDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 857 -----SIQNEKRANELEQSVDHM--KYQKIQLQRKLREENEKRKQLDAVIKRDQQK--IKEIQLKTGQEEGLKPKAEDLD 927
Cdd:TIGR04523 544 edelnKDDFELKKENLEKEIDEKnkEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdlIKEIEEKEKKISSLEKELEKAK 623
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034670642 928 ACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKK 977
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
702-1065 |
1.43e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 702 LVELSDTQDETQKSDLENEDlkIDCLQESQeLNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 781
Cdd:PTZ00121 1032 LTEYGNNDDVLKEKDIIDED--IDGNHEGK-AEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 782 QYSLKVTKLEHDAEQAK-VELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQvlqKKQQDSKKLASLSIQN 860
Cdd:PTZ00121 1109 GKAEEARKAEEAKKKAEdARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA---RKAEDAKKAEAARKAE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 861 E-KRANELEQSVDHMKYQKIQLQRKLREENEKR-----KQLDAVIKRDQQKIKEIQLKTGQEE---GLKPKAEDLDACNL 931
Cdd:PTZ00121 1186 EvRKAEELRKAEDARKAEAARKAEEERKAEEARkaedaKKAEAVKKAEEAKKDAEEAKKAEEErnnEEIRKFEEARMAHF 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 932 KRRKGSFGS-----IDHLQKLDEQKKWLD----EEVEKVLNQRQELEEL-EADLKKREAIVSKKEALLQEKSHLENKKLR 1001
Cdd:PTZ00121 1266 ARRQAAIKAeearkADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAkKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034670642 1002 SSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDE 1065
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
787-1203 |
1.78e-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: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 787 VTKLEHDAEQAKVELIETQKQLQELENKD----------LSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASL 856
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKSTESELKKKEKRRdemlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGT 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 857 SIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAV--IKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRR 934
Cdd:TIGR00606 777 IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 935 KgsfgSIDHLQKLDEQKKWLDEEVEKVLNQRQELEEleadlkKREAIVSKKEALLQEKSHLENKKLRSSQALntdslkis 1014
Cdd:TIGR00606 857 E----QIQHLKSKTNELKSEKLQIGTNLQRRQQFEE------QLVELSTEVQSLIREIKDAKEQDSPLETFL-------- 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1015 trlnlleQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRvlspeeEHVLFQLEEGIEALEAA 1094
Cdd:TIGR00606 919 -------EKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK------DDYLKQKETELNTVNAQ 985
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1095 I---EYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEirtilfryfnkvvNLREAERKQQLYNEEM-KMKVLER 1170
Cdd:TIGR00606 986 LeecEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKREN-------------ELKEVEEELKQHLKEMgQMQVLQM 1052
|
410 420 430
....*....|....*....|....*....|...
gi 1034670642 1171 DNMVRELESALDHLKLQCDRRLTLQQKEHEQKM 1203
Cdd:TIGR00606 1053 KQEHQKLEENIDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
781-1077 |
3.02e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 781 KQYSLKVTKLEHDAEQAKVELIETQKQLQELENKdlsdvamKVKLQKEFRKKMDAAKlrvQVLQKKQQDSKKLASLSiqn 860
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEK-------RDELNAQVKELREEAQ---ELREKRDELNEKVKELK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 861 EKRaNELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ---LKTGQEEGLKPKAEDLDAcnlkrrkgs 937
Cdd:COG1340 78 EER-DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevLSPEEEKELVEKIKELEK--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 938 fgSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKK-REAIVSKKEALLQEKSHLENKKlRSSQALNTDSLKISTR 1016
Cdd:COG1340 148 --ELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQELHEEMIELYKEADELR-KEADELHKEIVEAQEK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034670642 1017 LNLLEQELSEKNVQLQtSTAEEKTKISEQVEVLQKEKDQ--LQKRRHNVDEKLKNGRVLSPEE 1077
Cdd:COG1340 225 ADELHEEIIELQKELR-ELRKELKKLRKKQRALKREKEKeeLEEKAEEIFEKLKKGEKLTTEE 286
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
736-916 |
3.37e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 736 QKLKNSERILTEAKQKMRELTINIkmkEDLIKELIKTGNDAKsvskQYSLKVTKLEHDAEQAKVELIETQKQLQELENKD 815
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKL---NELIASLEELERELE----QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 816 LSdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIqnekRANELEQSvdhmkyqkiqlQRKLREENEKRKQl 895
Cdd:PRK00409 568 LE------EAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV----KAHELIEA-----------RKRLNKANEKKEK- 625
|
170 180
....*....|....*....|.
gi 1034670642 896 daviKRDQQKIKEIQLKTGQE 916
Cdd:PRK00409 626 ----KKKKQKEKQEELKVGDE 642
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-1058 |
3.61e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 704 ELSDTQDETQKSDLENEDLKIDCLQESQELNLQK--LKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 781
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 782 QYSLKVTKLEHDAEQAKVELIETQKQLQELenkdlsdvamkvklqkefRKKMDAAKLRVQVLQKKQQdskklaslsiQNE 861
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDEL------------------RAELTLLNEEAANLRERLE----------SLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 862 KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ-LKTGQEEGLKPKAEDLDACNLKRRKGSfgs 940
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnERASLEEALALLRSELEELSEELRELE--- 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 941 iDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKkrEAIVSKKEALLQEKSHLENKKLrssqalnTDSLKISTRLNLL 1020
Cdd:TIGR02168 908 -SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ--ERLSEEYSLTLEEAEALENKIE-------DDEEEARRRLKRL 977
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1034670642 1021 EQELSE-KNVQLQT-----STAEEKTKISEQVEVLQKEKDQLQK 1058
Cdd:TIGR02168 978 ENKIKElGPVNLAAieeyeELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
840-1000 |
3.78e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 840 VQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQR--KLREENEKRKQLDAVIKRDQQKikeiqlktgqEE 917
Cdd:PRK12705 22 VVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERnqQRQEARREREELQREEERLVQK----------EE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 918 GLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQE------LEELEADLKKREAIVSKKealLQE 991
Cdd:PRK12705 92 QLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEqarkllLKLLDAELEEEKAQRVKK---IEE 168
|
....*....
gi 1034670642 992 KSHLENKKL 1000
Cdd:PRK12705 169 EADLEAERK 177
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
635-1111 |
3.98e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 635 PMYSLDRIFAG-------FRTRSQMLLGHIEEqdkvlhcqfsDNSDDEESEGQeksgtRCRSRSWIQKPDSvcslveLSD 707
Cdd:pfam12128 177 PLRHIDKIAKAmhskegkFRDVKSMIVAILED----------DGVVPPKSRLN-----RQQVEHWIRDIQA------IAG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 708 TQDETQKSDLENEDLKIdclQESQELNLQKLK--------NSERILTEAKQKMRELTINIKMKEDLIKELIKTGN----- 774
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNT---LESAELRLSHLHfgyksdetLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNgelsa 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 775 -DAKSVSKQYSLKVTKLEH------DAEQAKVEL-----IETQKQLQELENKDLSDVAMKVklQKEFRKKMDAAKLR--- 839
Cdd:pfam12128 313 aDAAVAKDRSELEALEDQHgafldaDIETAAADQeqlpsWQSELENLEERLKALTGKHQDV--TAKYNRRRSKIKEQnnr 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 840 -VQVLQKKQQDSKKLASLSIQNEKRANE-LEQSVDHMKYQKI------QLQRKLREENEKRKQLDAVIKRD---QQKIKE 908
Cdd:pfam12128 391 dIAGIKDKLAKIREARDRQLAVAEDDLQaLESELREQLEAGKlefneeEYRLKSRLGELKLRLNQATATPElllQLENFD 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 909 IQLKTGQEEGLKPKAEDLDACNLKRRKGSfgsidhlqKLDEQKKWLDEEVEKVLNQRQELEELE---------------- 972
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARK--------RRDQASEALRQASRRLEERQSALDELElqlfpqagtllhflrk 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 973 --ADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKIS-TRLNL-----LEQELSEKNVQLQTS--TAEEKTK- 1041
Cdd:pfam12128 543 eaPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDlKRIDVpewaaSEEELRERLDKAEEAlqSAREKQAa 622
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034670642 1042 ISEQVEVLQKEKDQLQKRRHNVDEKLKNGRV----LSPEEEHVLFQLEegiEALEAAIEYRNESIQNRQKSLRA 1111
Cdd:pfam12128 623 AEEQLVQANGELEKASREETFARTALKNARLdlrrLFDEKQSEKDKKN---KALAERKDSANERLNSLEAQLKQ 693
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
714-1214 |
6.44e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 714 KSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHD 793
Cdd:pfam10174 218 RNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 794 AEQAKVELIETQKQLQELENKDlSDVAMKVKLQKE-----------FRKKMDAAKLRV----QVLQKKQqdsKKLASLSI 858
Cdd:pfam10174 298 LSKKESELLALQTKLETLTNQN-SDCKQHIEVLKEsltakeqraaiLQTEVDALRLRLeekeSFLNKKT---KQLQDLTE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 859 QNEKRANELEQSVDHM--KYQKIQ-LQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDldACNLKRRK 935
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLdvKERKINvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEE--ALSEKERI 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 936 gsfgsidhLQKLDEQKKWLDEEvekvlnQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKIST 1015
Cdd:pfam10174 452 --------IERLKEQREREDRE------RLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDS 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1016 RLNLLEQELSEK------------NVQLQTSTAEEKTKISEQVEVLQKE----KDQLQKRRHNVDEKLKNGRvlspEEEH 1079
Cdd:pfam10174 518 KLKSLEIAVEQKkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEvaryKEESGKAQAEVERLLGILR----EVEN 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1080 VLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREaERKQQLy 1159
Cdd:pfam10174 594 EKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALE-KTRQEL- 671
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1034670642 1160 nEEMKMKVLERDNMVRELESALDhlKLQCDRRLTLQQKeHEQKMQLLLHHFKEQD 1214
Cdd:pfam10174 672 -DATKARLSSTQQSLAEKDGHLT--NLRAERRKQLEEI-LEMKQEALLAAISEKD 722
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
883-1246 |
7.66e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 883 RKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRrkGSFGSIDHLQKLDEQKkwlDEEVEKVL 962
Cdd:PLN02939 38 RRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQ--KSTSSDDDHNRASMQR---DEAIAAID 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 963 NQRQE------------LEELEADLKKREA-IVSKKEALLQEKSHLEnKKLRSSQALNTdslkistRLNLLEQELSEKNV 1029
Cdd:PLN02939 113 NEQQTnskdgeqlsdfqLEDLVGMIQNAEKnILLLNQARLQALEDLE-KILTEKEALQG-------KINILEMRLSETDA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1030 QLQTStAEEKTkiseQVEVLQkekDQLQKRRHNVDEK--LKNGRVLSPEEEHVLFQLE-----EGIEALEAAI------E 1096
Cdd:PLN02939 185 RIKLA-AQEKI----HVEILE---EQLEKLRNELLIRgaTEGLCVHSLSKELDVLKEEnmllkDDIQFLKAELievaetE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1097 YRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTilfrYFNKVVNLREAERKQQLYNEEMKMkVLERD----N 1172
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDC----WWEKVENLQDLLDRATNQVEKAAL-VLDQNqdlrD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1173 MVRELESALDHLKLQ--CDRRLTLQQkeheQKMQLLLHHFKEQDGEgIMETFKTYEDKIQQ----LEKDLYFYKKTSRDH 1246
Cdd:PLN02939 332 KVDKLEASLKEANVSkfSSYKVELLQ----QKLKLLEERLQASDHE-IHSYIQLYQESIKEfqdtLSKLKEESKKRSLEH 406
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
732-1075 |
9.05e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 732 ELNLQKLKNSERILTEAKQKmrELTINIKMKEDLIKELIKTGNDakSVSKQYSLKVTKLEhdaeqakvelIETQKQLQEL 811
Cdd:PTZ00108 1005 ERELARLSNKVRFIKHVING--ELVITNAKKKDLVKELKKLGYV--RFKDIIKKKSEKIT----------AEEEEGAEED 1070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 812 ENKDLSDVAMKVKLQKEF----RKKM------DAAKLRVQvLQKKQQDSKKLASLSIQNEKRAnELEqsvdhmkyqkiQL 881
Cdd:PTZ00108 1071 DEADDEDDEEELGAAVSYdyllSMPIwsltkeKVEKLNAE-LEKKEKELEKLKNTTPKDMWLE-DLD-----------KF 1137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 882 QRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKV 961
Cdd:PTZ00108 1138 EEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKK 1217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 962 LNQRQELEELEADLKKREAIVSKKEALLQEKShLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTA---EE 1038
Cdd:PTZ00108 1218 SNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNN-SSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRpdgES 1296
|
330 340 350
....*....|....*....|....*....|....*..
gi 1034670642 1039 KTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSP 1075
Cdd:PTZ00108 1297 NGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTAR 1333
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
763-1005 |
9.68e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 763 EDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKdlSDVAMK--VKLQKEFRKKMDAAKLRV 840
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE--IDKLQAeiAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 841 QVLQKKQQDSKKLASL----SIQNE-KRANELEQSVDHMKyQKIQLQRKLREENE-KRKQLDAVIKRDQQKIKEIQLKTG 914
Cdd:COG3883 93 RALYRSGGSVSYLDVLlgseSFSDFlDRLSALSKIADADA-DLLEELKADKAELEaKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 915 QEEGLKPKAEDLdacnlkrrkgsfgsidhLQKLDEQKkwlDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSH 994
Cdd:COG3883 172 ELEAQQAEQEAL-----------------LAQLSAEE---AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
250
....*....|.
gi 1034670642 995 LENKKLRSSQA 1005
Cdd:COG3883 232 AAAAAAAAAAA 242
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
752-889 |
1.01e-03 |
|
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: 43.11 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 752 MRELTINIKMKEDLIKELIKTGNDA-----------KSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVA 820
Cdd:smart00435 233 LQEQLKELTAKDGNVAEKILAYNRAnrevailcnhqRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRK 312
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670642 821 MKVKLQKEFRkkmdaaKLRVQVLQKKQQDSKKLASlsiqnEKRANELEQSVdhmkyQKIQLQRKLREEN 889
Cdd:smart00435 313 LKSKFERDNE------KLDAEVKEKKKEKKKEEKK-----KKQIERLEERI-----EKLEVQATDKEEN 365
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
855-1205 |
1.16e-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: 43.42 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 855 SLSIQNEKRANELEQ--SVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLK 932
Cdd:pfam02463 146 IIAMMKPERRLEIEEeaAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 933 RRKgsfgsidhLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIvskkealLQEKSHLENKKLRSSQALNTDSLK 1012
Cdd:pfam02463 226 LLY--------LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEK-------LAQVLKENKEEEKEKKLQEEELKL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1013 ISTRLNLLEQELSEKNVQlqtstaeeKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALE 1092
Cdd:pfam02463 291 LAKEEEELKSELLKLERR--------KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1093 AAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIrtilfryfNKVVNLREAERKQQLYNEEMKMKVLERDN 1172
Cdd:pfam02463 363 KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--------EAQLLLELARQLEDLLKEEKKEELEILEE 434
|
330 340 350
....*....|....*....|....*....|...
gi 1034670642 1173 MVRELESALDHLKLQCDRRLTLQQKEHEQKMQL 1205
Cdd:pfam02463 435 EEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
785-997 |
1.30e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 785 LKVTKLEHDAEQAKvELIETQKQLQELENKdLSDVamkVKLQKEFRKKMDAAKLRVQVLQKKQQDskkLASLSIQNEKRA 864
Cdd:PRK02224 489 EEVEEVEERLERAE-DLVEAEDRIERLEER-REDL---EELIAERRETIEEKRERAEELRERAAE---LEAEAEEKREAA 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 865 NELEQSVDHMKYQKIQLQRKLREENEKRKQLDAV-------------IKRDQQKIKEIQLKTGQE-EGLKPK-------A 923
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadaedeIERLREKREALAELNDERrERLAEKrerkrelE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 924 EDLDACNL---KRRKGSFGSI-----DHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHL 995
Cdd:PRK02224 641 AEFDEARIeeaREDKERAEEYleqveEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYDEAEEL 720
|
..
gi 1034670642 996 EN 997
Cdd:PRK02224 721 ES 722
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
952-1161 |
1.39e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 952 KWLDEEVEKVlnqRQELEELEADL---KKREAIVS---KKEALLQEKSHLENKKlrssQALNTDSLKISTRLNLLEQELS 1025
Cdd:COG3206 178 EFLEEQLPEL---RKELEEAEAALeefRQKNGLVDlseEAKLLLQQLSELESQL----AEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1026 EKNVQL-QTSTAEEKTKISEQVEVLQKEKDQLQKR---RH----NVDEKLKNGRVlspeeehvlfQLEEGIEALEAAIEY 1097
Cdd:COG3206 251 SGPDALpELLQSPVIQQLRAQLAELEAELAELSARytpNHpdviALRAQIAALRA----------QLQQEAQRILASLEA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034670642 1098 RNESIQNRQKSLRASFHNLsRGEANVLEKLAclspVEIRTILfryfnkvvnlREAERKQQLYNE 1161
Cdd:COG3206 321 ELEALQAREASLQAQLAQL-EARLAELPELE----AELRRLE----------REVEVARELYES 369
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
799-1159 |
1.56e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 799 VELIETQKQLQELENKdLSDVAMKVKLQkefRKKMDAAKLRVQVLQKKQQDSKKLASLSIQneKRANELEQSVDHMKYQK 878
Cdd:PRK04863 837 AELRQLNRRRVELERA-LADHESQEQQQ---RSQLEQAKEGLSALNRLLPRLNLLADETLA--DRVEEIREQLDEAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 879 IQLQRKLREENEKRKQLdAVIKRDQQKIKEI-----QLKTGQEEgLKPKAEDLDacNLKRRKGSFGSIDHLQKLDEQkkw 953
Cdd:PRK04863 911 RFVQQHGNALAQLEPIV-SVLQSDPEQFEQLkqdyqQAQQTQRD-AKQQAFALT--EVVQRRAHFSYEDAAEMLAKN--- 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 954 lDEEVEKVlnqRQELEELEADLkkREAivskKEALLQEKSHLENK-----KLRSSQALNTDSLKistrlnLLEQELSEKN 1028
Cdd:PRK04863 984 -SDLNEKL---RQRLEQAEQER--TRA----REQLRQAQAQLAQYnqvlaSLKSSYDAKRQMLQ------ELKQELQDLG 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1029 VQLqTSTAEEKT-----KISEQVEVLQKEKDQLQKRRHNVDEKLKN--GRVLSPEEEhvLFQLEEGIEALEAAIeyrnes 1101
Cdd:PRK04863 1048 VPA-DSGAEERArarrdELHARLSANRSRRNQLEKQLTFCEAEMDNltKKLRKLERD--YHEMREQVVNAKAGW------ 1118
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1102 iqnrQKSLRASFHN-----LSRGEanvlekLACLSPVEIRTI------LFRY-------FNKVVNLRE----AERKQQLY 1159
Cdd:PRK04863 1119 ----CAVLRLVKDNgverrLHRRE------LAYLSADELRSMsdkalgALRLavadnehLRDVLRLSEdpkrPERKVQFY 1188
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
667-1213 |
1.68e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 667 QFSDNSDDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSDLEnedLKIDCLQE-SQELNLQKLKNSERIL 745
Cdd:TIGR00606 302 QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ---LQADRHQEhIRARDSLIQSLATRLE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 746 TEAKQKMRELTINIKMKEDLIKEliKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKL 825
Cdd:TIGR00606 379 LDGFERGPFSERQIKNFHTLVIE--RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 826 QKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANE-LEQSVDHMKYQKIQLQRKLREENEKRKQLD-------- 896
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTEtLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttrtq 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 897 -AVIKRDQ----QKIKEIQLKTGQE----EGLKPKAEDLDACNLKRRKGSFGSIDHL-------QKLDEQKKWLDEEVEK 960
Cdd:TIGR00606 537 mEMLTKDKmdkdEQIRKIKSRHSDEltslLGYFPNKKQLEDWLHSKSKEINQTRDRLaklnkelASLEQNKNHINNELES 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 961 VLNQRQELEE----------LEADL---KKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEK 1027
Cdd:TIGR00606 617 KEEQLSSYEDklfdvcgsqdEESDLerlKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1028 NVQLQTSTAEEKTKISEqvevLQKEKDQLQKRRhnvDEKLkngrVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQK 1107
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKS----TESELKKKEKRR---DEML----GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1108 SLRASFHNLsrGEANVLEKLA--CLSPVEIRTILFRYFnKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHL- 1184
Cdd:TIGR00606 766 DIEEQETLL--GTIMPEEESAkvCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVv 842
|
570 580 590
....*....|....*....|....*....|
gi 1034670642 1185 -KLQCDRRLTLQQKEHEQKMQLLLHHFKEQ 1213
Cdd:TIGR00606 843 sKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
959-1051 |
1.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 959 EKVLNQRQEL----EELEADLKKREAIVSKKEA-LLQEKSHLENKklrsSQALNtdslKISTRLNLLEQELSEKNVQLQT 1033
Cdd:PRK12704 57 EALLEAKEEIhklrNEFEKELRERRNELQKLEKrLLQKEENLDRK----LELLE----KREEELEKKEKELEQKQQELEK 128
|
90
....*....|....*...
gi 1034670642 1034 STAEEKTKISEQVEVLQK 1051
Cdd:PRK12704 129 KEEELEELIEEQLQELER 146
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
888-1204 |
2.00e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 888 ENEKRKQLDAVIKRdQQKIKEIQ----LKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLN 963
Cdd:pfam17380 267 ENEFLNQLLHIVQH-QKAVSERQqqekFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 964 QRQELEELEADLKKREaivskKEALLQEKSHLENKKLRSSQALNTDSLKISTRlnlLEQELsEKNVQLQTSTAEEKTKIS 1043
Cdd:pfam17380 346 RERELERIRQEERKRE-----LERIRQEEIAMEISRMRELERLQMERQQKNER---VRQEL-EAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1044 EQ-VEVLQKEKDQLQKRRHNVdeklkngRVLSPEEEHVLFQL-EEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEA 1121
Cdd:pfam17380 417 QQkVEMEQIRAEQEEARQREV-------RRLEEERAREMERVrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1122 NVLEKlaclspveirtilfryfnKVVNLREAERKQQLYNEEMKMKVLErdnmvRELESALDHLKLQCDRRLTLQQKEHEQ 1201
Cdd:pfam17380 490 EEQRR------------------KILEKELEERKQAMIEEERKRKLLE-----KEMEERQKAIYEEERRREAEEERRKQQ 546
|
...
gi 1034670642 1202 KMQ 1204
Cdd:pfam17380 547 EME 549
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
704-1083 |
2.09e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 704 ELSDTQDETQKSDLE--NEDLKIDCLQESQELNLQKLKNSERI----------LTEAKQKMRELTINIKMKEDLIKELIK 771
Cdd:pfam05557 112 ELSELRRQIQRAELElqSTNSELEELQERLDLLKAKASEAEQLrqnlekqqssLAEAEQRIKELEFEIQSQEQDSEIVKN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 772 TGNDAKSVSKQYSLKVTKLEH---------DAEQAKVELIETQKQLQELENKDLSDVAMKVKLQK--------------- 827
Cdd:pfam05557 192 SKSELARIPELEKELERLREHnkhlnenieNKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKleqelqswvklaqdt 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 828 --EFRKKMDAAKLRVQVLQKKQQDSKKLASLsiqnEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQK 905
Cdd:pfam05557 272 glNLRSPEDLSRRIEQLQQREIVLKEENSSL----TSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 906 I----KEIQlktGQEEGLKPKAEDLDACN-----LKRRKGSFGSIDHLQ-KLDEQKKWLDEEVEKVLNQRQELEELEADL 975
Cdd:pfam05557 348 VllltKERD---GYRAILESYDKELTMSNyspqlLERIEEAEDMTQKMQaHNEEMEAQLSVAEEELGGYKQQAQTLEREL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 976 KKREAIVSKKEA---------LLQEKSHL--ENKKLRSSqalntdslKISTRLNLLEQEL-------SEKNVQLQ---TS 1034
Cdd:pfam05557 425 QALRQQESLADPsyskeevdsLRRKLETLelERQRLREQ--------KNELEMELERRCLqgdydpkKTKVLHLSmnpAA 496
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1034670642 1035 TAEEKTKisEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQ 1083
Cdd:pfam05557 497 EAYQQRK--NQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFK 543
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
769-1092 |
2.10e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 769 LIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELEnKDLSDVAMK-VKLQKEFRKKMDAAKLRVQ----VL 843
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQ-KRIRLLEKReAEAEEALREQAELNRLKKKyleaLN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 844 QKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKA 923
Cdd:pfam05557 90 KKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 924 EDL------------DACNLKRRKGSFGSIDHLQK----LDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEA 987
Cdd:pfam05557 170 QRIkelefeiqsqeqDSEIVKNSKSELARIPELEKelerLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 988 LLQEKSHLEnKKLRSSQALNTDslkisTRLNLLEQE-LSEKNVQLQtstaEEKTKISEQVEVLQKEKDQLQKRRHNVDEK 1066
Cdd:pfam05557 250 LELEKEKLE-QELQSWVKLAQD-----TGLNLRSPEdLSRRIEQLQ----QREIVLKEENSSLTSSARQLEKARRELEQE 319
|
330 340
....*....|....*....|....*.
gi 1034670642 1067 LKNGRVLSPEEEHVLFQLEEGIEALE 1092
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQ 345
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
715-910 |
2.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 715 SDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslKVTKLEHDA 794
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------------EIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 795 EQAKVELIETQKQLQE-----------LENKDLSDVAMKVKLQKEFrkkMDAAKlrvQVLQKKQQDSKKLASLSIQNEKR 863
Cdd:COG3883 82 EERREELGERARALYRsggsvsyldvlLGSESFSDFLDRLSALSKI---ADADA---DLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034670642 864 ANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ 910
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
959-1102 |
2.59e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 959 EKVLNQRQELEELEADL----KKREAIVSKKEALLQEKShlENKKLRSSqalntdslkistrlnlLEQELSEKNVQLQTs 1034
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKE--EIHKLRNE----------------FEKELRERRNELQK- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034670642 1035 tAEEKTK-----ISEQVEVLQKEKDQLQKRRHNVDEKLKNgrvlspeeehvLFQLEEGIEALEAAIEYRNESI 1102
Cdd:PRK12704 87 -LEKRLLqkeenLDRKLELLEKREEELEKKEKELEQKQQE-----------LEKKEEELEELIEEQLQELERI 147
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
798-1057 |
3.28e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 798 KVELI-------ETQKQLQEL---ENKDLSDVAMKVKLQKEFRKKMDAAKLrvqvLQKKQQDSKKLASL-SIQNEKRANE 866
Cdd:PRK05771 8 KVLIVtlksykdEVLEALHELgvvHIEDLKEELSNERLRKLRSLLTKLSEA----LDKLRSYLPKLNPLrEEKKKVSVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 867 LEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEiqlktgqeegLKP-KAEDLDACNLKRRKGS---FGSID 942
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIER----------LEPwGNFDLDLSLLLGFKYVsvfVGTVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 943 HlQKLDEQKKWLDEEVEKVLNQRQELEELEA-DLKKREAIVSK--KEALLQEKSHLENKKLrsSQALNtdslKISTRLNL 1019
Cdd:PRK05771 154 E-DKLEELKLESDVENVEYISTDKGYVYVVVvVLKELSDEVEEelKKLGFERLELEEEGTP--SELIR----EIKEELEE 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034670642 1020 LEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQ 1057
Cdd:PRK05771 227 IEKERESLLEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
838-991 |
3.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 838 LRVQVLQKKQQDSKKLASLSIQN-EKRANEL-EQSVDHMKYQKIQLQRKL-REENEKRKQLDAVIKRDQQKikeiqlktg 914
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEaKKEAEAIkKEALLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQK--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 915 qEEGLKPKAEDLDacnlKRRK---GSFGSIDHLQK-LDEQKKWLDEEVEKvlnQRQELEELeADLKKREAivskKEALLQ 990
Cdd:PRK12704 95 -EENLDRKLELLE----KREEeleKKEKELEQKQQeLEKKEEELEELIEE---QLQELERI-SGLTAEEA----KEILLE 161
|
.
gi 1034670642 991 E 991
Cdd:PRK12704 162 K 162
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
699-1085 |
3.57e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 699 VCSLVELSDTQDETQKSDLENEDLKIDCLQESQELNLQKL-KNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAK 777
Cdd:TIGR00606 682 VCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKeKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 778 SVSKQYSLKVTKLEH-DAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASL 856
Cdd:TIGR00606 762 RLKNDIEEQETLLGTiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 857 SIQNE----------KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDL 926
Cdd:TIGR00606 842 VSKIElnrkliqdqqEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 927 dacnLKRRKGSFGSIDHLQKLDEQK-KWLDEEVEKVLNQRQELEELEAD-----LKKREAIVSKKEALLQE-KSHLE--N 997
Cdd:TIGR00606 922 ----QQEKEELISSKETSNKKAQDKvNDIKEKVKNIHGYMKDIENKIQDgkddyLKQKETELNTVNAQLEEcEKHQEkiN 997
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 998 KKLRSSQAlNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISE--QVEVLQkEKDQLQKRRHNVD-----EKLKNG 1070
Cdd:TIGR00606 998 EDMRLMRQ-DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEmgQMQVLQ-MKQEHQKLEENIDlikrnHVLALG 1075
|
410
....*....|....*
gi 1034670642 1071 RVLSPEEEHVLFQLE 1085
Cdd:TIGR00606 1076 RQKGYEKEIKHFKKE 1090
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
733-910 |
3.75e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 733 LNLQKLKNSeriLTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELE 812
Cdd:COG1579 10 LDLQELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 813 N-KDLSDvamkvkLQKEfrkkMDAAKLRVQVLQKKQqdskklaslsIQNEKRANELEQSVDHMKYQKIQLQRKLreeNEK 891
Cdd:COG1579 87 NnKEYEA------LQKE----IESLKRRISDLEDEI----------LELMERIEELEEELAELEAELAELEAEL---EEK 143
|
170
....*....|....*....
gi 1034670642 892 RKQLDAVIKRDQQKIKEIQ 910
Cdd:COG1579 144 KAELDEELAELEAELEELE 162
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
749-977 |
3.83e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 749 KQKMRELTINIK---MKEDLIKELIKTGND----AKSVSKQ----YSLKVTKLEHDAEQAKVELIETQKQLQEL--ENKD 815
Cdd:PHA02562 173 KDKIRELNQQIQtldMKIDHIQQQIKTYNKnieeQRKKNGEniarKQNKYDELVEEAKTIKAEIEELTDELLNLvmDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 816 LSDVAMKVKlQKEFRKKMDAAKL-RVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQ 894
Cdd:PHA02562 253 PSAALNKLN-TAAAKIKSKIEQFqKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 895 LDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDAcnlkrrkgsfgsidHLQKLDEQKKWLDEEVEKVLNQRQELEELEAD 974
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKA--------------AIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
...
gi 1034670642 975 LKK 977
Cdd:PHA02562 398 LVK 400
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
704-1234 |
5.56e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 704 ELSDTQDETQ----KSDLENEDLKIDCLQ-ESQELNLQKLKNSerilteaKQKMRELTINIK--MKEDLIKELIKTGNDA 776
Cdd:TIGR01612 688 AIDNTEDKAKlddlKSKIDKEYDKIQNMEtATVELHLSNIENK-------KNELLDIIVEIKkhIHGEINKDLNKILEDF 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 777 KSVSKQYSLKVtkleHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASl 856
Cdd:TIGR01612 761 KNKEKELSNKI----NDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIIN- 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 857 SIQNEKraNELEQSVDhmKYqkIQLQRKLREE-NEKRKQLDAVIKRDQQKIKEIQLKtgqeeglkpkaedldacnlkrrk 935
Cdd:TIGR01612 836 EMKFMK--DDFLNKVD--KF--INFENNCKEKiDSEHEQFAELTNKIKAEISDDKLN----------------------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 936 gsfgsiDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALlqEKSHLENKKLRSSQALNTDSLKISt 1015
Cdd:TIGR01612 887 ------DYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESI--EKFHNKQNILKEILNKNIDTIKES- 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1016 rlNLLEQELSEK--NVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKngrvlSPEEEHVLFQLEEGIEA--- 1090
Cdd:TIGR01612 958 --NLIEKSYKDKfdNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLG-----KNKENMLYHQFDEKEKAtnd 1030
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1091 LEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEK-LACLSpveiRTILFRYFNKVVNLREAERKQQLYN--EEMKMKV 1167
Cdd:TIGR01612 1031 IEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKnIELLN----KEILEEAEINITNFNEIKEKLKHYNfdDFGKEEN 1106
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670642 1168 LERDNMVRELESALDHLKLQCDRRLTlQQKEHEQKMQLLLHHFKEQ--DGEGIMETfKTYEDKIQQLEK 1234
Cdd:TIGR01612 1107 IKYADEINKIKDDIKNLDQKIDHHIK-ALEEIKKKSENYIDEIKAQinDLEDVADK-AISNDDPEEIEK 1173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
816-1112 |
5.88e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 816 LSDVAMKVKLQKEFRKKMDAAKLRVQVLQK----KQQDSKKLASLSIQNE------KRANELEQSvdhmkYQKIQLQRKL 885
Cdd:COG3206 96 LERVVDKLNLDEDPLGEEASREAAIERLRKnltvEPVKGSNVIEISYTSPdpelaaAVANALAEA-----YLEQNLELRR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 886 REENEKRKQLDAVIKRDQQKIKEIQLKtgqeegLKpkaedldacNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQR 965
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAA------LE---------EFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 966 QELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQaLNTDSLKISTRLN-------LLEQELSEKNVQLQTSTAEE 1038
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE-LEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRI 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034670642 1039 KTKISEQVEVLQKEKDQLQKRRHNVDEKLKNgrvlSPEEEHVLFQLEEGIEALEAAieYrnESIQNRQKSLRAS 1112
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLEREVEVAREL--Y--ESLLQRLEEARLA 380
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
714-1130 |
7.28e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 714 KSDLENEDLKIDCLQESQELNLQKLKNSERIlteakQKMRE-LTINIKMKEDLIKELIKtgndAKSVSKQYSLKVTKLEH 792
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLLQLENFDERI-----ERAREeQEAANAEVERLQSELRQ----ARKRRDQASEALRQASR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 793 DAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQ------VLQKKQQDSKKLASLSIQNEK-RAN 865
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRtdldpeVWDGSVGGELNLYGVKLDLKRiDVP 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 866 ELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLK-TGQEEGLKPKAEDL-----------DACN--L 931
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREeTFARTALKNARLDLrrlfdekqsekDKKNkaL 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 932 KRRKGSFGsiDHLQKLDEQKKWLDEEVEKVLNQRQEleeleadlKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSL 1011
Cdd:pfam12128 674 AERKDSAN--ERLNSLEAQLKQLDKKHQAWLEEQKE--------QKREARTEKQAYWQVVEGALDAQLALLKAAIAARRS 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1012 KISTRLNLLEQ----ELSEKNVQLQTStaeekTKISEQVEVLQKEKDQLQKRRHNVDE----------KLKNGRVLSPEE 1077
Cdd:pfam12128 744 GAKAELKALETwykrDLASLGVDPDVI-----AKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlQRRPRLATQLSN 818
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034670642 1078 -EHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLS---RGEANVLEKLACL 1130
Cdd:pfam12128 819 iERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSenlRGLRCEMSKLATL 875
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
704-1096 |
7.58e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 704 ELSDTQDETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQY 783
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 784 SLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKR 863
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 864 ANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIK----RDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFG 939
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLgrtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 940 SIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALntdslkistRLNL 1019
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE---------REEL 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1020 LEQELSEKNVQLQTstAEEKTKISEQVEVLQKEKDQLQKRRhnvdEKLknGRV--LSPEE--------EHVLFQ---LEE 1086
Cdd:COG1196 738 LEELLEEEELLEEE--ALEELPEPPDLEELERELERLEREI----EAL--GPVnlLAIEEyeeleeryDFLSEQredLEE 809
|
410
....*....|
gi 1034670642 1087 GIEALEAAIE 1096
Cdd:COG1196 810 ARETLEEAIE 819
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
791-1255 |
8.08e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 791 EHDaEQAKvELIETQKQLQELEnkdlsdvaMKVKLQKEfrkKMDAAKLRVQVLQKKQQdSKKLASLSIQNE----KRANE 866
Cdd:pfam10174 124 EHE-RQAK-ELFLLRKTLEEME--------LRIETQKQ---TLGARDESIKKLLEMLQ-SKGLPKKSGEEDwertRRIAE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 867 LEQSVDHMK---YQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDL-DACNLKRRKGSFGSID 942
Cdd:pfam10174 190 AEMQLGHLEvllDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLeDEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 943 HLQKLdeqkkwldEEVEKVLNQ----RQELEELEADLKKRE----AIVSKKEALLQEKS----HLE------NKKLRSSQ 1004
Cdd:pfam10174 270 REEEI--------KQMEVYKSHskfmKNKIDQLKQELSKKEsellALQTKLETLTNQNSdckqHIEvlkeslTAKEQRAA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1005 ALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISE-------------QVEVLQKEKDQLQKRRHNVDEKLKN-- 1069
Cdd:pfam10174 342 ILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEirdlkdmldvkerKINVLQKKIENLQEQLRDKDKQLAGlk 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1070 GRVLSPEEEH-----VLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLspveiRTILFRYFN 1144
Cdd:pfam10174 422 ERVKSLQTDSsntdtALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSAL-----QPELTEKES 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 1145 KVVNLREAERKQqlyneemKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQlllhhfkEQDGEGIMetfkt 1224
Cdd:pfam10174 497 SLIDLKEHASSL-------ASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEA-------VRTNPEIN----- 557
|
490 500 510
....*....|....*....|....*....|.
gi 1034670642 1225 yeDKIQQLEKDLYFYKKTSRDHKKKLKELVG 1255
Cdd:pfam10174 558 --DRIRLLEQEVARYKEESGKAQAEVERLLG 586
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
820-919 |
8.60e-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: 38.33 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 820 AMKVKLQKEFRKKMDAAKLRVQVLQKKQQD-SKKLASLSI-QNEKRANELEQSVdhMKYQkiQLQRKLREENEKRKQldA 897
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKlQKDAATLSEaAREKKEKELQKKV--QEFQ--RKQQKLQQDLQKRQQ--E 91
|
90 100
....*....|....*....|..
gi 1034670642 898 VIKRDQQKIKEIQLKTGQEEGL 919
Cdd:smart00935 92 ELQKILDKINKAIKEVAKKKGY 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-978 |
8.88e-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: 40.81 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 703 VELSDTQDETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQ 782
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 783 YSLKVTKLEHDAEQAKVELIETQKQLQELEN-KDLSDVAMKvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNE 861
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNeRASLEEALA-LLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 862 KRANELEQSVDHMKyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTgqeeglkpKAEDLDACNLkrrkgsfGSI 941
Cdd:TIGR02168 929 LRLEGLEVRIDNLQ-ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN--------KIKELGPVNL-------AAI 992
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034670642 942 DHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKR 978
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
861-992 |
9.39e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670642 861 EKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKI------KEIQLKTGQEEGLKPKAEDLDacnlKRR 934
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYEALQKEIESLKRRISDLE----DEI 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670642 935 KGSFGSIDHLQK-LDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEK 992
Cdd:COG1579 113 LELMERIEELEEeLAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| |
